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Plasmepsin_2.pdb
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Plasmepsin_2.pdb
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HEADER HYDROLASE 08-JUN-15 5BWY
TITLE STRUCTURE OF PROPLASMEPSIN II FROM PLASMODIUM FALCIPARUM, SPACE GROUP
TITLE 2 P43212
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLASMEPSIN-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 78-453;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_TAXID: 5833;
SOURCE 4 GENE: PFAG_05140;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS MALARIA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.RECACHA,I.AKOPJANA,K.TARS,K.JAUDZEMS
REVDAT 4 20-FEB-19 5BWY 1 REMARK LINK
REVDAT 3 18-APR-18 5BWY 1 JRNL
REVDAT 2 17-JAN-18 5BWY 1 REMARK
REVDAT 1 16-DEC-15 5BWY 0
JRNL AUTH R.RECACHA,K.JAUDZEMS,I.AKOPJANA,A.JIRGENSONS,K.TARS
JRNL TITL CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM PROPLASMEPSIN IV:
JRNL TITL 2 THE PLASTICITY OF PROPLASMEPSINS.
JRNL REF ACTA CRYSTALLOGR F STRUCT V. 72 659 2016
JRNL REF 2 BIOL COMMUN
JRNL REFN ESSN 2053-230X
JRNL PMID 27599854
JRNL DOI 10.1107/S2053230X16011663
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.K.BERNSTEIN,M.M.CHERNEY,H.LOETSCHER,R.G.RIDLEY,M.N.JAMES
REMARK 1 TITL CRYSTAL STRUCTURE OF THE NOVEL ASPARTIC PROTEINASE ZYMOGEN
REMARK 1 TITL 2 PROPLASMEPSIN II FROM PLASMODIUM FALCIPARUM.
REMARK 1 REF NAT. STRUCT. BIOL. V. 6 32 1999
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 9886289
REMARK 1 DOI 10.1038/4905
REMARK 1 REFERENCE 2
REMARK 1 AUTH N.K.BERNSTEIN,M.M.CHERNEY,C.A.YOWELL,J.B.DAME,M.N.JAMES
REMARK 1 TITL STRUCTURAL INSIGHTS INTO THE ACTIVATION OF P. VIVAX
REMARK 1 TITL 2 PLASMEPSIN.
REMARK 1 REF J. MOL. BIOL. V. 329 505 2003
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 12767832
REMARK 1 DOI 10.1016/S0022-2836(03)00444-3
REMARK 2
REMARK 2 RESOLUTION. 2.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.69
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 14249
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.280
REMARK 3 FREE R VALUE TEST SET COUNT : 752
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 44.6964 - 4.5201 1.00 2854 154 0.1710 0.1744
REMARK 3 2 4.5201 - 3.5882 1.00 2704 154 0.1741 0.2387
REMARK 3 3 3.5882 - 3.1348 1.00 2673 144 0.2136 0.2853
REMARK 3 4 3.1348 - 2.8482 1.00 2645 149 0.2632 0.3245
REMARK 3 5 2.8482 - 2.6441 1.00 2621 151 0.3290 0.3509
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 3102
REMARK 3 ANGLE : 0.764 4222
REMARK 3 CHIRALITY : 0.029 477
REMARK 3 PLANARITY : 0.003 541
REMARK 3 DIHEDRAL : 15.353 1125
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 78P THROUGH 30 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5595 -4.1984 19.8573
REMARK 3 T TENSOR
REMARK 3 T11: 0.6463 T22: 0.5691
REMARK 3 T33: 0.4624 T12: -0.0726
REMARK 3 T13: 0.0426 T23: -0.1012
REMARK 3 L TENSOR
REMARK 3 L11: 2.2228 L22: 3.1162
REMARK 3 L33: 7.7428 L12: 0.3401
REMARK 3 L13: -1.0866 L23: 0.2340
REMARK 3 S TENSOR
REMARK 3 S11: 0.3010 S12: 0.3262 S13: -0.1451
REMARK 3 S21: -0.7867 S22: -0.0834 S23: -0.3578
REMARK 3 S31: -0.5563 S32: 0.6991 S33: -0.2529
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 31 THROUGH 186 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.5022 -11.6806 38.9101
REMARK 3 T TENSOR
REMARK 3 T11: 0.4816 T22: 0.3312
REMARK 3 T33: 0.2607 T12: -0.0642
REMARK 3 T13: 0.0143 T23: -0.0704
REMARK 3 L TENSOR
REMARK 3 L11: 2.7415 L22: 4.0514
REMARK 3 L33: 3.8918 L12: -0.8524
REMARK 3 L13: 0.3657 L23: -2.2101
REMARK 3 S TENSOR
REMARK 3 S11: -0.0903 S12: 0.1804 S13: -0.1425
REMARK 3 S21: -0.2156 S22: 0.1359 S23: -0.0153
REMARK 3 S31: 0.4894 S32: 0.4182 S33: -0.0188
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 187 THROUGH 329 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.9271 -0.3597 17.3616
REMARK 3 T TENSOR
REMARK 3 T11: 0.8564 T22: 0.3874
REMARK 3 T33: 0.3850 T12: -0.0448
REMARK 3 T13: -0.1364 T23: 0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 4.1790 L22: 2.5661
REMARK 3 L33: 6.5971 L12: -1.2632
REMARK 3 L13: -1.3351 L23: 0.9999
REMARK 3 S TENSOR
REMARK 3 S11: 0.1930 S12: 0.6837 S13: 0.0378
REMARK 3 S21: -1.1193 S22: 0.0523 S23: 0.2835
REMARK 3 S31: -0.5272 S32: -0.4053 S33: -0.2689
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5BWY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000210682.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.972
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14252
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.640
REMARK 200 RESOLUTION RANGE LOW (A) : 44.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.70000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1PFZ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE, 0.1 M SODIUM
REMARK 280 ACETATE, 25% PEG 3350, PH 4.6, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.75000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 44.69000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 44.69000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 86.62500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 44.69000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 44.69000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 28.87500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 44.69000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.69000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 86.62500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 44.69000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.69000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 28.87500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 57.75000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 119P CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 SG CYS A 249 CB CYS A 285 1.91
REMARK 500 OD1 ASP A 10 O HOH A 401 1.97
REMARK 500 O LEU A 102P O HOH A 402 2.02
REMARK 500 O THR A 65 O HOH A 403 2.08
REMARK 500 OD2 ASP A 34 O HOH A 404 2.08
REMARK 500 O GLY A 180 O HOH A 405 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 102P 30.47 -94.19
REMARK 500 LYS A 119P -8.42 64.32
REMARK 500 ASP A 24 -73.18 -79.56
REMARK 500 ILE A 277 45.75 -108.75
REMARK 500 PRO A 282 105.35 -49.34
REMARK 500 PRO A 297 107.36 -56.57
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5BWY A 78P 329 UNP W7FL77 W7FL77_PLAFA 78 453
SEQRES 1 A 376 GLU HIS LEU THR ILE GLY PHE LYS VAL GLU ASN ALA HIS
SEQRES 2 A 376 ASP ARG ILE LEU LYS THR ILE LYS THR HIS LYS LEU LYS
SEQRES 3 A 376 ASN TYR ILE LYS GLU SER VAL ASN PHE LEU ASN SER GLY
SEQRES 4 A 376 LEU THR LYS THR ASN TYR LEU GLY SER SER ASN ASP ASN
SEQRES 5 A 376 ILE GLU LEU VAL ASP PHE GLN ASN ILE MET PHE TYR GLY
SEQRES 6 A 376 ASP ALA GLU VAL GLY ASP ASN GLN GLN PRO PHE THR PHE
SEQRES 7 A 376 ILE LEU ASP THR GLY SER ALA ASN LEU TRP VAL PRO SER
SEQRES 8 A 376 VAL LYS CYS THR THR ALA GLY CYS LEU THR LYS HIS LEU
SEQRES 9 A 376 TYR ASP SER SER LYS SER ARG THR TYR GLU LYS ASP GLY
SEQRES 10 A 376 THR LYS VAL GLU MET ASN TYR VAL SER GLY THR VAL SER
SEQRES 11 A 376 GLY PHE PHE SER LYS ASP LEU VAL THR VAL GLY ASN LEU
SEQRES 12 A 376 SER LEU PRO TYR LYS PHE ILE GLU VAL ILE ASP THR ASN
SEQRES 13 A 376 GLY PHE GLU PRO THR TYR THR ALA SER THR PHE ASP GLY
SEQRES 14 A 376 ILE LEU GLY LEU GLY TRP LYS ASP LEU SER ILE GLY SER
SEQRES 15 A 376 VAL ASP PRO ILE VAL VAL GLU LEU LYS ASN GLN ASN LYS
SEQRES 16 A 376 ILE GLU ASN ALA LEU PHE THR PHE TYR LEU PRO VAL HIS
SEQRES 17 A 376 ASP LYS HIS THR GLY PHE LEU THR ILE GLY GLY ILE GLU
SEQRES 18 A 376 GLU ARG PHE TYR GLU GLY PRO LEU THR TYR GLU LYS LEU
SEQRES 19 A 376 ASN HIS ASP LEU TYR TRP GLN ILE THR LEU ASP ALA HIS
SEQRES 20 A 376 VAL GLY ASN ILE MET LEU GLU LYS ALA ASN CYS ILE VAL
SEQRES 21 A 376 ASP SER GLY THR SER ALA ILE THR VAL PRO THR ASP PHE
SEQRES 22 A 376 LEU ASN LYS MET LEU GLN ASN LEU ASP VAL ILE LYS VAL
SEQRES 23 A 376 PRO PHE LEU PRO PHE TYR VAL THR LEU CYS ASN ASN SER
SEQRES 24 A 376 LYS LEU PRO THR PHE GLU PHE THR SER GLU ASN GLY LYS
SEQRES 25 A 376 TYR THR LEU GLU PRO GLU TYR TYR LEU GLN HIS ILE GLU
SEQRES 26 A 376 ASP VAL GLY PRO GLY LEU CYS MET LEU ASN ILE ILE GLY
SEQRES 27 A 376 LEU ASP PHE PRO VAL PRO THR PHE ILE LEU GLY ASP PRO
SEQRES 28 A 376 PHE MET ARG LYS TYR PHE THR VAL PHE ASP TYR ASP ASN
SEQRES 29 A 376 HIS SER VAL GLY ILE ALA LEU ALA LYS LYS ASN LEU
FORMUL 2 HOH *51(H2 O)
HELIX 1 AA1 ASN A 88P HIS A 100P 1 13
HELIX 2 AA2 ASN A 104P ASN A 114P 1 11
HELIX 3 AA3 GLU A 7 GLN A 12 5 6
HELIX 4 AA4 ASP A 59 SER A 63 5 5
HELIX 5 AA5 PHE A 111 THR A 116 1 6
HELIX 6 AA6 PRO A 138 GLN A 146 1 9
HELIX 7 AA7 GLU A 174 ARG A 176 5 3
HELIX 8 AA8 PRO A 223 LEU A 231 1 9
HELIX 9 AA9 GLU A 269 TYR A 273 1 5
HELIX 10 AB1 GLY A 302 LYS A 308 1 7
SHEET 1 AA1 9 GLU A 67 TYR A 77 0
SHEET 2 AA1 9 GLY A 80 VAL A 93 -1 O GLY A 84 N VAL A 73
SHEET 3 AA1 9 ILE A 14 VAL A 22 -1 N GLU A 21 O THR A 92
SHEET 4 AA1 9 LEU A 80P GLU A 87P-1 N GLU A 87P O ILE A 14
SHEET 5 AA1 9 THR A 165 ILE A 170 -1 O LEU A 168 N ILE A 82P
SHEET 6 AA1 9 LEU A 153 TYR A 157 -1 N TYR A 157 O PHE A 167
SHEET 7 AA1 9 TYR A 309 ASP A 314 -1 O PHE A 313 N PHE A 154
SHEET 8 AA1 9 SER A 319 ALA A 325 -1 O GLY A 321 N VAL A 312
SHEET 9 AA1 9 TYR A 178 LYS A 186 -1 N THR A 183 O ILE A 322
SHEET 1 AA213 GLU A 67 TYR A 77 0
SHEET 2 AA213 GLY A 80 VAL A 93 -1 O GLY A 84 N VAL A 73
SHEET 3 AA213 LEU A 96 THR A 108 -1 O LEU A 96 N VAL A 93
SHEET 4 AA213 LEU A 40 PRO A 43 1 N VAL A 42 O ILE A 103
SHEET 5 AA213 GLY A 122 GLY A 125 -1 O ILE A 123 N TRP A 41
SHEET 6 AA213 PHE A 29 ASP A 34 1 N ILE A 32 O LEU A 124
SHEET 7 AA213 ILE A 14 VAL A 22 -1 N TYR A 17 O PHE A 31
SHEET 8 AA213 LEU A 80P GLU A 87P-1 N GLU A 87P O ILE A 14
SHEET 9 AA213 THR A 165 ILE A 170 -1 O LEU A 168 N ILE A 82P
SHEET 10 AA213 LEU A 153 TYR A 157 -1 N TYR A 157 O PHE A 167
SHEET 11 AA213 TYR A 309 ASP A 314 -1 O PHE A 313 N PHE A 154
SHEET 12 AA213 SER A 319 ALA A 325 -1 O GLY A 321 N VAL A 312
SHEET 13 AA213 TYR A 178 LYS A 186 -1 N THR A 183 O ILE A 322
SHEET 1 AA3 7 LYS A 265 LEU A 268 0
SHEET 2 AA3 7 PHE A 257 THR A 260 -1 N PHE A 259 O TYR A 266
SHEET 3 AA3 7 GLN A 194 VAL A 201 -1 N ASP A 198 O THR A 260
SHEET 4 AA3 7 ILE A 204 VAL A 213 -1 O CYS A 211 N ILE A 195
SHEET 5 AA3 7 THR A 298 LEU A 301 1 O LEU A 301 N ILE A 212
SHEET 6 AA3 7 ILE A 220 VAL A 222 -1 N THR A 221 O ILE A 300
SHEET 7 AA3 7 ILE A 289 GLY A 291 1 O ILE A 290 N VAL A 222
SHEET 1 AA4 4 ILE A 237 LYS A 238 0
SHEET 2 AA4 4 TYR A 245 LEU A 248 -1 O VAL A 246 N ILE A 237
SHEET 3 AA4 4 LEU A 284 LEU A 287 -1 O CYS A 285 N THR A 247
SHEET 4 AA4 4 LEU A 274 HIS A 276 -1 N GLN A 275 O MET A 286
SSBOND 1 CYS A 47 CYS A 52 1555 1555 2.03
SSBOND 2 CYS A 249 CYS A 285 1555 1555 2.03
CRYST1 89.380 89.380 115.500 90.00 90.00 90.00 P 43 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011188 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011188 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008658 0.00000
ATOM 1 N GLU A 78P -23.414 7.785 48.131 1.00 89.94 N
ANISOU 1 N GLU A 78P 15116 10036 9023 -1052 2269 -1576 N
ATOM 2 CA GLU A 78P -24.048 6.748 48.938 1.00 91.31 C
ANISOU 2 CA GLU A 78P 14859 10588 9248 -1095 2224 -1530 C
ATOM 3 C GLU A 78P -23.878 5.365 48.315 1.00 81.40 C
ANISOU 3 C GLU A 78P 13025 9641 8263 -1212 1904 -1369 C
ATOM 4 O GLU A 78P -23.621 4.386 49.016 1.00 71.94 O
ANISOU 4 O GLU A 78P 11594 8664 7077 -1519 1761 -1317 O
ATOM 5 CB GLU A 78P -25.534 7.051 49.125 1.00 94.11 C
ANISOU 5 CB GLU A 78P 15126 11052 9578 -583 2493 -1557 C
ATOM 6 CG GLU A 78P -26.297 5.956 49.845 1.00 86.92 C
ANISOU 6 CG GLU A 78P 13733 10565 8727 -640 2474 -1501 C
ATOM 7 CD GLU A 78P -27.795 6.103 49.696 1.00 96.19 C
ANISOU 7 CD GLU A 78P 14640 11967 9942 -111 2692 -1503 C
ATOM 8 OE1 GLU A 78P -28.230 6.960 48.898 1.00103.52 O
ANISOU 8 OE1 GLU A 78P 15708 12744 10883 359 2805 -1519 O
ATOM 9 OE2 GLU A 78P -28.537 5.360 50.371 1.00101.16 O
ANISOU 9 OE2 GLU A 78P 14913 12947 10578 -161 2752 -1482 O
ATOM 10 N HIS A 79P -24.030 5.291 46.996 1.00 69.06 N
ANISOU 10 N HIS A 79P 11277 8071 6893 -956 1798 -1291 N
ATOM 11 CA HIS A 79P -23.886 4.029 46.281 1.00 55.26 C
ANISOU 11 CA HIS A 79P 9040 6569 5389 -1044 1512 -1159 C
ATOM 12 C HIS A 79P -22.447 3.827 45.830 1.00 54.79 C
ANISOU 12 C HIS A 79P 9052 6395 5371 -1384 1294 -1130 C
ATOM 13 O HIS A 79P -21.757 4.785 45.481 1.00 69.33 O
ANISOU 13 O HIS A 79P 11263 7966 7115 -1437 1358 -1192 O
ATOM 14 CB HIS A 79P -24.827 3.980 45.078 1.00 56.38 C
ANISOU 14 CB HIS A 79P 8913 6816 5693 -604 1496 -1099 C
ATOM 15 CG HIS A 79P -26.269 4.157 45.433 1.00 56.57 C
ANISOU 15 CG HIS A 79P 8769 7042 5681 -235 1701 -1124 C
ATOM 16 ND1 HIS A 79P -26.953 3.267 46.234 1.00 59.24 N
ANISOU 16 ND1 HIS A 79P 8760 7705 6043 -354 1717 -1106 N
ATOM 17 CD2 HIS A 79P -27.159 5.121 45.099 1.00 63.51 C
ANISOU 17 CD2 HIS A 79P 9772 7870 6491 266 1908 -1161 C
ATOM 18 CE1 HIS A 79P -28.200 3.675 46.378 1.00 65.90 C
ANISOU 18 CE1 HIS A 79P 9472 8729 6840 34 1933 -1144 C
ATOM 19 NE2 HIS A 79P -28.353 4.798 45.698 1.00 70.79 N
ANISOU 19 NE2 HIS A 79P 10363 9131 7404 448 2044 -1175 N
ATOM 20 N LEU A 80P -21.999 2.576 45.838 1.00 52.92 N
ANISOU 20 N LEU A 80P 8471 6366 5269 -1612 1051 -1035 N
ATOM 21 CA LEU A 80P -20.626 2.254 45.469 1.00 55.02 C
ANISOU 21 CA LEU A 80P 8727 6599 5578 -1901 840 -1000 C
ATOM 22 C LEU A 80P -20.383 2.383 43.967 1.00 53.48 C
ANISOU 22 C LEU A 80P 8473 6315 5531 -1728 764 -966 C
ATOM 23 O LEU A 80P -20.981 1.666 43.165 1.00 44.03 O
ANISOU 23 O LEU A 80P 6975 5243 4511 -1521 668 -893 O
ATOM 24 CB LEU A 80P -20.267 0.839 45.925 1.00 45.05 C
ANISOU 24 CB LEU A 80P 7145 5568 4404 -2115 615 -896 C
ATOM 25 CG LEU A 80P -18.918 0.328 45.413 1.00 43.50 C
ANISOU 25 CG LEU A 80P 6843 5402 4284 -2314 383 -841 C
ATOM 26 CD1 LEU A 80P -17.773 1.153 45.977 1.00 55.27 C
ANISOU 26 CD1 LEU A 80P 8604 6824 5574 -2619 396 -925 C
ATOM 27 CD2 LEU A 80P -18.733 -1.140 45.738 1.00 49.44 C
ANISOU 27 CD2 LEU A 80P 7306 6344 5133 -2408 174 -717 C
ATOM 28 N THR A 81P -19.497 3.301 43.597 1.00 52.05 N
ANISOU 28 N THR A 81P 8601 5924 5253 -1852 815 -1025 N
ATOM 29 CA THR A 81P -19.088 3.460 42.208 1.00 48.01 C
ANISOU 29 CA THR A 81P 8079 5320 4841 -1749 756 -990 C
ATOM 30 C THR A 81P -17.607 3.144 42.064 1.00 44.07 C
ANISOU 30 C THR A 81P 7512 4883 4349 -2114 600 -983 C
ATOM 31 O THR A 81P -16.773 3.739 42.743 1.00 61.05 O
ANISOU 31 O THR A 81P 9890 6976 6331 -2440 648 -1060 O
ATOM 32 CB THR A 81P -19.350 4.886 41.691 1.00 47.12 C
ANISOU 32 CB THR A 81P 8421 4890 4594 -1553 985 -1051 C
ATOM 33 OG1 THR A 81P -20.748 5.185 41.783 1.00 59.57 O
ANISOU 33 OG1 THR A 81P 10019 6455 6161 -1133 1128 -1050 O
ATOM 34 CG2 THR A 81P -18.904 5.015 40.247 1.00 46.35 C
ANISOU 34 CG2 THR A 81P 8335 4703 4572 -1468 927 -999 C
ATOM 35 N ILE A 82P -17.276 2.204 41.187 1.00 47.16 N
ANISOU 35 N ILE A 82P 7580 5415 4921 -2064 418 -901 N
ATOM 36 CA ILE A 82P -15.879 1.868 40.954 1.00 43.10 C
ANISOU 36 CA ILE A 82P 6946 5007 4423 -2343 283 -891 C
ATOM 37 C ILE A 82P -15.467 2.207 39.528 1.00 46.48 C
ANISOU 37 C ILE A 82P 7420 5337 4902 -2262 309 -884 C
ATOM 38 O ILE A 82P -16.267 2.116 38.597 1.00 46.50 O
ANISOU 38 O ILE A 82P 7395 5274 4998 -1948 324 -844 O
ATOM 39 CB ILE A 82P -15.590 0.377 41.227 1.00 40.11 C
ANISOU 39 CB ILE A 82P 6173 4883 4183 -2370 52 -799 C
ATOM 40 CG1 ILE A 82P -16.402 -0.518 40.293 1.00 38.47 C
ANISOU 40 CG1 ILE A 82P 5743 4701 4171 -2069 -24 -729 C
ATOM 41 CG2 ILE A 82P -15.893 0.036 42.675 1.00 52.09 C
ANISOU 41 CG2 ILE A 82P 7683 6498 5612 -2488 27 -789 C
ATOM 42 CD1 ILE A 82P -16.050 -1.982 40.411 1.00 37.41 C
ANISOU 42 CD1 ILE A 82P 5311 4738 4164 -2089 -229 -642 C
ATOM 43 N GLY A 83P -14.214 2.616 39.370 1.00 48.75 N
ANISOU 43 N GLY A 83P 7772 5645 5107 -2566 316 -926 N
ATOM 44 CA GLY A 83P -13.674 2.922 38.062 1.00 44.39 C
ANISOU 44 CA GLY A 83P 7266 5024 4576 -2551 361 -920 C
ATOM 45 C GLY A 83P -12.877 1.752 37.531 1.00 52.09 C
ANISOU 45 C GLY A 83P 7824 6264 5702 -2563 174 -863 C
ATOM 46 O GLY A 83P -12.226 1.036 38.293 1.00 47.59 O
ANISOU 46 O GLY A 83P 6997 5930 5153 -2720 30 -848 O
ATOM 47 N PHE A 84P -12.932 1.551 36.220 1.00 55.67 N
ANISOU 47 N PHE A 84P 8232 6679 6242 -2368 178 -830 N
ATOM 48 CA PHE A 84P -12.188 0.471 35.591 1.00 39.30 C
ANISOU 48 CA PHE A 84P 5809 4824 4298 -2335 37 -791 C
ATOM 49 C PHE A 84P -11.557 0.918 34.278 1.00 50.05 C
ANISOU 49 C PHE A 84P 7253 6143 5621 -2363 144 -807 C
ATOM 50 O PHE A 84P -11.991 1.896 33.668 1.00 51.73 O
ANISOU 50 O PHE A 84P 7805 6118 5734 -2310 300 -818 O
ATOM 51 CB PHE A 84P -13.097 -0.739 35.357 1.00 38.61 C
ANISOU 51 CB PHE A 84P 5516 4773 4383 -2021 -107 -728 C
ATOM 52 CG PHE A 84P -14.352 -0.426 34.589 1.00 50.76 C
ANISOU 52 CG PHE A 84P 7215 6136 5934 -1742 -49 -718 C
ATOM 53 CD1 PHE A 84P -14.345 -0.382 33.204 1.00 43.70 C
ANISOU 53 CD1 PHE A 84P 6364 5190 5049 -1590 -25 -712 C
ATOM 54 CD2 PHE A 84P -15.546 -0.199 35.254 1.00 55.16 C
ANISOU 54 CD2 PHE A 84P 7857 6623 6477 -1616 -21 -713 C
ATOM 55 CE1 PHE A 84P -15.500 -0.100 32.500 1.00 41.96 C
ANISOU 55 CE1 PHE A 84P 6268 4860 4815 -1314 -3 -693 C
ATOM 56 CE2 PHE A 84P -16.706 0.078 34.553 1.00 56.56 C
ANISOU 56 CE2 PHE A 84P 8119 6714 6656 -1325 15 -699 C
ATOM 57 CZ PHE A 84P -16.682 0.124 33.174 1.00 47.64 C
ANISOU 57 CZ PHE A 84P 7027 5545 5527 -1171 8 -684 C
ATOM 58 N LYS A 85P -10.520 0.202 33.857 1.00 40.15 N
ANISOU 58 N LYS A 85P 5703 5123 4430 -2425 71 -802 N
ATOM 59 CA ALYS A 85P -9.873 0.471 32.579 0.43 41.01 C
ANISOU 59 CA ALYS A 85P 5843 5238 4500 -2451 182 -818 C
ATOM 60 CA BLYS A 85P -9.879 0.480 32.582 0.57 41.01 C
ANISOU 60 CA BLYS A 85P 5846 5236 4500 -2452 183 -818 C
ATOM 61 C LYS A 85P -10.517 -0.358 31.481 1.00 47.40 C
ANISOU 61 C LYS A 85P 6585 5997 5427 -2090 115 -779 C
ATOM 62 O LYS A 85P -11.077 -1.419 31.745 1.00 59.27 O
ANISOU 62 O LYS A 85P 7905 7549 7066 -1884 -45 -747 O
ATOM 63 CB ALYS A 85P -8.373 0.175 32.647 0.43 42.57 C
ANISOU 63 CB ALYS A 85P 5725 5766 4683 -2699 167 -848 C
ATOM 64 CB BLYS A 85P -8.377 0.212 32.668 0.57 42.60 C
ANISOU 64 CB BLYS A 85P 5738 5766 4683 -2707 170 -849 C
ATOM 65 CG ALYS A 85P -7.538 1.298 33.235 0.43 47.56 C
ANISOU 65 CG ALYS A 85P 6478 6462 5133 -3161 293 -917 C
ATOM 66 CG BLYS A 85P -7.672 1.061 33.711 0.57 47.86 C
ANISOU 66 CG BLYS A 85P 6454 6534 5197 -3136 222 -908 C
ATOM 67 CD ALYS A 85P -6.071 1.142 32.861 0.43 48.16 C
ANISOU 67 CD ALYS A 85P 6221 6907 5172 -3400 325 -954 C
ATOM 68 CD BLYS A 85P -7.805 2.545 33.394 0.57 51.01 C
ANISOU 68 CD BLYS A 85P 7331 6642 5408 -3381 460 -961 C
ATOM 69 CE ALYS A 85P -5.881 1.169 31.351 0.43 47.54 C
ANISOU 69 CE ALYS A 85P 6195 6773 5094 -3285 471 -951 C
ATOM 70 CE BLYS A 85P -7.348 3.412 34.560 0.57 50.59 C
ANISOU 70 CE BLYS A 85P 7426 6615 5182 -3823 511 -1041 C
ATOM 71 NZ ALYS A 85P -4.452 1.018 30.962 0.43 50.09 N
ANISOU 71 NZ ALYS A 85P 6157 7499 5375 -3511 537 -994 N
ATOM 72 NZ BLYS A 85P -8.289 3.338 35.716 0.57 47.32 N
ANISOU 72 NZ BLYS A 85P 7129 6070 4781 -3700 420 -1032 N
ATOM 73 N VAL A 86P -10.439 0.132 30.248 1.00 46.81 N
ANISOU 73 N VAL A 86P 6692 5820 5275 -2043 241 -784 N
ATOM 74 CA VAL A 86P -11.035 -0.567 29.117 1.00 39.21 C
ANISOU 74 CA VAL A 86P 5703 4818 4377 -1730 178 -762 C
ATOM 75 C VAL A 86P -10.022 -0.790 28.001 1.00 40.30 C
ANISOU 75 C VAL A 86P 5753 5080 4478 -1769 264 -788 C
ATOM 76 O VAL A 86P -9.303 0.129 27.609 1.00 43.84 O
ANISOU 76 O VAL A 86P 6361 5514 4784 -1997 448 -804 O
ATOM 77 CB VAL A 86P -12.243 0.205 28.544 1.00 39.26 C
ANISOU 77 CB VAL A 86P 6052 4574 4290 -1528 230 -728 C
ATOM 78 CG1 VAL A 86P -12.900 -0.588 27.433 1.00 38.53 C
ANISOU 78 CG1 VAL A 86P 5898 4498 4243 -1234 124 -716 C
ATOM 79 CG2 VAL A 86P -13.252 0.511 29.637 1.00 39.99 C
ANISOU 79 CG2 VAL A 86P 6221 4570 4403 -1465 186 -711 C
ATOM 80 N GLU A 87P -9.960 -2.021 27.508 1.00 39.56 N
ANISOU 80 N GLU A 87P 5429 5102 4499 -1563 152 -798 N
ATOM 81 CA GLU A 87P -9.207 -2.328 26.301 1.00 44.22 C
ANISOU 81 CA GLU A 87P 5965 5791 5045 -1517 244 -832 C
ATOM 82 C GLU A 87P -10.188 -2.788 25.234 1.00 53.00 C
ANISOU 82 C GLU A 87P 7226 6763 6148 -1234 178 -833 C
ATOM 83 O GLU A 87P -10.958 -3.722 25.455 1.00 54.04 O
ANISOU 83 O GLU A 87P 7267 6869 6397 -1055 5 -836 O
ATOM 84 CB GLU A 87P -8.148 -3.400 26.561 1.00 43.79 C
ANISOU 84 CB GLU A 87P 5531 6005 5100 -1494 192 -862 C
ATOM 85 CG GLU A 87P -7.119 -3.532 25.450 1.00 50.08 C
ANISOU 85 CG GLU A 87P 6233 6967 5826 -1493 349 -910 C
ATOM 86 CD GLU A 87P -6.748 -4.975 25.164 1.00 59.79 C
ANISOU 86 CD GLU A 87P 7219 8325 7174 -1214 265 -943 C
ATOM 87 OE1 GLU A 87P -7.666 -5.812 25.041 1.00 63.89 O
ANISOU 87 OE1 GLU A 87P 7830 8670 7776 -982 121 -943 O
ATOM 88 OE2 GLU A 87P -5.539 -5.273 25.064 1.00 68.86 O
ANISOU 88 OE2 GLU A 87P 8089 9754 8322 -1227 352 -973 O
ATOM 89 N ASN A 88P -10.171 -2.125 24.083 1.00 48.33 N
ANISOU 89 N ASN A 88P 6880 6089 5394 -1222 313 -831 N
ATOM 90 CA ASN A 88P -11.121 -2.437 23.023 1.00 41.29 C
ANISOU 90 CA ASN A 88P 6149 5095 4443 -969 235 -831 C
ATOM 91 C ASN A 88P -10.437 -2.919 21.749 1.00 48.15 C
ANISOU 91 C ASN A 88P 7018 6050 5227 -910 326 -886 C
ATOM 92 O ASN A 88P -9.221 -3.121 21.724 1.00 43.24 O
ANISOU 92 O ASN A 88P 6218 5592 4620 -1034 454 -926 O
ATOM 93 CB ASN A 88P -11.993 -1.214 22.728 1.00 41.46 C
ANISOU 93 CB ASN A 88P 6531 4920 4301 -917 282 -758 C
ATOM 94 CG ASN A 88P -11.177 0.035 22.469 1.00 46.80 C
ANISOU 94 CG ASN A 88P 7472 5511 4800 -1146 530 -726 C
ATOM 95 OD1 ASN A 88P -10.207 0.013 21.713 1.00 49.93 O
ANISOU 95 OD1 ASN A 88P 7863 5998 5111 -1267 679 -756 O
ATOM 96 ND2 ASN A 88P -11.564 1.135 23.104 1.00 44.26 N
ANISOU 96 ND2 ASN A 88P 7403 5005 4406 -1220 597 -671 N
ATOM 97 N ALA A 89P -11.227 -3.107 20.696 1.00 54.49 N
ANISOU 97 N ALA A 89P 8004 6776 5925 -715 261 -893 N
ATOM 98 CA ALA A 89P -10.701 -3.562 19.416 1.00 43.91 C
ANISOU 98 CA ALA A 89P 6720 5498 4466 -645 350 -957 C
ATOM 99 C ALA A 89P -9.769 -2.520 18.819 1.00 45.94 C
ANISOU 99 C ALA A 89P 7154 5768 4533 -828 620 -925 C
ATOM 100 O ALA A 89P -8.702 -2.854 18.307 1.00 47.38 O
ANISOU 100 O ALA A 89P 7219 6102 4680 -893 780 -987 O
ATOM 101 CB ALA A 89P -11.832 -3.872 18.457 1.00 50.90 C
ANISOU 101 CB ALA A 89P 7793 6313 5235 -432 200 -971 C
ATOM 102 N HIS A 90P -10.178 -1.257 18.900 1.00 48.55 N
ANISOU 102 N HIS A 90P 7780 5935 4730 -909 686 -829 N
ATOM 103 CA HIS A 90P -9.391 -0.141 18.383 1.00 48.79 C
ANISOU 103 CA HIS A 90P 8074 5914 4550 -1137 960 -784 C
ATOM 104 C HIS A 90P -7.985 -0.114 18.971 1.00 51.16 C
ANISOU 104 C HIS A 90P 8094 6419 4926 -1459 1137 -839 C
ATOM 105 O HIS A 90P -7.018 0.190 18.274 1.00 52.01 O
ANISOU 105 O HIS A 90P 8238 6635 4888 -1647 1374 -861 O
ATOM 106 CB HIS A 90P -10.102 1.181 18.667 1.00 49.33 C
ANISOU 106 CB HIS A 90P 8540 5715 4489 -1161 994 -670 C
ATOM 107 CG HIS A 90P -9.324 2.390 18.256 1.00 55.55 C
ANISOU 107 CG HIS A 90P 9680 6381 5045 -1450 1292 -617 C
ATOM 108 ND1 HIS A 90P -8.434 3.026 19.103 1.00 56.74 N
ANISOU 108 ND1 HIS A 90P 9789 6551 5218 -1841 1463 -638 N
ATOM 109 CD2 HIS A 90P -9.300 3.087 17.099 1.00 55.31 C
ANISOU 109 CD2 HIS A 90P 10077 6206 4733 -1441 1456 -544 C
ATOM 110 CE1 HIS A 90P -7.903 4.058 18.481 1.00 60.94 C
ANISOU 110 CE1 HIS A 90P 10713 6942 5499 -2090 1732 -588 C
ATOM 111 NE2 HIS A 90P -8.407 4.120 17.259 1.00 63.37 N
ANISOU 111 NE2 HIS A 90P 11328 7135 5617 -1842 1742 -521 N
ATOM 112 N ASP A 91P -7.879 -0.437 20.256 1.00 53.12 N
ANISOU 112 N ASP A 91P 8045 6756 5381 -1528 1019 -860 N
ATOM 113 CA ASP A 91P -6.584 -0.527 20.920 1.00 55.48 C
ANISOU 113 CA ASP A 91P 7999 7325 5754 -1803 1127 -912 C
ATOM 114 C ASP A 91P -5.766 -1.685 20.357 1.00 56.46 C
ANISOU 114 C ASP A 91P 7779 7729 5946 -1662 1154 -994 C
ATOM 115 O ASP A 91P -4.599 -1.522 20.000 1.00 52.50 O
ANISOU 115 O ASP A 91P 7112 7471 5363 -1858 1367 -1036 O
ATOM 116 CB ASP A 91P -6.766 -0.696 22.431 1.00 53.84 C
ANISOU 116 CB ASP A 91P 7574 7154 5730 -1859 955 -905 C
ATOM 117 CG ASP A 91P -7.190 0.589 23.118 1.00 69.43 C
ANISOU 117 CG ASP A 91P 9866 8903 7612 -2083 1008 -852 C
ATOM 118 OD1 ASP A 91P -6.752 0.822 24.264 1.00 73.33 O
ANISOU 118 OD1 ASP A 91P 10201 9499 8162 -2324 990 -870 O
ATOM 119 OD2 ASP A 91P -7.953 1.370 22.512 1.00 75.59 O
ANISOU 119 OD2 ASP A 91P 11077 9402 8243 -2004 1069 -793 O
ATOM 120 N ARG A 92P -6.397 -2.851 20.273 1.00 55.09 N
ANISOU 120 N ARG A 92P 7510 7517 5905 -1327 954 -1023 N
ATOM 121 CA ARG A 92P -5.736 -4.066 19.809 1.00 51.25 C
ANISOU 121 CA ARG A 92P 6758 7228 5488 -1122 968 -1108 C
ATOM 122 C ARG A 92P -5.323 -3.966 18.343 1.00 62.42 C
ANISOU 122 C ARG A 92P 8336 8683 6699 -1093 1185 -1157 C
ATOM 123 O ARG A 92P -4.284 -4.494 17.943 1.00 55.06 O
ANISOU 123 O ARG A 92P 7160 8003 5758 -1050 1339 -1230 O
ATOM 124 CB ARG A 92P -6.659 -5.267 20.014 1.00 52.31 C
ANISOU 124 CB ARG A 92P 6879 7222 5774 -814 715 -1131 C
ATOM 125 CG ARG A 92P -6.130 -6.305 20.986 1.00 51.59 C
ANISOU 125 CG ARG A 92P 6435 7282 5886 -698 606 -1148 C
ATOM 126 CD ARG A 92P -7.206 -6.713 21.980 1.00 49.57 C
ANISOU 126 CD ARG A 92P 6215 6841 5776 -634 353 -1100 C
ATOM 127 NE ARG A 92P -8.495 -6.943 21.334 1.00 53.63 N
ANISOU 127 NE ARG A 92P 7013 7118 6247 -512 235 -1118 N
ATOM 128 CZ ARG A 92P -9.668 -6.629 21.876 1.00 53.38 C
ANISOU 128 CZ ARG A 92P 7097 6936 6248 -549 82 -1065 C
ATOM 129 NH1 ARG A 92P -9.715 -6.069 23.076 1.00 46.26 N
ANISOU 129 NH1 ARG A 92P 6103 6052 5420 -697 45 -994 N
ATOM 130 NH2 ARG A 92P -10.794 -6.873 21.218 1.00 54.15 N
ANISOU 130 NH2 ARG A 92P 7388 6899 6288 -440 -32 -1090 N
ATOM 131 N ILE A 93P -6.144 -3.287 17.550 1.00 63.66 N
ANISOU 131 N ILE A 93P 8907 8606 6674 -1091 1199 -1111 N
ATOM 132 CA ILE A 93P -5.888 -3.128 16.124 1.00 55.28 C
ANISOU 132 CA ILE A 93P 8079 7551 5374 -1066 1393 -1142 C
ATOM 133 C ILE A 93P -4.668 -2.248 15.871 1.00 63.10 C
ANISOU 133 C ILE A 93P 9034 8727 6215 -1401 1720 -1133 C
ATOM 134 O ILE A 93P -3.797 -2.600 15.073 1.00 60.65 O
ANISOU 134 O ILE A 93P 8607 8629 5807 -1395 1930 -1208 O
ATOM 135 CB ILE A 93P -7.112 -2.531 15.404 1.00 60.59 C
ANISOU 135 CB ILE A 93P 9220 7945 5858 -968 1299 -1066 C
ATOM 136 CG1 ILE A 93P -8.218 -3.580 15.290 1.00 58.39 C
ANISOU 136 CG1 ILE A 93P 8941 7575 5671 -661 1009 -1115 C
ATOM 137 CG2 ILE A 93P -6.733 -2.026 14.021 1.00 62.13 C
ANISOU 137 CG2 ILE A 93P 9723 8138 5745 -1024 1539 -1060 C
ATOM 138 CD1 ILE A 93P -9.514 -3.043 14.731 1.00 53.78 C
ANISOU 138 CD1 ILE A 93P 8721 6798 4916 -536 858 -1038 C
ATOM 139 N LEU A 94P -4.608 -1.108 16.556 1.00 65.53 N
ANISOU 139 N LEU A 94P 9451 8957 6490 -1712 1779 -1052 N
ATOM 140 CA LEU A 94P -3.481 -0.188 16.422 1.00 61.79 C
ANISOU 140 CA LEU A 94P 8967 8650 5860 -2131 2093 -1049 C
ATOM 141 C LEU A 94P -2.169 -0.875 16.769 1.00 62.96 C
ANISOU 141 C LEU A 94P 8532 9258 6131 -2213 2195 -1149 C
ATOM 142 O LEU A 94P -1.152 -0.660 16.108 1.00 75.35 O
ANISOU 142 O LEU A 94P 9991 11087 7553 -2417 2483 -1194 O
ATOM 143 CB LEU A 94P -3.675 1.039 17.312 1.00 67.76 C
ANISOU 143 CB LEU A 94P 9946 9217 6583 -2466 2108 -968 C
ATOM 144 CG LEU A 94P -4.688 2.078 16.834 1.00 74.01 C
ANISOU 144 CG LEU A 94P 11379 9572 7167 -2440 2124 -850 C
ATOM 145 CD1 LEU A 94P -4.690 3.270 17.771 1.00 76.39 C
ANISOU 145 CD1 LEU A 94P 11911 9685 7427 -2788 2192 -796 C
ATOM 146 CD2 LEU A 94P -4.379 2.509 15.408 1.00 81.42 C
ANISOU 146 CD2 LEU A 94P 12666 10464 7806 -2507 2384 -820 C
ATOM 147 N LYS A 95P -2.206 -1.697 17.814 1.00 59.38 N
ANISOU 147 N LYS A 95P 7705 8923 5934 -2040 1961 -1174 N
ATOM 148 CA LYS A 95P -1.066 -2.520 18.195 1.00 61.05 C
ANISOU 148 CA LYS A 95P 7343 9580 6274 -1984 1999 -1252 C
ATOM 149 C LYS A 95P -0.601 -3.359 17.011 1.00 79.82 C
ANISOU 149 C LYS A 95P 9636 12111 8582 -1703 2157 -1339 C
ATOM 150 O LYS A 95P 0.579 -3.366 16.672 1.00 82.70 O
ANISOU 150 O LYS A 95P 9679 12870 8874 -1822 2405 -1400 O
ATOM 151 CB LYS A 95P -1.431 -3.420 19.377 1.00 59.14 C
ANISOU 151 CB LYS A 95P 6839 9339 6294 -1729 1686 -1240 C
ATOM 152 CG LYS A 95P -0.385 -4.466 19.727 1.00 65.52 C
ANISOU 152 CG LYS A 95P 7094 10567 7233 -1518 1680 -1299 C
ATOM 153 CD LYS A 95P 0.759 -3.876 20.534 1.00 73.05 C
ANISOU 153 CD LYS A 95P 7619 11965 8173 -1887 1766 -1300 C
ATOM 154 CE LYS A 95P 1.724 -4.963 20.985 1.00 75.31 C
ANISOU 154 CE LYS A 95P 7322 12701 8592 -1590 1710 -1335 C
ATOM 155 NZ LYS A 95P 2.909 -4.409 21.699 1.00 74.32 N
ANISOU 155 NZ LYS A 95P 6700 13114 8423 -1958 1784 -1345 N
ATOM 156 N THR A 96P -1.547 -4.044 16.374 1.00 74.11 N
ANISOU 156 N THR A 96P 9204 11092 7862 -1349 2023 -1354 N
ATOM 157 CA THR A 96P -1.255 -4.908 15.236 1.00 62.99 C
ANISOU 157 CA THR A 96P 7805 9761 6368 -1057 2156 -1456 C
ATOM 158 C THR A 96P -0.691 -4.124 14.052 1.00 70.97 C
ANISOU 158 C THR A 96P 9006 10872 7086 -1292 2502 -1471 C
ATOM 159 O THR A 96P 0.251 -4.568 13.394 1.00 77.37 O
ANISOU 159 O THR A 96P 9593 11984 7820 -1211 2746 -1565 O
ATOM 160 CB THR A 96P -2.514 -5.668 14.776 1.00 60.65 C
ANISOU 160 CB THR A 96P 7859 9098 6086 -722 1925 -1478 C
ATOM 161 OG1 THR A 96P -3.097 -6.356 15.890 1.00 58.50 O
ANISOU 161 OG1 THR A 96P 7450 8711 6066 -558 1624 -1455 O
ATOM 162 CG2 THR A 96P -2.164 -6.675 13.693 1.00 69.27 C
ANISOU 162 CG2 THR A 96P 8974 10259 7087 -419 2058 -1612 C
ATOM 163 N ILE A 97P -1.271 -2.958 13.785 1.00 65.74 N
ANISOU 163 N ILE A 97P 8779 9952 6248 -1566 2538 -1374 N
ATOM 164 CA ILE A 97P -0.835 -2.121 12.673 1.00 69.37 C
ANISOU 164 CA ILE A 97P 9523 10439 6394 -1821 2868 -1358 C
ATOM 165 C ILE A 97P 0.611 -1.667 12.838 1.00 81.51 C
ANISOU 165 C ILE A 97P 10671 12418 7883 -2202 3189 -1397 C
ATOM 166 O ILE A 97P 1.418 -1.789 11.917 1.00 87.65 O
ANISOU 166 O ILE A 97P 11361 13453 8489 -2241 3493 -1467 O
ATOM 167 CB ILE A 97P -1.731 -0.876 12.516 1.00 67.99 C
ANISOU 167 CB ILE A 97P 9931 9867 6036 -2028 2836 -1216 C
ATOM 168 CG1 ILE A 97P -3.156 -1.285 12.141 1.00 68.53 C
ANISOU 168 CG1 ILE A 97P 10356 9586 6095 -1648 2538 -1182 C
ATOM 169 CG2 ILE A 97P -1.161 0.070 11.472 1.00 71.82 C
ANISOU 169 CG2 ILE A 97P 10743 10369 6176 -2350 3207 -1178 C
ATOM 170 CD1 ILE A 97P -4.080 -0.111 11.904 1.00 76.01 C
ANISOU 170 CD1 ILE A 97P 11869 10169 6841 -1740 2496 -1030 C
ATOM 171 N LYS A 98P 0.936 -1.152 14.019 1.00 86.52 N
ANISOU 171 N LYS A 98P 11054 13169 8652 -2499 3124 -1360 N
ATOM 172 CA LYS A 98P 2.263 -0.600 14.264 1.00 95.89 C
ANISOU 172 CA LYS A 98P 11854 14809 9770 -2954 3404 -1399 C
ATOM 173 C LYS A 98P 3.296 -1.683 14.578 1.00 96.01 C
ANISOU 173 C LYS A 98P 11144 15377 9957 -2723 3423 -1509 C
ATOM 174 O LYS A 98P 4.493 -1.475 14.377 1.00100.97 O
ANISOU 174 O LYS A 98P 11380 16497 10488 -2994 3712 -1571 O
ATOM 175 CB LYS A 98P 2.211 0.428 15.399 1.00 97.77 C
ANISOU 175 CB LYS A 98P 12144 14961 10043 -3408 3326 -1331 C
ATOM 176 CG LYS A 98P 2.601 -0.109 16.767 1.00104.98 C
ANISOU 176 CG LYS A 98P 12481 16186 11222 -3366 3093 -1366 C
ATOM 177 CD LYS A 98P 2.646 1.002 17.805 1.00114.94 C
ANISOU 177 CD LYS A 98P 13834 17384 12455 -3892 3062 -1324 C
ATOM 178 CE LYS A 98P 2.890 0.444 19.196 1.00111.06 C
ANISOU 178 CE LYS A 98P 12825 17170 12203 -3816 2784 -1346 C
ATOM 179 NZ LYS A 98P 3.767 -0.761 19.155 1.00112.10 N
ANISOU 179 NZ LYS A 98P 12291 17834 12467 -3472 2769 -1418 N
ATOM 180 N THR A 99P 2.836 -2.835 15.058 1.00 92.43 N
ANISOU 180 N THR A 99P 10522 14853 9744 -2217 3127 -1529 N
ATOM 181 CA THR A 99P 3.731 -3.959 15.320 1.00 93.53 C
ANISOU 181 CA THR A 99P 10049 15452 10037 -1877 3130 -1616 C
ATOM 182 C THR A 99P 4.342 -4.447 14.013 1.00 92.33 C
ANISOU 182 C THR A 99P 9851 15507 9722 -1670 3448 -1720 C
ATOM 183 O THR A 99P 5.517 -4.815 13.958 1.00 97.64 O
ANISOU 183 O THR A 99P 9975 16727 10395 -1611 3651 -1798 O
ATOM 184 CB THR A 99P 2.997 -5.129 16.018 1.00 94.85 C
ANISOU 184 CB THR A 99P 10188 15388 10462 -1360 2762 -1604 C
ATOM 185 OG1 THR A 99P 2.689 -4.763 17.369 1.00 89.65 O
ANISOU 185 OG1 THR A 99P 9433 14674 9955 -1549 2499 -1519 O
ATOM 186 CG2 THR A 99P 3.853 -6.388 16.028 1.00 98.05 C
ANISOU 186 CG2 THR A 99P 10101 16173 10982 -891 2800 -1689 C
ATOM 187 N HIS A 100P 3.539 -4.422 12.955 1.00 94.06 N
ANISOU 187 N HIS A 100P 10641 15318 9781 -1557 3493 -1723 N
ATOM 188 CA HIS A 100P 3.966 -4.938 11.662 1.00 92.42 C
ANISOU 188 CA HIS A 100P 10489 15238 9389 -1332 3781 -1832 C
ATOM 189 C HIS A 100P 4.092 -3.845 10.607 1.00 90.05 C
ANISOU 189 C HIS A 100P 10571 14894 8750 -1755 4109 -1804 C
ATOM 190 O HIS A 100P 4.214 -4.141 9.419 1.00 89.23 O
ANISOU 190 O HIS A 100P 10671 14796 8436 -1602 4339 -1879 O
ATOM 191 CB HIS A 100P 2.993 -6.013 11.186 1.00 88.95 C
ANISOU 191 CB HIS A 100P 10408 14394 8996 -812 3571 -1885 C
ATOM 192 CG HIS A 100P 2.835 -7.146 12.157 1.00 95.35 C
ANISOU 192 CG HIS A 100P 10937 15182 10111 -396 3274 -1906 C
ATOM 193 ND1 HIS A 100P 1.605 -7.577 12.597 1.00 99.00 N
ANISOU 193 ND1 HIS A 100P 11719 15186 10712 -215 2912 -1864 N
ATOM 194 CD2 HIS A 100P 3.758 -7.918 12.770 1.00102.71 C
ANISOU 194 CD2 HIS A 100P 11310 16503 11213 -128 3294 -1954 C
ATOM 195 CE1 HIS A 100P 1.779 -8.579 13.446 1.00 97.32 C
ANISOU 195 CE1 HIS A 100P 11199 15040 10738 122 2734 -1882 C
ATOM 196 NE2 HIS A 100P 3.065 -8.807 13.569 1.00 97.72 N
ANISOU 196 NE2 HIS A 100P 10730 15589 10812 211 2947 -1929 N
ATOM 197 N LYS A 101P 4.064 -2.591 11.051 1.00 97.53 N
ANISOU 197 N LYS A 101P 11658 15774 9625 -2290 4141 -1696 N
ATOM 198 CA LYS A 101P 4.243 -1.440 10.168 1.00 97.12 C
ANISOU 198 CA LYS A 101P 12014 15652 9235 -2755 4470 -1643 C
ATOM 199 C LYS A 101P 3.280 -1.460 8.997 1.00 95.19 C
ANISOU 199 C LYS A 101P 12448 14956 8763 -2530 4458 -1609 C
ATOM 200 O LYS A 101P 3.688 -1.346 7.841 1.00 99.57 O
ANISOU 200 O LYS A 101P 13185 15613 9034 -2595 4783 -1647 O
ATOM 201 CB LYS A 101P 5.674 -1.384 9.641 1.00 98.02 C
ANISOU 201 CB LYS A 101P 11678 16366 9197 -2998 4915 -1741 C
ATOM 202 CG LYS A 101P 6.722 -1.406 10.719 1.00 98.56 C
ANISOU 202 CG LYS A 101P 11012 16940 9497 -3171 4861 -1763 C
ATOM 203 CD LYS A 101P 7.334 -0.039 10.877 1.00110.36 C
ANISOU 203 CD LYS A 101P 12585 18439 10906 -3818 4940 -1667 C
ATOM 204 CE LYS A 101P 8.599 0.125 10.046 1.00116.74 C
ANISOU 204 CE LYS A 101P 13116 19642 11596 -3974 5237 -1702 C
ATOM 205 NZ LYS A 101P 8.723 1.495 9.476 1.00118.51 N
ANISOU 205 NZ LYS A 101P 13843 19596 11589 -4534 5400 -1613 N
ATOM 206 N LEU A 102P 1.999 -1.620 9.294 1.00 91.62 N
ANISOU 206 N LEU A 102P 12349 14043 8419 -2269 4080 -1540 N
ATOM 207 CA LEU A 102P 0.999 -1.603 8.246 1.00 81.11 C
ANISOU 207 CA LEU A 102P 11638 12321 6859 -2063 4010 -1499 C
ATOM 208 C LEU A 102P 0.421 -0.205 8.092 1.00 84.07 C
ANISOU 208 C LEU A 102P 12593 12343 7007 -2405 4040 -1323 C
ATOM 209 O LEU A 102P -0.738 -0.052 7.724 1.00 79.27 O
ANISOU 209 O LEU A 102P 12475 11349 6295 -2199 3817 -1237 O
ATOM 210 CB LEU A 102P -0.102 -2.621 8.542 1.00 77.09 C
ANISOU 210 CB LEU A 102P 11176 11556 6561 -1579 3590 -1534 C
ATOM 211 CG LEU A 102P 0.442 -4.006 8.895 1.00 77.54 C
ANISOU 211 CG LEU A 102P 10713 11884 6866 -1226 3542 -1690 C
ATOM 212 CD1 LEU A 102P -0.687 -4.994 9.128 1.00 73.62 C
ANISOU 212 CD1 LEU A 102P 10350 11084 6539 -819 3152 -1726 C
ATOM 213 CD2 LEU A 102P 1.369 -4.493 7.794 1.00 81.33 C
ANISOU 213 CD2 LEU A 102P 11097 12661 7145 -1122 3906 -1826 C
ATOM 214 N LYS A 103P 1.233 0.810 8.379 1.00 90.57 N
ANISOU 214 N LYS A 103P 13368 13307 7738 -2924 4316 -1272 N
ATOM 215 CA LYS A 103P 0.810 2.193 8.185 1.00 93.86 C
ANISOU 215 CA LYS A 103P 14415 13350 7898 -3273 4412 -1103 C
ATOM 216 C LYS A 103P 0.388 2.541 6.746 1.00 94.11 C
ANISOU 216 C LYS A 103P 15061 13121 7575 -3164 4516 -1014 C
ATOM 217 O LYS A 103P -0.464 3.412 6.567 1.00 94.83 O
ANISOU 217 O LYS A 103P 15735 12770 7526 -3160 4391 -846 O
ATOM 218 CB LYS A 103P 1.913 3.159 8.665 1.00 96.24 C
ANISOU 218 CB LYS A 103P 14510 13830 8225 -3853 4634 -1080 C
ATOM 219 CG LYS A 103P 2.006 3.313 10.172 1.00 99.38 C
ANISOU 219 CG LYS A 103P 14565 14318 8879 -4064 4485 -1101 C
ATOM 220 CD LYS A 103P 0.866 4.217 10.656 1.00 95.84 C
ANISOU 220 CD LYS A 103P 14726 13305 8384 -4097 4294 -952 C
ATOM 221 CE LYS A 103P 1.025 4.623 12.110 1.00 92.72 C
ANISOU 221 CE LYS A 103P 14086 12942 8202 -4391 4173 -965 C
ATOM 222 NZ LYS A 103P -0.092 5.488 12.593 1.00 95.18 N
ANISOU 222 NZ LYS A 103P 15002 12695 8469 -4369 4007 -829 N
ATOM 223 N ASN A 104P 0.936 1.846 5.746 1.00 92.03 N
ANISOU 223 N ASN A 104P 14651 13115 7200 -3008 4689 -1117 N
ATOM 224 CA ASN A 104P 0.580 2.094 4.351 1.00 94.98 C
ANISOU 224 CA ASN A 104P 15552 13274 7262 -2875 4738 -1034 C
ATOM 225 C ASN A 104P -0.001 0.893 3.550 1.00 90.78 C
ANISOU 225 C ASN A 104P 15094 12773 6624 -2381 4616 -1156 C
ATOM 226 O ASN A 104P -0.241 1.033 2.343 1.00111.40 O
ANISOU 226 O ASN A 104P 18104 15260 8962 -2273 4648 -1099 O
ATOM 227 CB ASN A 104P 1.786 2.668 3.593 1.00100.59 C
ANISOU 227 CB ASN A 104P 16194 14191 7835 -3225 5094 -1017 C
ATOM 228 CG ASN A 104P 3.121 2.200 4.138 1.00108.09 C
ANISOU 228 CG ASN A 104P 16394 15681 8993 -3415 5309 -1170 C
ATOM 229 OD1 ASN A 104P 3.481 1.030 4.041 1.00119.39 O
ANISOU 229 OD1 ASN A 104P 17398 17454 10512 -3112 5357 -1336 O
ATOM 230 ND2 ASN A 104P 3.876 3.136 4.711 1.00110.09 N
ANISOU 230 ND2 ASN A 104P 16493 16012 9322 -3907 5427 -1121 N
ATOM 231 N TYR A 105P -0.219 -0.275 4.164 1.00 87.60 N
ANISOU 231 N TYR A 105P 14323 12513 6449 -2079 4449 -1323 N
ATOM 232 CA TYR A 105P -1.047 -1.282 3.495 1.00 86.32 C
ANISOU 232 CA TYR A 105P 14332 12232 6234 -1615 4199 -1415 C
ATOM 233 C TYR A 105P -2.482 -0.789 3.446 1.00 83.97 C
ANISOU 233 C TYR A 105P 14542 11523 5840 -1474 3832 -1257 C
ATOM 234 O TYR A 105P -3.091 -0.769 2.381 1.00 85.39 O
ANISOU 234 O TYR A 105P 15190 11566 5689 -1322 3782 -1226 O
ATOM 235 CB TYR A 105P -0.970 -2.641 4.189 1.00 83.91 C
ANISOU 235 CB TYR A 105P 13490 12083 6307 -1284 3995 -1593 C
ATOM 236 CG TYR A 105P -2.111 -3.587 3.799 1.00 83.53 C
ANISOU 236 CG TYR A 105P 13673 11811 6254 -874 3637 -1671 C
ATOM 237 CD1 TYR A 105P -2.270 -4.027 2.481 1.00 84.42 C
ANISOU 237 CD1 TYR A 105P 14139 11908 6028 -712 3728 -1766 C
ATOM 238 CD2 TYR A 105P -3.023 -4.055 4.750 1.00 83.39 C
ANISOU 238 CD2 TYR A 105P 13520 11616 6547 -686 3216 -1661 C
ATOM 239 CE1 TYR A 105P -3.317 -4.872 2.124 1.00 83.04 C
ANISOU 239 CE1 TYR A 105P 14181 11550 5820 -405 3392 -1855 C
ATOM 240 CE2 TYR A 105P -4.059 -4.905 4.390 1.00 80.15 C
ANISOU 240 CE2 TYR A 105P 13307 11032 6113 -389 2901 -1744 C
ATOM 241 CZ TYR A 105P -4.202 -5.307 3.083 1.00 84.11 C
ANISOU 241 CZ TYR A 105P 14159 11527 6274 -263 2981 -1845 C
ATOM 242 OH TYR A 105P -5.237 -6.152 2.735 1.00 78.24 O
ANISOU 242 OH TYR A 105P 13611 10632 5484 -27 2656 -1947 O
ATOM 243 N ILE A 106P -3.005 -0.376 4.599 1.00 94.52 N
ANISOU 243 N ILE A 106P 15773 12696 7445 -1515 3580 -1157 N
ATOM 244 CA ILE A 106P -4.375 0.115 4.689 1.00 85.28 C
ANISOU 244 CA ILE A 106P 15008 11181 6214 -1343 3232 -1004 C
ATOM 245 C ILE A 106P -4.594 1.364 3.851 1.00 94.29 C
ANISOU 245 C ILE A 106P 16806 12094 6927 -1492 3395 -806 C
ATOM 246 O ILE A 106P -5.546 1.427 3.070 1.00100.89 O
ANISOU 246 O ILE A 106P 18063 12766 7503 -1236 3197 -728 O
ATOM 247 CB ILE A 106P -4.777 0.428 6.141 1.00 78.87 C
ANISOU 247 CB ILE A 106P 13961 10251 5755 -1388 3002 -936 C
ATOM 248 CG1 ILE A 106P -4.763 -0.843 6.994 1.00 72.22 C
ANISOU 248 CG1 ILE A 106P 12545 9581 5315 -1190 2782 -1101 C
ATOM 249 CG2 ILE A 106P -6.150 1.090 6.187 1.00 74.05 C
ANISOU 249 CG2 ILE A 106P 13780 9311 5045 -1198 2700 -764 C
ATOM 250 CD1 ILE A 106P -3.926 -0.721 8.244 1.00 72.50 C
ANISOU 250 CD1 ILE A 106P 12112 9778 5655 -1433 2873 -1122 C
ATOM 251 N LYS A 107P -3.718 2.352 4.019 1.00 92.91 N
ANISOU 251 N LYS A 107P 16693 11910 6700 -1902 3722 -717 N
ATOM 252 CA LYS A 107P -3.843 3.617 3.303 1.00 93.44 C
ANISOU 252 CA LYS A 107P 17285 11686 6532 -2031 3800 -498 C
ATOM 253 C LYS A 107P -4.055 3.449 1.801 1.00 92.44 C
ANISOU 253 C LYS A 107P 17474 11553 6095 -1830 3799 -469 C
ATOM 254 O LYS A 107P -4.845 4.169 1.189 1.00 97.04 O
ANISOU 254 O LYS A 107P 18559 11851 6461 -1680 3656 -285 O
ATOM 255 CB LYS A 107P -2.613 4.488 3.537 1.00 99.11 C
ANISOU 255 CB LYS A 107P 17901 12456 7299 -2545 4153 -470 C
ATOM 256 CG LYS A 107P -2.930 5.677 4.405 1.00103.90 C
ANISOU 256 CG LYS A 107P 18781 12713 7983 -2747 4102 -320 C
ATOM 257 CD LYS A 107P -4.039 6.485 3.743 1.00108.71 C
ANISOU 257 CD LYS A 107P 20067 12886 8355 -2476 3922 -107 C
ATOM 258 CE LYS A 107P -4.082 7.895 4.243 1.00113.83 C
ANISOU 258 CE LYS A 107P 21117 13131 9003 -2721 3992 39 C
ATOM 259 NZ LYS A 107P -4.937 8.773 3.393 1.00112.15 N
ANISOU 259 NZ LYS A 107P 21586 12508 8519 -2461 3895 247 N
ATOM 260 N GLU A 108P -3.347 2.493 1.214 1.00 95.56 N
ANISOU 260 N GLU A 108P 17572 12272 6464 -1805 3961 -653 N
ATOM 261 CA GLU A 108P -3.448 2.241 -0.218 1.00100.39 C
ANISOU 261 CA GLU A 108P 18454 12917 6773 -1641 3985 -656 C
ATOM 262 C GLU A 108P -4.692 1.420 -0.523 1.00 92.92 C
ANISOU 262 C GLU A 108P 17633 11919 5755 -1205 3584 -710 C
ATOM 263 O GLU A 108P -5.331 1.603 -1.560 1.00 94.99 O
ANISOU 263 O GLU A 108P 18279 12076 5735 -1031 3442 -618 O
ATOM 264 CB GLU A 108P -2.196 1.522 -0.727 1.00 97.56 C
ANISOU 264 CB GLU A 108P 17730 12930 6408 -1758 4327 -846 C
ATOM 265 CG GLU A 108P -0.911 2.315 -0.551 1.00100.73 C
ANISOU 265 CG GLU A 108P 17954 13463 6856 -2217 4719 -804 C
ATOM 266 CD GLU A 108P -0.837 3.543 -1.439 1.00105.17 C
ANISOU 266 CD GLU A 108P 19041 13784 7133 -2438 4860 -599 C
ATOM 267 OE1 GLU A 108P -1.703 3.705 -2.323 1.00106.16 O
ANISOU 267 OE1 GLU A 108P 19645 13688 7001 -2197 4679 -491 O
ATOM 268 OE2 GLU A 108P 0.093 4.352 -1.248 1.00108.04 O
ANISOU 268 OE2 GLU A 108P 19339 14184 7526 -2863 5143 -552 O
ATOM 269 N SER A 109P -5.032 0.518 0.394 1.00 88.71 N
ANISOU 269 N SER A 109P 16764 11470 5471 -1050 3391 -865 N
ATOM 270 CA SER A 109P -6.205 -0.336 0.245 1.00 86.63 C
ANISOU 270 CA SER A 109P 16562 11176 5178 -689 2988 -949 C
ATOM 271 C SER A 109P -7.491 0.480 0.271 1.00 86.09 C
ANISOU 271 C SER A 109P 16861 10857 4992 -520 2647 -725 C
ATOM 272 O SER A 109P -8.503 0.076 -0.301 1.00 86.29 O
ANISOU 272 O SER A 109P 17036 10883 4867 -247 2316 -734 O
ATOM 273 CB SER A 109P -6.236 -1.401 1.342 1.00 82.71 C
ANISOU 273 CB SER A 109P 15603 10785 5036 -595 2855 -1151 C
ATOM 274 OG SER A 109P -5.070 -2.206 1.302 1.00 88.66 O
ANISOU 274 OG SER A 109P 15990 11785 5913 -665 3154 -1354 O
ATOM 275 N VAL A 110P -7.450 1.627 0.941 1.00 85.81 N
ANISOU 275 N VAL A 110P 16959 10622 5025 -678 2726 -531 N
ATOM 276 CA VAL A 110P -8.579 2.547 0.927 1.00 91.01 C
ANISOU 276 CA VAL A 110P 18000 11022 5559 -476 2458 -296 C
ATOM 277 C VAL A 110P -8.714 3.180 -0.449 1.00 97.00 C
ANISOU 277 C VAL A 110P 19206 11687 5964 -412 2497 -141 C
ATOM 278 O VAL A 110P -9.741 3.034 -1.107 1.00 93.20 O
ANISOU 278 O VAL A 110P 18909 11216 5288 -98 2179 -85 O
ATOM 279 CB VAL A 110P -8.439 3.659 1.984 1.00 90.10 C
ANISOU 279 CB VAL A 110P 17971 10662 5602 -663 2571 -139 C
ATOM 280 CG1 VAL A 110P -9.684 4.528 1.995 1.00 93.73 C
ANISOU 280 CG1 VAL A 110P 18819 10853 5942 -355 2286 91 C
ATOM 281 CG2 VAL A 110P -8.214 3.060 3.359 1.00 81.10 C
ANISOU 281 CG2 VAL A 110P 16383 9637 4796 -765 2558 -293 C
ATOM 282 N ASN A 111P -7.655 3.857 -0.887 1.00105.09 N
ANISOU 282 N ASN A 111P 20379 12651 6900 -728 2883 -82 N
ATOM 283 CA ASN A 111P -7.653 4.594 -2.149 1.00103.93 C
ANISOU 283 CA ASN A 111P 20703 12375 6412 -720 2974 79 C