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T0762ref_4Q5T.pdb
4753 lines (4753 loc) · 376 KB
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T0762ref_4Q5T.pdb
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HEADER TRANSPORT PROTEIN 17-APR-14 4Q5T
TITLE CRYSTAL STRUCTURE OF AN ATMB (PUTATIVE MEMBRANE LIPOPROTEIN) FROM
TITLE 2 STREPTOCOCCUS MUTANS UA159 AT 1.91 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 24-280;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS MUTANS UA159;
SOURCE 3 ORGANISM_TAXID: 210007;
SOURCE 4 STRAIN: ATCC 700610 / UA159;
SOURCE 5 GENE: ATMB, SMU_1941;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: PB1;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS METHIONINE-BINDING, NLPA LIPOPROTEIN, PF03180 FAMILY, STRUCTURAL
KEYWDS 2 GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, PSI-BIOLOGY, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 18-JUN-14 4Q5T 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF AN ATMB (PUTATIVE MEMBRANE LIPOPROTEIN)
JRNL TITL 2 FROM STREPTOCOCCUS MUTANS UA159 AT 1.91 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.220
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 23128
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 1189
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 28.7805 - 3.8108 0.99 2894 137 0.1720 0.1890
REMARK 3 2 3.8108 - 3.0258 0.99 2755 149 0.1668 0.2455
REMARK 3 3 3.0258 - 2.6436 1.00 2755 158 0.1741 0.2237
REMARK 3 4 2.6436 - 2.4020 1.00 2743 153 0.1648 0.2211
REMARK 3 5 2.4020 - 2.2299 0.99 2710 150 0.1815 0.2352
REMARK 3 6 2.2299 - 2.0985 1.00 2742 140 0.1966 0.2595
REMARK 3 7 2.0985 - 1.9934 0.99 2655 155 0.2362 0.2989
REMARK 3 8 1.9934 - 1.9070 0.98 2685 147 0.2941 0.2929
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.870
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.68
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.45
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 : 0.012 2103
REMARK 3 ANGLE : 1.239 2830
REMARK 3 CHIRALITY : 0.072 319
REMARK 3 PLANARITY : 0.005 358
REMARK 3 DIHEDRAL : 16.777 813
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain A
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1157 37.3778 37.3935
REMARK 3 T TENSOR
REMARK 3 T11: 0.2627 T22: 0.2262
REMARK 3 T33: 0.2316 T12: 0.0051
REMARK 3 T13: 0.0313 T23: -0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 0.0729 L22: 0.6194
REMARK 3 L33: 1.6865 L12: -0.1657
REMARK 3 L13: 0.2717 L23: 0.9582
REMARK 3 S TENSOR
REMARK 3 S11: -0.0608 S12: 0.0301 S13: 0.0402
REMARK 3 S21: 0.1291 S22: -0.0620 S23: 0.0894
REMARK 3 S31: 0.5374 S32: 0.0357 S33: -0.0179
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. ZERO OCCUPANCY HYDROGENS WERE
REMARK 3 INCLUDED DURING REFINEMENT TO IMPROVE THE ANTI-BUMPING
REMARK 3 RESTRAINTS. 2. ATOM RECORDS CONTAIN SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS. 3. ANISOU RECORDS CONTAIN SUM OF TLS AND RESIDUAL U
REMARK 3 FACTORS. 4. A MET-INHIBITION PROTOCOL WAS USED FOR
REMARK 3 SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75
REMARK 3 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 5. LIGAND SELENOMETHIONINE HAS BEEN MODELED BASED
REMARK 3 ON DENSITY AND ANOMALOUS DIFFERENCE FOURIER MAP. 6. NONAETHYLENE
REMARK 3 GLYCOL (2PE) MOLECULES FROM THE CRYSTALLIZATION SOLUTION ARE
REMARK 3 MODELED.
REMARK 4
REMARK 4 4Q5T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085640.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-SEP-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979068,0.979338,0.953725
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : KOHZU: DOUBLE CRYSTAL SI(111)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23167
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.910
REMARK 200 RESOLUTION RANGE LOW (A) : 28.777
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.44800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD,SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.200M SODIUM CHLORIDE, 50.00%
REMARK 280 POLYETHYLENE GLYCOL 400, 0.0100M BARIUM CHLORIDE, 0.1M CHES PH
REMARK 280 9.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
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 47.61000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 47.61000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 29.01050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.02650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.01050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.02650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 47.61000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.01050
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 53.02650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 47.61000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.01050
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 53.02650
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: CRYSTAL PACKING ANALYSIS SUGGESTS THE ASSIGNMENT OF A
REMARK 300 MONOMER AS THE SIGNIFICANT OLIGOMERIZATION STATE.
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 535 LIES ON A SPECIAL POSITION.
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 56 CG CD CE NZ
REMARK 470 LYS A 97 CD CE NZ
REMARK 470 LYS A 100 CG CD CE NZ
REMARK 470 ASP A 168 CG OD1 OD2
REMARK 470 GLU A 228 CG CD OE1 OE2
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 O HOH A 525 O HOH A 526 2.17
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 PHE A 86 -10.94 -158.32
REMARK 500 THR A 109 -89.01 -121.11
REMARK 500 HIS A 260 53.56 -90.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 2PE A 301
REMARK 610 2PE A 302
REMARK 610 2PE A 303
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2PE A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2PE A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2PE A 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: JCSG-417498 RELATED DB: TARGETTRACK
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS CONSTRUCT WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING
REMARK 999 ONLY A GLYCINE (0) FOLLOWED BY RESIDUES 25-280 OF THE TARGET
REMARK 999 SEQUENCE.
DBREF 4Q5T A 25 280 UNP I6L927 I6L927_STRMU 25 280
SEQADV 4Q5T GLY A 0 UNP I6L927 LEADER SEQUENCE
SEQRES 1 A 257 GLY GLN LYS ASN ASP LYS ASN THR LEU THR VAL GLY VAL
SEQRES 2 A 257 MSE THR MSE THR ASP SER ASP LYS GLU ARG TRP ASP LYS
SEQRES 3 A 257 ILE GLU GLU LEU LEU LYS LYS GLU ASN ILE LYS LEU LYS
SEQRES 4 A 257 PHE LYS GLU PHE THR ASP TYR SER GLN PRO ASN LYS ALA
SEQRES 5 A 257 LEU LYS ASN GLY GLU ILE ASP ILE ASN SER PHE GLN HIS
SEQRES 6 A 257 TYR ASN PHE LEU ASN ASN TRP ASN LYS GLU ASN LYS GLY
SEQRES 7 A 257 ASP LEU VAL THR VAL ALA GLU THR TYR ILE SER PRO ILE
SEQRES 8 A 257 ASN LEU PHE SER GLY THR GLU ASN GLY LYS ALA LYS TYR
SEQRES 9 A 257 SER SER ALA LYS GLU ILE PRO ASN GLY GLY GLN ILE ALA
SEQRES 10 A 257 ILE PRO ASN ASP ALA THR ASN GLU SER ARG ALA LEU TYR
SEQRES 11 A 257 VAL LEU GLN ASP ALA GLY LEU ILE LYS LEU ASN VAL SER
SEQRES 12 A 257 GLY ASP GLU LEU ALA THR VAL LYS ASN ILE LYS SER ASN
SEQRES 13 A 257 PRO LYS ASN LEU ASP ILE LYS GLU VAL ASP ALA SER GLN
SEQRES 14 A 257 THR ALA ARG ASN LEU ALA SER VAL ASP ALA ALA VAL VAL
SEQRES 15 A 257 ASN ASN SER TYR ALA VAL PRO ALA LYS ILE ASP PHE LYS
SEQRES 16 A 257 THR SER LEU TYR LYS GLU LYS VAL ASN GLU GLY SER LYS
SEQRES 17 A 257 GLN TRP ILE ASN ILE ILE ALA ALA GLN LYS ASN TRP LYS
SEQRES 18 A 257 LYS SER LYS LYS ALA ALA ALA ILE LYS LYS LEU ILE LYS
SEQRES 19 A 257 ALA TYR HIS THR ASP ALA VAL LYS LYS VAL ILE LYS LYS
SEQRES 20 A 257 THR ALA LYS GLY VAL ASP GLU PRO VAL TRP
MODRES 4Q5T MSE A 37 MET SELENOMETHIONINE
MODRES 4Q5T MSE A 39 MET SELENOMETHIONINE
HET MSE A 37 8
HET MSE A 39 8
HET MSE A 300 9
HET 2PE A 301 16
HET 2PE A 302 14
HET 2PE A 303 10
HETNAM MSE SELENOMETHIONINE
HETNAM 2PE NONAETHYLENE GLYCOL
FORMUL 1 MSE 3(C5 H11 N O2 SE)
FORMUL 3 2PE 3(C18 H38 O10)
FORMUL 6 HOH *154(H2 O)
HELIX 1 1 GLY A 0 ASP A 28 5 5
HELIX 2 2 THR A 40 LYS A 56 1 17
HELIX 3 3 GLN A 71 ASN A 78 1 8
HELIX 4 4 TYR A 89 LYS A 100 1 12
HELIX 5 5 SER A 129 ILE A 133 5 5
HELIX 6 6 ASP A 144 ALA A 158 1 15
HELIX 7 7 THR A 172 LYS A 174 5 3
HELIX 8 8 ASP A 189 SER A 191 5 3
HELIX 9 9 GLN A 192 LEU A 197 1 6
HELIX 10 10 ASN A 206 VAL A 211 1 6
HELIX 11 11 ASP A 216 LYS A 218 5 3
HELIX 12 12 ASN A 227 GLN A 232 5 6
HELIX 13 13 ASN A 242 SER A 246 5 5
HELIX 14 14 LYS A 248 HIS A 260 1 13
HELIX 15 15 THR A 261 LYS A 273 1 13
SHEET 1 A 6 LYS A 60 PHE A 66 0
SHEET 2 A 6 THR A 31 MSE A 37 1 N VAL A 34 O LYS A 62
SHEET 3 A 6 ILE A 83 HIS A 88 1 O SER A 85 N GLY A 35
SHEET 4 A 6 ILE A 234 ALA A 239 -1 O ILE A 236 N GLN A 87
SHEET 5 A 6 VAL A 104 ILE A 111 -1 N TYR A 110 O ASN A 235
SHEET 6 A 6 GLU A 277 PRO A 278 -1 O GLU A 277 N ILE A 111
SHEET 1 B 5 ASP A 184 VAL A 188 0
SHEET 2 B 5 GLN A 138 PRO A 142 1 N ILE A 141 O VAL A 188
SHEET 3 B 5 ALA A 202 VAL A 205 1 O VAL A 204 N ALA A 140
SHEET 4 B 5 ASN A 115 SER A 118 -1 N PHE A 117 O ALA A 203
SHEET 5 B 5 SER A 220 LYS A 223 -1 O LEU A 221 N LEU A 116
SHEET 1 C 2 THR A 120 GLU A 121 0
SHEET 2 C 2 LYS A 124 ALA A 125 -1 O LYS A 124 N GLU A 121
SHEET 1 D 2 LYS A 162 LEU A 163 0
SHEET 2 D 2 ILE A 176 SER A 178 -1 O LYS A 177 N LYS A 162
LINK C VAL A 36 N MSE A 37 1555 1555 1.33
LINK C MSE A 37 N THR A 38 1555 1555 1.33
LINK C THR A 38 N MSE A 39 1555 1555 1.33
LINK C MSE A 39 N THR A 40 1555 1555 1.33
SITE 1 AC1 5 ASP A 216 PHE A 217 LYS A 218 LYS A 273
SITE 2 AC1 5 VAL A 275
SITE 1 AC2 8 LYS A 77 ASP A 102 LYS A 126 GLY A 136
SITE 2 AC2 8 SER A 199 GLN A 240 ASN A 242 HOH A 543
SITE 1 AC3 4 ALA A 194 ALA A 213 LYS A 214 HOH A 527
CRYST1 58.021 106.053 95.220 90.00 90.00 90.00 C 2 2 21 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 0.017235 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009429 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010502 0.00000
ATOM 1 N GLY A 0 1.848 29.514 9.547 1.00 56.43 N
ANISOU 1 N GLY A 0 7348 6935 7160 -77 -132 -1065 N
ATOM 2 CA GLY A 0 1.360 29.909 10.895 1.00 54.69 C
ANISOU 2 CA GLY A 0 7057 6751 6973 -188 -91 -1123 C
ATOM 3 C GLY A 0 2.412 30.722 11.624 1.00 53.23 C
ANISOU 3 C GLY A 0 6872 6568 6785 -149 -90 -993 C
ATOM 4 O GLY A 0 3.481 31.003 11.062 1.00 45.30 O
ANISOU 4 O GLY A 0 5914 5545 5753 -43 -120 -869 O
ATOM 5 N GLN A 25 2.117 31.091 12.875 1.00 54.30 N
ANISOU 5 N GLN A 25 6953 6731 6946 -238 -54 -1027 N
ATOM 6 CA GLN A 25 2.975 31.990 13.653 1.00 51.91 C
ANISOU 6 CA GLN A 25 6631 6440 6651 -206 -59 -925 C
ATOM 7 C GLN A 25 4.447 31.587 13.787 1.00 45.47 C
ANISOU 7 C GLN A 25 5921 5578 5778 -152 -26 -760 C
ATOM 8 O GLN A 25 5.312 32.448 13.690 1.00 41.85 O
ANISOU 8 O GLN A 25 5445 5135 5322 -73 -62 -668 O
ATOM 9 CB GLN A 25 2.413 32.208 15.054 1.00 59.01 C
ANISOU 9 CB GLN A 25 7471 7371 7579 -321 -12 -990 C
ATOM 10 CG GLN A 25 1.720 33.548 15.221 1.00 74.87 C
ANISOU 10 CG GLN A 25 9343 9451 9651 -304 -82 -1076 C
ATOM 11 CD GLN A 25 1.692 34.019 16.659 1.00 84.32 C
ANISOU 11 CD GLN A 25 10492 10676 10870 -378 -45 -1079 C
ATOM 12 OE1 GLN A 25 2.308 33.410 17.537 1.00 86.99 O
ANISOU 12 OE1 GLN A 25 10904 10974 11172 -433 31 -1002 O
ATOM 13 NE2 GLN A 25 0.983 35.116 16.907 1.00 89.47 N
ANISOU 13 NE2 GLN A 25 11026 11395 11574 -371 -106 -1171 N
ATOM 14 N LYS A 26 4.740 30.300 13.995 1.00 34.58 N
ANISOU 14 N LYS A 26 4656 4144 4340 -191 39 -730 N
ATOM 15 CA LYS A 26 6.125 29.863 14.178 1.00 32.79 C
ANISOU 15 CA LYS A 26 4529 3880 4049 -127 63 -592 C
ATOM 16 C LYS A 26 6.971 30.155 12.927 1.00 33.45 C
ANISOU 16 C LYS A 26 4622 3974 4113 5 7 -511 C
ATOM 17 O LYS A 26 8.185 30.336 13.028 1.00 32.34 O
ANISOU 17 O LYS A 26 4510 3841 3937 74 8 -403 O
ATOM 18 CB LYS A 26 6.175 28.366 14.546 1.00 37.26 C
ANISOU 18 CB LYS A 26 5237 4375 4544 -184 131 -590 C
ATOM 19 CG LYS A 26 7.555 27.829 14.963 1.00 44.84 C
ANISOU 19 CG LYS A 26 6312 5298 5427 -116 155 -468 C
ATOM 20 CD LYS A 26 8.035 28.467 16.275 1.00 52.56 C
ANISOU 20 CD LYS A 26 7258 6295 6417 -138 179 -426 C
ATOM 21 CE LYS A 26 9.230 27.754 16.887 1.00 54.80 C
ANISOU 21 CE LYS A 26 7669 6538 6616 -84 207 -336 C
ATOM 22 NZ LYS A 26 10.256 27.422 15.872 1.00 57.90 N
ANISOU 22 NZ LYS A 26 8108 6937 6956 47 170 -262 N
ATOM 23 N ASN A 27 6.329 30.166 11.754 1.00 32.84 N
ANISOU 23 N ASN A 27 4522 3902 4054 38 -39 -571 N
ATOM 24 CA ASN A 27 7.018 30.391 10.478 1.00 35.27 C
ANISOU 24 CA ASN A 27 4848 4216 4337 156 -90 -504 C
ATOM 25 C ASN A 27 6.739 31.761 9.825 1.00 37.88 C
ANISOU 25 C ASN A 27 5090 4587 4715 207 -164 -524 C
ATOM 26 O ASN A 27 7.026 31.983 8.652 1.00 35.87 O
ANISOU 26 O ASN A 27 4853 4333 4442 293 -210 -495 O
ATOM 27 CB ASN A 27 6.725 29.245 9.520 1.00 38.94 C
ANISOU 27 CB ASN A 27 5390 4641 4764 178 -90 -535 C
ATOM 28 CG ASN A 27 7.378 27.993 9.971 1.00 36.75 C
ANISOU 28 CG ASN A 27 5233 4316 4416 166 -33 -480 C
ATOM 29 OD1 ASN A 27 8.590 27.849 9.831 1.00 34.45 O
ANISOU 29 OD1 ASN A 27 4992 4027 4069 248 -32 -376 O
ATOM 30 ND2 ASN A 27 6.611 27.125 10.632 1.00 38.23 N
ANISOU 30 ND2 ASN A 27 5469 4462 4596 59 17 -553 N
ATOM 31 N ASP A 28 6.222 32.660 10.645 1.00 35.14 N
ANISOU 31 N ASP A 28 4661 4270 4422 156 -176 -573 N
ATOM 32 CA ASP A 28 6.023 34.074 10.318 1.00 40.90 C
ANISOU 32 CA ASP A 28 5320 5031 5190 200 -249 -588 C
ATOM 33 C ASP A 28 7.275 34.867 10.685 1.00 37.37 C
ANISOU 33 C ASP A 28 4878 4598 4725 233 -244 -463 C
ATOM 34 O ASP A 28 7.618 35.001 11.876 1.00 42.36 O
ANISOU 34 O ASP A 28 5487 5241 5366 182 -203 -433 O
ATOM 35 CB ASP A 28 4.851 34.596 11.156 1.00 53.68 C
ANISOU 35 CB ASP A 28 6846 6680 6869 126 -263 -712 C
ATOM 36 CG ASP A 28 4.435 36.003 10.790 1.00 64.49 C
ANISOU 36 CG ASP A 28 8155 8077 8273 181 -354 -755 C
ATOM 37 OD1 ASP A 28 5.242 36.757 10.193 1.00 56.13 O
ANISOU 37 OD1 ASP A 28 7130 7008 7190 256 -394 -664 O
ATOM 38 OD2 ASP A 28 3.278 36.350 11.112 1.00 73.17 O
ANISOU 38 OD2 ASP A 28 9176 9209 9416 146 -388 -889 O
ATOM 39 N LYS A 29 7.929 35.431 9.677 1.00 34.01 N
ANISOU 39 N LYS A 29 4479 4173 4270 313 -285 -397 N
ATOM 40 CA LYS A 29 9.133 36.226 9.882 1.00 35.27 C
ANISOU 40 CA LYS A 29 4641 4353 4406 336 -278 -286 C
ATOM 41 C LYS A 29 8.906 37.576 10.604 1.00 32.76 C
ANISOU 41 C LYS A 29 4261 4053 4133 308 -315 -301 C
ATOM 42 O LYS A 29 9.869 38.203 11.004 1.00 32.88 O
ANISOU 42 O LYS A 29 4270 4087 4134 306 -300 -217 O
ATOM 43 CB LYS A 29 9.815 36.504 8.543 1.00 43.30 C
ANISOU 43 CB LYS A 29 5711 5368 5374 414 -308 -222 C
ATOM 44 CG LYS A 29 10.480 35.305 7.895 1.00 55.55 C
ANISOU 44 CG LYS A 29 7325 6914 6867 456 -268 -174 C
ATOM 45 CD LYS A 29 11.072 35.704 6.553 1.00 63.90 C
ANISOU 45 CD LYS A 29 8427 7976 7875 528 -298 -120 C
ATOM 46 CE LYS A 29 11.606 34.508 5.802 1.00 75.43 C
ANISOU 46 CE LYS A 29 9946 9437 9278 580 -270 -88 C
ATOM 47 NZ LYS A 29 12.289 34.917 4.547 1.00 80.98 N
ANISOU 47 NZ LYS A 29 10690 10153 9926 644 -290 -30 N
ATOM 48 N ASN A 30 7.661 38.023 10.742 1.00 33.22 N
ANISOU 48 N ASN A 30 4269 4111 4240 289 -366 -413 N
ATOM 49 CA ASN A 30 7.384 39.352 11.294 1.00 45.87 C
ANISOU 49 CA ASN A 30 5822 5728 5879 280 -418 -437 C
ATOM 50 C ASN A 30 6.698 39.320 12.668 1.00 44.85 C
ANISOU 50 C ASN A 30 5615 5624 5801 203 -394 -509 C
ATOM 51 O ASN A 30 6.217 40.339 13.158 1.00 39.93 O
ANISOU 51 O ASN A 30 4940 5019 5213 197 -446 -557 O
ATOM 52 CB ASN A 30 6.567 40.185 10.294 1.00 45.16 C
ANISOU 52 CB ASN A 30 5742 5624 5793 344 -519 -513 C
ATOM 53 CG ASN A 30 7.355 40.512 9.022 1.00 51.47 C
ANISOU 53 CG ASN A 30 6629 6393 6533 414 -545 -427 C
ATOM 54 OD1 ASN A 30 7.227 39.825 8.008 1.00 55.09 O
ANISOU 54 OD1 ASN A 30 7132 6834 6965 458 -549 -440 O
ATOM 55 ND2 ASN A 30 8.170 41.560 9.073 1.00 53.99 N
ANISOU 55 ND2 ASN A 30 6978 6707 6829 419 -560 -343 N
ATOM 56 N THR A 31 6.659 38.144 13.277 1.00 36.06 N
ANISOU 56 N THR A 31 4507 4511 4685 145 -317 -518 N
ATOM 57 CA THR A 31 6.149 37.986 14.637 1.00 38.12 C
ANISOU 57 CA THR A 31 4712 4792 4982 60 -276 -573 C
ATOM 58 C THR A 31 7.188 37.308 15.527 1.00 41.63 C
ANISOU 58 C THR A 31 5199 5224 5396 27 -192 -474 C
ATOM 59 O THR A 31 7.836 36.342 15.123 1.00 39.30 O
ANISOU 59 O THR A 31 4977 4903 5051 49 -150 -415 O
ATOM 60 CB THR A 31 4.873 37.133 14.677 1.00 46.29 C
ANISOU 60 CB THR A 31 5721 5832 6035 -1 -257 -709 C
ATOM 61 OG1 THR A 31 3.868 37.730 13.860 1.00 50.50 O
ANISOU 61 OG1 THR A 31 6207 6385 6594 41 -342 -821 O
ATOM 62 CG2 THR A 31 4.336 37.036 16.093 1.00 45.26 C
ANISOU 62 CG2 THR A 31 5535 5727 5934 -101 -208 -770 C
ATOM 63 N LEU A 32 7.347 37.835 16.739 1.00 34.09 N
ANISOU 63 N LEU A 32 4199 4287 4465 -14 -175 -461 N
ATOM 64 CA LEU A 32 8.187 37.213 17.735 1.00 32.55 C
ANISOU 64 CA LEU A 32 4044 4082 4243 -42 -102 -388 C
ATOM 65 C LEU A 32 7.376 36.934 18.971 1.00 33.32 C
ANISOU 65 C LEU A 32 4109 4183 4366 -134 -60 -466 C
ATOM 66 O LEU A 32 6.685 37.805 19.481 1.00 31.62 O
ANISOU 66 O LEU A 32 3812 4002 4201 -164 -95 -531 O
ATOM 67 CB LEU A 32 9.327 38.124 18.123 1.00 38.01 C
ANISOU 67 CB LEU A 32 4717 4793 4931 -3 -113 -289 C
ATOM 68 CG LEU A 32 10.663 37.996 17.435 1.00 43.33 C
ANISOU 68 CG LEU A 32 5441 5469 5552 65 -105 -182 C
ATOM 69 CD1 LEU A 32 11.625 38.946 18.154 1.00 43.40 C
ANISOU 69 CD1 LEU A 32 5412 5510 5569 74 -107 -111 C
ATOM 70 CD2 LEU A 32 11.187 36.559 17.460 1.00 40.00 C
ANISOU 70 CD2 LEU A 32 5103 5023 5071 78 -43 -152 C
ATOM 71 N THR A 33 7.496 35.718 19.482 1.00 31.01 N
ANISOU 71 N THR A 33 3893 3856 4033 -180 14 -459 N
ATOM 72 CA THR A 33 6.846 35.376 20.721 1.00 29.13 C
ANISOU 72 CA THR A 33 3648 3615 3805 -279 68 -521 C
ATOM 73 C THR A 33 7.935 35.379 21.781 1.00 38.00 C
ANISOU 73 C THR A 33 4811 4725 4901 -263 105 -426 C
ATOM 74 O THR A 33 8.956 34.679 21.668 1.00 31.02 O
ANISOU 74 O THR A 33 4020 3809 3959 -212 132 -343 O
ATOM 75 CB THR A 33 6.100 34.033 20.647 1.00 42.22 C
ANISOU 75 CB THR A 33 5379 5233 5427 -359 128 -593 C
ATOM 76 OG1 THR A 33 5.012 34.155 19.728 1.00 49.61 O
ANISOU 76 OG1 THR A 33 6254 6196 6398 -374 88 -701 O
ATOM 77 CG2 THR A 33 5.537 33.674 22.001 1.00 37.18 C
ANISOU 77 CG2 THR A 33 4751 4588 4786 -475 197 -650 C
ATOM 78 N VAL A 34 7.717 36.220 22.783 1.00 30.40 N
ANISOU 78 N VAL A 34 3774 3795 3983 -297 99 -446 N
ATOM 79 CA VAL A 34 8.709 36.470 23.810 1.00 28.90 C
ANISOU 79 CA VAL A 34 3599 3602 3779 -273 120 -364 C
ATOM 80 C VAL A 34 8.221 35.904 25.135 1.00 28.32 C
ANISOU 80 C VAL A 34 3562 3507 3693 -365 187 -410 C
ATOM 81 O VAL A 34 7.127 36.243 25.581 1.00 30.82 O
ANISOU 81 O VAL A 34 3806 3851 4051 -444 189 -505 O
ATOM 82 CB VAL A 34 8.949 37.978 23.953 1.00 31.55 C
ANISOU 82 CB VAL A 34 3828 3988 4171 -235 55 -342 C
ATOM 83 CG1 VAL A 34 10.037 38.250 24.932 1.00 25.26 C
ANISOU 83 CG1 VAL A 34 3041 3195 3362 -205 74 -260 C
ATOM 84 CG2 VAL A 34 9.307 38.567 22.626 1.00 37.68 C
ANISOU 84 CG2 VAL A 34 4586 4778 4951 -162 -8 -307 C
ATOM 85 N GLY A 35 9.039 35.064 25.767 1.00 26.57 N
ANISOU 85 N GLY A 35 3453 3237 3407 -350 240 -347 N
ATOM 86 CA GLY A 35 8.773 34.563 27.106 1.00 30.09 C
ANISOU 86 CA GLY A 35 3958 3649 3825 -427 305 -372 C
ATOM 87 C GLY A 35 9.347 35.461 28.224 1.00 27.40 C
ANISOU 87 C GLY A 35 3560 3337 3513 -399 293 -330 C
ATOM 88 O GLY A 35 10.528 35.782 28.251 1.00 28.49 O
ANISOU 88 O GLY A 35 3701 3484 3638 -304 268 -245 O
ATOM 89 N VAL A 36 8.497 35.818 29.169 1.00 29.30 N
ANISOU 89 N VAL A 36 3748 3597 3788 -486 314 -398 N
ATOM 90 CA VAL A 36 8.875 36.710 30.274 1.00 25.81 C
ANISOU 90 CA VAL A 36 3244 3184 3379 -468 301 -371 C
ATOM 91 C VAL A 36 8.244 36.192 31.539 1.00 36.77 C
ANISOU 91 C VAL A 36 4686 4544 4741 -569 373 -425 C
ATOM 92 O VAL A 36 7.372 35.332 31.486 1.00 29.22 O
ANISOU 92 O VAL A 36 3790 3559 3752 -669 429 -497 O
ATOM 93 CB VAL A 36 8.415 38.155 30.015 1.00 27.14 C
ANISOU 93 CB VAL A 36 3250 3428 3635 -456 224 -406 C
ATOM 94 CG1 VAL A 36 9.268 38.786 28.968 1.00 25.83 C
ANISOU 94 CG1 VAL A 36 3051 3281 3484 -355 158 -334 C
ATOM 95 CG2 VAL A 36 6.967 38.227 29.628 1.00 28.54 C
ANISOU 95 CG2 VAL A 36 3358 3639 3848 -539 217 -529 C
HETATM 96 N MSE A 37 8.700 36.680 32.685 1.00 34.59 N
ANISOU 96 N MSE A 37 4396 4274 4472 -550 376 -393 N
HETATM 97 CA MSE A 37 7.948 36.459 33.902 1.00 36.57 C
ANISOU 97 CA MSE A 37 4670 4514 4711 -655 438 -455 C
HETATM 98 C MSE A 37 6.727 37.362 33.889 1.00 32.70 C
ANISOU 98 C MSE A 37 4018 4106 4299 -728 409 -560 C
HETATM 99 O MSE A 37 6.649 38.314 33.100 1.00 30.16 O
ANISOU 99 O MSE A 37 3576 3841 4040 -672 328 -567 O
HETATM 100 CB MSE A 37 8.796 36.736 35.141 1.00 34.31 C
ANISOU 100 CB MSE A 37 4417 4211 4409 -604 445 -393 C
HETATM 101 CG MSE A 37 10.105 35.951 35.170 1.00 39.59 C
ANISOU 101 CG MSE A 37 5233 4812 4998 -504 456 -300 C
HETATM 102 SE MSE A 37 9.876 34.016 34.922 0.75 35.04 SE
ANISOU 102 SE MSE A 37 4900 4119 4294 -566 541 -316 SE
HETATM 103 CE MSE A 37 9.130 33.515 36.643 1.00 33.52 C
ANISOU 103 CE MSE A 37 4822 3868 4046 -701 638 -372 C
ATOM 104 N THR A 38 5.784 37.044 34.772 1.00 38.55 N
ANISOU 104 N THR A 38 4768 4853 5027 -850 474 -647 N
ATOM 105 CA THR A 38 4.636 37.897 35.054 1.00 38.62 C
ANISOU 105 CA THR A 38 4619 4953 5101 -918 451 -762 C
ATOM 106 C THR A 38 5.120 39.328 35.135 1.00 38.97 C
ANISOU 106 C THR A 38 4537 5052 5217 -811 353 -719 C
ATOM 107 O THR A 38 6.041 39.648 35.893 1.00 33.11 O
ANISOU 107 O THR A 38 3822 4287 4470 -748 346 -633 O
ATOM 108 CB THR A 38 3.972 37.476 36.368 1.00 53.28 C
ANISOU 108 CB THR A 38 6514 6807 6923 -1046 541 -830 C
ATOM 109 OG1 THR A 38 4.992 37.151 37.313 1.00 68.20 O
ANISOU 109 OG1 THR A 38 8530 8622 8760 -1002 575 -727 O
ATOM 110 CG2 THR A 38 3.115 36.237 36.170 1.00 60.59 C
ANISOU 110 CG2 THR A 38 7534 7701 7787 -1189 635 -914 C
HETATM 111 N MSE A 39 4.511 40.180 34.316 1.00 39.96 N
ANISOU 111 N MSE A 39 4533 5246 5403 -786 272 -782 N
HETATM 112 CA MSE A 39 5.026 41.518 34.070 1.00 36.74 C
ANISOU 112 CA MSE A 39 4033 4875 5053 -677 168 -733 C
HETATM 113 C MSE A 39 4.709 42.491 35.185 1.00 36.19 C
ANISOU 113 C MSE A 39 3867 4860 5026 -684 138 -772 C
HETATM 114 O MSE A 39 3.554 42.671 35.538 1.00 36.80 O
ANISOU 114 O MSE A 39 3861 5000 5122 -757 141 -897 O
HETATM 115 CB MSE A 39 4.435 42.086 32.788 1.00 38.39 C
ANISOU 115 CB MSE A 39 4162 5126 5299 -641 84 -794 C
HETATM 116 CG MSE A 39 4.840 41.350 31.524 1.00 41.72 C
ANISOU 116 CG MSE A 39 4665 5500 5688 -609 91 -746 C
HETATM 117 SE MSE A 39 4.694 42.606 29.999 0.75 63.65 SE
ANISOU 117 SE MSE A 39 7357 8314 8512 -503 -49 -761 SE
HETATM 118 CE MSE A 39 5.285 41.442 28.565 1.00 61.21 C
ANISOU 118 CE MSE A 39 7167 7940 8151 -474 -15 -693 C
ATOM 119 N THR A 40 5.739 43.147 35.698 1.00 37.19 N
ANISOU 119 N THR A 40 3996 4970 5166 -606 105 -671 N
ATOM 120 CA THR A 40 5.541 44.296 36.579 1.00 35.08 C
ANISOU 120 CA THR A 40 3628 4754 4947 -587 50 -697 C
ATOM 121 C THR A 40 5.152 45.488 35.715 1.00 37.28 C
ANISOU 121 C THR A 40 3805 5083 5276 -527 -68 -738 C
ATOM 122 O THR A 40 5.150 45.391 34.474 1.00 30.61 O
ANISOU 122 O THR A 40 2978 4226 4427 -497 -100 -734 O
ATOM 123 CB THR A 40 6.808 44.658 37.321 1.00 30.40 C
ANISOU 123 CB THR A 40 3071 4128 4353 -518 46 -579 C
ATOM 124 OG1 THR A 40 7.780 45.165 36.394 1.00 32.39 O
ANISOU 124 OG1 THR A 40 3330 4362 4615 -428 -16 -488 O
ATOM 125 CG2 THR A 40 7.353 43.456 38.033 1.00 31.49 C
ANISOU 125 CG2 THR A 40 3336 4202 4427 -549 148 -529 C
ATOM 126 N ASP A 41 4.790 46.602 36.349 1.00 29.67 N
ANISOU 126 N ASP A 41 2746 4173 4356 -505 -136 -782 N
ATOM 127 CA ASP A 41 4.458 47.806 35.597 1.00 30.77 C
ANISOU 127 CA ASP A 41 2811 4347 4532 -436 -261 -820 C
ATOM 128 C ASP A 41 5.662 48.290 34.815 1.00 28.25 C
ANISOU 128 C ASP A 41 2549 3974 4210 -352 -310 -690 C
ATOM 129 O ASP A 41 5.540 48.738 33.668 1.00 33.43 O
ANISOU 129 O ASP A 41 3208 4625 4868 -307 -381 -700 O
ATOM 130 CB ASP A 41 3.968 48.938 36.512 1.00 39.56 C
ANISOU 130 CB ASP A 41 3852 5509 5669 -406 -325 -864 C
ATOM 131 CG ASP A 41 2.610 48.651 37.117 1.00 52.21 C
ANISOU 131 CG ASP A 41 5439 7159 7240 -456 -278 -973 C
ATOM 132 OD1 ASP A 41 1.824 47.873 36.521 1.00 57.21 O
ANISOU 132 OD1 ASP A 41 6071 7813 7855 -509 -237 -1058 O
ATOM 133 OD2 ASP A 41 2.333 49.209 38.196 1.00 56.75 O
ANISOU 133 OD2 ASP A 41 6002 7753 7808 -442 -278 -974 O
ATOM 134 N SER A 42 6.831 48.225 35.438 1.00 26.18 N
ANISOU 134 N SER A 42 2334 3675 3940 -333 -271 -576 N
ATOM 135 CA SER A 42 8.051 48.603 34.728 1.00 24.76 C
ANISOU 135 CA SER A 42 2202 3455 3750 -268 -300 -459 C
ATOM 136 C SER A 42 8.301 47.688 33.518 1.00 26.21 C
ANISOU 136 C SER A 42 2459 3605 3895 -269 -262 -430 C
ATOM 137 O SER A 42 8.833 48.137 32.492 1.00 25.36 O
ANISOU 137 O SER A 42 2374 3480 3780 -223 -309 -378 O
ATOM 138 CB SER A 42 9.244 48.580 35.668 1.00 20.98 C
ANISOU 138 CB SER A 42 1749 2956 3265 -248 -259 -362 C
ATOM 139 OG SER A 42 10.450 48.838 34.961 1.00 25.55 O
ANISOU 139 OG SER A 42 2368 3512 3830 -198 -275 -262 O
ATOM 140 N ASP A 43 7.949 46.407 33.645 1.00 21.72 N
ANISOU 140 N ASP A 43 1935 3022 3295 -324 -174 -461 N
ATOM 141 CA ASP A 43 8.140 45.451 32.506 1.00 25.15 C
ANISOU 141 CA ASP A 43 2444 3422 3689 -323 -138 -438 C
ATOM 142 C ASP A 43 7.215 45.848 31.346 1.00 26.56 C
ANISOU 142 C ASP A 43 2585 3623 3885 -315 -207 -518 C
ATOM 143 O ASP A 43 7.619 45.902 30.167 1.00 26.28 O
ANISOU 143 O ASP A 43 2587 3566 3834 -271 -238 -475 O
ATOM 144 CB ASP A 43 7.879 44.008 32.907 1.00 28.00 C
ANISOU 144 CB ASP A 43 2877 3756 4007 -388 -34 -463 C
ATOM 145 CG ASP A 43 8.914 43.455 33.873 1.00 33.56 C
ANISOU 145 CG ASP A 43 3653 4423 4675 -375 30 -379 C
ATOM 146 OD1 ASP A 43 10.095 43.884 33.852 1.00 31.90 O
ANISOU 146 OD1 ASP A 43 3451 4206 4462 -303 7 -287 O
ATOM 147 OD2 ASP A 43 8.541 42.557 34.664 1.00 33.68 O
ANISOU 147 OD2 ASP A 43 3724 4415 4657 -438 107 -413 O
ATOM 148 N LYS A 44 5.968 46.130 31.686 1.00 34.03 N
ANISOU 148 N LYS A 44 3455 4616 4858 -354 -235 -641 N
ATOM 149 CA LYS A 44 4.998 46.573 30.702 1.00 36.02 C
ANISOU 149 CA LYS A 44 3662 4899 5124 -334 -313 -741 C
ATOM 150 C LYS A 44 5.494 47.815 29.980 1.00 35.65 C
ANISOU 150 C LYS A 44 3619 4838 5089 -246 -421 -687 C
ATOM 151 O LYS A 44 5.458 47.884 28.753 1.00 30.71 O
ANISOU 151 O LYS A 44 3029 4192 4447 -206 -464 -686 O
ATOM 152 CB LYS A 44 3.649 46.854 31.370 1.00 41.71 C
ANISOU 152 CB LYS A 44 4281 5692 5873 -379 -336 -895 C
ATOM 153 CG LYS A 44 2.974 45.608 31.976 1.00 46.56 C
ANISOU 153 CG LYS A 44 4897 6325 6468 -491 -223 -970 C
ATOM 154 CD LYS A 44 2.024 45.964 33.151 1.00 75.42 C
ANISOU 154 CD LYS A 44 8451 10057 10147 -549 -219 -1089 C
ATOM 155 CE LYS A 44 1.318 44.747 33.758 1.00 72.00 C
ANISOU 155 CE LYS A 44 8030 9643 9685 -681 -98 -1172 C
ATOM 156 NZ LYS A 44 0.681 45.025 35.089 1.00 69.27 N
ANISOU 156 NZ LYS A 44 7645 9345 9331 -717 -63 -1221 N
ATOM 157 N GLU A 45 5.953 48.805 30.731 1.00 35.01 N
ANISOU 157 N GLU A 45 3511 4762 5029 -219 -464 -644 N
ATOM 158 CA GLU A 45 6.352 50.048 30.111 1.00 34.52 C
ANISOU 158 CA GLU A 45 3465 4681 4970 -149 -568 -601 C
ATOM 159 C GLU A 45 7.563 49.868 29.188 1.00 31.76 C
ANISOU 159 C GLU A 45 3203 4278 4585 -125 -544 -475 C
ATOM 160 O GLU A 45 7.597 50.431 28.098 1.00 27.34 O
ANISOU 160 O GLU A 45 2685 3694 4007 -82 -612 -466 O
ATOM 161 CB GLU A 45 6.592 51.139 31.160 1.00 31.72 C
ANISOU 161 CB GLU A 45 3068 4341 4644 -132 -619 -583 C
ATOM 162 CG GLU A 45 6.413 52.520 30.578 1.00 51.56 C
ANISOU 162 CG GLU A 45 5592 6842 7157 -67 -751 -600 C
ATOM 163 CD GLU A 45 6.183 53.585 31.637 1.00 56.98 C
ANISOU 163 CD GLU A 45 6226 7555 7871 -47 -817 -629 C
ATOM 164 OE1 GLU A 45 5.684 53.239 32.732 1.00 48.90 O
ANISOU 164 OE1 GLU A 45 5162 6567 6849 -82 -750 -664 O
ATOM 165 OE2 GLU A 45 6.508 54.763 31.363 1.00 57.95 O
ANISOU 165 OE2 GLU A 45 6402 7642 7975 1 -897 -585 O
ATOM 166 N ARG A 46 8.554 49.085 29.606 1.00 27.38 N
ANISOU 166 N ARG A 46 2680 3709 4015 -148 -450 -385 N
ATOM 167 CA ARG A 46 9.708 48.876 28.741 1.00 27.80 C
ANISOU 167 CA ARG A 46 2802 3730 4031 -124 -425 -280 C
ATOM 168 C ARG A 46 9.329 48.090 27.450 1.00 25.64 C
ANISOU 168 C ARG A 46 2577 3438 3727 -118 -413 -306 C
ATOM 169 O ARG A 46 9.820 48.392 26.345 1.00 28.81 O
ANISOU 169 O ARG A 46 3029 3817 4101 -86 -443 -257 O
ATOM 170 CB ARG A 46 10.846 48.185 29.509 1.00 25.97 C
ANISOU 170 CB ARG A 46 2589 3496 3783 -135 -336 -196 C
ATOM 171 CG ARG A 46 10.627 46.711 29.844 1.00 25.74 C
ANISOU 171 CG ARG A 46 2591 3460 3731 -166 -244 -219 C
ATOM 172 CD ARG A 46 11.773 46.217 30.676 1.00 21.74 C
ANISOU 172 CD ARG A 46 2111 2948 3202 -154 -179 -143 C
ATOM 173 NE ARG A 46 11.662 46.761 32.035 1.00 22.70 N
ANISOU 173 NE ARG A 46 2181 3087 3357 -167 -185 -158 N
ATOM 174 CZ ARG A 46 12.427 46.415 33.054 1.00 24.92 C
ANISOU 174 CZ ARG A 46 2477 3366 3626 -156 -136 -116 C
ATOM 175 NH1 ARG A 46 13.352 45.478 32.915 1.00 28.81 N
ANISOU 175 NH1 ARG A 46 3037 3842 4067 -127 -79 -62 N
ATOM 176 NH2 ARG A 46 12.257 47.002 34.233 1.00 23.97 N
ANISOU 176 NH2 ARG A 46 2308 3262 3539 -164 -150 -133 N
ATOM 177 N TRP A 47 8.484 47.063 27.587 1.00 26.60 N
ANISOU 177 N TRP A 47 2688 3569 3849 -155 -365 -382 N
ATOM 178 CA TRP A 47 8.099 46.289 26.420 1.00 29.00 C
ANISOU 178 CA TRP A 47 3035 3857 4127 -151 -354 -412 C
ATOM 179 C TRP A 47 7.163 47.081 25.510 1.00 34.81 C
ANISOU 179 C TRP A 47 3752 4599 4874 -114 -456 -496 C
ATOM 180 O TRP A 47 7.171 46.902 24.296 1.00 31.74 O
ANISOU 180 O TRP A 47 3412 4188 4458 -82 -477 -490 O
ATOM 181 CB TRP A 47 7.506 44.952 26.834 1.00 26.47 C
ANISOU 181 CB TRP A 47 2720 3539 3796 -211 -269 -470 C
ATOM 182 CG TRP A 47 8.586 43.967 27.191 1.00 30.77 C
ANISOU 182 CG TRP A 47 3335 4055 4302 -219 -179 -375 C
ATOM 183 CD1 TRP A 47 8.884 43.492 28.435 1.00 26.73 C
ANISOU 183 CD1 TRP A 47 2833 3538 3784 -252 -114 -356 C
ATOM 184 CD2 TRP A 47 9.540 43.366 26.294 1.00 29.08 C
ANISOU 184 CD2 TRP A 47 3195 3812 4042 -179 -153 -292 C
ATOM 185 NE1 TRP A 47 9.946 42.609 28.366 1.00 33.91 N
ANISOU 185 NE1 TRP A 47 3824 4416 4643 -228 -55 -272 N
ATOM 186 CE2 TRP A 47 10.373 42.525 27.069 1.00 33.51 C
ANISOU 186 CE2 TRP A 47 3807 4357 4569 -183 -77 -233 C
ATOM 187 CE3 TRP A 47 9.762 43.449 24.912 1.00 24.99 C
ANISOU 187 CE3 TRP A 47 2709 3282 3503 -135 -188 -266 C
ATOM 188 CZ2 TRP A 47 11.410 41.760 26.506 1.00 24.78 C
ANISOU 188 CZ2 TRP A 47 2774 3232 3409 -140 -40 -157 C
ATOM 189 CZ3 TRP A 47 10.786 42.683 24.355 1.00 29.69 C
ANISOU 189 CZ3 TRP A 47 3373 3861 4048 -103 -142 -187 C
ATOM 190 CH2 TRP A 47 11.596 41.852 25.155 1.00 25.15 C
ANISOU 190 CH2 TRP A 47 2838 3278 3440 -103 -72 -137 C
ATOM 191 N ASP A 48 6.357 47.951 26.103 1.00 30.72 N
ANISOU 191 N ASP A 48 3167 4115 4391 -111 -523 -580 N
ATOM 192 CA ASP A 48 5.620 48.956 25.342 1.00 33.96 C
ANISOU 192 CA ASP A 48 3571 4528 4803 -52 -643 -656 C
ATOM 193 C ASP A 48 6.509 49.776 24.419 1.00 32.47 C
ANISOU 193 C ASP A 48 3467 4288 4582 3 -699 -557 C
ATOM 194 O ASP A 48 6.252 49.905 23.211 1.00 34.58 O
ANISOU 194 O ASP A 48 3788 4529 4821 48 -752 -578 O
ATOM 195 CB ASP A 48 4.936 49.921 26.288 1.00 44.95 C
ANISOU 195 CB ASP A 48 4886 5962 6229 -44 -714 -737 C
ATOM 196 CG ASP A 48 3.459 49.854 26.184 1.00 60.22 C
ANISOU 196 CG ASP A 48 6749 7953 8178 -39 -763 -911 C
ATOM 197 OD1 ASP A 48 2.920 48.788 26.529 1.00 66.38 O
ANISOU 197 OD1 ASP A 48 7486 8769 8968 -107 -680 -975 O
ATOM 198 OD2 ASP A 48 2.844 50.855 25.744 1.00 72.91 O
ANISOU 198 OD2 ASP A 48 8351 9570 9783 33 -886 -989 O
ATOM 199 N LYS A 49 7.567 50.335 24.980 1.00 29.40 N
ANISOU 199 N LYS A 49 3094 3885 4193 -6 -685 -451 N
ATOM 200 CA LYS A 49 8.465 51.162 24.183 1.00 27.92 C
ANISOU 200 CA LYS A 49 2989 3652 3969 24 -726 -358 C
ATOM 201 C LYS A 49 9.151 50.308 23.090 1.00 31.36 C
ANISOU 201 C LYS A 49 3491 4064 4362 23 -663 -290 C
ATOM 202 O LYS A 49 9.243 50.719 21.939 1.00 31.49 O
ANISOU 202 O LYS A 49 3581 4043 4339 57 -712 -273 O
ATOM 203 CB LYS A 49 9.490 51.823 25.090 1.00 25.28 C
ANISOU 203 CB LYS A 49 2643 3318 3643 1 -709 -268 C
ATOM 204 CG LYS A 49 10.485 52.718 24.388 1.00 30.58 C
ANISOU 204 CG LYS A 49 3396 3948 4273 7 -739 -174 C
ATOM 205 CD LYS A 49 9.818 53.860 23.663 1.00 32.66 C
ANISOU 205 CD LYS A 49 3727 4169 4513 54 -864 -223 C
ATOM 206 CE LYS A 49 9.114 54.782 24.623 1.00 45.23 C
ANISOU 206 CE LYS A 49 5272 5773 6140 73 -949 -292 C
ATOM 207 NZ LYS A 49 8.649 56.013 23.915 1.00 48.75 N
ANISOU 207 NZ LYS A 49 5811 6165 6547 129 -1083 -329 N
ATOM 208 N ILE A 50 9.633 49.125 23.447 1.00 32.41 N
ANISOU 208 N ILE A 50 3604 4214 4494 -10 -559 -252 N
ATOM 209 CA ILE A 50 10.202 48.219 22.446 1.00 31.31 C
ANISOU 209 CA ILE A 50 3523 4060 4312 -2 -504 -201 C
ATOM 210 C ILE A 50 9.210 47.927 21.303 1.00 26.09 C
ANISOU 210 C ILE A 50 2893 3382 3640 29 -549 -280 C
ATOM 211 O ILE A 50 9.552 47.975 20.127 1.00 29.20 O
ANISOU 211 O ILE A 50 3355 3748 3992 60 -566 -243 O
ATOM 212 CB ILE A 50 10.665 46.906 23.108 1.00 32.40 C
ANISOU 212 CB ILE A 50 3645 4216 4447 -33 -397 -172 C
ATOM 213 CG1 ILE A 50 11.901 47.177 23.963 1.00 25.81 C
ANISOU 213 CG1 ILE A 50 2796 3399 3609 -43 -356 -84 C
ATOM 214 CG2 ILE A 50 10.995 45.854 22.051 1.00 27.36 C
ANISOU 214 CG2 ILE A 50 3066 3564 3765 -16 -351 -144 C
ATOM 215 CD1 ILE A 50 12.194 46.124 24.975 1.00 25.32 C
ANISOU 215 CD1 ILE A 50 2720 3352 3549 -63 -273 -75 C
ATOM 216 N GLU A 51 7.976 47.608 21.657 1.00 27.90 N
ANISOU 216 N GLU A 51 3066 3632 3901 20 -567 -398 N
ATOM 217 CA GLU A 51 6.949 47.368 20.672 1.00 33.37 C
ANISOU 217 CA GLU A 51 3772 4320 4588 53 -616 -495 C
ATOM 218 C GLU A 51 6.798 48.589 19.800 1.00 44.37 C
ANISOU 218 C GLU A 51 5219 5681 5958 119 -729 -505 C
ATOM 219 O GLU A 51 6.791 48.490 18.563 1.00 42.58 O
ANISOU 219 O GLU A 51 5062 5422 5694 161 -757 -500 O
ATOM 220 CB GLU A 51 5.611 47.082 21.340 1.00 35.48 C
ANISOU 220 CB GLU A 51 3952 4634 4896 25 -627 -640 C
ATOM 221 CG GLU A 51 5.373 45.654 21.747 1.00 50.90 C
ANISOU 221 CG GLU A 51 5881 6604 6853 -42 -522 -668 C
ATOM 222 CD GLU A 51 3.911 45.393 22.087 1.00 61.15 C
ANISOU 222 CD GLU A 51 7098 7955 8182 -76 -537 -835 C
ATOM 223 OE1 GLU A 51 3.084 45.237 21.160 1.00 63.06 O
ANISOU 223 OE1 GLU A 51 7336 8206 8419 -46 -583 -932 O
ATOM 224 OE2 GLU A 51 3.581 45.346 23.286 1.00 64.27 O
ANISOU 224 OE2 GLU A 51 7429 8387 8603 -135 -501 -877 O
ATOM 225 N GLU A 52 6.667 49.746 20.445 1.00 34.31 N
ANISOU 225 N GLU A 52 3925 4410 4700 130 -799 -520 N
ATOM 226 CA GLU A 52 6.453 50.965 19.688 1.00 31.46 C
ANISOU 226 CA GLU A 52 3639 4008 4308 196 -918 -538 C
ATOM 227 C GLU A 52 7.580 51.136 18.697 1.00 35.15 C
ANISOU 227 C GLU A 52 4217 4420 4717 201 -898 -413 C
ATOM 228 O GLU A 52 7.335 51.485 17.564 1.00 36.72 O
ANISOU 228 O GLU A 52 4503 4575 4872 255 -964 -431 O
ATOM 229 CB GLU A 52 6.352 52.210 20.580 1.00 39.24 C
ANISOU 229 CB GLU A 52 4604 4995 5309 205 -993 -552 C
ATOM 230 CG GLU A 52 6.073 53.525 19.816 1.00 65.46 C
ANISOU 230 CG GLU A 52 8028 8259 8584 281 -1131 -578 C
ATOM 231 CD GLU A 52 6.831 54.744 20.379 1.00 78.96 C
ANISOU 231 CD GLU A 52 9786 9934 10280 266 -1169 -496 C
ATOM 232 OE1 GLU A 52 7.032 54.833 21.613 1.00 74.42 O
ANISOU 232 OE1 GLU A 52 9127 9399 9750 224 -1134 -482 O
ATOM 233 OE2 GLU A 52 7.228 55.622 19.574 1.00 86.27 O
ANISOU 233 OE2 GLU A 52 10844 10788 11145 293 -1233 -446 O
ATOM 234 N LEU A 53 8.813 50.901 19.113 1.00 30.38 N
ANISOU 234 N LEU A 53 3613 3823 4109 146 -808 -294 N
ATOM 235 CA LEU A 53 9.936 51.084 18.212 1.00 32.59 C
ANISOU 235 CA LEU A 53 3985 4067 4329 139 -780 -184 C
ATOM 236 C LEU A 53 9.942 50.050 17.095 1.00 41.93 C
ANISOU 236 C LEU A 53 5205 5245 5482 160 -739 -180 C
ATOM 237 O LEU A 53 10.526 50.296 16.039 1.00 45.87 O
ANISOU 237 O LEU A 53 5797 5709 5923 171 -743 -120 O
ATOM 238 CB LEU A 53 11.251 50.965 18.955 1.00 32.86 C
ANISOU 238 CB LEU A 53 3987 4132 4366 79 -689 -77 C
ATOM 239 CG LEU A 53 11.555 52.053 19.972 1.00 34.48 C
ANISOU 239 CG LEU A 53 4169 4340 4593 52 -721 -55 C
ATOM 240 CD1 LEU A 53 12.689 51.583 20.874 1.00 34.10 C
ANISOU 240 CD1 LEU A 53 4059 4339 4560 3 -620 21 C
ATOM 241 CD2 LEU A 53 11.944 53.318 19.291 1.00 38.76 C
ANISOU 241 CD2 LEU A 53 4819 4827 5082 52 -787 -12 C
ATOM 242 N LEU A 54 9.315 48.899 17.331 1.00 33.42 N
ANISOU 242 N LEU A 54 4062 4199 4438 158 -695 -243 N
ATOM 243 CA LEU A 54 9.358 47.806 16.356 1.00 33.09 C
ANISOU 243 CA LEU A 54 4053 4152 4368 175 -650 -238 C
ATOM 244 C LEU A 54 8.251 47.913 15.291 1.00 38.27 C
ANISOU 244 C LEU A 54 4751 4779 5012 239 -736 -336 C
ATOM 245 O LEU A 54 8.317 47.253 14.248 1.00 34.21 O
ANISOU 245 O LEU A 54 4285 4248 4464 266 -720 -327 O
ATOM 246 CB LEU A 54 9.309 46.455 17.075 1.00 26.87 C
ANISOU 246 CB LEU A 54 3198 3402 3610 137 -558 -252 C
ATOM 247 CG LEU A 54 10.617 45.949 17.716 1.00 28.06 C
ANISOU 247 CG LEU A 54 3338 3575 3747 99 -462 -147 C
ATOM 248 CD1 LEU A 54 10.411 44.639 18.504 1.00 28.41 C
ANISOU 248 CD1 LEU A 54 3342 3641 3811 68 -385 -174 C
ATOM 249 CD2 LEU A 54 11.669 45.743 16.633 1.00 32.73 C
ANISOU 249 CD2 LEU A 54 3998 4159 4277 120 -432 -58 C
ATOM 250 N LYS A 55 7.232 48.732 15.541 1.00 42.18 N
ANISOU 250 N LYS A 55 5225 5272 5530 272 -834 -438 N
ATOM 251 CA LYS A 55 6.242 49.025 14.496 1.00 44.92 C
ANISOU 251 CA LYS A 55 5622 5591 5855 351 -935 -539 C
ATOM 252 C LYS A 55 6.940 49.524 13.220 1.00 41.62 C
ANISOU 252 C LYS A 55 5344 5107 5362 391 -964 -455 C
ATOM 253 O LYS A 55 6.613 49.095 12.111 1.00 40.28 O
ANISOU 253 O LYS A 55 5227 4914 5162 442 -985 -487 O
ATOM 254 CB LYS A 55 5.231 50.061 14.970 1.00 52.52 C
ANISOU 254 CB LYS A 55 6556 6562 6837 395 -1051 -655 C
ATOM 255 CG LYS A 55 4.281 49.566 16.037 1.00 58.92 C
ANISOU 255 CG LYS A 55 7227 7447 7714 363 -1034 -774 C
ATOM 256 CD LYS A 55 3.182 50.587 16.293 1.00 64.41 C
ANISOU 256 CD LYS A 55 7893 8160 8419 428 -1165 -913 C
ATOM 257 CE LYS A 55 2.270 50.164 17.425 1.00 72.49 C
ANISOU 257 CE LYS A 55 8768 9271 9504 383 -1141 -1036 C
ATOM 258 NZ LYS A 55 0.965 50.871 17.372 1.00 78.17 N
ANISOU 258 NZ LYS A 55 9444 10031 10227 464 -1274 -1217 N
ATOM 259 N LYS A 56 7.933 50.390 13.389 1.00 40.88 N
ANISOU 259 N LYS A 56 5310 4985 5236 360 -958 -348 N
ATOM 260 CA LYS A 56 8.704 50.935 12.268 1.00 48.22 C
ANISOU 260 CA LYS A 56 6381 5854 6087 373 -971 -261 C
ATOM 261 C LYS A 56 9.329 49.842 11.405 1.00 53.86 C
ANISOU 261 C LYS A 56 7114 6579 6772 364 -884 -200 C
ATOM 262 O LYS A 56 9.638 50.062 10.234 1.00 53.73 O
ANISOU 262 O LYS A 56 7212 6514 6688 392 -902 -162 O
ATOM 263 CB LYS A 56 9.816 51.842 12.796 1.00 51.90 C
ANISOU 263 CB LYS A 56 6882 6307 6529 306 -944 -153 C
ATOM 264 N GLU A 57 9.531 48.668 11.994 1.00 47.70 N
ANISOU 264 N GLU A 57 6231 5856 6036 326 -790 -192 N
ATOM 265 CA GLU A 57 10.151 47.549 11.302 1.00 43.29 C
ANISOU 265 CA GLU A 57 5684 5314 5450 323 -708 -137 C
ATOM 266 C GLU A 57 9.098 46.533 10.929 1.00 38.87 C
ANISOU 266 C GLU A 57 5090 4761 4917 366 -720 -237 C
ATOM 267 O GLU A 57 9.425 45.437 10.470 1.00 48.37 O
ANISOU 267 O GLU A 57 6294 5979 6107 367 -656 -210 O
ATOM 268 CB GLU A 57 11.181 46.875 12.218 1.00 55.10 C
ANISOU 268 CB GLU A 57 7107 6866 6963 259 -598 -60 C
ATOM 269 CG GLU A 57 12.303 47.793 12.708 1.00 57.92 C
ANISOU 269 CG GLU A 57 7474 7233 7298 207 -573 31 C
ATOM 270 CD GLU A 57 13.358 48.049 11.639 1.00 65.28 C
ANISOU 270 CD GLU A 57 8495 8157 8152 197 -544 119 C
ATOM 271 OE1 GLU A 57 13.087 47.748 10.455 1.00 67.43 O
ANISOU 271 OE1 GLU A 57 8838 8398 8383 242 -565 106 O
ATOM 272 OE2 GLU A 57 14.463 48.530 11.984 1.00 68.75 O
ANISOU 272 OE2 GLU A 57 8930 8625 8567 140 -497 194 O
ATOM 273 N ASN A 58 7.834 46.868 11.169 1.00 33.92 N
ANISOU 273 N ASN A 58 4428 4130 4328 399 -802 -361 N
ATOM 274 CA ASN A 58 6.741 45.945 10.883 1.00 41.46 C
ANISOU 274 CA ASN A 58 5337 5103 5313 428 -813 -477 C
ATOM 275 C ASN A 58 6.862 44.597 11.626 1.00 41.91 C
ANISOU 275 C ASN A 58 5312 5205 5407 363 -706 -472 C
ATOM 276 O ASN A 58 6.462 43.543 11.100 1.00 44.34 O
ANISOU 276 O ASN A 58 5617 5516 5714 374 -680 -516 O
ATOM 277 CB ASN A 58 6.668 45.710 9.364 1.00 54.03 C
ANISOU 277 CB ASN A 58 7024 6654 6853 499 -847 -480 C
ATOM 278 CG ASN A 58 5.321 45.180 8.910 1.00 70.68 C
ANISOU 278 CG ASN A 58 9097 8773 8987 551 -902 -631 C
ATOM 279 OD1 ASN A 58 4.351 45.165 9.673 1.00 74.82 O
ANISOU 279 OD1 ASN A 58 9527 9337 9563 536 -928 -748 O
ATOM 280 ND2 ASN A 58 5.253 44.738 7.652 1.00 76.83 N
ANISOU 280 ND2 ASN A 58 9945 9521 9726 611 -919 -636 N
ATOM 281 N ILE A 59 7.413 44.630 12.838 1.00 30.10 N
ANISOU 281 N ILE A 59 3763 3736 3936 299 -647 -420 N
ATOM 282 CA ILE A 59 7.479 43.430 13.698 1.00 27.53 C
ANISOU 282 CA ILE A 59 3379 3443 3637 238 -553 -421 C
ATOM 283 C ILE A 59 6.403 43.521 14.780 1.00 34.04 C
ANISOU 283 C ILE A 59 4113 4301 4520 197 -568 -535 C
ATOM 284 O ILE A 59 6.256 44.552 15.432 1.00 37.24 O
ANISOU 284 O ILE A 59 4485 4717 4947 194 -616 -551 O