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6MSR.pdb
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6MSR.pdb
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HEADER DE NOVO PROTEIN 17-OCT-18 6MSR
TITLE CRYSTAL STRUCTURE OF PRO-2.5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRO-2.5;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DE NOVO PROTEIN, COMPUTATIONAL DESIGN, HELICAL BUNDLE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.BICK,S.E.BOYKEN,D.BAKER
REVDAT 2 29-MAY-19 6MSR 1 TITLE JRNL
REVDAT 1 08-MAY-19 6MSR 0
JRNL AUTH S.E.BOYKEN,M.A.BENHAIM,F.BUSCH,M.JIA,M.J.BICK,H.CHOI,
JRNL AUTH 2 J.C.KLIMA,Z.CHEN,C.WALKEY,A.MILEANT,A.SAHASRABUDDHE,K.Y.WEI,
JRNL AUTH 3 E.A.HODGE,S.BYRON,A.QUIJANO-RUBIO,B.SANKARAN,N.P.KING,
JRNL AUTH 4 J.LIPPINCOTT-SCHWARTZ,V.H.WYSOCKI,K.K.LEE,D.BAKER
JRNL TITL DE NOVO DESIGN OF TUNABLE, PH-DRIVEN CONFORMATIONAL CHANGES.
JRNL REF SCIENCE V. 364 658 2019
JRNL REFN ESSN 1095-9203
JRNL PMID 31097662
JRNL DOI 10.1126/SCIENCE.AAV7897
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2992: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 3 NUMBER OF REFLECTIONS : 30055
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.243
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.680
REMARK 3 FREE R VALUE TEST SET COUNT : 1407
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 28.7222 - 3.3378 0.97 3023 145 0.2099 0.2208
REMARK 3 2 3.3378 - 2.6499 0.99 3015 148 0.2313 0.3173
REMARK 3 3 2.6499 - 2.3151 0.99 2971 153 0.2339 0.2422
REMARK 3 4 2.3151 - 2.1035 0.99 2938 150 0.2675 0.2796
REMARK 3 5 2.1035 - 1.9528 0.98 2906 137 0.2734 0.2568
REMARK 3 6 1.9528 - 1.8377 0.95 2858 139 0.2774 0.3075
REMARK 3 7 1.8377 - 1.7456 0.94 2769 133 0.3017 0.3405
REMARK 3 8 1.7456 - 1.6697 0.93 2790 141 0.3294 0.3827
REMARK 3 9 1.6697 - 1.6054 0.90 2699 132 0.3642 0.3166
REMARK 3 10 1.6054 - 1.5500 0.89 2679 129 0.3900 0.3889
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.150
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 1771
REMARK 3 ANGLE : 0.447 2423
REMARK 3 CHIRALITY : 0.030 310
REMARK 3 PLANARITY : 0.002 323
REMARK 3 DIHEDRAL : 20.530 1124
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.4089 17.2149 29.7212
REMARK 3 T TENSOR
REMARK 3 T11: 0.2734 T22: 0.5300
REMARK 3 T33: 0.3733 T12: -0.0145
REMARK 3 T13: 0.0030 T23: 0.1557
REMARK 3 L TENSOR
REMARK 3 L11: 0.1854 L22: 1.3115
REMARK 3 L33: 3.0117 L12: -0.2531
REMARK 3 L13: 0.9829 L23: 0.1753
REMARK 3 S TENSOR
REMARK 3 S11: -0.2998 S12: 0.3249 S13: 0.0292
REMARK 3 S21: -0.2306 S22: -0.3676 S23: -0.1578
REMARK 3 S31: -0.2480 S32: 1.5866 S33: -0.0056
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 39 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5755 12.0555 31.0038
REMARK 3 T TENSOR
REMARK 3 T11: 0.2841 T22: 0.2628
REMARK 3 T33: 0.2255 T12: 0.0823
REMARK 3 T13: 0.0376 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 1.2008 L22: 0.8890
REMARK 3 L33: 0.3989 L12: 0.3739
REMARK 3 L13: 0.5447 L23: 0.1571
REMARK 3 S TENSOR
REMARK 3 S11: -0.1741 S12: 0.2451 S13: -0.1470
REMARK 3 S21: -0.2439 S22: -0.1721 S23: -0.0096
REMARK 3 S31: 0.5466 S32: 0.2989 S33: -0.0045
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1923 7.4657 29.2668
REMARK 3 T TENSOR
REMARK 3 T11: 0.5606 T22: 0.3494
REMARK 3 T33: 0.3879 T12: -0.1107
REMARK 3 T13: 0.1491 T23: -0.0678
REMARK 3 L TENSOR
REMARK 3 L11: 1.2565 L22: 0.2354
REMARK 3 L33: 2.8913 L12: -0.7226
REMARK 3 L13: -0.4049 L23: -0.5017
REMARK 3 S TENSOR
REMARK 3 S11: -0.1883 S12: 0.5021 S13: -0.0763
REMARK 3 S21: -0.4825 S22: -0.2761 S23: 0.0495
REMARK 3 S31: 1.0478 S32: -0.9161 S33: -0.0285
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 39 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8620 15.5424 30.6099
REMARK 3 T TENSOR
REMARK 3 T11: 0.2443 T22: 0.3667
REMARK 3 T33: 0.2498 T12: -0.0245
REMARK 3 T13: -0.0016 T23: -0.0423
REMARK 3 L TENSOR
REMARK 3 L11: 0.7864 L22: 1.3089
REMARK 3 L33: 0.5065 L12: -0.0590
REMARK 3 L13: -0.1690 L23: -0.7831
REMARK 3 S TENSOR
REMARK 3 S11: -0.0235 S12: 0.3406 S13: -0.0274
REMARK 3 S21: -0.2462 S22: -0.1456 S23: 0.0869
REMARK 3 S31: 0.2586 S32: -1.0159 S33: -0.0005
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 0 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.3642 25.6051 29.6453
REMARK 3 T TENSOR
REMARK 3 T11: 0.4554 T22: 0.3433
REMARK 3 T33: 0.3779 T12: 0.1365
REMARK 3 T13: -0.1193 T23: -0.0861
REMARK 3 L TENSOR
REMARK 3 L11: 0.7108 L22: 0.7259
REMARK 3 L33: 4.7176 L12: 0.7473
REMARK 3 L13: -0.3561 L23: 1.2266
REMARK 3 S TENSOR
REMARK 3 S11: -0.1804 S12: 0.2483 S13: 0.0358
REMARK 3 S21: -0.2853 S22: -0.2988 S23: -0.0593
REMARK 3 S31: -1.2466 S32: -0.9141 S33: -0.0268
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 39 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5117 22.3719 29.3417
REMARK 3 T TENSOR
REMARK 3 T11: 0.2932 T22: 0.2093
REMARK 3 T33: 0.2294 T12: -0.0520
REMARK 3 T13: -0.0417 T23: 0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 1.3428 L22: 1.6844
REMARK 3 L33: 0.6035 L12: -0.4050
REMARK 3 L13: -0.8150 L23: 0.7039
REMARK 3 S TENSOR
REMARK 3 S11: -0.1728 S12: 0.2958 S13: 0.0995
REMARK 3 S21: -0.2869 S22: -0.1336 S23: -0.0433
REMARK 3 S31: -0.8460 S32: 0.2747 S33: -0.0020
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 6MSR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237521.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JAN-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 0.999994
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JUN 17, 2015
REMARK 200 DATA SCALING SOFTWARE : XDS JUN 17, 2015
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42699
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.17
REMARK 200 R MERGE FOR SHELL (I) : 3.49700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.8.1
REMARK 200 STARTING MODEL: COMPUTATIONALLY DESIGNED MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M POTASSIUM ACETATE AND 20% W/V
REMARK 280 PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 28.80900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 16.64050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 28.80900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 16.64050
REMARK 290 SMTRY3 4 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 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 GLU A 2 CD OE1 OE2
REMARK 470 ARG A 6 NE CZ NH1 NH2
REMARK 470 LYS A 20 CG CD CE NZ
REMARK 470 ARG A 21 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 31 CD OE1 OE2
REMARK 470 GLU A 32 CG CD OE1 OE2
REMARK 470 LYS A 34 CG CD CE NZ
REMARK 470 LYS A 35 CG CD CE NZ
REMARK 470 ARG A 47 CD NE CZ NH1 NH2
REMARK 470 LYS A 75 NZ
REMARK 470 ARG B 6 CD NE CZ NH1 NH2
REMARK 470 LYS B 7 CD CE NZ
REMARK 470 LYS B 13 NZ
REMARK 470 LYS B 20 CG CD CE NZ
REMARK 470 ARG B 21 CD NE CZ NH1 NH2
REMARK 470 SER B 25 OG
REMARK 470 SER B 29 OG
REMARK 470 GLU B 31 CG CD OE1 OE2
REMARK 470 GLU B 32 CD OE1 OE2
REMARK 470 LYS B 34 CE NZ
REMARK 470 LYS B 35 CE NZ
REMARK 470 ASN B 36 CG OD1 ND2
REMARK 470 LYS B 75 CD CE NZ
REMARK 470 ARG C 6 CD NE CZ NH1 NH2
REMARK 470 LYS C 7 CD CE NZ
REMARK 470 LYS C 13 CE NZ
REMARK 470 ARG C 21 CD NE CZ NH1 NH2
REMARK 470 ARG C 27 CG CD NE CZ NH1 NH2
REMARK 470 SER C 29 OG
REMARK 470 GLU C 31 CG CD OE1 OE2
REMARK 470 GLU C 32 CG CD OE1 OE2
REMARK 470 LYS C 34 CD CE NZ
REMARK 470 LYS C 35 CG CD CE NZ
REMARK 470 ASN C 36 CG OD1 ND2
REMARK 470 LYS C 75 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 OD1 ASN A 53 HD21 ASN C 53 1.58
REMARK 500 HD21 ASN B 53 OD1 ASN C 53 1.60
REMARK 500 OE2 GLU A 11 O HOH A 101 1.97
REMARK 500 OE2 GLU B 58 O HOH B 101 2.00
REMARK 500 OE1 GLU C 68 O HOH C 101 2.01
REMARK 500 O HOH C 130 O HOH C 140 2.03
REMARK 500 O HOH A 136 O HOH A 137 2.03
REMARK 500 O LYS B 13 O HOH B 102 2.07
REMARK 500 O HOH B 106 O HOH B 138 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 HH22 ARG A 72 OXT LYS C 75 4646 1.45
REMARK 500 O HOH A 142 O HOH C 118 4646 1.99
REMARK 500 O HOH A 147 O HOH C 102 4646 2.00
REMARK 500 NH2 ARG A 72 OXT LYS C 75 4646 2.00
REMARK 500 O HOH A 153 O HOH C 143 3545 2.04
REMARK 500 O HOH B 132 O HOH C 157 1545 2.06
REMARK 500 O HOH A 133 O HOH B 113 2655 2.08
REMARK 500 O HOH A 148 O HOH B 138 3555 2.15
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6MSR A 0 75 PDB 6MSR 6MSR 0 75
DBREF 6MSR B 0 75 PDB 6MSR 6MSR 0 75
DBREF 6MSR C 0 75 PDB 6MSR 6MSR 0 75
SEQRES 1 A 76 GLY SER GLU TYR GLU ILE ARG LYS ALA LEU GLU GLU LEU
SEQRES 2 A 76 LYS ALA SER THR ALA GLU LEU LYS ARG ALA THR ALA SER
SEQRES 3 A 76 LEU ARG ALA SER THR GLU GLU LEU LYS LYS ASN PRO SER
SEQRES 4 A 76 GLU ASP ALA LEU VAL GLU ASN ASN ARG LEU ILE VAL GLU
SEQRES 5 A 76 HIS ASN ALA ILE ILE VAL GLU ASN ASN ARG ILE ILE ALA
SEQRES 6 A 76 ALA VAL LEU GLU LEU ILE VAL ARG ALA ILE LYS
SEQRES 1 B 76 GLY SER GLU TYR GLU ILE ARG LYS ALA LEU GLU GLU LEU
SEQRES 2 B 76 LYS ALA SER THR ALA GLU LEU LYS ARG ALA THR ALA SER
SEQRES 3 B 76 LEU ARG ALA SER THR GLU GLU LEU LYS LYS ASN PRO SER
SEQRES 4 B 76 GLU ASP ALA LEU VAL GLU ASN ASN ARG LEU ILE VAL GLU
SEQRES 5 B 76 HIS ASN ALA ILE ILE VAL GLU ASN ASN ARG ILE ILE ALA
SEQRES 6 B 76 ALA VAL LEU GLU LEU ILE VAL ARG ALA ILE LYS
SEQRES 1 C 76 GLY SER GLU TYR GLU ILE ARG LYS ALA LEU GLU GLU LEU
SEQRES 2 C 76 LYS ALA SER THR ALA GLU LEU LYS ARG ALA THR ALA SER
SEQRES 3 C 76 LEU ARG ALA SER THR GLU GLU LEU LYS LYS ASN PRO SER
SEQRES 4 C 76 GLU ASP ALA LEU VAL GLU ASN ASN ARG LEU ILE VAL GLU
SEQRES 5 C 76 HIS ASN ALA ILE ILE VAL GLU ASN ASN ARG ILE ILE ALA
SEQRES 6 C 76 ALA VAL LEU GLU LEU ILE VAL ARG ALA ILE LYS
FORMUL 4 HOH *161(H2 O)
HELIX 1 AA1 SER A 1 ASN A 36 1 36
HELIX 2 AA2 SER A 38 LYS A 75 1 38
HELIX 3 AA3 SER B 1 ASN B 36 1 36
HELIX 4 AA4 SER B 38 LYS B 75 1 38
HELIX 5 AA5 SER C 1 ASN C 36 1 36
HELIX 6 AA6 SER C 38 LYS C 75 1 38
CRYST1 57.618 33.281 114.455 90.00 99.56 90.00 C 1 2 1 12
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 0.017356 0.000000 0.002922 0.00000
SCALE2 0.000000 0.030047 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008860 0.00000
ATOM 1 N GLY A 0 33.676 7.900 51.062 1.00 46.28 N
ANISOU 1 N GLY A 0 6163 4909 6512 1009 712 128 N
ATOM 2 CA GLY A 0 34.030 7.867 52.502 1.00 48.93 C
ANISOU 2 CA GLY A 0 6567 5205 6821 1037 733 174 C
ATOM 3 C GLY A 0 35.344 8.544 52.830 1.00 45.14 C
ANISOU 3 C GLY A 0 6032 4783 6336 1161 747 365 C
ATOM 4 O GLY A 0 35.365 9.699 53.245 1.00 42.44 O
ANISOU 4 O GLY A 0 5692 4372 6062 1099 665 419 O
ATOM 5 H1 GLY A 0 33.349 7.108 50.819 1.00 55.58 H
ATOM 6 H2 GLY A 0 33.063 8.530 50.922 1.00 55.58 H
ATOM 7 H3 GLY A 0 34.403 8.080 50.582 1.00 55.58 H
ATOM 8 HA2 GLY A 0 33.331 8.310 53.008 1.00 58.76 H
ATOM 9 HA3 GLY A 0 34.090 6.942 52.791 1.00 58.76 H
ATOM 10 N SER A 1 36.446 7.823 52.646 1.00 44.74 N
ANISOU 10 N SER A 1 5921 4887 6190 1341 819 490 N
ATOM 11 CA SER A 1 37.717 8.271 53.190 1.00 38.88 C
ANISOU 11 CA SER A 1 5086 4288 5399 1484 796 707 C
ATOM 12 C SER A 1 38.187 9.545 52.497 1.00 32.85 C
ANISOU 12 C SER A 1 4134 3640 4706 1465 697 894 C
ATOM 13 O SER A 1 37.922 9.776 51.313 1.00 31.03 O
ANISOU 13 O SER A 1 3819 3446 4526 1426 703 874 O
ATOM 14 CB SER A 1 38.768 7.168 53.060 1.00 35.52 C
ANISOU 14 CB SER A 1 4601 4077 4817 1682 865 788 C
ATOM 15 OG SER A 1 39.615 7.345 51.940 1.00 33.74 O
ANISOU 15 OG SER A 1 4158 4123 4540 1776 856 926 O
ATOM 16 H SER A 1 36.482 7.080 52.215 1.00 53.73 H
ATOM 17 HA SER A 1 37.614 8.472 54.133 1.00 46.70 H
ATOM 18 HB2 SER A 1 39.314 7.168 53.861 1.00 42.67 H
ATOM 19 HB3 SER A 1 38.311 6.317 52.969 1.00 42.67 H
ATOM 20 HG SER A 1 40.200 6.743 51.924 1.00 40.53 H
ATOM 21 N GLU A 2 38.855 10.400 53.276 1.00 33.61 N
ANISOU 21 N GLU A 2 4170 3824 4774 1393 548 1062 N
ATOM 22 CA GLU A 2 39.510 11.578 52.726 1.00 34.41 C
ANISOU 22 CA GLU A 2 4073 4167 4833 1165 347 1208 C
ATOM 23 C GLU A 2 40.492 11.206 51.629 1.00 30.74 C
ANISOU 23 C GLU A 2 3352 4068 4259 1261 380 1336 C
ATOM 24 O GLU A 2 40.642 11.951 50.653 1.00 31.48 O
ANISOU 24 O GLU A 2 3306 4307 4350 1093 287 1397 O
ATOM 25 CB GLU A 2 40.212 12.325 53.860 1.00 36.17 C
ANISOU 25 CB GLU A 2 4287 4473 4984 1031 163 1341 C
ATOM 26 CG GLU A 2 41.487 13.031 53.472 1.00 40.46 C
ANISOU 26 CG GLU A 2 4565 5405 5404 886 -12 1564 C
ATOM 27 H GLU A 2 38.943 10.320 54.128 1.00 40.37 H
ATOM 28 HA GLU A 2 38.851 12.170 52.332 1.00 41.33 H
ATOM 29 HB2 GLU A 2 39.604 12.995 54.207 1.00 43.45 H
ATOM 30 HB3 GLU A 2 40.435 11.686 54.555 1.00 43.45 H
ATOM 31 N TYR A 3 41.145 10.050 51.749 1.00 29.16 N
ANISOU 31 N TYR A 3 3101 4019 3960 1539 511 1373 N
ATOM 32 CA TYR A 3 42.115 9.653 50.736 1.00 32.27 C
ANISOU 32 CA TYR A 3 3242 4788 4231 1666 550 1490 C
ATOM 33 C TYR A 3 41.432 9.328 49.414 1.00 30.20 C
ANISOU 33 C TYR A 3 2993 4447 4033 1720 666 1382 C
ATOM 34 O TYR A 3 41.870 9.784 48.351 1.00 31.12 O
ANISOU 34 O TYR A 3 2913 4809 4102 1631 619 1470 O
ATOM 35 CB TYR A 3 42.921 8.450 51.217 1.00 35.33 C
ANISOU 35 CB TYR A 3 3631 5319 4473 1931 650 1500 C
ATOM 36 CG TYR A 3 43.832 7.900 50.146 1.00 39.96 C
ANISOU 36 CG TYR A 3 4040 6240 4902 2021 703 1545 C
ATOM 37 CD1 TYR A 3 43.495 6.752 49.438 1.00 43.26 C
ANISOU 37 CD1 TYR A 3 4626 6539 5272 2133 834 1383 C
ATOM 38 CD2 TYR A 3 45.025 8.537 49.833 1.00 42.05 C
ANISOU 38 CD2 TYR A 3 3989 6934 5053 1949 595 1750 C
ATOM 39 CE1 TYR A 3 44.324 6.252 48.459 1.00 46.04 C
ANISOU 39 CE1 TYR A 3 4852 7169 5471 2225 864 1431 C
ATOM 40 CE2 TYR A 3 45.858 8.050 48.849 1.00 44.60 C
ANISOU 40 CE2 TYR A 3 4173 7554 5220 2026 654 1783 C
ATOM 41 CZ TYR A 3 45.502 6.912 48.163 1.00 46.18 C
ANISOU 41 CZ TYR A 3 4560 7608 5377 2186 788 1626 C
ATOM 42 OH TYR A 3 46.336 6.416 47.188 1.00 47.28 O
ANISOU 42 OH TYR A 3 4588 8025 5352 2279 825 1667 O
ATOM 43 H TYR A 3 41.046 9.490 52.394 1.00 35.04 H
ATOM 44 HA TYR A 3 42.725 10.393 50.594 1.00 38.77 H
ATOM 45 HB2 TYR A 3 43.470 8.718 51.971 1.00 42.44 H
ATOM 46 HB3 TYR A 3 42.310 7.746 51.485 1.00 42.44 H
ATOM 47 HD1 TYR A 3 42.697 6.314 49.628 1.00 51.95 H
ATOM 48 HD2 TYR A 3 45.267 9.307 50.297 1.00 50.50 H
ATOM 49 HE1 TYR A 3 44.094 5.477 48.001 1.00 55.29 H
ATOM 50 HE2 TYR A 3 46.654 8.488 48.650 1.00 53.57 H
ATOM 51 HH TYR A 3 46.885 7.006 46.953 1.00 56.78 H
ATOM 52 N AGLU A 4 40.362 8.534 49.456 0.60 30.93 N
ANISOU 52 N AGLU A 4 3364 4196 4191 1746 786 1142 N
ATOM 53 N BGLU A 4 40.363 8.531 49.459 0.40 30.91 N
ANISOU 53 N BGLU A 4 3362 4193 4188 1746 787 1142 N
ATOM 54 CA AGLU A 4 39.694 8.145 48.218 0.60 30.28 C
ANISOU 54 CA AGLU A 4 3346 4023 4136 1710 849 997 C
ATOM 55 CA BGLU A 4 39.678 8.143 48.230 0.40 30.39 C
ANISOU 55 CA BGLU A 4 3364 4032 4152 1709 849 995 C
ATOM 56 C AGLU A 4 39.086 9.351 47.511 0.60 28.03 C
ANISOU 56 C AGLU A 4 2983 3670 4000 1567 778 1021 C
ATOM 57 C BGLU A 4 39.097 9.357 47.515 0.40 28.05 C
ANISOU 57 C BGLU A 4 2982 3674 4000 1567 778 1024 C
ATOM 58 O AGLU A 4 39.083 9.413 46.276 0.60 27.25 O
ANISOU 58 O AGLU A 4 2799 3668 3887 1555 790 1020 O
ATOM 59 O BGLU A 4 39.125 9.430 46.280 0.40 27.43 O
ANISOU 59 O BGLU A 4 2813 3704 3908 1556 788 1029 O
ATOM 60 CB AGLU A 4 38.622 7.096 48.503 0.60 31.93 C
ANISOU 60 CB AGLU A 4 3832 3927 4373 1665 908 755 C
ATOM 61 CB BGLU A 4 38.582 7.125 48.544 0.40 31.87 C
ANISOU 61 CB BGLU A 4 3829 3908 4371 1659 907 751 C
ATOM 62 CG AGLU A 4 39.162 5.761 48.983 0.60 35.80 C
ANISOU 62 CG AGLU A 4 4409 4471 4723 1800 962 742 C
ATOM 63 CG BGLU A 4 39.055 5.683 48.555 0.40 35.30 C
ANISOU 63 CG BGLU A 4 4340 4411 4663 1790 965 721 C
ATOM 64 CD AGLU A 4 40.005 5.046 47.949 0.60 37.44 C
ANISOU 64 CD AGLU A 4 4526 4907 4793 1938 992 803 C
ATOM 65 CD BGLU A 4 38.585 4.918 49.777 0.40 36.66 C
ANISOU 65 CD BGLU A 4 4703 4395 4830 1769 983 624 C
ATOM 66 OE1AGLU A 4 39.737 5.208 46.741 0.60 37.65 O
ANISOU 66 OE1AGLU A 4 4503 4955 4847 1894 989 773 O
ATOM 67 OE1BGLU A 4 37.562 5.306 50.380 0.40 35.52 O
ANISOU 67 OE1BGLU A 4 4657 4043 4796 1613 955 517 O
ATOM 68 OE2AGLU A 4 40.940 4.317 48.348 0.60 39.09 O
ANISOU 68 OE2AGLU A 4 4723 5273 4856 2096 1013 875 O
ATOM 69 OE2BGLU A 4 39.252 3.928 50.141 0.40 39.31 O
ANISOU 69 OE2BGLU A 4 5086 4812 5039 1909 1018 659 O
ATOM 70 H AGLU A 4 40.009 8.213 50.171 0.60 37.16 H
ATOM 71 H BGLU A 4 40.019 8.206 50.177 0.40 37.13 H
ATOM 72 HA AGLU A 4 40.352 7.748 47.625 0.60 36.38 H
ATOM 73 HA BGLU A 4 40.317 7.723 47.633 0.40 36.51 H
ATOM 74 HB2AGLU A 4 38.030 7.438 49.191 0.60 38.36 H
ATOM 75 HB2BGLU A 4 38.218 7.321 49.421 0.40 38.29 H
ATOM 76 HB3AGLU A 4 38.124 6.934 47.686 0.60 38.36 H
ATOM 77 HB3BGLU A 4 37.886 7.201 47.872 0.40 38.29 H
ATOM 78 HG2AGLU A 4 39.715 5.910 49.766 0.60 43.00 H
ATOM 79 HG2BGLU A 4 38.711 5.232 47.768 0.40 42.41 H
ATOM 80 HG3AGLU A 4 38.416 5.184 49.209 0.60 43.00 H
ATOM 81 HG3BGLU A 4 40.025 5.670 48.548 0.40 42.41 H
ATOM 82 N ILE A 5 38.572 10.322 48.271 1.00 27.04 N
ANISOU 82 N ILE A 5 2925 3361 3989 1402 670 1021 N
ATOM 83 CA ILE A 5 38.009 11.519 47.655 1.00 24.67 C
ANISOU 83 CA ILE A 5 2624 2976 3772 1136 527 989 C
ATOM 84 C ILE A 5 39.117 12.358 47.037 1.00 26.97 C
ANISOU 84 C ILE A 5 2679 3630 3938 971 376 1196 C
ATOM 85 O ILE A 5 39.010 12.815 45.892 1.00 28.65 O
ANISOU 85 O ILE A 5 2824 3907 4155 868 335 1203 O
ATOM 86 CB ILE A 5 37.192 12.325 48.682 1.00 25.98 C
ANISOU 86 CB ILE A 5 2972 2855 4044 958 418 897 C
ATOM 87 CG1 ILE A 5 35.921 11.560 49.063 1.00 26.76 C
ANISOU 87 CG1 ILE A 5 3290 2600 4277 1086 579 673 C
ATOM 88 CG2 ILE A 5 36.852 13.693 48.124 1.00 23.99 C
ANISOU 88 CG2 ILE A 5 2717 2563 3836 683 220 898 C
ATOM 89 CD1 ILE A 5 35.113 12.197 50.166 1.00 26.29 C
ANISOU 89 CD1 ILE A 5 3404 2315 4271 923 486 550 C
ATOM 90 H ILE A 5 38.539 10.311 49.130 1.00 32.49 H
ATOM 91 HA ILE A 5 37.403 11.248 46.947 1.00 29.64 H
ATOM 92 HB ILE A 5 37.728 12.445 49.482 1.00 31.22 H
ATOM 93 HG12 ILE A 5 35.351 11.500 48.281 1.00 32.15 H
ATOM 94 HG13 ILE A 5 36.172 10.672 49.360 1.00 32.15 H
ATOM 95 HG21 ILE A 5 36.165 14.098 48.677 1.00 28.83 H
ATOM 96 HG22 ILE A 5 37.650 14.244 48.131 1.00 28.83 H
ATOM 97 HG23 ILE A 5 36.527 13.591 47.216 1.00 28.83 H
ATOM 98 HD11 ILE A 5 34.451 11.561 50.480 1.00 31.59 H
ATOM 99 HD12 ILE A 5 35.708 12.440 50.893 1.00 31.59 H
ATOM 100 HD13 ILE A 5 34.673 12.988 49.819 1.00 31.59 H
ATOM 101 N ARG A 6 40.207 12.561 47.780 1.00 27.26 N
ANISOU 101 N ARG A 6 2586 3915 3856 937 291 1370 N
ATOM 102 CA ARG A 6 41.352 13.286 47.243 1.00 31.01 C
ANISOU 102 CA ARG A 6 2809 4778 4196 770 156 1584 C
ATOM 103 C ARG A 6 41.816 12.671 45.927 1.00 31.97 C
ANISOU 103 C ARG A 6 2751 5161 4235 921 281 1627 C
ATOM 104 O ARG A 6 42.059 13.380 44.945 1.00 32.53 O
ANISOU 104 O ARG A 6 2702 5397 4263 741 199 1708 O
ATOM 105 CB ARG A 6 42.489 13.289 48.266 1.00 36.68 C
ANISOU 105 CB ARG A 6 3397 5745 4794 778 81 1752 C
ATOM 106 CG ARG A 6 43.736 14.023 47.818 1.00 42.32 C
ANISOU 106 CG ARG A 6 3826 6894 5360 586 -62 1986 C
ATOM 107 CD ARG A 6 44.930 13.687 48.709 1.00 44.63 C
ANISOU 107 CD ARG A 6 3950 7484 5524 680 -90 2140 C
ATOM 108 H ARG A 6 40.307 12.291 48.591 1.00 32.75 H
ATOM 109 HA ARG A 6 41.095 14.206 47.075 1.00 37.26 H
ATOM 110 HB2 ARG A 6 42.173 13.716 49.077 1.00 44.06 H
ATOM 111 HB3 ARG A 6 42.740 12.371 48.451 1.00 44.06 H
ATOM 112 HG2 ARG A 6 43.952 13.765 46.909 1.00 50.83 H
ATOM 113 HG3 ARG A 6 43.581 14.979 47.864 1.00 50.83 H
ATOM 114 N LYS A 7 41.942 11.342 45.892 1.00 31.38 N
ANISOU 114 N LYS A 7 2676 5120 4125 1256 476 1573 N
ATOM 115 CA LYS A 7 42.407 10.669 44.683 1.00 35.20 C
ANISOU 115 CA LYS A 7 3006 5856 4513 1444 601 1608 C
ATOM 116 C LYS A 7 41.415 10.831 43.538 1.00 28.74 C
ANISOU 116 C LYS A 7 2300 4823 3798 1388 636 1475 C
ATOM 117 O LYS A 7 41.817 11.012 42.381 1.00 30.56 O
ANISOU 117 O LYS A 7 2380 5284 3949 1360 641 1549 O
ATOM 118 CB LYS A 7 42.654 9.187 44.968 1.00 41.17 C
ANISOU 118 CB LYS A 7 3917 6561 5167 1711 751 1492 C
ATOM 119 CG LYS A 7 43.985 8.902 45.647 1.00 49.67 C
ANISOU 119 CG LYS A 7 4844 7959 6068 1788 725 1633 C
ATOM 120 CD LYS A 7 45.143 9.119 44.684 1.00 55.13 C
ANISOU 120 CD LYS A 7 5283 9081 6583 1750 698 1785 C
ATOM 121 CE LYS A 7 46.452 9.344 45.430 1.00 58.22 C
ANISOU 121 CE LYS A 7 5466 9826 6829 1721 619 1959 C
ATOM 122 NZ LYS A 7 46.596 10.761 45.880 1.00 58.89 N
ANISOU 122 NZ LYS A 7 5373 10027 6976 1412 435 2122 N
ATOM 123 H LYS A 7 41.767 10.812 46.546 1.00 37.69 H
ATOM 124 HA LYS A 7 43.248 11.070 44.411 1.00 42.29 H
ATOM 125 HB2 LYS A 7 41.950 8.861 45.550 1.00 49.45 H
ATOM 126 HB3 LYS A 7 42.641 8.702 44.128 1.00 49.45 H
ATOM 127 HG2 LYS A 7 44.097 9.500 46.403 1.00 59.64 H
ATOM 128 HG3 LYS A 7 44.004 7.980 45.948 1.00 59.64 H
ATOM 129 HD2 LYS A 7 45.243 8.336 44.120 1.00 66.20 H
ATOM 130 HD3 LYS A 7 44.965 9.900 44.138 1.00 66.20 H
ATOM 131 HE2 LYS A 7 46.477 8.772 46.214 1.00 69.91 H
ATOM 132 HE3 LYS A 7 47.196 9.135 44.843 1.00 69.91 H
ATOM 133 HZ1 LYS A 7 47.336 10.853 46.365 1.00 70.71 H
ATOM 134 HZ2 LYS A 7 46.644 11.301 45.174 1.00 70.71 H
ATOM 135 HZ3 LYS A 7 45.895 10.995 46.376 1.00 70.71 H
ATOM 136 N ALA A 8 40.114 10.759 43.836 1.00 29.63 N
ANISOU 136 N ALA A 8 2672 4505 4082 1373 663 1276 N
ATOM 137 CA ALA A 8 39.109 10.891 42.787 1.00 29.88 C
ANISOU 137 CA ALA A 8 2815 4316 4221 1329 686 1133 C
ATOM 138 C ALA A 8 39.094 12.302 42.220 1.00 28.66 C
ANISOU 138 C ALA A 8 2605 4212 4073 1002 494 1200 C
ATOM 139 O ALA A 8 38.881 12.492 41.017 1.00 30.15 O
ANISOU 139 O ALA A 8 2773 4423 4259 965 494 1178 O
ATOM 140 CB ALA A 8 37.730 10.520 43.331 1.00 28.03 C
ANISOU 140 CB ALA A 8 2849 3636 4167 1374 751 905 C
ATOM 141 H ALA A 8 39.793 10.637 44.625 1.00 35.60 H
ATOM 142 HA ALA A 8 39.323 10.276 42.068 1.00 35.89 H
ATOM 143 HB1 ALA A 8 37.085 10.559 42.608 1.00 33.68 H
ATOM 144 HB2 ALA A 8 37.765 9.621 43.694 1.00 33.68 H
ATOM 145 HB3 ALA A 8 37.485 11.149 44.027 1.00 33.68 H
ATOM 146 N LEU A 9 39.309 13.305 43.073 1.00 26.48 N
ANISOU 146 N LEU A 9 2327 3938 3796 761 318 1281 N
ATOM 147 CA LEU A 9 39.359 14.680 42.594 1.00 29.15 C
ANISOU 147 CA LEU A 9 2641 4317 4116 435 110 1358 C
ATOM 148 C LEU A 9 40.593 14.933 41.738 1.00 33.40 C
ANISOU 148 C LEU A 9 2918 5297 4475 355 79 1576 C
ATOM 149 O LEU A 9 40.535 15.729 40.793 1.00 35.00 O
ANISOU 149 O LEU A 9 3108 5541 4650 154 -24 1614 O
ATOM 150 CB LEU A 9 39.330 15.648 43.774 1.00 30.90 C
ANISOU 150 CB LEU A 9 2950 4429 4363 211 -82 1396 C
ATOM 151 CG LEU A 9 37.976 15.828 44.457 1.00 32.10 C
ANISOU 151 CG LEU A 9 3370 4138 4688 203 -104 1177 C
ATOM 152 CD1 LEU A 9 38.102 16.804 45.617 1.00 34.51 C
ANISOU 152 CD1 LEU A 9 3755 4374 4983 -4 -303 1237 C
ATOM 153 CD2 LEU A 9 36.930 16.308 43.464 1.00 29.26 C
ANISOU 153 CD2 LEU A 9 3138 3550 4430 120 -151 1024 C
ATOM 154 H LEU A 9 39.427 13.217 43.920 1.00 31.82 H
ATOM 155 HA LEU A 9 38.575 14.847 42.048 1.00 35.02 H
ATOM 156 HB2 LEU A 9 39.951 15.325 44.446 1.00 37.13 H
ATOM 157 HB3 LEU A 9 39.610 16.521 43.456 1.00 37.13 H
ATOM 158 HG LEU A 9 37.679 14.973 44.807 1.00 38.56 H
ATOM 159 HD11 LEU A 9 37.243 16.879 46.062 1.00 41.45 H
ATOM 160 HD12 LEU A 9 38.768 16.472 46.239 1.00 41.45 H
ATOM 161 HD13 LEU A 9 38.373 17.670 45.274 1.00 41.45 H
ATOM 162 HD21 LEU A 9 36.238 16.792 43.942 1.00 35.16 H
ATOM 163 HD22 LEU A 9 37.354 16.892 42.816 1.00 35.16 H
ATOM 164 HD23 LEU A 9 36.545 15.539 43.014 1.00 35.16 H
ATOM 165 N GLU A 10 41.715 14.280 42.057 1.00 33.14 N
ANISOU 165 N GLU A 10 2676 5606 4309 508 163 1719 N
ATOM 166 CA GLU A 10 42.889 14.356 41.193 1.00 34.56 C
ANISOU 166 CA GLU A 10 2574 6248 4308 476 173 1916 C
ATOM 167 C GLU A 10 42.621 13.688 39.852 1.00 35.54 C
ANISOU 167 C GLU A 10 2687 6400 4417 666 330 1841 C
ATOM 168 O GLU A 10 43.038 14.197 38.805 1.00 37.90 O
ANISOU 168 O GLU A 10 2859 6925 4618 526 291 1945 O
ATOM 169 CB GLU A 10 44.093 13.721 41.889 1.00 39.96 C
ANISOU 169 CB GLU A 10 3034 7291 4858 643 233 2062 C
ATOM 170 CG GLU A 10 44.832 14.684 42.805 1.00 49.94 C
ANISOU 170 CG GLU A 10 4195 8717 6062 363 31 2234 C
ATOM 171 CD GLU A 10 45.343 14.029 44.070 1.00 59.99 C
ANISOU 171 CD GLU A 10 5432 10053 7309 551 66 2260 C
ATOM 172 OE1 GLU A 10 46.516 14.256 44.433 1.00 64.72 O
ANISOU 172 OE1 GLU A 10 5811 11013 7768 472 -7 2441 O
ATOM 173 OE2 GLU A 10 44.564 13.293 44.706 1.00 62.62 O
ANISOU 173 OE2 GLU A 10 5983 10058 7754 764 167 2088 O
ATOM 174 H GLU A 10 41.820 13.792 42.757 1.00 39.81 H
ATOM 175 HA GLU A 10 43.103 15.287 41.027 1.00 41.51 H
ATOM 176 HB2 GLU A 10 43.786 12.974 42.427 1.00 47.99 H
ATOM 177 HB3 GLU A 10 44.717 13.410 41.216 1.00 47.99 H
ATOM 178 HG2 GLU A 10 45.594 15.049 42.329 1.00 59.97 H
ATOM 179 HG3 GLU A 10 44.229 15.399 43.062 1.00 59.97 H
ATOM 180 N GLU A 11 41.920 12.551 39.859 1.00 33.30 N
ANISOU 180 N GLU A 11 2551 5881 4220 977 502 1663 N
ATOM 181 CA GLU A 11 41.484 11.947 38.603 1.00 33.84 C
ANISOU 181 CA GLU A 11 2666 5900 4293 1150 632 1565 C
ATOM 182 C GLU A 11 40.661 12.934 37.788 1.00 32.69 C
ANISOU 182 C GLU A 11 2648 5538 4236 892 509 1494 C
ATOM 183 O GLU A 11 40.880 13.104 36.582 1.00 33.65 O
ANISOU 183 O GLU A 11 2693 5817 4276 861 522 1543 O
ATOM 184 CB GLU A 11 40.653 10.698 38.875 1.00 40.19 C
ANISOU 184 CB GLU A 11 3707 6372 5193 1435 783 1348 C
ATOM 185 CG GLU A 11 41.407 9.408 39.027 1.00 48.23 C
ANISOU 185 CG GLU A 11 4798 7487 6041 1630 869 1315 C
ATOM 186 CD GLU A 11 40.461 8.254 39.295 1.00 54.70 C
ANISOU 186 CD GLU A 11 5930 7914 6938 1736 932 1074 C
ATOM 187 OE1 GLU A 11 39.718 7.852 38.372 1.00 57.52 O
ANISOU 187 OE1 GLU A 11 6431 8083 7341 1743 955 933 O
ATOM 188 OE2 GLU A 11 40.434 7.771 40.443 1.00 61.05 O
ANISOU 188 OE2 GLU A 11 6831 8609 7756 1773 941 1031 O
ATOM 189 H GLU A 11 41.689 12.116 40.564 1.00 40.00 H
ATOM 190 HA GLU A 11 42.272 11.692 38.097 1.00 40.66 H
ATOM 191 HB2 GLU A 11 40.161 10.838 39.699 1.00 48.28 H
ATOM 192 HB3 GLU A 11 40.036 10.580 38.136 1.00 48.28 H
ATOM 193 HG2 GLU A 11 41.896 9.222 38.210 1.00 57.93 H
ATOM 194 HG3 GLU A 11 42.023 9.480 39.773 1.00 57.93 H
ATOM 195 N LEU A 12 39.681 13.572 38.434 1.00 30.25 N
ANISOU 195 N LEU A 12 2545 4861 4086 723 391 1368 N
ATOM 196 CA LEU A 12 38.809 14.507 37.733 1.00 28.87 C
ANISOU 196 CA LEU A 12 2521 4447 4000 503 257 1275 C
ATOM 197 C LEU A 12 39.607 15.629 37.092 1.00 32.97 C
ANISOU 197 C LEU A 12 2905 5245 4378 209 98 1470 C
ATOM 198 O LEU A 12 39.313 16.044 35.966 1.00 32.08 O
ANISOU 198 O LEU A 12 2840 5098 4251 116 56 1446 O
ATOM 199 CB LEU A 12 37.778 15.077 38.704 1.00 27.73 C
ANISOU 199 CB LEU A 12 2594 3920 4024 376 139 1126 C
ATOM 200 CG LEU A 12 36.718 16.003 38.110 1.00 27.82 C
ANISOU 200 CG LEU A 12 2793 3634 4141 190 -10 988 C
ATOM 201 CD1 LEU A 12 35.904 15.281 37.060 1.00 29.13 C
ANISOU 201 CD1 LEU A 12 3048 3631 4390 378 119 818 C
ATOM 202 CD2 LEU A 12 35.835 16.535 39.230 1.00 27.73 C
ANISOU 202 CD2 LEU A 12 2967 3299 4269 95 -120 854 C
ATOM 203 H LEU A 12 39.502 13.481 39.270 1.00 36.34 H
ATOM 204 HA LEU A 12 38.338 14.032 37.030 1.00 34.69 H
ATOM 205 HB2 LEU A 12 37.309 14.334 39.114 1.00 33.32 H
ATOM 206 HB3 LEU A 12 38.252 15.585 39.381 1.00 33.32 H
ATOM 207 HG LEU A 12 37.141 16.756 37.669 1.00 33.42 H
ATOM 208 HD11 LEU A 12 35.115 15.807 36.855 1.00 35.00 H
ATOM 209 HD12 LEU A 12 36.444 15.172 36.262 1.00 35.00 H
ATOM 210 HD13 LEU A 12 35.643 14.413 37.404 1.00 35.00 H
ATOM 211 HD21 LEU A 12 35.145 17.100 38.848 1.00 33.32 H
ATOM 212 HD22 LEU A 12 35.429 15.786 39.695 1.00 33.32 H
ATOM 213 HD23 LEU A 12 36.381 17.049 39.845 1.00 33.32 H
ATOM 214 N LYS A 13 40.627 16.132 37.790 1.00 37.80 N
ANISOU 214 N LYS A 13 3353 6134 4876 48 3 1667 N
ATOM 215 CA LYS A 13 41.465 17.175 37.209 1.00 44.30 C
ANISOU 215 CA LYS A 13 4035 7252 5546 -260 -148 1874 C
ATOM 216 C LYS A 13 42.180 16.672 35.961 1.00 42.01 C
ANISOU 216 C LYS A 13 3543 7313 5105 -146 -7 1975 C
ATOM 217 O LYS A 13 42.254 17.383 34.952 1.00 40.56 O
ANISOU 217 O LYS A 13 3359 7206 4847 -349 -88 2039 O
ATOM 218 CB LYS A 13 42.468 17.672 38.249 1.00 52.03 C
ANISOU 218 CB LYS A 13 4858 8481 6429 -436 -266 2069 C
ATOM 219 CG LYS A 13 42.180 19.069 38.781 1.00 57.51 C
ANISOU 219 CG LYS A 13 5715 8983 7154 -806 -542 2099 C
ATOM 220 CD LYS A 13 42.156 19.088 40.307 1.00 61.17 C
ANISOU 220 CD LYS A 13 6241 9318 7682 -794 -607 2083 C
ATOM 221 CE LYS A 13 42.481 20.473 40.857 1.00 65.28 C
ANISOU 221 CE LYS A 13 6822 9839 8143 -1181 -894 2218 C
ATOM 222 NZ LYS A 13 41.586 21.534 40.318 1.00 66.70 N
ANISOU 222 NZ LYS A 13 7260 9708 8376 -1411 -1082 2123 N
ATOM 223 H LYS A 13 40.850 15.893 38.585 1.00 45.41 H
ATOM 224 HA LYS A 13 40.907 17.925 36.950 1.00 53.21 H
ATOM 225 HB2 LYS A 13 42.460 17.063 39.004 1.00 62.48 H
ATOM 226 HB3 LYS A 13 43.350 17.688 37.846 1.00 62.48 H
ATOM 227 HG2 LYS A 13 42.872 19.678 38.478 1.00 69.06 H
ATOM 228 HG3 LYS A 13 41.314 19.364 38.458 1.00 69.06 H
ATOM 229 HD2 LYS A 13 41.271 18.837 40.617 1.00 73.45 H
ATOM 230 HD3 LYS A 13 42.816 18.463 40.647 1.00 73.45 H
ATOM 231 HE2 LYS A 13 42.383 20.461 41.822 1.00 78.38 H
ATOM 232 HE3 LYS A 13 43.393 20.701 40.618 1.00 78.38 H
ATOM 233 HZ1 LYS A 13 41.821 22.327 40.648 1.00 80.09 H
ATOM 234 HZ2 LYS A 13 41.646 21.561 39.431 1.00 80.09 H
ATOM 235 HZ3 LYS A 13 40.742 21.365 40.546 1.00 80.09 H
ATOM 236 N ALA A 14 42.710 15.447 36.005 1.00 38.20 N
ANISOU 236 N ALA A 14 2904 7045 4564 189 201 1988 N
ATOM 237 CA ALA A 14 43.373 14.889 34.830 1.00 37.61 C
ANISOU 237 CA ALA A 14 2644 7310 4336 347 348 2070 C
ATOM 238 C ALA A 14 42.410 14.788 33.653 1.00 39.17 C
ANISOU 238 C ALA A 14 3037 7241 4606 407 391 1911 C
ATOM 239 O ALA A 14 42.764 15.131 32.519 1.00 41.32 O
ANISOU 239 O ALA A 14 3228 7715 4755 311 390 2000 O
ATOM 240 CB ALA A 14 43.962 13.518 35.161 1.00 36.30 C
ANISOU 240 CB ALA A 14 2353 7339 4100 744 548 2065 C
ATOM 241 H ALA A 14 42.700 14.928 36.690 1.00 45.88 H
ATOM 242 HA ALA A 14 44.103 15.474 34.573 1.00 45.18 H
ATOM 243 HB1 ALA A 14 44.389 13.158 34.367 1.00 43.60 H
ATOM 244 HB2 ALA A 14 44.615 13.618 35.871 1.00 43.60 H
ATOM 245 HB3 ALA A 14 43.248 12.928 35.448 1.00 43.60 H
ATOM 246 N SER A 15 41.186 14.315 33.902 1.00 41.47 N
ANISOU 246 N SER A 15 3585 7083 5090 560 427 1676 N
ATOM 247 CA SER A 15 40.182 14.254 32.845 1.00 39.05 C
ANISOU 247 CA SER A 15 3476 6492 4870 606 445 1509 C
ATOM 248 C SER A 15 39.809 15.647 32.356 1.00 38.92 C
ANISOU 248 C SER A 15 3569 6350 4869 240 229 1526 C
ATOM 249 O SER A 15 39.709 15.880 31.145 1.00 39.57 O
ANISOU 249 O SER A 15 3685 6459 4892 195 222 1527 O
ATOM 250 CB SER A 15 38.946 13.516 33.352 1.00 35.13 C
ANISOU 250 CB SER A 15 3214 5552 4582 810 513 1259 C
ATOM 251 OG SER A 15 37.867 13.635 32.444 1.00 32.78 O
ANISOU 251 OG SER A 15 3118 4944 4392 805 486 1085 O
ATOM 252 H SER A 15 40.914 14.027 34.666 1.00 49.81 H
ATOM 253 HA SER A 15 40.545 13.761 32.093 1.00 46.91 H
ATOM 254 HB2 SER A 15 39.163 12.577 33.460 1.00 42.20 H
ATOM 255 HB3 SER A 15 38.681 13.895 34.205 1.00 42.20 H
ATOM 256 HG SER A 15 38.064 13.270 31.714 1.00 39.37 H
ATOM 257 N THR A 16 39.580 16.578 33.285 1.00 40.31 N
ANISOU 257 N THR A 16 3828 6373 5115 -14 44 1534 N
ATOM 258 CA THR A 16 39.346 17.970 32.920 1.00 40.45 C
ANISOU 258 CA THR A 16 3965 6289 5117 -374 -191 1571 C
ATOM 259 C THR A 16 40.458 18.513 32.033 1.00 45.49 C
ANISOU 259 C THR A 16 4414 7337 5531 -575 -227 1808 C
ATOM 260 O THR A 16 40.187 19.304 31.122 1.00 44.98 O
ANISOU 260 O THR A 16 4469 7195 5427 -778 -349 1811 O
ATOM 261 CB THR A 16 39.204 18.806 34.190 1.00 39.01 C
ANISOU 261 CB THR A 16 3867 5957 4999 -591 -380 1583 C
ATOM 262 OG1 THR A 16 38.002 18.413 34.868 1.00 37.98 O
ANISOU 262 OG1 THR A 16 3938 5416 5076 -426 -352 1340 O
ATOM 263 CG2 THR A 16 39.147 20.290 33.874 1.00 40.72 C
ANISOU 263 CG2 THR A 16 4210 6103 5157 -976 -649 1654 C
ATOM 264 H THR A 16 39.555 16.430 34.131 1.00 48.42 H
ATOM 265 HA THR A 16 38.519 18.039 32.418 1.00 48.59 H
ATOM 266 HB THR A 16 39.974 18.662 34.762 1.00 46.86 H
ATOM 267 HG1 THR A 16 38.025 17.590 35.038 1.00 45.62 H
ATOM 268 HG21 THR A 16 38.745 20.772 34.613 1.00 48.90 H
ATOM 269 HG22 THR A 16 40.043 20.632 33.724 1.00 48.90 H
ATOM 270 HG23 THR A 16 38.616 20.439 33.075 1.00 48.90 H
ATOM 271 N ALA A 17 41.701 18.073 32.254 1.00 40.88 N
ANISOU 271 N ALA A 17 3537 7202 4795 -515 -119 2004 N
ATOM 272 CA ALA A 17 42.817 18.548 31.441 1.00 42.08 C
ANISOU 272 CA ALA A 17 3470 7799 4722 -711 -134 2241 C
ATOM 273 C ALA A 17 42.732 18.022 30.015 1.00 43.03 C
ANISOU 273 C ALA A 17 3582 7998 4768 -539 14 2202 C
ATOM 274 O ALA A 17 42.962 18.773 29.062 1.00 48.29 O
ANISOU 274 O ALA A 17 4254 8780 5312 -777 -66 2302 O
ATOM 275 CB ALA A 17 44.140 18.137 32.080 1.00 43.30 C
ANISOU 275 CB ALA A 17 3287 8430 4735 -657 -47 2443 C
ATOM 276 H ALA A 17 41.922 17.506 32.861 1.00 49.10 H
ATOM 277 HA ALA A 17 42.783 19.517 31.407 1.00 50.54 H
ATOM 278 HB1 ALA A 17 44.870 18.486 31.545 1.00 52.00 H
ATOM 279 HB2 ALA A 17 44.184 18.502 32.978 1.00 52.00 H
ATOM 280 HB3 ALA A 17 44.187 17.169 32.114 1.00 52.00 H
ATOM 281 N GLU A 18 42.417 16.737 29.842 1.00 44.84 N
ANISOU 281 N GLU A 18 3816 8164 5059 -131 225 2063 N
ATOM 282 CA GLU A 18 42.173 16.221 28.499 1.00 48.38 C
ANISOU 282 CA GLU A 18 4314 8614 5456 53 351 1996 C
ATOM 283 C GLU A 18 41.060 17.008 27.815 1.00 44.82 C
ANISOU 283 C GLU A 18 4162 7755 5111 -131 196 1853 C
ATOM 284 O GLU A 18 41.176 17.390 26.644 1.00 45.38 O
ANISOU 284 O GLU A 18 4258 7917 5068 -234 178 1905 O
ATOM 285 CB GLU A 18 41.804 14.740 28.555 1.00 53.37 C
ANISOU 285 CB GLU A 18 4979 9136 6164 513 564 1835 C
ATOM 286 CG GLU A 18 42.915 13.789 28.936 1.00 60.23 C
ANISOU 286 CG GLU A 18 5571 10423 6891 778 738 1958 C
ATOM 287 CD GLU A 18 42.503 12.343 28.722 1.00 62.34 C
ANISOU 287 CD GLU A 18 5933 10550 7203 1232 931 1792 C
ATOM 288 OE1 GLU A 18 42.122 11.991 27.585 1.00 61.60 O
ANISOU 288 OE1 GLU A 18 5941 10380 7083 1373 1005 1713 O
ATOM 289 OE2 GLU A 18 42.541 11.562 29.694 1.00 63.39 O
ANISOU 289 OE2 GLU A 18 6154 10545 7387 1399 949 1705 O
ATOM 290 H GLU A 18 42.341 16.155 30.471 1.00 53.86 H
ATOM 291 HA GLU A 18 42.988 16.311 27.980 1.00 58.10 H
ATOM 292 HB2 GLU A 18 41.097 14.629 29.210 1.00 64.09 H
ATOM 293 HB3 GLU A 18 41.488 14.473 27.678 1.00 64.09 H
ATOM 294 HG2 GLU A 18 43.694 13.969 28.387 1.00 72.32 H
ATOM 295 HG3 GLU A 18 43.134 13.909 29.873 1.00 72.32 H
ATOM 296 N LEU A 19 39.963 17.247 28.539 1.00 41.06 N
ANISOU 296 N LEU A 19 3920 6832 4848 -163 82 1665 N
ATOM 297 CA LEU A 19 38.835 17.977 27.978 1.00 42.29 C
ANISOU 297 CA LEU A 19 4366 6585 5117 -308 -79 1504 C
ATOM 298 C LEU A 19 39.276 19.320 27.415 1.00 47.88 C
ANISOU 298 C LEU A 19 5097 7417 5677 -703 -278 1665 C
ATOM 299 O LEU A 19 38.835 19.723 26.333 1.00 43.33 O
ANISOU 299 O LEU A 19 4681 6709 5074 -777 -344 1611 O
ATOM 300 CB LEU A 19 37.766 18.161 29.052 1.00 38.46 C
ANISOU 300 CB LEU A 19 4076 5680 4857 -315 -185 1310 C
ATOM 301 CG LEU A 19 36.369 18.565 28.592 1.00 36.69 C
ANISOU 301 CG LEU A 19 4151 4995 4796 -338 -310 1071 C
ATOM 302 CD1 LEU A 19 35.936 17.814 27.357 1.00 36.87 C
ANISOU 302 CD1 LEU A 19 4237 4943 4827 -109 -180 957 C
ATOM 303 CD2 LEU A 19 35.378 18.324 29.738 1.00 34.30 C
ANISOU 303 CD2 LEU A 19 3972 4347 4713 -237 -326 869 C
ATOM 304 H LEU A 19 39.849 16.997 29.354 1.00 49.31 H
ATOM 305 HA LEU A 19 38.447 17.467 27.250 1.00 50.79 H
ATOM 306 HB2 LEU A 19 37.674 17.320 29.526 1.00 46.20 H
ATOM 307 HB3 LEU A 19 38.073 18.852 29.661 1.00 46.20 H
ATOM 308 HG LEU A 19 36.377 19.506 28.354 1.00 44.08 H
ATOM 309 HD11 LEU A 19 34.987 17.957 27.216 1.00 44.28 H
ATOM 310 HD12 LEU A 19 36.437 18.144 26.594 1.00 44.28 H
ATOM 311 HD13 LEU A 19 36.112 16.868 27.484 1.00 44.28 H
ATOM 312 HD21 LEU A 19 34.484 18.547 29.435 1.00 41.20 H
ATOM 313 HD22 LEU A 19 35.415 17.390 29.997 1.00 41.20 H
ATOM 314 HD23 LEU A 19 35.622 18.885 30.491 1.00 41.20 H
ATOM 315 N LYS A 20 40.164 20.019 28.124 1.00 61.41 N
ANISOU 315 N LYS A 20 6663 9384 7284 -967 -384 1870 N
ATOM 316 CA LYS A 20 40.674 21.289 27.619 1.00 65.77 C
ANISOU 316 CA LYS A 20 7240 10077 7673 -1374 -579 2048 C
ATOM 317 C LYS A 20 41.459 21.088 26.328 1.00 66.34 C
ANISOU 317 C LYS A 20 7152 10519 7534 -1373 -451 2198 C
ATOM 318 O LYS A 20 41.210 21.763 25.322 1.00 68.09 O
ANISOU 318 O LYS A 20 7537 10651 7682 -1555 -555 2203 O
ATOM 319 CB LYS A 20 41.545 21.960 28.681 1.00 67.41 C
ANISOU 319 CB LYS A 20 7300 10512 7801 -1647 -706 2249 C
ATOM 320 H LYS A 20 40.482 19.784 28.888 1.00 73.73 H
ATOM 321 HA LYS A 20 39.925 21.876 27.428 1.00 78.97 H
ATOM 322 N ARG A 21 42.420 20.160 26.338 1.00 60.97 N
ANISOU 322 N ARG A 21 6158 10263 6744 -1159 -226 2320 N
ATOM 323 CA ARG A 21 43.194 19.891 25.132 1.00 63.72 C
ANISOU 323 CA ARG A 21 6332 10998 6880 -1118 -80 2459 C
ATOM 324 C ARG A 21 42.296 19.455 23.983 1.00 63.33 C
ANISOU 324 C ARG A 21 6506 10669 6886 -904 -10 2269 C
ATOM 325 O ARG A 21 42.610 19.717 22.817 1.00 66.54 O
ANISOU 325 O ARG A 21 6908 11245 7127 -995 13 2357 O
ATOM 326 CB ARG A 21 44.251 18.823 25.413 1.00 63.21 C
ANISOU 326 CB ARG A 21 5908 11404 6706 -838 157 2575 C
ATOM 327 H ARG A 21 42.640 19.682 27.019 1.00 73.20 H
ATOM 328 HA ARG A 21 43.653 20.703 24.867 1.00 76.51 H
ATOM 329 N ALA A 22 41.176 18.796 24.289 1.00 55.28 N
ANISOU 329 N ALA A 22 5686 9226 6093 -629 23 2012 N
ATOM 330 CA ALA A 22 40.260 18.359 23.244 1.00 53.95 C
ANISOU 330 CA ALA A 22 5739 8766 5994 -424 74 1819 C
ATOM 331 C ALA A 22 39.380 19.501 22.755 1.00 49.52 C
ANISOU 331 C ALA A 22 5487 7835 5493 -704 -170 1725 C
ATOM 332 O ALA A 22 39.154 19.638 21.548 1.00 50.38 O
ANISOU 332 O ALA A 22 5724 7892 5527 -709 -176 1697 O
ATOM 333 CB ALA A 22 39.394 17.206 23.750 1.00 54.42 C
ANISOU 333 CB ALA A 22 5890 8522 6265 -43 195 1584 C
ATOM 334 H ALA A 22 40.927 18.592 25.087 1.00 66.38 H
ATOM 335 HA ALA A 22 40.781 18.036 22.492 1.00 64.79 H
ATOM 336 HB1 ALA A 22 38.762 16.957 23.057 1.00 65.35 H
ATOM 337 HB2 ALA A 22 39.966 16.451 23.962 1.00 65.35 H
ATOM 338 HB3 ALA A 22 38.918 17.493 24.544 1.00 65.35 H
ATOM 339 N THR A 23 38.874 20.329 23.672 1.00 46.85 N
ANISOU 339 N THR A 23 5286 7234 5280 -924 -379 1670 N
ATOM 340 CA THR A 23 38.019 21.440 23.267 1.00 46.08 C
ANISOU 340 CA THR A 23 5502 6773 5232 -1169 -633 1568 C
ATOM 341 C THR A 23 38.777 22.417 22.377 1.00 51.94 C
ANISOU 341 C THR A 23 6248 7757 5731 -1511 -744 1783 C
ATOM 342 O THR A 23 38.253 22.864 21.350 1.00 53.42 O
ANISOU 342 O THR A 23 6665 7748 5885 -1583 -841 1710 O
ATOM 343 CB THR A 23 37.460 22.155 24.497 1.00 42.51 C
ANISOU 343 CB THR A 23 5181 6041 4929 -1329 -838 1487 C
ATOM 344 OG1 THR A 23 36.701 21.230 25.286 1.00 37.32 O
ANISOU 344 OG1 THR A 23 4531 5156 4493 -1019 -723 1282 O
ATOM 345 CG2 THR A 23 36.578 23.323 24.080 1.00 42.45 C
ANISOU 345 CG2 THR A 23 5514 5659 4957 -1559 -1118 1371 C
ATOM 346 H THR A 23 39.007 20.271 24.520 1.00 56.26 H
ATOM 347 HA THR A 23 37.269 21.089 22.761 1.00 55.34 H
ATOM 348 HB THR A 23 38.191 22.504 25.032 1.00 51.05 H
ATOM 349 HG1 THR A 23 36.222 21.647 25.836 1.00 44.83 H
ATOM 350 HG21 THR A 23 36.064 23.638 24.840 1.00 50.99 H
ATOM 351 HG22 THR A 23 37.127 24.050 23.748 1.00 50.99 H
ATOM 352 HG23 THR A 23 35.968 23.044 23.380 1.00 50.99 H
ATOM 353 N ALA A 24 40.015 22.754 22.748 1.00 51.01 N
ANISOU 353 N ALA A 24 5879 8070 5434 -1734 -732 2051 N
ATOM 354 CA ALA A 24 40.823 23.643 21.920 1.00 54.39 C
ANISOU 354 CA ALA A 24 6282 8775 5610 -2087 -820 2279 C
ATOM 355 C ALA A 24 41.057 23.042 20.540 1.00 58.34 C
ANISOU 355 C ALA A 24 6729 9463 5974 -1913 -630 2301 C
ATOM 356 O ALA A 24 40.831 23.698 19.517 1.00 58.00 O
ANISOU 356 O ALA A 24 6894 9314 5829 -2091 -738 2308 O
ATOM 357 CB ALA A 24 42.155 23.935 22.613 1.00 57.00 C
ANISOU 357 CB ALA A 24 6296 9583 5778 -2324 -809 2563 C
ATOM 358 H ALA A 24 40.405 22.485 23.466 1.00 61.26 H
ATOM 359 HA ALA A 24 40.351 24.483 21.807 1.00 65.32 H
ATOM 360 HB1 ALA A 24 42.673 24.540 22.060 1.00 68.44 H
ATOM 361 HB2 ALA A 24 41.979 24.343 23.475 1.00 68.44 H
ATOM 362 HB3 ALA A 24 42.637 23.102 22.734 1.00 68.44 H
ATOM 363 N SER A 25 41.508 21.785 20.492 1.00 62.40 N
ANISOU 363 N SER A 25 6986 10250 6475 -1551 -351 2307 N
ATOM 364 CA SER A 25 41.783 21.147 19.209 1.00 65.53 C
ANISOU 364 CA SER A 25 7325 10848 6727 -1350 -159 2330 C
ATOM 365 C SER A 25 40.520 21.041 18.364 1.00 62.20 C
ANISOU 365 C SER A 25 7256 9943 6433 -1194 -216 2078 C
ATOM 366 O SER A 25 40.569 21.200 17.139 1.00 62.45 O
ANISOU 366 O SER A 25 7386 10020 6321 -1228 -198 2109 O
ATOM 367 CB SER A 25 42.400 19.768 19.437 1.00 68.71 C
ANISOU 367 CB SER A 25 7423 11579 7105 -943 130 2351 C
ATOM 368 OG SER A 25 43.603 19.871 20.180 1.00 74.58 O
ANISOU 368 OG SER A 25 7825 12794 7719 -1078 177 2583 O
ATOM 369 H SER A 25 41.660 21.288 21.177 1.00 74.93 H
ATOM 370 HA SER A 25 42.424 21.686 18.720 1.00 78.68 H
ATOM 371 HB2 SER A 25 41.771 19.217 19.929 1.00 82.50 H
ATOM 372 HB3 SER A 25 42.594 19.362 18.577 1.00 82.50 H
ATOM 373 HG SER A 25 43.468 20.305 20.886 1.00 89.54 H