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PDBsum entry 3qxa

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Immune system PDB id
3qxa
Jmol
Contents
Protein chains
179 a.a.
190 a.a.
14 a.a.
12 a.a.
Waters ×154
HEADER    IMMUNE SYSTEM                           01-MAR-11   3QXA
TITLE     HLA-DR1 BOUND WITH CLIP PEPTIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;
COMPND   3 CHAIN: A, D;
COMPND   4 FRAGMENT: UNP RESIDUES 26-207;
COMPND   5 SYNONYM: MHC CLASS II ANTIGEN DRA;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-1 BETA CHAIN;
COMPND   9 CHAIN: B, E;
COMPND  10 FRAGMENT: UNP RESIDUES 30-219;
COMPND  11 SYNONYM: MHC CLASS II ANTIGEN DRB1*1, DR-1, DR1;
COMPND  12 ENGINEERED: YES;
COMPND  13 MOL_ID: 3;
COMPND  14 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN GAMMA CHAIN
COMPND  15 PEPTIDE;
COMPND  16 CHAIN: C, F;
COMPND  17 FRAGMENT: CLIP REGION;
COMPND  18 SYNONYM: HLA-DR ANTIGENS-ASSOCIATED INVARIANT CHAIN, IA ANTIGEN-
COMPND  19 ASSOCIATED INVARIANT CHAIN, II, P33;
COMPND  20 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: HLA-DR1, HLA-DRA, HLA-DRA1;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 MOL_ID: 2;
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  12 ORGANISM_COMMON: HUMAN;
SOURCE  13 ORGANISM_TAXID: 9606;
SOURCE  14 GENE: HLA-DR1, HLA-DRB1;
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  19 MOL_ID: 3;
SOURCE  20 SYNTHETIC: YES;
SOURCE  21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  22 ORGANISM_COMMON: HUMAN;
SOURCE  23 ORGANISM_TAXID: 9606;
SOURCE  24 OTHER_DETAILS: THIS CHEMICALLY SYNTHESIZED SEQUENCE OCCURS NATURALLY
SOURCE  25 IN HUMANS
KEYWDS    MHC CLASS II, IMMUNE SYSTEM
EXPDTA    X-RAY DIFFRACTION
AUTHOR    C.A.PAINTER,L.J.STERN
REVDAT   3   14-DEC-11 3QXA    1       JRNL
REVDAT   2   30-NOV-11 3QXA    1       JRNL
REVDAT   1   16-NOV-11 3QXA    0
JRNL        AUTH   C.A.PAINTER,M.P.NEGRONI,K.A.KELLERSBERGER,Z.ZAVALA-RUIZ,
JRNL        AUTH 2 J.E.EVANS,L.J.STERN
JRNL        TITL   CONFORMATIONAL LABILITY IN THE CLASS II MHC 310 HELIX AND
JRNL        TITL 2 ADJACENT EXTENDED STRAND DICTATE HLA-DM SUSCEPTIBILITY AND
JRNL        TITL 3 PEPTIDE EXCHANGE.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 108 19329 2011
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   22084083
JRNL        DOI    10.1073/PNAS.1108074108
REMARK   2
REMARK   2 RESOLUTION.    2.71 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT 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 : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.71
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.45
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8
REMARK   3   NUMBER OF REFLECTIONS             : 25637
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195
REMARK   3   R VALUE            (WORKING SET) : 0.193
REMARK   3   FREE R VALUE                     : 0.235
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.770
REMARK   3   FREE R VALUE TEST SET COUNT      : 1223
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 37.4506 -  5.6363    1.00     2968   143  0.2230 0.2736
REMARK   3     2  5.6363 -  4.4761    0.99     2816   153  0.1697 0.2025
REMARK   3     3  4.4761 -  3.9109    0.99     2761   162  0.1680 0.1964
REMARK   3     4  3.9109 -  3.5537    0.99     2766   133  0.1792 0.2026
REMARK   3     5  3.5537 -  3.2991    0.99     2727   132  0.1843 0.2450
REMARK   3     6  3.2991 -  3.1047    0.97     2724   124  0.1963 0.2352
REMARK   3     7  3.1047 -  2.9493    0.96     2643   127  0.2101 0.3096
REMARK   3     8  2.9493 -  2.8209    0.94     2599   129  0.2257 0.2590
REMARK   3     9  2.8209 -  2.7124    0.88     2410   120  0.2459 0.3184
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.10
REMARK   3   SHRINKAGE RADIUS   : 0.83
REMARK   3   K_SOL              : 0.35
REMARK   3   B_SOL              : 20.00
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.360
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.890
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.86
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 4.72680
REMARK   3    B22 (A**2) : 4.12970
REMARK   3    B33 (A**2) : 16.96430
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : -0.00000
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      :  0.002           6429
REMARK   3   ANGLE     :  0.627           8735
REMARK   3   CHIRALITY :  0.041            939
REMARK   3   PLANARITY :  0.002           1143
REMARK   3   DIHEDRAL  : 14.325           2358
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : 6
REMARK   3   TLS GROUP : 1
REMARK   3    SELECTION: (chain 'A' and ((resseq 4:78))) or (chain 'C' and
REMARK   3               ((resseq 87:101))) or (chain 'B' and ((resseq 1:92)))
REMARK   3    ORIGIN FOR THE GROUP (A): -30.2460   7.7583  -0.3464
REMARK   3    T TENSOR
REMARK   3      T11:   0.0677 T22:   0.0346
REMARK   3      T33:  -0.0127 T12:   0.0212
REMARK   3      T13:  -0.0479 T23:   0.0315
REMARK   3    L TENSOR
REMARK   3      L11:   0.0765 L22:   0.1077
REMARK   3      L33:   0.0903 L12:   0.0096
REMARK   3      L13:  -0.0379 L23:  -0.0001
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0106 S12:   0.1483 S13:   0.0087
REMARK   3      S21:  -0.1292 S22:  -0.0452 S23:   0.0585
REMARK   3      S31:   0.0291 S32:  -0.0655 S33:  -0.1079
REMARK   3   TLS GROUP : 2
REMARK   3    SELECTION: (chain 'E' and ((resseq 1:92))) or (chain 'D' and
REMARK   3               ((resseq 4:80))) or (chain 'F' and ((resseq 87:101)))
REMARK   3    ORIGIN FOR THE GROUP (A): -21.2935  18.6914  33.9843
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0263 T22:   0.0748
REMARK   3      T33:   0.0486 T12:   0.0234
REMARK   3      T13:  -0.1059 T23:  -0.0295
REMARK   3    L TENSOR
REMARK   3      L11:   0.1135 L22:   0.1409
REMARK   3      L33:   0.1270 L12:  -0.0968
REMARK   3      L13:   0.0986 L23:  -0.0506
REMARK   3    S TENSOR
REMARK   3      S11:   0.0149 S12:  -0.1447 S13:  -0.0059
REMARK   3      S21:   0.0509 S22:   0.0650 S23:   0.0939
REMARK   3      S31:  -0.0340 S32:  -0.0708 S33:   0.0785
REMARK   3   TLS GROUP : 3
REMARK   3    SELECTION: chain 'D' and ((resseq 83:182))
REMARK   3    ORIGIN FOR THE GROUP (A): -14.1693  -7.9991  32.1143
REMARK   3    T TENSOR
REMARK   3      T11:   0.0358 T22:   0.0468
REMARK   3      T33:   0.1084 T12:  -0.0107
REMARK   3      T13:  -0.1912 T23:   0.0272
REMARK   3    L TENSOR
REMARK   3      L11:   0.0022 L22:   0.0612
REMARK   3      L33:   0.0824 L12:  -0.0040
REMARK   3      L13:   0.0002 L23:  -0.0565
REMARK   3    S TENSOR
REMARK   3      S11:   0.0433 S12:   0.0084 S13:  -0.0894
REMARK   3      S21:  -0.0290 S22:   0.0557 S23:   0.0554
REMARK   3      S31:   0.0822 S32:  -0.0245 S33:   0.1109
REMARK   3   TLS GROUP : 4
REMARK   3    SELECTION: chain 'E' and ((resseq 93:190))
REMARK   3    ORIGIN FOR THE GROUP (A):   9.6433  -3.2473  23.2027
REMARK   3    T TENSOR
REMARK   3      T11:  -0.0137 T22:   0.1360
REMARK   3      T33:   0.1761 T12:   0.0870
REMARK   3      T13:  -0.0151 T23:  -0.0978
REMARK   3    L TENSOR
REMARK   3      L11:   0.0696 L22:   0.0790
REMARK   3      L33:   0.0299 L12:  -0.0739
REMARK   3      L13:  -0.0167 L23:   0.0284
REMARK   3    S TENSOR
REMARK   3      S11:   0.0493 S12:   0.0958 S13:  -0.0635
REMARK   3      S21:  -0.0402 S22:   0.0301 S23:  -0.1459
REMARK   3      S31:   0.0553 S32:   0.0922 S33:  -0.0083
REMARK   3   TLS GROUP : 5
REMARK   3    SELECTION: chain 'B' and ((resseq 94:190))
REMARK   3    ORIGIN FOR THE GROUP (A): -19.8333 -25.7127  17.1241
REMARK   3    T TENSOR
REMARK   3      T11:   0.1678 T22:   0.0817
REMARK   3      T33:   0.1817 T12:  -0.0088
REMARK   3      T13:  -0.1107 T23:   0.0129
REMARK   3    L TENSOR
REMARK   3      L11:   0.0097 L22:   0.0244
REMARK   3      L33:   0.0196 L12:   0.0140
REMARK   3      L13:  -0.0047 L23:   0.0019
REMARK   3    S TENSOR
REMARK   3      S11:   0.0507 S12:  -0.0251 S13:  -0.0990
REMARK   3      S21:   0.0084 S22:   0.0151 S23:  -0.0271
REMARK   3      S31:   0.0626 S32:  -0.0038 S33:   0.0073
REMARK   3   TLS GROUP : 6
REMARK   3    SELECTION: chain 'A' and ((resseq 83:182))
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.0822  -6.3851   6.5981
REMARK   3    T TENSOR
REMARK   3      T11:   0.0506 T22:   0.1107
REMARK   3      T33:   0.0864 T12:   0.0286
REMARK   3      T13:  -0.0132 T23:  -0.0429
REMARK   3    L TENSOR
REMARK   3      L11:   0.0508 L22:   0.0555
REMARK   3      L33:   0.0861 L12:  -0.0076
REMARK   3      L13:  -0.0427 L23:  -0.0462
REMARK   3    S TENSOR
REMARK   3      S11:   0.0019 S12:   0.0513 S13:  -0.0428
REMARK   3      S21:  -0.0320 S22:   0.0163 S23:  -0.0562
REMARK   3      S31:   0.0797 S32:   0.0381 S33:   0.0099
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 3QXA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064219.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSLS
REMARK 200  BEAMLINE                       : X29A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : VERTICALLY FOCUSING MIRROR AND
REMARK 200                                   HORIZONTALLY FOCUSING
REMARK 200                                   MONOCHROMATOR
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26368
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700
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     (%) : 99.9
REMARK 200  DATA REDUNDANCY                : 7.000
REMARK 200  R MERGE                    (I) : 0.12500
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 10.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.40200
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1SJE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, 10% GLYCEROL, 100MM SODIUM
REMARK 280  ACETATE PH 5.6, 5MM DTT, VAPOR DIFFUSION, HANGING DROP,
REMARK 280  TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y,Z+1/2
REMARK 290       3555   -X,Y+1/2,-Z+1/2
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       32.64800
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.78650
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.94350
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.78650
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.64800
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.94350
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 7200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 7160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     ILE A     1
REMARK 465     LYS A     2
REMARK 465     GLU A     3
REMARK 465     ILE D     1
REMARK 465     LYS D     2
REMARK 465     GLU D     3
REMARK 465     PRO C    87
REMARK 465     PRO F    87
REMARK 465     VAL F    88
REMARK 465     ALA F   101
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475   M RES C SSEQI
REMARK 475     ALA A  182
REMARK 475     ALA D  182
REMARK 475     GLY E    1
REMARK 475     GLN F  100
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480   M RES C SSEQI ATOMS
REMARK 480     LYS A   38   CD   CE   NZ
REMARK 480     LYS A   39   CG   CD   CE   NZ
REMARK 480     GLU A   46   CD   OE1  OE2
REMARK 480     GLU A   55   CD   OE1  OE2
REMARK 480     LEU A   60   CD1  CD2
REMARK 480     LEU A   92   CD2
REMARK 480     GLU A  101   OE1  OE2
REMARK 480     ASN A  118   ND2
REMARK 480     ARG A  123   NH1  NH2
REMARK 480     VAL A  128   CG1
REMARK 480     THR A  130   CB   OG1  CG2
REMARK 480     ARG A  164   CZ   NH1  NH2
REMARK 480     LEU A  174   CD1  CD2
REMARK 480     THR B    3   CG2
REMARK 480     GLU B   22   CG   CD   OE1  OE2
REMARK 480     GLU B   35   CG   CD   OE1  OE2
REMARK 480     ARG B   55   NH1  NH2
REMARK 480     GLU B   59   OE1  OE2
REMARK 480     LYS B   65   NZ
REMARK 480     LEU B   67   CD2
REMARK 480     LYS B  105   CE   NZ
REMARK 480     GLU B  137   OE1  OE2
REMARK 480     ARG B  166   CZ   NH1  NH2
REMARK 480     THR B  181   CG2
REMARK 480     SER B  182   OG
REMARK 480     LYS D   38   CD   CE   NZ
REMARK 480     LYS D   39   CE   NZ
REMARK 480     GLU D   46   CB   CG   CD   OE1  OE2
REMARK 480     PHE D   48   CB
REMARK 480     ARG D   50   CG   CD   NE   CZ   NH1  NH2
REMARK 480     GLU D   55   CG   CD   OE1  OE2
REMARK 480     GLN D   57   CD   OE1  NE2
REMARK 480     LEU D   92   CD2
REMARK 480     VAL D   97   CG2
REMARK 480     ASN D  118   ND2
REMARK 480     LYS D  126   CB   CG   CD   CE   NZ
REMARK 480     VAL D  128   CG1
REMARK 480     THR D  130   CB   OG1  CG2
REMARK 480     ARG D  164   CZ   NH1  NH2
REMARK 480     GLU E   35   CG   CD   OE1  OE2
REMARK 480     GLU E   59   OE1  OE2
REMARK 480     TYR E   60   CG   CD1  CD2  CE1  CE2  CZ   OH
REMARK 480     LYS E   65   CG   CD   CE   NZ
REMARK 480     ASP E   66   OD1  OD2
REMARK 480     LEU E   67   CD2
REMARK 480     GLU E   69   OE1
REMARK 480     GLN E   70   CG   CD   OE1  NE2
REMARK 480     GLN E  110   CB   CG   CD   OE1  NE2
REMARK 480     GLN E  136   CB   CG
REMARK 480     LYS E  139   CD   CE   NZ
REMARK 480     ARG E  166   CG   CD   NE   CZ   NH1  NH2
REMARK 480     THR E  181   CA   CB   OG1  CG2
REMARK 480     SER E  182   CB   OG
REMARK 480     ARG E  189   CG   CD   NE   CZ   NH1  NH2
REMARK 480     VAL C   88   CB   CG1  CG2
REMARK 480     GLN C  100   N
REMARK 480     ALA C  101   CA   C    O    CB
REMARK 480     LYS F   90   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   O    HOH D   184     O    HOH D   224              1.86
REMARK 500   O    GLN E    70     O    HOH E   196              2.00
REMARK 500   O    HOH E   205     O    HOH E   213              2.05
REMARK 500   O    SER E    42     O    HOH E   201              2.05
REMARK 500   O    ASN D    94     O    HOH D   207              2.09
REMARK 500   O    HOH D   201     O    HOH E   204              2.10
REMARK 500   OE2  GLU A    30     O    HOH A   204              2.13
REMARK 500   OE2  GLU D    47     O    HOH D   214              2.15
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   O    HOH B   205     O    HOH B   210     4555     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    SER A  95      155.29    179.22
REMARK 500    VAL A 136     -172.03    -69.05
REMARK 500    ASN B  33     -103.16     63.59
REMARK 500    TYR B  78      -62.79   -122.93
REMARK 500    THR B  90      -64.24   -131.93
REMARK 500    THR D 113      148.03   -170.44
REMARK 500    ASN E  19       71.13     50.67
REMARK 500    ASN E  33     -101.60     53.70
REMARK 500    TYR E  78      -60.59   -134.61
REMARK 500    THR E  90      -73.96   -122.12
REMARK 500    GLN E 110        4.49     83.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QXD   RELATED DB: PDB
DBREF  3QXA A    1   182  UNP    P01903   DRA_HUMAN       26    207
DBREF  3QXA B    1   190  UNP    P04229   2B11_HUMAN      30    219
DBREF  3QXA D    1   182  UNP    P01903   DRA_HUMAN       26    207
DBREF  3QXA E    1   190  UNP    P04229   2B11_HUMAN      30    219
DBREF  3QXA C   87   101  UNP    P04233   HG2A_HUMAN     103    117
DBREF  3QXA F   87   101  UNP    P04233   HG2A_HUMAN     103    117
SEQRES   1 A  182  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES   2 A  182  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES   3 A  182  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES   4 A  182  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES   5 A  182  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES   6 A  182  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES   7 A  182  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES   8 A  182  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES   9 A  182  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES  10 A  182  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES  11 A  182  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES  12 A  182  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES  13 A  182  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES  14 A  182  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES   1 B  190  GLY ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE
SEQRES   2 B  190  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG LEU
SEQRES   3 B  190  LEU GLU ARG CYS ILE TYR ASN GLN GLU GLU SER VAL ARG
SEQRES   4 B  190  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES   5 B  190  LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES   6 B  190  ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR
SEQRES   7 B  190  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES   8 B  190  GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO SER
SEQRES   9 B  190  LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES  10 B  190  SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES  11 B  190  TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES  12 B  190  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES  13 B  190  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES  14 B  190  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES  15 B  190  PRO LEU THR VAL GLU TRP ARG ALA
SEQRES   1 D  182  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES   2 D  182  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES   3 D  182  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES   4 D  182  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES   5 D  182  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES   6 D  182  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES   7 D  182  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES   8 D  182  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES   9 D  182  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES  10 D  182  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES  11 D  182  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES  12 D  182  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES  13 D  182  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES  14 D  182  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES   1 E  190  GLY ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE
SEQRES   2 E  190  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG LEU
SEQRES   3 E  190  LEU GLU ARG CYS ILE TYR ASN GLN GLU GLU SER VAL ARG
SEQRES   4 E  190  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES   5 E  190  LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES   6 E  190  ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR
SEQRES   7 E  190  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES   8 E  190  GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO SER
SEQRES   9 E  190  LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES  10 E  190  SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES  11 E  190  TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES  12 E  190  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES  13 E  190  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES  14 E  190  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES  15 E  190  PRO LEU THR VAL GLU TRP ARG ALA
SEQRES   1 C   15  PRO VAL SER LYS MET ARG MET ALA THR PRO LEU LEU MET
SEQRES   2 C   15  GLN ALA
SEQRES   1 F   15  PRO VAL SER LYS MET ARG MET ALA THR PRO LEU LEU MET
SEQRES   2 F   15  GLN ALA
FORMUL   7  HOH   *154(H2 O)
HELIX    1   1 LEU A   45  PHE A   51  5                                   7
HELIX    2   2 ALA A   56  SER A   77  1                                  22
HELIX    3   3 THR B   51  LEU B   53  5                                   3
HELIX    4   4 GLY B   54  SER B   63  1                                  10
HELIX    5   5 GLN B   64  TYR B   78  1                                  15
HELIX    6   6 TYR B   78  GLU B   87  1                                  10
HELIX    7   7 SER B   88  THR B   90  5                                   3
HELIX    8   8 LEU D   45  PHE D   51  5                                   7
HELIX    9   9 GLU D   55  SER D   77  1                                  23
HELIX   10  10 THR E   51  LEU E   53  5                                   3
HELIX   11  11 GLY E   54  ASN E   62  1                                   9
HELIX   12  12 GLN E   64  TYR E   78  1                                  15
HELIX   13  13 TYR E   78  GLU E   87  1                                  10
SHEET    1   A 8 GLU A  40  TRP A  43  0
SHEET    2   A 8 ASP A  29  ASP A  35 -1  N  HIS A  33   O  VAL A  42
SHEET    3   A 8 SER A  19  PHE A  26 -1  N  PHE A  26   O  ASP A  29
SHEET    4   A 8 HIS A   5  ASN A  15 -1  N  ALA A  10   O  MET A  23
SHEET    5   A 8 PHE B   7  PHE B  18 -1  O  PHE B  17   N  HIS A   5
SHEET    6   A 8 ARG B  23  TYR B  32 -1  O  LEU B  27   N  GLU B  14
SHEET    7   A 8 GLU B  35  ASP B  41 -1  O  PHE B  40   N  GLU B  28
SHEET    8   A 8 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39
SHEET    1   B 4 GLU A  88  THR A  93  0
SHEET    2   B 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92
SHEET    3   B 4 PHE A 145  PHE A 153 -1  O  HIS A 149   N  CYS A 107
SHEET    4   B 4 SER A 133  GLU A 134 -1  N  SER A 133   O  TYR A 150
SHEET    1   C 4 GLU A  88  THR A  93  0
SHEET    2   C 4 ASN A 103  PHE A 112 -1  O  ILE A 106   N  LEU A  92
SHEET    3   C 4 PHE A 145  PHE A 153 -1  O  HIS A 149   N  CYS A 107
SHEET    4   C 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  ARG A 146
SHEET    1   D 4 LYS A 126  VAL A 128  0
SHEET    2   D 4 ASN A 118  ARG A 123 -1  N  ARG A 123   O  LYS A 126
SHEET    3   D 4 VAL A 160  GLU A 166 -1  O  ASP A 162   N  LEU A 122
SHEET    4   D 4 LEU A 174  GLU A 179 -1  O  TRP A 178   N  TYR A 161
SHEET    1   E 4 LYS B  98  PRO B 103  0
SHEET    2   E 4 ASN B 113  PHE B 122 -1  O  SER B 118   N  THR B 100
SHEET    3   E 4 PHE B 155  THR B 163 -1  O  THR B 163   N  ASN B 113
SHEET    4   E 4 VAL B 142  SER B 144 -1  N  VAL B 143   O  MET B 160
SHEET    1   F 4 LYS B  98  PRO B 103  0
SHEET    2   F 4 ASN B 113  PHE B 122 -1  O  SER B 118   N  THR B 100
SHEET    3   F 4 PHE B 155  THR B 163 -1  O  THR B 163   N  ASN B 113
SHEET    4   F 4 ILE B 148  GLN B 149 -1  N  ILE B 148   O  GLN B 156
SHEET    1   G 4 GLN B 136  GLU B 137  0
SHEET    2   G 4 GLU B 128  ARG B 133 -1  N  ARG B 133   O  GLN B 136
SHEET    3   G 4 VAL B 170  GLU B 176 -1  O  GLN B 174   N  ARG B 130
SHEET    4   G 4 LEU B 184  ARG B 189 -1  O  LEU B 184   N  VAL B 175
SHEET    1   H 8 GLU D  40  TRP D  43  0
SHEET    2   H 8 ASP D  29  ASP D  35 -1  N  HIS D  33   O  VAL D  42
SHEET    3   H 8 SER D  19  PHE D  26 -1  N  PHE D  26   O  ASP D  29
SHEET    4   H 8 HIS D   5  ASN D  15 -1  N  ILE D   8   O  ASP D  25
SHEET    5   H 8 PHE E   7  PHE E  18 -1  O  PHE E   7   N  ASN D  15
SHEET    6   H 8 ARG E  23  TYR E  32 -1  O  LEU E  27   N  GLU E  14
SHEET    7   H 8 GLU E  35  ASP E  41 -1  O  PHE E  40   N  GLU E  28
SHEET    8   H 8 TYR E  47  ALA E  49 -1  O  ARG E  48   N  ARG E  39
SHEET    1   I 4 GLU D  88  THR D  93  0
SHEET    2   I 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92
SHEET    3   I 4 PHE D 145  PHE D 153 -1  O  HIS D 149   N  CYS D 107
SHEET    4   I 4 SER D 133  GLU D 134 -1  N  SER D 133   O  TYR D 150
SHEET    1   J 4 GLU D  88  THR D  93  0
SHEET    2   J 4 ASN D 103  PHE D 112 -1  O  ILE D 106   N  LEU D  92
SHEET    3   J 4 PHE D 145  PHE D 153 -1  O  HIS D 149   N  CYS D 107
SHEET    4   J 4 LEU D 138  PRO D 139 -1  N  LEU D 138   O  ARG D 146
SHEET    1   K 4 LYS D 126  VAL D 128  0
SHEET    2   K 4 ASN D 118  ARG D 123 -1  N  ARG D 123   O  LYS D 126
SHEET    3   K 4 TYR D 161  GLU D 166 -1  O  ASP D 162   N  LEU D 122
SHEET    4   K 4 LEU D 174  TRP D 178 -1  O  TRP D 178   N  TYR D 161
SHEET    1   L 4 LYS E  98  PRO E 103  0
SHEET    2   L 4 ASN E 113  PHE E 122 -1  O  SER E 118   N  THR E 100
SHEET    3   L 4 PHE E 155  THR E 163 -1  O  LEU E 161   N  LEU E 115
SHEET    4   L 4 VAL E 142  SER E 144 -1  N  VAL E 143   O  MET E 160
SHEET    1   M 4 LYS E  98  PRO E 103  0
SHEET    2   M 4 ASN E 113  PHE E 122 -1  O  SER E 118   N  THR E 100
SHEET    3   M 4 PHE E 155  THR E 163 -1  O  LEU E 161   N  LEU E 115
SHEET    4   M 4 ILE E 148  GLN E 149 -1  N  ILE E 148   O  GLN E 156
SHEET    1   N 4 GLN E 136  GLU E 138  0
SHEET    2   N 4 GLU E 128  ARG E 133 -1  N  ARG E 133   O  GLN E 136
SHEET    3   N 4 VAL E 170  GLU E 176 -1  O  GLN E 174   N  ARG E 130
SHEET    4   N 4 LEU E 184  ARG E 189 -1  O  LEU E 184   N  VAL E 175
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.03
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.04
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.03
SSBOND   4 CYS D  107    CYS D  163                          1555   1555  2.03
SSBOND   5 CYS E   15    CYS E   79                          1555   1555  2.04
SSBOND   6 CYS E  117    CYS E  173                          1555   1555  2.03
CISPEP   1 ASN A   15    PRO A   16          0         2.17
CISPEP   2 THR A  113    PRO A  114          0         3.39
CISPEP   3 TYR B  123    PRO B  124          0         2.97
CISPEP   4 ASN D   15    PRO D   16          0         2.33
CISPEP   5 THR D  113    PRO D  114          0         0.83
CISPEP   6 TYR E  123    PRO E  124          0         1.64
CISPEP   7 VAL C   88    SER C   89          0        -6.73
CRYST1   65.296   95.887  151.573  90.00  90.00  90.00 P 21 21 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      0.015315  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010429  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006597        0.00000
      
PROCHECK
Go to PROCHECK summary
 References