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PDBsum entry 1aqd

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Top Page protein Protein-protein interface(s) links
Complex (mhc protein/antigen) PDB id
1aqd
Jmol
Contents
Protein chains
179 a.a. *
187 a.a. *
14 a.a. *
13 a.a. *
Waters ×152
* Residue conservation analysis
HEADER    COMPLEX (MHC PROTEIN/ANTIGEN)           28-JUL-97   1AQD
TITLE     HLA-DR1 (DRA, DRB1 0101) HUMAN CLASS II HISTOCOMPATIBILITY
TITLE    2 PROTEIN (EXTRACELLULAR DOMAIN) COMPLEXED WITH ENDOGENOUS
TITLE    3 PEPTIDE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: HLA-DR1 CLASS II HISTOCOMPATIBILITY PROTEIN;
COMPND   3 CHAIN: A, D, G, J;
COMPND   4 FRAGMENT: SECRETED EXTRACELLULAR DOMAINS;
COMPND   5 SYNONYM: DRA, DRB1 01010;
COMPND   6 ENGINEERED: YES;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: HLA-DR1 CLASS II HISTOCOMPATIBILITY PROTEIN;
COMPND   9 CHAIN: B, E, H, K;
COMPND  10 FRAGMENT: SECRETED EXTRACELLULAR DOMAINS;
COMPND  11 SYNONYM: DRA, DRB1 01010;
COMPND  12 ENGINEERED: YES;
COMPND  13 MOL_ID: 3;
COMPND  14 MOLECULE: HLA-A2;
COMPND  15 CHAIN: C, F, I, L;
COMPND  16 FRAGMENT: ANTIGENIC PEPTIDE;
COMPND  17 ENGINEERED: YES;
COMPND  18 OTHER_DETAILS: HLA-DR1 IS A CLASS II MHC PROTEIN, HLA-A2
COMPND  19 IS A CLASS I HISTOCOMPATIBILITY ANTIGEN
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 ORGAN: PLASMA;
SOURCE   6 TISSUE: LYMPHOID;
SOURCE   7 CELLULAR_LOCATION: PLASMA MEMBRANE;
SOURCE   8 GENE: DRA*0101, DRB1*0101;
SOURCE   9 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE  10 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE  12 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE  13 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  14 EXPRESSION_SYSTEM_VECTOR: PVL1392-BASED;
SOURCE  15 MOL_ID: 2;
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  17 ORGANISM_COMMON: HUMAN;
SOURCE  18 ORGANISM_TAXID: 9606;
SOURCE  19 ORGAN: PLASMA;
SOURCE  20 TISSUE: LYMPHOID;
SOURCE  21 CELLULAR_LOCATION: PLASMA MEMBRANE;
SOURCE  22 GENE: DRA*0101, DRB1*0101;
SOURCE  23 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE  24 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE  26 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE  27 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE  28 EXPRESSION_SYSTEM_VECTOR: PVL1392-BASED;
SOURCE  29 MOL_ID: 3;
SOURCE  30 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE  31 ORGANISM_COMMON: HUMAN;
SOURCE  32 ORGANISM_TAXID: 9606
KEYWDS    COMPLEX (MHC PROTEIN/ANTIGEN), HISTOCOMPATIBILITY ANTIGEN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    V.L.MURTHY,L.J.STERN
REVDAT   2   24-FEB-09 1AQD    1       VERSN
REVDAT   1   28-JAN-98 1AQD    0
JRNL        AUTH   V.L.MURTHY,L.J.STERN
JRNL        TITL   THE CLASS II MHC PROTEIN HLA-DR1 IN COMPLEX WITH
JRNL        TITL 2 AN ENDOGENOUS PEPTIDE: IMPLICATIONS FOR THE
JRNL        TITL 3 STRUCTURAL BASIS OF THE SPECIFICITY OF PEPTIDE
JRNL        TITL 4 BINDING.
JRNL        REF    STRUCTURE                     V.   5  1385 1997
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   9351812
JRNL        DOI    10.1016/S0969-2126(97)00288-8
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   V.L.MURTHY
REMARK   1  TITL   THREE DIMENSIONAL STRUCTURE OF A HUMAN CLASS II
REMARK   1  TITL 2 MHC PROTEIN HLA-DR1 BOUND TO AN ENDOGENOUS PEPTIDE
REMARK   1  REF    THESIS                                     1996
REMARK   1  PUBL   CAMBRIDGE, MA : MASSACHUSETTS INSTITUTE OF
REMARK   1  PUBL 2 TECHNOLOGY (THESIS)
REMARK   1  REFN
REMARK   1 REFERENCE 2
REMARK   1  AUTH   L.J.STERN,J.H.BROWN,T.S.JARDETZKY,J.C.GORGA,
REMARK   1  AUTH 2 R.G.URBAN,J.L.STROMINGER,D.C.WILEY
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE HUMAN CLASS II MHC
REMARK   1  TITL 2 PROTEIN HLA-DR1 COMPLEXED WITH AN INFLUENZA VIRUS
REMARK   1  TITL 3 PEPTIDE
REMARK   1  REF    NATURE                        V. 368   215 1994
REMARK   1  REFN                   ISSN 0028-0836
REMARK   1 REFERENCE 3
REMARK   1  AUTH   J.H.BROWN,T.S.JARDETZKY,J.C.GORGA,L.J.STERN,
REMARK   1  AUTH 2 R.G.URBAN,J.L.STROMINGER,D.C.WILEY
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF THE HUMAN CLASS II
REMARK   1  TITL 2 HISTOCOMPATIBILITY ANTIGEN HLA-DR1
REMARK   1  REF    NATURE                        V. 364    33 1993
REMARK   1  REFN                   ISSN 0028-0836
REMARK   2
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.1
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.0
REMARK   3   NUMBER OF REFLECTIONS             : 68842
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.216
REMARK   3   FREE R VALUE                     : 0.279
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 6884
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 8
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.45
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.57
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 70.00
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 6930
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3190
REMARK   3   BIN FREE R VALUE                    : 0.3540
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 770
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 11867
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 0
REMARK   3   SOLVENT ATOMS            : 152
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 37.20
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.80
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  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.30
REMARK   3   ESD FROM SIGMAA              (A) : 0.27
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.40
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.016
REMARK   3   BOND ANGLES            (DEGREES) : 2.60
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.00
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.150 ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 0.200 ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : 0.200 ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 0.250 ; NULL
REMARK   3
REMARK   3  NCS MODEL : RESTRAINTS (INTER AND INTRADIMER)
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : 0.1   ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : 0.1   ; NULL
REMARK   3   GROUP  2  POSITIONAL            (A) : 0.1   ; NULL
REMARK   3   GROUP  2  B-FACTOR           (A**2) : 0.1   ; NULL
REMARK   3   GROUP  3  POSITIONAL            (A) : 0.1   ; NULL
REMARK   3   GROUP  3  B-FACTOR           (A**2) : 0.1   ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PARAMHCSDX.PRO
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL
REMARK   3  PARAMETER FILE  3  : PARAM3_MOD.CHO
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL
REMARK   3  TOPOLOGY FILE  3   : TOPH3.CHO
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: REFMAC USED IN LATER STAGES OF
REMARK   3  REFINEMENT.
REMARK   4
REMARK   4 1AQD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : FEB-95
REMARK 200  TEMPERATURE           (KELVIN) : 98
REMARK 200  PH                             : 3.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : CHESS
REMARK 200  BEAMLINE                       : F1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : FUJI
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 73538
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.0
REMARK 200  DATA REDUNDANCY                : 2.100
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.07000
REMARK 200   FOR THE DATA SET  : 14.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.57
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.0
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.33100
REMARK 200   FOR SHELL         : 4.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: PDB ENTRY 1DLH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 56.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS GREW AS NEEDLES FROM 10MG/
REMARK 280  ML HLA-DR1 / PEPTIDE COMPLEX, 15% PEG 4000, 100MM GLYCINE, PH
REMARK 280  3.5, AT ROOM TEMPERATURE, OVER ONE WEEK.
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       67.25700
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.16000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       67.25700
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       67.16000
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, 3, 4
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:
REMARK 300 THERE ARE FOUR MOLECULES IN THIS COORDINATE SET
REMARK 300 EACH MOLECULE HAS ONE ALPHA CHAIN  : RESIDUES 3-182
REMARK 300 EACH MOLECULE HAS ONE BETA CHAIN   : RESIDUES 4-190
REMARK 300 EACH MOLECULE HAS ONE PEPTIDE CHAIN: RESIDUES 3-14
REMARK 300
REMARK 300 MOLECULE THREE IS THE MOST WELL DEFINED.
REMARK 300 MOLECULES 1 - 2 AND 3 - 4 EACH FORM THE SO-CALLED "DIMER
REMARK 300 OF DIMERS".
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: 7400 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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: 7370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I
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: 3
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: 7360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 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 350
REMARK 350 BIOMOLECULE: 4
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: 7440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, L
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     ALA A   182
REMARK 465     PRO A   183
REMARK 465     SER A   184
REMARK 465     PRO A   185
REMARK 465     LEU A   186
REMARK 465     PRO A   187
REMARK 465     GLU A   188
REMARK 465     THR A   189
REMARK 465     THR A   190
REMARK 465     GLU A   191
REMARK 465     ASN A   192
REMARK 465     GLY B     1
REMARK 465     ASP B     2
REMARK 465     THR B     3
REMARK 465     ARG B   191
REMARK 465     SER B   192
REMARK 465     GLU B   193
REMARK 465     SER B   194
REMARK 465     ALA B   195
REMARK 465     GLN B   196
REMARK 465     SER B   197
REMARK 465     LYS B   198
REMARK 465     VAL C     1
REMARK 465     ILE D     1
REMARK 465     LYS D     2
REMARK 465     PHE D   180
REMARK 465     ASP D   181
REMARK 465     ALA D   182
REMARK 465     PRO D   183
REMARK 465     SER D   184
REMARK 465     PRO D   185
REMARK 465     LEU D   186
REMARK 465     PRO D   187
REMARK 465     GLU D   188
REMARK 465     THR D   189
REMARK 465     THR D   190
REMARK 465     GLU D   191
REMARK 465     ASN D   192
REMARK 465     GLY E     1
REMARK 465     ASP E     2
REMARK 465     THR E     3
REMARK 465     ARG E   191
REMARK 465     SER E   192
REMARK 465     GLU E   193
REMARK 465     SER E   194
REMARK 465     ALA E   195
REMARK 465     GLN E   196
REMARK 465     SER E   197
REMARK 465     LYS E   198
REMARK 465     VAL F     1
REMARK 465     GLY F     2
REMARK 465     ILE G     1
REMARK 465     LYS G     2
REMARK 465     PHE G   180
REMARK 465     ASP G   181
REMARK 465     ALA G   182
REMARK 465     PRO G   183
REMARK 465     SER G   184
REMARK 465     PRO G   185
REMARK 465     LEU G   186
REMARK 465     PRO G   187
REMARK 465     GLU G   188
REMARK 465     THR G   189
REMARK 465     THR G   190
REMARK 465     GLU G   191
REMARK 465     ASN G   192
REMARK 465     GLY H     1
REMARK 465     ASP H     2
REMARK 465     THR H     3
REMARK 465     ARG H   191
REMARK 465     SER H   192
REMARK 465     GLU H   193
REMARK 465     SER H   194
REMARK 465     ALA H   195
REMARK 465     GLN H   196
REMARK 465     SER H   197
REMARK 465     LYS H   198
REMARK 465     VAL I     1
REMARK 465     ILE J     1
REMARK 465     LYS J     2
REMARK 465     PHE J   180
REMARK 465     ASP J   181
REMARK 465     ALA J   182
REMARK 465     PRO J   183
REMARK 465     SER J   184
REMARK 465     PRO J   185
REMARK 465     LEU J   186
REMARK 465     PRO J   187
REMARK 465     GLU J   188
REMARK 465     THR J   189
REMARK 465     THR J   190
REMARK 465     GLU J   191
REMARK 465     ASN J   192
REMARK 465     GLY K     1
REMARK 465     ASP K     2
REMARK 465     THR K     3
REMARK 465     SER K   192
REMARK 465     GLU K   193
REMARK 465     SER K   194
REMARK 465     ALA K   195
REMARK 465     GLN K   196
REMARK 465     SER K   197
REMARK 465     LYS K   198
REMARK 465     VAL L     1
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     ALA C  15    O
REMARK 470     ALA F  15    O
REMARK 470     ALA I  15    O
REMARK 470     ALA L  15    O
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     GLN B   64
REMARK 475     GLN K   64
REMARK 475     THR K  106
REMARK 475     GLN K  107
REMARK 475     PRO K  108
REMARK 475     LEU K  109
REMARK 475     GLN K  110
REMARK 475     HIS K  111
REMARK 475     ARG K  166
REMARK 475     SER K  167
REMARK 475     GLY K  168
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     GLU A    4   CB    CG    CD    OE1   OE2
REMARK 480     SER A   19   OG
REMARK 480     LYS A   39   CD    CE    NZ
REMARK 480     ARG A   50   CG    CD    NE    CZ    NH1   NH2
REMARK 480     SER A   53   OG
REMARK 480     GLU A   55   CG    CD    OE1   OE2
REMARK 480     LEU A   60   CG    CD1   CD2
REMARK 480     LYS A   67   CE    NZ
REMARK 480     GLU A   71   CG    CD    OE1   OE2
REMARK 480     LYS A   75   CG    CD    CE    NZ
REMARK 480     ARG A  100   CD    NE    CZ    NH1   NH2
REMARK 480     VAL A  117   CG1   CG2
REMARK 480     LYS A  126   CG    CD    CE    NZ
REMARK 480     GLU A  141   CG    CD    OE1   OE2
REMARK 480     GLU A  166   CD    OE1   OE2
REMARK 480     ASP A  171   CB    CG    OD1   OD2
REMARK 480     GLU A  172   CD    OE1   OE2
REMARK 480     LEU A  175   CG    CD1   CD2
REMARK 480     ASN B   19   CB    CG    OD1   ND2
REMARK 480     GLU B   22   CD    OE1   OE2
REMARK 480     ARG B   23   CB    CG    CD    NE    CZ    NH1   NH2
REMARK 480     ARG B   29   CD    NE    CZ    NH1   NH2
REMARK 480     GLU B   35   CB    CG    CD    OE1   OE2
REMARK 480     SER B   42   CB    OG
REMARK 480     LYS B   65   CB    CG    CD    CE    NZ
REMARK 480     ASP B   66   CG    OD1   OD2
REMARK 480     GLN B   70   CB    CG    CD    OE1   NE2
REMARK 480     LYS B   98   CB    CG    CD    CE    NZ
REMARK 480     GLN B  107   CB    CG    CD    OE1   NE2
REMARK 480     LYS B  139   CD    CE    NZ
REMARK 480     SER B  144   CB    OG
REMARK 480     ARG B  166   NE    CZ    NH1   NH2
REMARK 480     SER B  167   OG
REMARK 480     VAL B  170   CB    CG1   CG2
REMARK 480     GLU B  176   CD    OE1   OE2
REMARK 480     THR B  181   CB    OG1   CG2
REMARK 480     SER B  182   OG
REMARK 480     ARG B  189   CB    CG    CD    NE    CZ    NH1   NH2
REMARK 480     TYR C   11   CB    CG    CD1   CD2   CE1   CE2   CZ
REMARK 480     TYR C   11   OH
REMARK 480     GLU D    4   CB    CG    CD    OE1   OE2
REMARK 480     SER D   19   OG
REMARK 480     ARG D   50   CG    CD    NE    CZ    NH1   NH2
REMARK 480     SER D   53   OG
REMARK 480     GLU D   55   CG    CD    OE1   OE2
REMARK 480     LEU D   60   CG    CD1   CD2
REMARK 480     LYS D   67   CD    CE    NZ
REMARK 480     GLU D   71   CG    CD    OE1   OE2
REMARK 480     LYS D   75   CG    CD    CE    NZ
REMARK 480     VAL D  117   CG1   CG2
REMARK 480     ARG D  123   CD    NE    CZ    NH1   NH2
REMARK 480     LYS D  126   CG    CD    CE    NZ
REMARK 480     GLU D  141   CG    CD    OE1   OE2
REMARK 480     ASP D  171   CB    CG    OD1   OD2
REMARK 480     GLU D  172   CD    OE1   OE2
REMARK 480     LEU D  175   CG    CD1   CD2
REMARK 480     ASN E   19   CB    CG    OD1   ND2
REMARK 480     GLU E   22   CD    OE1   OE2
REMARK 480     GLN E   34   CD    OE1   NE2
REMARK 480     GLU E   35   CB    CG    CD    OE1   OE2
REMARK 480     GLU E   59   CG    CD    OE1   OE2
REMARK 480     GLN E   64   CD    OE1   NE2
REMARK 480     LYS E   65   CB    CG    CD    CE    NZ
REMARK 480     ASP E   66   CG    OD1   OD2
REMARK 480     GLN E   70   CB    CG    CD    OE1   NE2
REMARK 480     LYS E   98   CB    CG    CD    CE    NZ
REMARK 480     GLN E  107   CB    CG    CD    OE1   NE2
REMARK 480     PRO E  108   CB    CG    CD
REMARK 480     LEU E  109   CB    CG    CD1   CD2
REMARK 480     GLN E  110   CB    CG    CD    OE1   NE2
REMARK 480     HIS E  111   C     O     CB    CG    ND1   CD2   CE1
REMARK 480     HIS E  111   NE2
REMARK 480     LYS E  139   CD    CE    NZ
REMARK 480     GLU E  176   CD    OE1   OE2
REMARK 480     THR E  181   CB    OG1   CG2
REMARK 480     SER E  182   OG
REMARK 480     ARG E  189   CB    CG    CD    NE    CZ    NH1   NH2
REMARK 480     TYR F   11   CB    CG    CD1   CD2   CE1   CE2   CZ
REMARK 480     TYR F   11   OH
REMARK 480     TYR F   14   CB    CG    CD1   CD2   CE1   CE2   CZ
REMARK 480     TYR F   14   OH
REMARK 480     GLU G    4   CB    CG    CD    OE1   OE2
REMARK 480     SER G   19   OG
REMARK 480     GLU G   55   CG    CD    OE1   OE2
REMARK 480     LEU G   60   CG    CD1   CD2
REMARK 480     GLU G   71   CG    CD    OE1   OE2
REMARK 480     ARG G  100   CD    NE    CZ    NH1   NH2
REMARK 480     VAL G  117   CG1   CG2
REMARK 480     LYS G  126   CG    CD    CE    NZ
REMARK 480     GLU G  141   CG    CD    OE1   OE2
REMARK 480     GLU G  166   CD    OE1   OE2
REMARK 480     ASP G  171   CB    CG    OD1   OD2
REMARK 480     GLU G  172   CD    OE1   OE2
REMARK 480     LEU G  175   CG    CD1   CD2
REMARK 480     GLU H   22   CD    OE1   OE2
REMARK 480     ARG H   23   CB    CG    CD    NE    CZ    NH1   NH2
REMARK 480     GLU H   35   CB    CG    CD    OE1   OE2
REMARK 480     SER H   42   CB    OG
REMARK 480     GLU H   59   CB    CG    CD    OE1   OE2
REMARK 480     LYS H   65   CB    CG    CD    CE    NZ
REMARK 480     LYS H   98   CB    CG    CD    CE    NZ
REMARK 480     PRO H  108   CB    CG    CD
REMARK 480     LEU H  109   CB    CG    CD1   CD2
REMARK 480     GLN H  110   CB    CG    CD    OE1   NE2
REMARK 480     GLU H  128   CD    OE1   OE2
REMARK 480     LYS H  139   CD    CE    NZ
REMARK 480     SER H  144   CB    OG
REMARK 480     VAL H  170   CB    CG1   CG2
REMARK 480     GLU H  176   CD    OE1   OE2
REMARK 480     THR H  181   CB    OG1   CG2
REMARK 480     SER H  182   OG
REMARK 480     ARG H  189   CB    CG    CD    NE    CZ    NH1   NH2
REMARK 480     TYR I   11   CB    CG    CD1   CD2   CE1   CE2   CZ
REMARK 480     TYR I   11   OH
REMARK 480     SER J   19   OG
REMARK 480     LYS J   39   CD    CE    NZ
REMARK 480     ARG J   50   CG    CD    NE    CZ    NH1   NH2
REMARK 480     LEU J   60   CG    CD1   CD2
REMARK 480     LYS J   67   CD    CE    NZ
REMARK 480     GLU J   71   CG    CD    OE1   OE2
REMARK 480     LYS J   75   CG    CD    CE    NZ
REMARK 480     VAL J  117   CG1   CG2
REMARK 480     LYS J  126   CG    CD    CE    NZ
REMARK 480     GLU J  141   CG    CD    OE1   OE2
REMARK 480     ASP J  171   CB    CG    OD1   OD2
REMARK 480     LEU J  175   CG    CD1   CD2
REMARK 480     ASN K   19   OD1   ND2
REMARK 480     GLU K   22   CD    OE1   OE2
REMARK 480     ARG K   23   NE    CZ    NH1   NH2
REMARK 480     GLU K   35   CB    CG    CD    OE1   OE2
REMARK 480     GLU K   59   CB    CG    CD    OE1   OE2
REMARK 480     LYS K   65   CB    CG    CD    CE    NZ
REMARK 480     ASP K   66   CG    OD1   OD2
REMARK 480     GLN K   70   CB    CG    CD    OE1   NE2
REMARK 480     LYS K   98   CB    CG    CD    CE    NZ
REMARK 480     GLU K  128   CD    OE1   OE2
REMARK 480     LYS K  139   CD    CE    NZ
REMARK 480     GLU K  176   CD    OE1   OE2
REMARK 480     THR K  181   CB    OG1   CG2
REMARK 480     SER K  182   OG
REMARK 480     ARG K  191   C     O     NE    CZ    NH1   NH2
REMARK 480     TYR L   11   CB    CG    CD1   CD2   CE1   CE2   CZ
REMARK 480     TYR L   11   OH
REMARK 480     TYR L   14   CB    CG    CD1   CD2   CE1   CE2   CZ
REMARK 480     TYR L   14   OH
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ARG A 123   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES
REMARK 500    LEU B 147   CB  -  CG  -  CD2 ANGL. DEV. = -10.8 DEGREES
REMARK 500    ARG E  23   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES
REMARK 500    ARG E  39   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES
REMARK 500    ARG E  94   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES
REMARK 500    ARG H   6   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES
REMARK 500    ARG H  71   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ARG J 146   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES
REMARK 500    ARG K 133   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG L   6   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG L   6   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES
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    GLU A  47       -5.06    -55.74
REMARK 500    THR A 113      142.03   -170.51
REMARK 500    ASN B  33      -96.63     64.03
REMARK 500    THR B  90      -72.37   -122.67
REMARK 500    THR B 106       49.16    -92.89
REMARK 500    PRO B 108      140.57    -36.95
REMARK 500    LEU B 109      136.65    -32.39
REMARK 500    GLN B 110       14.31     87.76
REMARK 500    SER C   3     -102.16     48.79
REMARK 500    ASN E  33      -97.83     63.03
REMARK 500    THR E  90      -78.81   -122.66
REMARK 500    GLN E 110      -12.20     69.26
REMARK 500    ILE E 127      149.38   -170.38
REMARK 500    ASN H  33      -99.46     57.55
REMARK 500    TYR H  60      -78.60    -47.85
REMARK 500    TYR H  78      -64.63   -109.68
REMARK 500    THR H  90      -79.01   -126.32
REMARK 500    GLN H 107       96.92    -60.29
REMARK 500    PRO H 108      148.12    -26.39
REMARK 500    ASP H 152       20.47   -140.11
REMARK 500    TRP H 153       34.50     75.63
REMARK 500    THR J 130      109.33    -45.75
REMARK 500    ASN K  33     -104.97     57.98
REMARK 500    LYS K  65      -35.47     25.89
REMARK 500    THR K  90      -77.58   -125.52
REMARK 500    VAL K 164       80.47   -152.15
REMARK 500    SER K 167      -13.73     54.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    TYR B 123         0.08    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF  1AQD A    1   192  UNP    P01903   2DRA_HUMAN      26    217
DBREF  1AQD B    1   198  UNP    P04229   2B11_HUMAN      30    227
DBREF  1AQD C    1    15  UNP    P01892   1A02_HUMAN     127    141
DBREF  1AQD D    1   192  UNP    P01903   2DRA_HUMAN      26    217
DBREF  1AQD E    1   198  UNP    P04229   2B11_HUMAN      30    227
DBREF  1AQD F    1    15  UNP    P01892   1A02_HUMAN     127    141
DBREF  1AQD G    1   192  UNP    P01903   2DRA_HUMAN      26    217
DBREF  1AQD H    1   198  UNP    P04229   2B11_HUMAN      30    227
DBREF  1AQD I    1    15  UNP    P01892   1A02_HUMAN     127    141
DBREF  1AQD J    1   192  UNP    P01903   2DRA_HUMAN      26    217
DBREF  1AQD K    1   198  UNP    P04229   2B11_HUMAN      30    227
DBREF  1AQD L    1    15  UNP    P01892   1A02_HUMAN     127    141
SEQRES   1 A  192  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES   2 A  192  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES   3 A  192  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES   4 A  192  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES   5 A  192  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES   6 A  192  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES   7 A  192  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES   8 A  192  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES   9 A  192  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES  10 A  192  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES  11 A  192  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES  12 A  192  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES  13 A  192  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES  14 A  192  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES  15 A  192  PRO SER PRO LEU PRO GLU THR THR GLU ASN
SEQRES   1 B  198  GLY ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE
SEQRES   2 B  198  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG LEU
SEQRES   3 B  198  LEU GLU ARG CYS ILE TYR ASN GLN GLU GLU SER VAL ARG
SEQRES   4 B  198  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES   5 B  198  LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES   6 B  198  ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR
SEQRES   7 B  198  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES   8 B  198  GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO SER
SEQRES   9 B  198  LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES  10 B  198  SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES  11 B  198  TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES  12 B  198  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES  13 B  198  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES  14 B  198  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES  15 B  198  PRO LEU THR VAL GLU TRP ARG ALA ARG SER GLU SER ALA
SEQRES  16 B  198  GLN SER LYS
SEQRES   1 C   15  VAL GLY SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN
SEQRES   2 C   15  TYR ALA
SEQRES   1 D  192  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES   2 D  192  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES   3 D  192  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES   4 D  192  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES   5 D  192  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES   6 D  192  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES   7 D  192  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES   8 D  192  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES   9 D  192  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES  10 D  192  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES  11 D  192  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES  12 D  192  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES  13 D  192  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES  14 D  192  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES  15 D  192  PRO SER PRO LEU PRO GLU THR THR GLU ASN
SEQRES   1 E  198  GLY ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE
SEQRES   2 E  198  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG LEU
SEQRES   3 E  198  LEU GLU ARG CYS ILE TYR ASN GLN GLU GLU SER VAL ARG
SEQRES   4 E  198  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES   5 E  198  LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES   6 E  198  ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR
SEQRES   7 E  198  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES   8 E  198  GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO SER
SEQRES   9 E  198  LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES  10 E  198  SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES  11 E  198  TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES  12 E  198  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES  13 E  198  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES  14 E  198  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES  15 E  198  PRO LEU THR VAL GLU TRP ARG ALA ARG SER GLU SER ALA
SEQRES  16 E  198  GLN SER LYS
SEQRES   1 F   15  VAL GLY SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN
SEQRES   2 F   15  TYR ALA
SEQRES   1 G  192  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES   2 G  192  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES   3 G  192  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES   4 G  192  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES   5 G  192  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES   6 G  192  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES   7 G  192  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES   8 G  192  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES   9 G  192  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES  10 G  192  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES  11 G  192  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES  12 G  192  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES  13 G  192  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES  14 G  192  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES  15 G  192  PRO SER PRO LEU PRO GLU THR THR GLU ASN
SEQRES   1 H  198  GLY ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE
SEQRES   2 H  198  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG LEU
SEQRES   3 H  198  LEU GLU ARG CYS ILE TYR ASN GLN GLU GLU SER VAL ARG
SEQRES   4 H  198  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES   5 H  198  LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES   6 H  198  ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR
SEQRES   7 H  198  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES   8 H  198  GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO SER
SEQRES   9 H  198  LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES  10 H  198  SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES  11 H  198  TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES  12 H  198  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES  13 H  198  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES  14 H  198  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES  15 H  198  PRO LEU THR VAL GLU TRP ARG ALA ARG SER GLU SER ALA
SEQRES  16 H  198  GLN SER LYS
SEQRES   1 I   15  VAL GLY SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN
SEQRES   2 I   15  TYR ALA
SEQRES   1 J  192  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR
SEQRES   2 J  192  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE
SEQRES   3 J  192  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS
SEQRES   4 J  192  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA
SEQRES   5 J  192  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA VAL
SEQRES   6 J  192  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN
SEQRES   7 J  192  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL
SEQRES   8 J  192  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL
SEQRES   9 J  192  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL
SEQRES  10 J  192  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR
SEQRES  11 J  192  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS
SEQRES  12 J  192  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER
SEQRES  13 J  192  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY
SEQRES  14 J  192  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA
SEQRES  15 J  192  PRO SER PRO LEU PRO GLU THR THR GLU ASN
SEQRES   1 K  198  GLY ASP THR ARG PRO ARG PHE LEU TRP GLN LEU LYS PHE
SEQRES   2 K  198  GLU CYS HIS PHE PHE ASN GLY THR GLU ARG VAL ARG LEU
SEQRES   3 K  198  LEU GLU ARG CYS ILE TYR ASN GLN GLU GLU SER VAL ARG
SEQRES   4 K  198  PHE ASP SER ASP VAL GLY GLU TYR ARG ALA VAL THR GLU
SEQRES   5 K  198  LEU GLY ARG PRO ASP ALA GLU TYR TRP ASN SER GLN LYS
SEQRES   6 K  198  ASP LEU LEU GLU GLN ARG ARG ALA ALA VAL ASP THR TYR
SEQRES   7 K  198  CYS ARG HIS ASN TYR GLY VAL GLY GLU SER PHE THR VAL
SEQRES   8 K  198  GLN ARG ARG VAL GLU PRO LYS VAL THR VAL TYR PRO SER
SEQRES   9 K  198  LYS THR GLN PRO LEU GLN HIS HIS ASN LEU LEU VAL CYS
SEQRES  10 K  198  SER VAL SER GLY PHE TYR PRO GLY SER ILE GLU VAL ARG
SEQRES  11 K  198  TRP PHE ARG ASN GLY GLN GLU GLU LYS ALA GLY VAL VAL
SEQRES  12 K  198  SER THR GLY LEU ILE GLN ASN GLY ASP TRP THR PHE GLN
SEQRES  13 K  198  THR LEU VAL MET LEU GLU THR VAL PRO ARG SER GLY GLU
SEQRES  14 K  198  VAL TYR THR CYS GLN VAL GLU HIS PRO SER VAL THR SER
SEQRES  15 K  198  PRO LEU THR VAL GLU TRP ARG ALA ARG SER GLU SER ALA
SEQRES  16 K  198  GLN SER LYS
SEQRES   1 L   15  VAL GLY SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN
SEQRES   2 L   15  TYR ALA
FORMUL  13  HOH   *152(H2 O)
HELIX    1   1 GLU A   46  PHE A   48  5                                   3
HELIX    2   2 ALA A   56  ARG A   76  1                                  21
HELIX    3   3 GLU B   52  SER B   63  5                                  12
HELIX    4   4 LYS B   65  ARG B   72  1                                   8
HELIX    5   5 ALA B   74  THR B   77  1                                   4
HELIX    6   6 CYS B   79  GLY B   86  1                                   8
HELIX    7   7 GLU D   46  ARG D   50  5                                   5
HELIX    8   8 ALA D   56  ARG D   76  1                                  21
HELIX    9   9 GLU E   52  SER E   63  1                                  12
HELIX   10  10 LYS E   65  THR E   77  1                                  13
HELIX   11  11 CYS E   79  GLY E   86  1                                   8
HELIX   12  12 GLU G   46  ARG G   50  5                                   5
HELIX   13  13 ALA G   56  ARG G   76  1                                  21
HELIX   14  14 GLU H   52  SER H   63  5                                  12
HELIX   15  15 LYS H   65  THR H   77  1                                  13
HELIX   16  16 CYS H   79  PHE H   89  1                                  11
HELIX   17  17 GLU J   46  ARG J   50  5                                   5
HELIX   18  18 ALA J   56  ARG J   76  1                                  21
HELIX   19  19 GLU K   52  SER K   63  5                                  12
HELIX   20  20 ASP K   66  THR K   77  1                                  12
HELIX   21  21 CYS K   79  GLY K   86  1                                   8
SHEET    1   A 4 ILE A   7  LEU A  14  0
SHEET    2   A 4 SER A  19  PHE A  26 -1  N  ASP A  25   O  ILE A   8
SHEET    3   A 4 ASP A  29  ASP A  35 -1  N  PHE A  32   O  PHE A  24
SHEET    4   A 4 GLU A  40  TRP A  43 -1  N  VAL A  42   O  HIS A  33
SHEET    1   B 3 GLU A  88  THR A  93  0
SHEET    2   B 3 PRO A 102  PHE A 112 -1  N  ASP A 110   O  GLU A  88
SHEET    3   B 3 PHE A 145  LEU A 154 -1  N  PHE A 153   O  ASN A 103
SHEET    1   C 4 LYS A 126  VAL A 128  0
SHEET    2   C 4 ASN A 118  ARG A 123 -1  N  ARG A 123   O  LYS A 126
SHEET    3   C 4 TYR A 161  GLU A 166 -1  N  GLU A 166   O  ASN A 118
SHEET    4   C 4 LEU A 174  TRP A 178 -1  N  TRP A 178   O  TYR A 161
SHEET    1   D 4 TRP B   9  PHE B  18  0
SHEET    2   D 4 ARG B  23  TYR B  32 -1  N  ILE B  31   O  GLN B  10
SHEET    3   D 4 GLU B  35  ASP B  41 -1  N  PHE B  40   O  GLU B  28
SHEET    4   D 4 TYR B  47  ALA B  49 -1  N  ARG B  48   O  ARG B  39
SHEET    1   E 4 LYS B  98  PRO B 103  0
SHEET    2   E 4 HIS B 112  PHE B 122 -1  N  SER B 120   O  LYS B  98
SHEET    3   E 4 PHE B 155  VAL B 164 -1  N  THR B 163   O  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 3 GLU B 128  ARG B 133  0
SHEET    2   F 3 VAL B 170  GLU B 176 -1  N  GLU B 176   O  GLU B 128
SHEET    3   F 3 LEU B 184  ARG B 189 -1  N  TRP B 188   O  TYR B 171
SHEET    1   G 4 ILE D   7  LEU D  14  0
SHEET    2   G 4 SER D  19  PHE D  26 -1  N  ASP D  25   O  ILE D   8
SHEET    3   G 4 ASP D  29  ASP D  35 -1  N  PHE D  32   O  PHE D  24
SHEET    4   G 4 GLU D  40  TRP D  43 -1  N  VAL D  42   O  HIS D  33
SHEET    1   H 3 GLU D  88  THR D  93  0
SHEET    2   H 3 PRO D 102  PHE D 112 -1  N  ASP D 110   O  GLU D  88
SHEET    3   H 3 PHE D 145  LEU D 154 -1  N  PHE D 153   O  ASN D 103
SHEET    1   I 4 LYS D 126  VAL D 128  0
SHEET    2   I 4 ASN D 118  ARG D 123 -1  N  ARG D 123   O  LYS D 126
SHEET    3   I 4 TYR D 161  GLU D 166 -1  N  GLU D 166   O  ASN D 118
SHEET    4   I 4 LEU D 174  TRP D 178 -1  N  TRP D 178   O  TYR D 161
SHEET    1   J 4 TRP E   9  PHE E  18  0
SHEET    2   J 4 ARG E  23  TYR E  32 -1  N  ILE E  31   O  GLN E  10
SHEET    3   J 4 GLU E  35  ASP E  41 -1  N  PHE E  40   O  GLU E  28
SHEET    4   J 4 GLU E  46  ALA E  49 -1  N  ARG E  48   O  ARG E  39
SHEET    1   K 4 LYS E  98  PRO E 103  0
SHEET    2   K 4 HIS E 112  PHE E 122 -1  N  SER E 120   O  LYS E  98
SHEET    3   K 4 PHE E 155  VAL E 164 -1  N  THR E 163   O  ASN E 113
SHEET    4   K 4 VAL E 142  SER E 144 -1  N  VAL E 143   O  MET E 160
SHEET    1   L 3 ILE E 127  ARG E 133  0
SHEET    2   L 3 VAL E 170  HIS E 177 -1  N  GLU E 176   O  GLU E 128
SHEET    3   L 3 LEU E 184  ARG E 189 -1  N  TRP E 188   O  TYR E 171
SHEET    1   M 4 ILE G   7  LEU G  14  0
SHEET    2   M 4 SER G  19  PHE G  26 -1  N  ASP G  25   O  ILE G   8
SHEET    3   M 4 ASP G  29  ASP G  35 -1  N  PHE G  32   O  PHE G  24
SHEET    4   M 4 GLU G  40  TRP G  43 -1  N  VAL G  42   O  HIS G  33
SHEET    1   N 3 GLU G  88  THR G  93  0
SHEET    2   N 3 PRO G 102  PHE G 112 -1  N  ASP G 110   O  GLU G  88
SHEET    3   N 3 PHE G 145  LEU G 154 -1  N  PHE G 153   O  ASN G 103
SHEET    1   O 4 LYS G 126  VAL G 128  0
SHEET    2   O 4 ASN G 118  ARG G 123 -1  N  ARG G 123   O  LYS G 126
SHEET    3   O 4 TYR G 161  GLU G 166 -1  N  GLU G 166   O  ASN G 118
SHEET    4   O 4 LEU G 174  TRP G 178 -1  N  TRP G 178   O  TYR G 161
SHEET    1   P 4 TRP H   9  PHE H  18  0
SHEET    2   P 4 ARG H  23  TYR H  32 -1  N  ILE H  31   O  GLN H  10
SHEET    3   P 4 GLU H  35  ASP H  41 -1  N  PHE H  40   O  GLU H  28
SHEET    4   P 4 TYR H  47  ALA H  49 -1  N  ARG H  48   O  ARG H  39
SHEET    1   Q 4 LYS H  98  PRO H 103  0
SHEET    2   Q 4 HIS H 112  PHE H 122 -1  N  SER H 120   O  LYS H  98
SHEET    3   Q 4 PHE H 155  VAL H 164 -1  N  THR H 163   O  ASN H 113
SHEET    4   Q 4 VAL H 142  SER H 144 -1  N  VAL H 143   O  MET H 160
SHEET    1   R 3 ILE H 127  ARG H 133  0
SHEET    2   R 3 VAL H 170  HIS H 177 -1  N  GLU H 176   O  GLU H 128
SHEET    3   R 3 LEU H 184  ARG H 189 -1  N  TRP H 188   O  TYR H 171
SHEET    1   S 4 ILE J   7  LEU J  14  0
SHEET    2   S 4 SER J  19  PHE J  26 -1  N  ASP J  25   O  ILE J   8
SHEET    3   S 4 ASP J  29  ASP J  35 -1  N  PHE J  32   O  PHE J  24
SHEET    4   S 4 GLU J  40  TRP J  43 -1  N  VAL J  42   O  HIS J  33
SHEET    1   T 3 GLU J  88  THR J  93  0
SHEET    2   T 3 PRO J 102  PHE J 112 -1  N  ASP J 110   O  GLU J  88
SHEET    3   T 3 PHE J 145  LEU J 154 -1  N  PHE J 153   O  ASN J 103
SHEET    1   U 4 LYS J 126  VAL J 128  0
SHEET    2   U 4 ASN J 118  ARG J 123 -1  N  ARG J 123   O  LYS J 126
SHEET    3   U 4 TYR J 161  GLU J 166 -1  N  GLU J 166   O  ASN J 118
SHEET    4   U 4 LEU J 174  TRP J 178 -1  N  TRP J 178   O  TYR J 161
SHEET    1   V 4 TRP K   9  PHE K  18  0
SHEET    2   V 4 ARG K  23  TYR K  32 -1  N  ILE K  31   O  GLN K  10
SHEET    3   V 4 GLU K  35  ASP K  41 -1  N  PHE K  40   O  GLU K  28
SHEET    4   V 4 TYR K  47  ALA K  49 -1  N  ARG K  48   O  ARG K  39
SHEET    1   W 4 LYS K  98  PRO K 103  0
SHEET    2   W 4 HIS K 112  PHE K 122 -1  N  SER K 120   O  LYS K  98
SHEET    3   W 4 PHE K 155  VAL K 164 -1  N  THR K 163   O  ASN K 113
SHEET    4   W 4 VAL K 142  SER K 144 -1  N  VAL K 143   O  MET K 160
SHEET    1   X 3 ILE K 127  ARG K 133  0
SHEET    2   X 3 VAL K 170  HIS K 177 -1  N  GLU K 176   O  GLU K 128
SHEET    3   X 3 LEU K 184  ARG K 189 -1  N  TRP K 188   O  TYR K 171
SSBOND   1 CYS A  107    CYS A  163                          1555   1555  2.02
SSBOND   2 CYS B   15    CYS B   79                          1555   1555  2.09
SSBOND   3 CYS B  117    CYS B  173                          1555   1555  2.02
SSBOND   4 CYS D  107    CYS D  163                          1555   1555  2.05
SSBOND   5 CYS E   15    CYS E   79                          1555   1555  2.08
SSBOND   6 CYS E  117    CYS E  173                          1555   1555  2.04
SSBOND   7 CYS G  107    CYS G  163                          1555   1555  2.05
SSBOND   8 CYS H   15    CYS H   79                          1555   1555  2.09
SSBOND   9 CYS H  117    CYS H  173                          1555   1555  2.01
SSBOND  10 CYS J  107    CYS J  163                          1555   1555  2.03
SSBOND  11 CYS K   15    CYS K   79                          1555   1555  2.07
SSBOND  12 CYS K  117    CYS K  173                          1555   1555  2.02
CISPEP   1 ASN A   15    PRO A   16          0        -1.04
CISPEP   2 THR A  113    PRO A  114          0         1.69
CISPEP   3 TYR B  123    PRO B  124          0        -0.39
CISPEP   4 ASN D   15    PRO D   16          0         1.00
CISPEP   5 THR D  113    PRO D  114          0         0.99
CISPEP   6 TYR E  123    PRO E  124          0        -2.25
CISPEP   7 ASN G   15    PRO G   16          0         0.08
CISPEP   8 THR G  113    PRO G  114          0         3.25
CISPEP   9 TYR H  123    PRO H  124          0         1.60
CISPEP  10 ASN J   15    PRO J   16          0         0.16
CISPEP  11 THR J  113    PRO J  114          0         0.56
CISPEP  12 TYR K  123    PRO K  124          0         3.62
CRYST1  134.514  134.320  131.232  90.00 104.82  90.00 C 1 2 1      16
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      0.007434  0.000000  0.001967        0.00000
SCALE2      0.000000  0.007445  0.000000        0.00000
SCALE3      0.000000  0.000000  0.007882        0.00000
MTRIX1   1 -0.791910  0.532550  0.298770       27.22638    1
MTRIX2   1  0.515170  0.320000  0.795110      -39.64445    1
MTRIX3   1  0.327830  0.783580 -0.527770       49.03718    1
MTRIX1   2  0.004580 -0.999410 -0.034070       45.13230    1
MTRIX2   2  0.999300  0.005840 -0.036830      -22.11342    1
MTRIX3   2  0.037000 -0.033880  0.998740      -61.74336    1
MTRIX1   3 -0.518980 -0.340980 -0.783830       83.35107    1
MTRIX2   3 -0.799160  0.518960  0.303360        3.81720    1
MTRIX3   3  0.303340  0.783840 -0.541830      -10.51804    1
      
PROCHECK
Go to PROCHECK summary
 References