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PDBsum entry 3ima

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Hydrolase/hydrolase inhibitor PDB id
3ima
Jmol
Contents
Protein chains
212 a.a.
84 a.a.
Ligands
ACT ×3
Waters ×576
HEADER    HYDROLASE/HYDROLASE INHIBITOR           10-AUG-09   3IMA
TITLE     COMPLEX STRCUTURE OF TAROCYSTATIN AND PAPAIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PAPAIN;
COMPND   3 CHAIN: A, C;
COMPND   4 FRAGMENT: PAPAIN DOMAIN;
COMPND   5 SYNONYM: PAPAYA PROTEINASE I, PPI;
COMPND   6 EC: 3.4.22.2;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: CYSTEINE PROTEINASE INHIBITOR;
COMPND   9 CHAIN: B, D;
COMPND  10 FRAGMENT: N-TERMINAL DOMAIN, UNP RESIDUES 2-92;
COMPND  11 SYNONYM: TAROCYSTATIN, CECPI;
COMPND  12 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: CARICA PAPAYA;
SOURCE   3 ORGANISM_COMMON: MAMON;
SOURCE   4 ORGANISM_TAXID: 3649;
SOURCE   5 OTHER_DETAILS: PAPAIN WAS PURCHASED FROM SIGMA CO. FOR CO-
SOURCE   6 CRYSTALLIZATION WITH CECPI.;
SOURCE   7 MOL_ID: 2;
SOURCE   8 ORGANISM_SCIENTIFIC: COLOCASIA ESCULENTA;
SOURCE   9 ORGANISM_COMMON: COCOYAM,DASHEEN,EDDO,ELEPHANT'S EAR,KALO,
SOURCE  10 MALANGA;
SOURCE  11 ORGANISM_TAXID: 4460;
SOURCE  12 GENE: CPI;
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: E.COLI BL21 (DE3);
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  17 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-1
KEYWDS    CYSTATIN, TAROCYSTATIN, CECPI, PAPAIN, PHYTOCYSTATIN,
KEYWDS   2 ALLERGEN, DISULFIDE BOND, HYDROLASE, PROTEASE, THIOL
KEYWDS   3 PROTEASE, ZYMOGEN, PROTEASE INHIBITOR, THIOL PROTEASE
KEYWDS   4 INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    M.H.CHU,K.L.LIU,K.W.YEH,Y.S.CHENG
REVDAT   1   16-FEB-10 3IMA    0
JRNL        AUTH   M.H.CHU,K.L.LIU,K.W.YEH,Y.S.CHENG
JRNL        TITL   COMPLEX STRCUTURE OF TAROCYSTATIN AND PAPAIN
JRNL        REF    TO BE PUBLISHED
JRNL        REFN
REMARK   2
REMARK   2 RESOLUTION.    2.03 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.1
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.03
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.89
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 98515.520
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.8
REMARK   3   NUMBER OF REFLECTIONS             : 37691
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) : 0.182
REMARK   3   FREE R VALUE                     : 0.233
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 3804
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 6
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.03
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.30
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5104
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2300
REMARK   3   BIN FREE R VALUE                    : 0.2860
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.20
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 579
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 4657
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 12
REMARK   3   SOLVENT ATOMS            : 576
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 10.60
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.70
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 5.23000
REMARK   3    B22 (A**2) : -0.87000
REMARK   3    B33 (A**2) : -4.37000
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  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.21
REMARK   3   ESD FROM SIGMAA              (A) : 0.18
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) : 0.27
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.23
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.012
REMARK   3   BOND ANGLES            (DEGREES) : 1.70
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.90
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.33
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) : 1.330 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.010 ; 2.000
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.190 ; 2.000
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.220 ; 2.500
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : FLAT MODEL
REMARK   3   KSOL        : 0.36
REMARK   3   BSOL        : 55.13
REMARK   3
REMARK   3  NCS MODEL : NONE
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM
REMARK   3  PARAMETER FILE  3  : ACT.PARAM
REMARK   3  PARAMETER FILE  4  : NULL
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP
REMARK   3  TOPOLOGY FILE  3   : ACT.TOP
REMARK   3  TOPOLOGY FILE  4   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3IMA COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-AUG-09.
REMARK 100 THE RCSB ID CODE IS RCSB054588.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 26-MAR-08
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 4.6
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : NSRRC
REMARK 200  BEAMLINE                       : BL13C1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97315
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39400
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.030
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0
REMARK 200  DATA REDUNDANCY                : 5.700
REMARK 200  R MERGE                    (I) : 0.10000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.10
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.7
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : 0.41000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1PPN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG MME 2000, 0.1M SODIUM
REMARK 280  ACETATE TRIHYDRATE PH 4.6, 0.2M AMMONIUM SULFATE, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K
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       18.03000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.79500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.86000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.79500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       18.03000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.86000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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     VAL B    10
REMARK 465     GLU B    11
REMARK 465     GLY B    12
REMARK 465     ALA B    13
REMARK 465     GLN B    14
REMARK 465     ASN B    15
REMARK 465     ILE B    92
REMARK 465     VAL D    10
REMARK 465     GLU D    11
REMARK 465     GLY D    12
REMARK 465     ALA D    13
REMARK 465     GLN D    14
REMARK 465     ASN D    15
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    ARG A  93     -166.15   -123.40
REMARK 500    VAL B  51     -141.81   -132.25
REMARK 500    CYS C 153      142.95    176.01
REMARK 500    ASP C 158       -0.61   -152.91
REMARK 500    LEU D   3      -65.57    -23.21
REMARK 500    ALA D  17      -86.90     72.24
REMARK 500    ARG D  42      157.40    177.93
REMARK 500    VAL D  51     -140.83   -129.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH D 293        DISTANCE =  5.64 ANGSTROMS
REMARK 525    HOH D 294        DISTANCE =  7.27 ANGSTROMS
REMARK 525    HOH A 261        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH A 262        DISTANCE =  5.15 ANGSTROMS
REMARK 525    HOH A 266        DISTANCE =  5.59 ANGSTROMS
REMARK 525    HOH B 483        DISTANCE =  5.31 ANGSTROMS
REMARK 525    HOH B 504        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH C 357        DISTANCE =  5.62 ANGSTROMS
REMARK 525    HOH C 404        DISTANCE =  5.83 ANGSTROMS
REMARK 525    HOH A 388        DISTANCE =  6.96 ANGSTROMS
REMARK 525    HOH A 395        DISTANCE =  6.08 ANGSTROMS
REMARK 525    HOH A 449        DISTANCE =  5.62 ANGSTROMS
REMARK 525    HOH A 497        DISTANCE =  5.14 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 300
DBREF  3IMA A    1   212  UNP    P00784   PAPA1_CARPA    134    345
DBREF  3IMA B    2    92  UNP    Q8L5J8   Q8L5J8_COLES     2     92
DBREF  3IMA C    1   212  UNP    P00784   PAPA1_CARPA    134    345
DBREF  3IMA D    2    92  UNP    Q8L5J8   Q8L5J8_COLES     2     92
SEQRES   1 A  212  ILE PRO GLU TYR VAL ASP TRP ARG GLN LYS GLY ALA VAL
SEQRES   2 A  212  THR PRO VAL LYS ASN GLN GLY SER CYS GLY SER OCS TRP
SEQRES   3 A  212  ALA PHE SER ALA VAL VAL THR ILE GLU GLY ILE ILE LYS
SEQRES   4 A  212  ILE ARG THR GLY ASN LEU ASN GLU TYR SER GLU GLN GLU
SEQRES   5 A  212  LEU LEU ASP CYS ASP ARG ARG SER TYR GLY CYS ASN GLY
SEQRES   6 A  212  GLY TYR PRO TRP SER ALA LEU GLN LEU VAL ALA GLN TYR
SEQRES   7 A  212  GLY ILE HIS TYR ARG ASN THR TYR PRO TYR GLU GLY VAL
SEQRES   8 A  212  GLN ARG TYR CYS ARG SER ARG GLU LYS GLY PRO TYR ALA
SEQRES   9 A  212  ALA LYS THR ASP GLY VAL ARG GLN VAL GLN PRO TYR ASN
SEQRES  10 A  212  GLU GLY ALA LEU LEU TYR SER ILE ALA ASN GLN PRO VAL
SEQRES  11 A  212  SER VAL VAL LEU GLU ALA ALA GLY LYS ASP PHE GLN LEU
SEQRES  12 A  212  TYR ARG GLY GLY ILE PHE VAL GLY PRO CYS GLY ASN LYS
SEQRES  13 A  212  VAL ASP HIS ALA VAL ALA ALA VAL GLY TYR GLY PRO ASN
SEQRES  14 A  212  TYR ILE LEU ILE LYS ASN SER TRP GLY THR GLY TRP GLY
SEQRES  15 A  212  GLU ASN GLY TYR ILE ARG ILE LYS ARG GLY THR GLY ASN
SEQRES  16 A  212  SER TYR GLY VAL CYS GLY LEU TYR THR SER SER PHE TYR
SEQRES  17 A  212  PRO VAL LYS ASN
SEQRES   1 B   91  ALA LEU MET GLY GLY ILE VAL ASP VAL GLU GLY ALA GLN
SEQRES   2 B   91  ASN SER ALA GLU VAL GLU GLU LEU ALA ARG PHE ALA VAL
SEQRES   3 B   91  ASP GLU HIS ASN LYS LYS GLU ASN ALA LEU LEU GLN PHE
SEQRES   4 B   91  SER ARG LEU VAL LYS ALA LYS GLN GLN VAL VAL SER GLY
SEQRES   5 B   91  ILE MET HIS HIS LEU THR VAL GLU VAL ILE GLU GLY GLY
SEQRES   6 B   91  LYS LYS LYS VAL TYR GLU ALA LYS VAL TRP VAL GLN ALA
SEQRES   7 B   91  TRP LEU ASN SER LYS LYS LEU HIS GLU PHE SER PRO ILE
SEQRES   1 C  212  ILE PRO GLU TYR VAL ASP TRP ARG GLN LYS GLY ALA VAL
SEQRES   2 C  212  THR PRO VAL LYS ASN GLN GLY SER CYS GLY SER OCS TRP
SEQRES   3 C  212  ALA PHE SER ALA VAL VAL THR ILE GLU GLY ILE ILE LYS
SEQRES   4 C  212  ILE ARG THR GLY ASN LEU ASN GLU TYR SER GLU GLN GLU
SEQRES   5 C  212  LEU LEU ASP CYS ASP ARG ARG SER TYR GLY CYS ASN GLY
SEQRES   6 C  212  GLY TYR PRO TRP SER ALA LEU GLN LEU VAL ALA GLN TYR
SEQRES   7 C  212  GLY ILE HIS TYR ARG ASN THR TYR PRO TYR GLU GLY VAL
SEQRES   8 C  212  GLN ARG TYR CYS ARG SER ARG GLU LYS GLY PRO TYR ALA
SEQRES   9 C  212  ALA LYS THR ASP GLY VAL ARG GLN VAL GLN PRO TYR ASN
SEQRES  10 C  212  GLU GLY ALA LEU LEU TYR SER ILE ALA ASN GLN PRO VAL
SEQRES  11 C  212  SER VAL VAL LEU GLU ALA ALA GLY LYS ASP PHE GLN LEU
SEQRES  12 C  212  TYR ARG GLY GLY ILE PHE VAL GLY PRO CYS GLY ASN LYS
SEQRES  13 C  212  VAL ASP HIS ALA VAL ALA ALA VAL GLY TYR GLY PRO ASN
SEQRES  14 C  212  TYR ILE LEU ILE LYS ASN SER TRP GLY THR GLY TRP GLY
SEQRES  15 C  212  GLU ASN GLY TYR ILE ARG ILE LYS ARG GLY THR GLY ASN
SEQRES  16 C  212  SER TYR GLY VAL CYS GLY LEU TYR THR SER SER PHE TYR
SEQRES  17 C  212  PRO VAL LYS ASN
SEQRES   1 D   91  ALA LEU MET GLY GLY ILE VAL ASP VAL GLU GLY ALA GLN
SEQRES   2 D   91  ASN SER ALA GLU VAL GLU GLU LEU ALA ARG PHE ALA VAL
SEQRES   3 D   91  ASP GLU HIS ASN LYS LYS GLU ASN ALA LEU LEU GLN PHE
SEQRES   4 D   91  SER ARG LEU VAL LYS ALA LYS GLN GLN VAL VAL SER GLY
SEQRES   5 D   91  ILE MET HIS HIS LEU THR VAL GLU VAL ILE GLU GLY GLY
SEQRES   6 D   91  LYS LYS LYS VAL TYR GLU ALA LYS VAL TRP VAL GLN ALA
SEQRES   7 D   91  TRP LEU ASN SER LYS LYS LEU HIS GLU PHE SER PRO ILE
MODRES 3IMA OCS A   25  CYS  CYSTEINESULFONIC ACID
MODRES 3IMA OCS C   25  CYS  CYSTEINESULFONIC ACID
HET    OCS  A  25       9
HET    OCS  C  25       9
HET    ACT  A 300       4
HET    ACT  A 301       4
HET    ACT  C 300       4
HETNAM     OCS CYSTEINESULFONIC ACID
HETNAM     ACT ACETATE ION
FORMUL   1  OCS    2(C3 H7 N O5 S)
FORMUL   5  ACT    3(C2 H3 O2 1-)
FORMUL   8  HOH   *576(H2 O)
HELIX    1   1 SER A   24  GLY A   43  1                                  20
HELIX    2   2 SER A   49  ASP A   57  1                                   9
HELIX    3   3 TYR A   61  GLY A   65  5                                   5
HELIX    4   4 TYR A   67  GLY A   79  1                                  13
HELIX    5   5 ARG A   96  GLY A  101  1                                   6
HELIX    6   6 ASN A  117  GLN A  128  1                                  12
HELIX    7   7 GLY A  138  TYR A  144  1                                   7
HELIX    8   8 GLY A  198  LEU A  202  5                                   5
HELIX    9   9 SER B   16  ASN B   35  1                                  20
HELIX   10  10 ALA B   79  ASN B   82  5                                   4
HELIX   11  11 SER C   24  GLY C   43  1                                  20
HELIX   12  12 SER C   49  ASP C   57  1                                   9
HELIX   13  13 TYR C   61  GLY C   65  5                                   5
HELIX   14  14 TYR C   67  TYR C   78  1                                  12
HELIX   15  15 ARG C   96  LYS C  100  5                                   5
HELIX   16  16 ASN C  117  GLN C  128  1                                  12
HELIX   17  17 GLY C  138  LEU C  143  1                                   6
HELIX   18  18 GLY C  198  LEU C  202  5                                   5
HELIX   19  19 ALA D   17  ASN D   35  1                                  19
HELIX   20  20 ALA D   79  ASN D   82  5                                   4
SHEET    1   A 3 VAL A   5  ASP A   6  0
SHEET    2   A 3 HIS A 159  GLY A 167 -1  O  TYR A 166   N  VAL A   5
SHEET    3   A 3 VAL A 130  LEU A 134 -1  N  VAL A 132   O  VAL A 161
SHEET    1   B 5 VAL A   5  ASP A   6  0
SHEET    2   B 5 HIS A 159  GLY A 167 -1  O  TYR A 166   N  VAL A   5
SHEET    3   B 5 TYR A 170  LYS A 174 -1  O  LYS A 174   N  ALA A 162
SHEET    4   B 5 TYR A 186  LYS A 190 -1  O  ILE A 187   N  ILE A 173
SHEET    5   B 5 ILE A 148  PHE A 149  1  N  PHE A 149   O  LYS A 190
SHEET    1   C 2 GLY A 109  GLN A 112  0
SHEET    2   C 2 PHE A 207  VAL A 210 -1  O  VAL A 210   N  GLY A 109
SHEET    1   D 5 ILE B   7  VAL B   8  0
SHEET    2   D 5 GLN B  39  VAL B  50 -1  O  GLN B  48   N  VAL B   8
SHEET    3   D 5 ILE B  54  GLU B  64 -1  O  THR B  59   N  LYS B  45
SHEET    4   D 5 LYS B  67  GLN B  78 -1  O  VAL B  77   N  ILE B  54
SHEET    5   D 5 SER B  83  SER B  90 -1  O  SER B  90   N  GLU B  72
SHEET    1   E 3 VAL C   5  ASP C   6  0
SHEET    2   E 3 HIS C 159  GLY C 167 -1  O  TYR C 166   N  VAL C   5
SHEET    3   E 3 VAL C 130  LEU C 134 -1  N  VAL C 132   O  VAL C 161
SHEET    1   F 5 VAL C   5  ASP C   6  0
SHEET    2   F 5 HIS C 159  GLY C 167 -1  O  TYR C 166   N  VAL C   5
SHEET    3   F 5 TYR C 170  LYS C 174 -1  O  TYR C 170   N  GLY C 167
SHEET    4   F 5 TYR C 186  LYS C 190 -1  O  ILE C 187   N  ILE C 173
SHEET    5   F 5 ILE C 148  PHE C 149  1  N  PHE C 149   O  ARG C 188
SHEET    1   G 2 GLY C 109  GLN C 112  0
SHEET    2   G 2 PHE C 207  VAL C 210 -1  O  TYR C 208   N  ARG C 111
SHEET    1   H 5 ILE D   7  VAL D   8  0
SHEET    2   H 5 GLN D  39  VAL D  50 -1  O  GLN D  48   N  VAL D   8
SHEET    3   H 5 ILE D  54  GLU D  64 -1  O  MET D  55   N  GLN D  49
SHEET    4   H 5 LYS D  67  GLN D  78 -1  O  TYR D  71   N  VAL D  60
SHEET    5   H 5 SER D  83  PRO D  91 -1  O  SER D  90   N  GLU D  72
SSBOND   1 CYS A   22    CYS A   63                          1555   1555  2.04
SSBOND   2 CYS A   56    CYS A   95                          1555   1555  2.05
SSBOND   3 CYS A  153    CYS A  200                          1555   1555  2.05
SSBOND   4 CYS C   22    CYS C   63                          1555   1555  2.04
SSBOND   5 CYS C   56    CYS C   95                          1555   1555  2.05
SSBOND   6 CYS C  153    CYS C  200                          1555   1555  2.03
LINK         C   SER A  24                 N   OCS A  25     1555   1555  1.32
LINK         C   OCS A  25                 N   TRP A  26     1555   1555  1.34
LINK         C   SER C  24                 N   OCS C  25     1555   1555  1.32
LINK         C   OCS C  25                 N   TRP C  26     1555   1555  1.33
CISPEP   1 GLY A  151    PRO A  152          0         0.06
CISPEP   2 GLY C  151    PRO C  152          0        -0.26
SITE     1 AC1  2 ASN A  18  ARG A  83
SITE     1 AC2  4 ARG A 111  GLN A 112  ARG A 188  HOH A 385
SITE     1 AC3  3 LYS C  17  ARG C  83  HOH C 219
CRYST1   36.060   99.720  165.590  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      0.027732  0.000000  0.000000        0.00000
SCALE2      0.000000  0.010028  0.000000        0.00000
SCALE3      0.000000  0.000000  0.006039        0.00000
      
PROCHECK
Go to PROCHECK summary
 References