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LongText Report for: 1JMY-pdb

Name Class
1JMY-pdb
HEADER    HYDROLASE                               20-JUL-01   1JMY
TITLE     TRUNCATED RECOMBINANT HUMAN BILE SALT STIMULATED LIPASE
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: BILE-SALT-ACTIVATED LIPASE;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: 1-518;
COMPND   5 EC: 3.1.1.3;
COMPND   6 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE   5 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE   6 EXPRESSION_SYSTEM_CELL_LINE: KIDNEY CELLS;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PNUT
KEYWDS    BSSL, BSDL, BILE SALT DEPENDENT LIPASE, BILE SALT
KEYWDS   2 STIMULATED LIPASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.A.MOORE,R.L.KINGSTON,K.M.LOOMES,O.HERNELL,L.BLACKBERG,
AUTHOR   2 H.M.BAKER,E.N.BAKER
REVDAT   2   26-SEP-01 1JMY    1       JRNL
REVDAT   1   08-AUG-01 1JMY    0
JRNL        AUTH   S.A.MOORE,R.L.KINGSTON,K.M.LOOMES,O.HERNELL,
JRNL        AUTH 2 L.BLACKBERG,H.M.BAKER,E.N.BAKER
JRNL        TITL   THE STRUCTURE OF TRUNCATED RECOMBINANT HUMAN BILE
JRNL        TITL 2 SALT-STIMULATED LIPASE REVEALS BILE
JRNL        TITL 3 SALT-INDEPENDENT CONFORMATIONAL FLEXIBILITY AT THE
JRNL        TITL 4 ACTIVE-SITE LOOP AND PROVIDES INSIGHTS INTO
JRNL        TITL 5 HEPARIN BINDING
JRNL        REF    J.MOL.BIOL.                   V. 312   511 2001
JRNL        REFN   ASTM JMOBAK  UK ISSN 0022-2836
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF
REMARK   1  TITL 2 NATIVE AND RECOMBINANT HUMAN BILE-SALT DEPENDENT
REMARK   1  TITL 3 LIPASE: STRATEGIES FOR IMPROVEMENT OF DIFFRACTION
REMARK   1  TITL 4 QUALITY
REMARK   1  REF    ACTA CRYSTALLOGR., SECT.D     V.  56   478 2000
REMARK   1  REFN   ASTM ABCRE6  DK ISSN 0907-4449
REMARK   2
REMARK   2 RESOLUTION. 2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.0
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 AND HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.6
REMARK   3   NUMBER OF REFLECTIONS             : 15613
REMARK   3
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : FREER
REMARK   3   FREE R VALUE TEST SET SELECTION  : 10% OF THE REFLECTION
REMARK   3                                      SET, RANDOMLY CHOSEN
REMARK   3   R VALUE            (WORKING SET) : 0.236
REMARK   3   FREE R VALUE                     : 0.276
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 1570
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           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
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            : 3990
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 5
REMARK   3   SOLVENT ATOMS            : 63
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 45.00
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.00
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 11.33000
REMARK   3    B22 (A**2) : 16.34600
REMARK   3    B33 (A**2) : -27.68200
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) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : TIGHTLY RESTRAINED INDIVIDUAL
REMARK   3                            B'S
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
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  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 1JMY COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-2001.
REMARK 100 THE RCSB ID CODE IS RCSB013953.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 1996
REMARK 200  TEMPERATURE           (KELVIN) : 113.0
REMARK 200  PH                             : 6.70
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : N
REMARK 200  RADIATION SOURCE               : ROTATING ANODE
REMARK 200  BEAMLINE                       : NULL
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU 200
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418
REMARK 200  MONOCHROMATOR                  : GRAPHITE PLUS 0.1 MM
REMARK 200                                   COLLIMATOR
REMARK 200  OPTICS                         : GRAPHITE MONOCHROMATOR
REMARK 200
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15613
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.6
REMARK 200  DATA REDUNDANCY                : 3.200
REMARK 200  R MERGE                    (I) : 0.10000
REMARK 200  R SYM                      (I) : 0.10000
REMARK 200   FOR THE DATA SET  : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000
REMARK 200  R SYM FOR SHELL            (I) : 0.35000
REMARK 200   FOR SHELL         : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
REMARK 200  REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: TRUNCATED CORE OF ACETYLCHOLINESTERASE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG-6000, PIPES/KOH, GLYCEROL
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   1/2-X,-Y,1/2+Z
REMARK 290       3555   -X,1/2+Y,1/2-Z
REMARK 290       4555   1/2+X,1/2-Y,-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       29.32000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       51.63000
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.04000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       51.63000
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.32000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.04000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 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     PRO A   273
REMARK 465     LEU A   274
REMARK 465     ALA A   275
REMARK 465     GLY A   276
REMARK 465     LEU A   277
REMARK 465     GLU A   278
REMARK 465     TYR A   279
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     LYS A  19    CG    CD    CE    NZ
REMARK 470     TYR A 123    CG    CD1   CD2   CE1   CE2   CZ    OH
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
REMARK 500   CG2  THR A   316     O    HOH     867              1.90
REMARK 500   N    ARG A    91     O    HOH     862              1.97
REMARK 500   O    HOH     833     O    HOH     860              2.19
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    ASP A  97   OD2   ASP A  97   CG     0.079
REMARK 500    LEU A 282   C     LEU A 282   CA    -0.040
REMARK 500    THR A 316   CG2   THR A 316   CB    -0.128
REMARK 500    THR A 449   CB    THR A 449   CA    -0.050
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    GLY A  21   N   -  CA  -  C   ANGL. DEV. = 13.7 DEGREES
REMARK 500    LEU A  23   CA  -  CB  -  CG  ANGL. DEV. =-22.3 DEGREES
REMARK 500    LEU A  23   N   -  CA  -  C   ANGL. DEV. = 14.7 DEGREES
REMARK 500    LEU A  23   C   -  N   -  CA  ANGL. DEV. = 13.1 DEGREES
REMARK 500    ASN A 121   N   -  CA  -  C   ANGL. DEV. = 13.9 DEGREES
REMARK 500    LYS A 271   N   -  CA  -  C   ANGL. DEV. = 10.5 DEGREES
REMARK 500    TYR A 284   N   -  CA  -  C   ANGL. DEV. = 14.8 DEGREES
REMARK 500    MET A 424   N   -  CA  -  C   ANGL. DEV. =-10.8 DEGREES
REMARK 500    TRP A 430   N   -  CA  -  C   ANGL. DEV. =-15.2 DEGREES
REMARK 500    ILE A 521   N   -  CA  -  C   ANGL. DEV. = 13.8 DEGREES
DBREF  1JMY A    1   518  GB     14734910 XP_035051.1     21    538
SEQADV 1JMY ARG A  331  GB   14734910  ALA   351 CONFLICT
SEQADV 1JMY PRO A  519  GB   14734910            CLONING ARTIFACT
SEQADV 1JMY GLY A  520  GB   14734910            CLONING ARTIFACT
SEQADV 1JMY ILE A  521  GB   14734910            CLONING ARTIFACT
SEQADV 1JMY HIS A  522  GB   14734910            CLONING ARTIFACT
SEQRES   1 A  522  ALA LYS LEU GLY ALA VAL TYR THR GLU GLY GLY PHE VAL
SEQRES   2 A  522  GLU GLY VAL ASN LYS LYS LEU GLY LEU LEU GLY ASP SER
SEQRES   3 A  522  VAL ASP ILE PHE LYS GLY ILE PRO PHE ALA ALA PRO THR
SEQRES   4 A  522  LYS ALA LEU GLU ASN PRO GLN PRO HIS PRO GLY TRP GLN
SEQRES   5 A  522  GLY THR LEU LYS ALA LYS ASN PHE LYS LYS ARG CYS LEU
SEQRES   6 A  522  GLN ALA THR ILE THR GLN ASP SER THR TYR GLY ASP GLU
SEQRES   7 A  522  ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO GLN GLY ARG
SEQRES   8 A  522  LYS GLN VAL SER ARG ASP LEU PRO VAL MET ILE TRP ILE
SEQRES   9 A  522  TYR GLY GLY ALA PHE LEU MET GLY SER GLY HIS GLY ALA
SEQRES  10 A  522  ASN PHE LEU ASN ASN TYR LEU TYR ASP GLY GLU GLU ILE
SEQRES  11 A  522  ALA THR ARG GLY ASN VAL ILE VAL VAL THR PHE ASN TYR
SEQRES  12 A  522  ARG VAL GLY PRO LEU GLY PHE LEU SER THR GLY ASP ALA
SEQRES  13 A  522  ASN LEU PRO GLY ASN TYR GLY LEU ARG ASP GLN HIS MET
SEQRES  14 A  522  ALA ILE ALA TRP VAL LYS ARG ASN ILE ALA ALA PHE GLY
SEQRES  15 A  522  GLY ASP PRO ASN ASN ILE THR LEU PHE GLY GLU SER ALA
SEQRES  16 A  522  GLY GLY ALA SER VAL SER LEU GLN THR LEU SER PRO TYR
SEQRES  17 A  522  ASN LYS GLY LEU ILE ARG ARG ALA ILE SER GLN SER GLY
SEQRES  18 A  522  VAL ALA LEU SER PRO TRP VAL ILE GLN LYS ASN PRO LEU
SEQRES  19 A  522  PHE TRP ALA LYS LYS VAL ALA GLU LYS VAL GLY CYS PRO
SEQRES  20 A  522  VAL GLY ASP ALA ALA ARG MET ALA GLN CYS LEU LYS VAL
SEQRES  21 A  522  THR ASP PRO ARG ALA LEU THR LEU ALA TYR LYS VAL PRO
SEQRES  22 A  522  LEU ALA GLY LEU GLU TYR PRO MET LEU HIS TYR VAL GLY
SEQRES  23 A  522  PHE VAL PRO VAL ILE ASP GLY ASP PHE ILE PRO ALA ASP
SEQRES  24 A  522  PRO ILE ASN LEU TYR ALA ASN ALA ALA ASP ILE ASP TYR
SEQRES  25 A  522  ILE ALA GLY THR ASN ASN MET ASP GLY HIS ILE PHE ALA
SEQRES  26 A  522  SER ILE ASP MET PRO ARG ILE ASN LYS GLY ASN LYS LYS
SEQRES  27 A  522  VAL THR GLU GLU ASP PHE TYR LYS LEU VAL SER GLU PHE
SEQRES  28 A  522  THR ILE THR LYS GLY LEU ARG GLY ALA LYS THR THR PHE
SEQRES  29 A  522  ASP VAL TYR THR GLU SER TRP ALA GLN ASP PRO SER GLN
SEQRES  30 A  522  GLU ASN LYS LYS LYS THR VAL VAL ASP PHE GLU THR ASP
SEQRES  31 A  522  VAL LEU PHE LEU VAL PRO THR GLU ILE ALA LEU ALA GLN
SEQRES  32 A  522  HIS ARG ALA ASN ALA LYS SER ALA LYS THR TYR ALA TYR
SEQRES  33 A  522  LEU PHE SER HIS PRO SER ARG MET PRO VAL TYR PRO LYS
SEQRES  34 A  522  TRP VAL GLY ALA ASP HIS ALA ASP ASP ILE GLN TYR VAL
SEQRES  35 A  522  PHE GLY LYS PRO PHE ALA THR PRO THR GLY TYR ARG PRO
SEQRES  36 A  522  GLN ASP ARG THR VAL SER LYS ALA MET ILE ALA TYR TRP
SEQRES  37 A  522  THR ASN PHE ALA LYS THR GLY ASP PRO ASN MET GLY ASP
SEQRES  38 A  522  SER ALA VAL PRO THR HIS TRP GLU PRO TYR THR THR GLU
SEQRES  39 A  522  ASN SER GLY TYR LEU GLU ILE THR LYS LYS MET GLY SER
SEQRES  40 A  522  SER SER MET LYS ARG SER LEU ARG THR ASN PHE PRO GLY
SEQRES  41 A  522  ILE HIS
HET    SO4    600       5
HETNAM     SO4 SULFATE ION
FORMUL   2  SO4    O4 S1 2-
FORMUL   3  HOH   *63(H2 O1)
HELIX    1   1 GLY A  127  GLY A  134  1                                   8
HELIX    2   2 VAL A  145  LEU A  151  1                                   7
HELIX    3   3 ASN A  161  ILE A  178  1                                  18
HELIX    4   4 ALA A  179  PHE A  181  5                                   3
HELIX    5   5 SER A  194  SER A  206  1                                  13
HELIX    6   6 PRO A  207  LYS A  210  5                                   4
HELIX    7   7 ASN A  232  GLY A  245  1                                  14
HELIX    8   8 ASP A  250  THR A  261  1                                  12
HELIX    9   9 ASP A  262  LEU A  268  1                                   7
HELIX   10  10 MET A  281  VAL A  285  5                                   5
HELIX   11  11 ASP A  299  LEU A  303  5                                   5
HELIX   12  12 LEU A  303  ALA A  308  5                                   6
HELIX   13  13 GLY A  321  MET A  329  1                                   9
HELIX   14  14 PRO A  330  ASN A  333  5                                   4
HELIX   15  15 GLU A  341  SER A  349  1                                   9
HELIX   16  16 GLY A  356  TYR A  367  1                                  12
HELIX   17  17 SER A  376  PHE A  393  1                                  18
HELIX   18  18 PHE A  393  ALA A  406  1                                  14
HELIX   19  19 ASP A  438  PHE A  443  1                                   6
HELIX   20  20 GLY A  444  THR A  449  1                                   6
HELIX   21  21 PRO A  450  TYR A  453  5                                   4
HELIX   22  22 ARG A  454  GLY A  475  1                                  22
HELIX   23  23 GLY A  506  SER A  508  5                                   3
SHEET    1   A 3 VAL A   6  THR A   8  0
SHEET    2   A 3 GLY A  11  GLU A  14 -1  N  GLY A  11   O  THR A   8
SHEET    3   A 3 THR A  54  LYS A  56  1  N  LEU A  55   O  PHE A  12
SHEET    1   B11 VAL A  16  LYS A  19  0
SHEET    2   B11 SER A  26  PRO A  34 -1  O  VAL A  27   N  LYS A  18
SHEET    3   B11 TYR A  82  GLN A  89 -1  N  LEU A  83   O  ILE A  33
SHEET    4   B11 ILE A 137  PHE A 141 -1  N  VAL A 138   O  TRP A  86
SHEET    5   B11 LEU A  98  ILE A 104  1  O  PRO A  99   N  ILE A 137
SHEET    6   B11 GLY A 183  GLU A 193  1  N  ASP A 184   O  LEU A  98
SHEET    7   B11 ARG A 215  GLN A 219  1  N  ARG A 215   O  ILE A 188
SHEET    8   B11 ASP A 311  ASN A 317  1  O  ASP A 311   N  ALA A 216
SHEET    9   B11 THR A 413  PHE A 418  1  O  TYR A 414   N  ALA A 314
SHEET   10   B11 TYR A 498  ILE A 501  1  O  LEU A 499   N  LEU A 417
SHEET   11   B11 MET A 510  LYS A 511 -1  N  LYS A 511   O  TYR A 498
SHEET    1   C 2 GLN A  66  ALA A  67  0
SHEET    2   C 2 THR A  74  TYR A  75 -1  O  TYR A  75   N  GLN A  66
SHEET    1   D 2 ASN A 118  PHE A 119  0
SHEET    2   D 2 ASN A 122  TYR A 123 -1  O  ASN A 122   N  PHE A 119
SSBOND   1 CYS A   64    CYS A   80
SSBOND   2 CYS A  246    CYS A  257
CRYST1   58.640   90.080  103.260  90.00  90.00  90.00 P 21 21 21    4
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      0.017053  0.000000  0.000000        0.00000
SCALE2      0.000000  0.011101  0.000000        0.00000
SCALE3      0.000000  0.000000  0.009684        0.00000

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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