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PDBsum entry 1q1c

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Isomerase PDB id
1q1c
Jmol
Contents
Protein chain
237 a.a. *
Ligands
DMS ×5
EDO
Waters ×210
* Residue conservation analysis
HEADER    ISOMERASE                               18-JUL-03   1Q1C
TITLE     CRYSTAL STRUCTURE OF N(1-260) OF HUMAN FKBP52
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: FK506-BINDING PROTEIN 4;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: RESIDUES (-19)-260;
COMPND   5 SYNONYM: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE, PPIASE,
COMPND   6 ROTAMASE, P59 PROTEIN, HSP BINDING IMMUNOPHILIN, HBI,
COMPND   7 FKBP52 PROTEIN, 52 KDA FK506 BINDING PROTEIN, FKBP59, N(1-
COMPND   8 260) OF FKBP52;
COMPND   9 EC: 5.2.1.8;
COMPND  10 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS    ROTAMASE, TPR REPEAT, NUCLEAR PROTEIN, PHOSPHORYLATION,
KEYWDS   2 ISOMERASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    B.WU,P.LI,Z.LOU,Y.DING,C.SHU,B.SHEN,Z.RAO
REVDAT   2   24-FEB-09 1Q1C    1       VERSN
REVDAT   1   22-JUN-04 1Q1C    0
JRNL        AUTH   B.WU,P.LI,Y.LIU,Z.LOU,Y.DING,C.SHU,S.YE,M.BARTLAM,
JRNL        AUTH 2 B.SHEN,Z.RAO
JRNL        TITL   3D STRUCTURE OF HUMAN FK506-BINDING PROTEIN 52:
JRNL        TITL 2 IMPLICATIONS FOR THE ASSEMBLY OF THE
JRNL        TITL 3 GLUCOCORTICOID RECEPTOR/HSP90/IMMUNOPHILIN
JRNL        TITL 4 HETEROCOMPLEX
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 101  8348 2004
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   15159550
JRNL        DOI    10.1073/PNAS.0305969101
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
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) : 1.90
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 23816
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE            (WORKING SET) : 0.208
REMARK   3   FREE R VALUE                     : 0.247
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 2362
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            : 1882
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 24
REMARK   3   SOLVENT ATOMS            : 210
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  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) : 0.019
REMARK   3   BOND ANGLES            (DEGREES) : 1.90
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
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  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 1Q1C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JUL-03.
REMARK 100 THE RCSB ID CODE IS RCSB019792.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 28-JUN-03
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : BSRF
REMARK 200  BEAMLINE                       : 3W1A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2800
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23816
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 53.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, TRIS, DMSO, PH 8.0, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,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       21.10900
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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     MET A   -19
REMARK 465     GLY A   -18
REMARK 465     SER A   -17
REMARK 465     SER A   -16
REMARK 465     HIS A   -15
REMARK 465     HIS A   -14
REMARK 465     HIS A   -13
REMARK 465     HIS A   -12
REMARK 465     HIS A   -11
REMARK 465     HIS A   -10
REMARK 465     SER A    -9
REMARK 465     SER A    -8
REMARK 465     GLY A    -7
REMARK 465     LEU A    -6
REMARK 465     VAL A    -5
REMARK 465     PRO A    -4
REMARK 465     ARG A    -3
REMARK 465     GLY A    -2
REMARK 465     SER A    -1
REMARK 465     HIS A     0
REMARK 465     MET A     1
REMARK 465     THR A     2
REMARK 465     ALA A     3
REMARK 465     GLU A     4
REMARK 465     GLU A     5
REMARK 465     MET A     6
REMARK 465     LYS A     7
REMARK 465     ALA A     8
REMARK 465     THR A     9
REMARK 465     GLU A    10
REMARK 465     SER A    11
REMARK 465     GLY A    12
REMARK 465     ALA A    13
REMARK 465     GLN A    14
REMARK 465     SER A    15
REMARK 465     ALA A    16
REMARK 465     PRO A    17
REMARK 465     LEU A    18
REMARK 465     PRO A    19
REMARK 465     MET A    20
REMARK 465     SER A   258
REMARK 465     TRP A   259
REMARK 465     GLU A   260
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   N    ILE A   192     O    HOH A   516              2.15
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    TYR A 202   CD1   TYR A 202   CE1     0.098
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  31       18.49     56.56
REMARK 500    ALA A 112     -104.21   -130.00
REMARK 500    PRO A 119     -152.35     22.05
REMARK 500    PRO A 120      -77.16    -11.67
REMARK 500    GLU A 159       93.77   -163.64
REMARK 500    TYR A 161      -42.01     84.39
REMARK 500    ASP A 180       15.90     58.42
REMARK 500    ALA A 226     -127.30   -124.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 301
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 302
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 303
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 304
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 305
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 306
DBREF  1Q1C A    2   260  UNP    Q02790   FKBP4_HUMAN      1    259
SEQADV 1Q1C MET A  -19  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C GLY A  -18  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C SER A  -17  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C SER A  -16  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C HIS A  -15  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C HIS A  -14  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C HIS A  -13  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C HIS A  -12  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C HIS A  -11  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C HIS A  -10  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C SER A   -9  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C SER A   -8  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C GLY A   -7  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C LEU A   -6  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C VAL A   -5  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C PRO A   -4  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C ARG A   -3  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C GLY A   -2  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C SER A   -1  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C HIS A    0  UNP  Q02790              EXPRESSION TAG
SEQADV 1Q1C MET A    1  UNP  Q02790              EXPRESSION TAG
SEQRES   1 A  280  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES   2 A  280  LEU VAL PRO ARG GLY SER HIS MET THR ALA GLU GLU MET
SEQRES   3 A  280  LYS ALA THR GLU SER GLY ALA GLN SER ALA PRO LEU PRO
SEQRES   4 A  280  MET GLU GLY VAL ASP ILE SER PRO LYS GLN ASP GLU GLY
SEQRES   5 A  280  VAL LEU LYS VAL ILE LYS ARG GLU GLY THR GLY THR GLU
SEQRES   6 A  280  MET PRO MET ILE GLY ASP ARG VAL PHE VAL HIS TYR THR
SEQRES   7 A  280  GLY TRP LEU LEU ASP GLY THR LYS PHE ASP SER SER LEU
SEQRES   8 A  280  ASP ARG LYS ASP LYS PHE SER PHE ASP LEU GLY LYS GLY
SEQRES   9 A  280  GLU VAL ILE LYS ALA TRP ASP ILE ALA ILE ALA THR MET
SEQRES  10 A  280  LYS VAL GLY GLU VAL CYS HIS ILE THR CYS LYS PRO GLU
SEQRES  11 A  280  TYR ALA TYR GLY SER ALA GLY SER PRO PRO LYS ILE PRO
SEQRES  12 A  280  PRO ASN ALA THR LEU VAL PHE GLU VAL GLU LEU PHE GLU
SEQRES  13 A  280  PHE LYS GLY GLU ASP LEU THR GLU GLU GLU ASP GLY GLY
SEQRES  14 A  280  ILE ILE ARG ARG ILE GLN THR ARG GLY GLU GLY TYR ALA
SEQRES  15 A  280  LYS PRO ASN GLU GLY ALA ILE VAL GLU VAL ALA LEU GLU
SEQRES  16 A  280  GLY TYR TYR LYS ASP LYS LEU PHE ASP GLN ARG GLU LEU
SEQRES  17 A  280  ARG PHE GLU ILE GLY GLU GLY GLU ASN LEU ASP LEU PRO
SEQRES  18 A  280  TYR GLY LEU GLU ARG ALA ILE GLN ARG MET GLU LYS GLY
SEQRES  19 A  280  GLU HIS SER ILE VAL TYR LEU LYS PRO SER TYR ALA PHE
SEQRES  20 A  280  GLY SER VAL GLY LYS GLU LYS PHE GLN ILE PRO PRO ASN
SEQRES  21 A  280  ALA GLU LEU LYS TYR GLU LEU HIS LEU LYS SER PHE GLU
SEQRES  22 A  280  LYS ALA LYS GLU SER TRP GLU
HET    DMS  A 301       4
HET    DMS  A 302       4
HET    DMS  A 303       4
HET    DMS  A 304       4
HET    DMS  A 305       4
HET    EDO  A 306       4
HETNAM     DMS DIMETHYL SULFOXIDE
HETNAM     EDO 1,2-ETHANEDIOL
HETSYN     EDO ETHYLENE GLYCOL
FORMUL   2  DMS    5(C2 H6 O S)
FORMUL   7  EDO    C2 H6 O2
FORMUL   8  HOH   *210(H2 O)
HELIX    1   1 ILE A   87  ALA A   95  1                                   9
HELIX    2   2 PRO A  109  ALA A  112  5                                   4
HELIX    3   3 GLU A  194  ASP A  199  5                                   6
HELIX    4   4 PRO A  201  GLN A  209  1                                   9
HELIX    5   5 PRO A  223  ALA A  226  5                                   4
HELIX    6   6 LYS A  232  GLN A  236  5                                   5
SHEET    1   A 6 VAL A  23  ASP A  24  0
SHEET    2   A 6 VAL A  33  ARG A  39 -1  O  LYS A  35   N  VAL A  23
SHEET    3   A 6 VAL A 102  CYS A 107 -1  O  VAL A 102   N  LYS A  38
SHEET    4   A 6 LEU A 128  LYS A 138 -1  O  LEU A 128   N  CYS A 107
SHEET    5   A 6 ARG A  52  LEU A  61 -1  N  ARG A  52   O  LYS A 138
SHEET    6   A 6 LYS A  66  SER A  69 -1  O  ASP A  68   N  GLY A  59
SHEET    1   B 6 VAL A  23  ASP A  24  0
SHEET    2   B 6 VAL A  33  ARG A  39 -1  O  LYS A  35   N  VAL A  23
SHEET    3   B 6 VAL A 102  CYS A 107 -1  O  VAL A 102   N  LYS A  38
SHEET    4   B 6 LEU A 128  LYS A 138 -1  O  LEU A 128   N  CYS A 107
SHEET    5   B 6 ARG A  52  LEU A  61 -1  N  ARG A  52   O  LYS A 138
SHEET    6   B 6 PHE A  77  ASP A  80 -1  O  PHE A  77   N  VAL A  55
SHEET    1   C 6 GLU A 140  ASP A 141  0
SHEET    2   C 6 ILE A 150  THR A 156 -1  O  ARG A 152   N  GLU A 140
SHEET    3   C 6 HIS A 216  LEU A 221 -1  O  HIS A 216   N  GLN A 155
SHEET    4   C 6 LEU A 243  GLU A 253 -1  O  LEU A 247   N  SER A 217
SHEET    5   C 6 ILE A 169  TYR A 178 -1  N  TYR A 177   O  LYS A 244
SHEET    6   C 6 LYS A 181  GLU A 191 -1  O  PHE A 183   N  GLY A 176
SITE     1 AC1  3 VAL A  86  ILE A  87  TRP A  90
SITE     1 AC2  2 LEU A 182  HOH A 356
SITE     1 AC3  1 TRP A  60
SITE     1 AC4  5 GLU A 166  GLY A 193  TYR A 202  GLN A 209
SITE     2 AC4  5 HOH A 503
SITE     1 AC5  2 GLY A 139  ARG A 153
SITE     1 AC6  3 TYR A 161  LYS A 163  HOH A 401
CRYST1   48.829   42.218   79.065  90.00 102.25  90.00 P 1 21 1      2
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      0.020480  0.000000  0.004447        0.00000
SCALE2      0.000000  0.023687  0.000000        0.00000
SCALE3      0.000000  0.000000  0.012943        0.00000
      
PROCHECK
Go to PROCHECK summary
 References