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PDBsum entry 3rau

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Top Page protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3rau
Jmol
Contents
Protein chain
358 a.a.
Ligands
ACT ×8
EDO ×2
GOL
Waters ×299
HEADER    HYDROLASE                               28-MAR-11   3RAU
TITLE     CRYSTAL STRUCTURE OF THE HD-PTP BRO1 DOMAIN
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 23;
COMPND   3 CHAIN: A, B;
COMPND   4 FRAGMENT: UNP RESIDUES 2-361;
COMPND   5 SYNONYM: HIS DOMAIN-CONTAINING PROTEIN TYROSINE PHOSPHATASE, HD-PTP,
COMPND   6 PROTEIN TYROSINE PHOSPHATASE TD14, PTP-TD14;
COMPND   7 EC: 3.1.3.48;
COMPND   8 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: PTPN23, KIAA1471;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS    BRO1 DOMAIN, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    R.L.MU,J.S.JIANG,G.SNYDER,P.SMITH,T.XIAO
REVDAT   2   16-NOV-11 3RAU    1       JRNL
REVDAT   1   14-SEP-11 3RAU    0
JRNL        AUTH   P.SETTE,R.MU,V.DUSSUPT,J.JIANG,G.SNYDER,P.SMITH,T.S.XIAO,
JRNL        AUTH 2 F.BOUAMR
JRNL        TITL   THE PHE105 LOOP OF ALIX BRO1 DOMAIN PLAYS A KEY ROLE IN
JRNL        TITL 2 HIV-1 RELEASE.
JRNL        REF    STRUCTURE                     V.  19  1485 2011
JRNL        REFN                   ISSN 0969-2126
JRNL        PMID   21889351
JRNL        DOI    10.1016/J.STR.2011.07.016
REMARK   2
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK   3               : ZWART
REMARK   3
REMARK   3    REFINEMENT TARGET : ML
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.96
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.080
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.0
REMARK   3   NUMBER OF REFLECTIONS             : 48044
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.174
REMARK   3   R VALUE            (WORKING SET) : 0.172
REMARK   3   FREE R VALUE                     : 0.215
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.120
REMARK   3   FREE R VALUE TEST SET COUNT      : 2460
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE
REMARK   3     1 46.9715 -  5.1084    0.99     2704   146  0.1802 0.2023
REMARK   3     2  5.1084 -  4.0554    0.99     2686   156  0.1486 0.1838
REMARK   3     3  4.0554 -  3.5430    0.99     2723   135  0.1509 0.1841
REMARK   3     4  3.5430 -  3.2191    0.99     2655   154  0.1654 0.1834
REMARK   3     5  3.2191 -  2.9884    0.98     2672   154  0.1740 0.2208
REMARK   3     6  2.9884 -  2.8123    0.97     2626   152  0.1754 0.2330
REMARK   3     7  2.8123 -  2.6714    0.97     2594   159  0.1743 0.2254
REMARK   3     8  2.6714 -  2.5551    0.95     2616   141  0.1742 0.2312
REMARK   3     9  2.5551 -  2.4568    0.95     2582   139  0.1736 0.2454
REMARK   3    10  2.4568 -  2.3720    0.94     2576   116  0.1712 0.2012
REMARK   3    11  2.3720 -  2.2978    0.94     2557   159  0.1763 0.2458
REMARK   3    12  2.2978 -  2.2322    0.92     2503   127  0.1726 0.2316
REMARK   3    13  2.2322 -  2.1734    0.92     2482   149  0.1736 0.2311
REMARK   3    14  2.1734 -  2.1204    0.90     2468   116  0.1818 0.2070
REMARK   3    15  2.1204 -  2.0722    0.89     2428   112  0.1902 0.2560
REMARK   3    16  2.0722 -  2.0281    0.86     2365   119  0.2126 0.2588
REMARK   3    17  2.0281 -  1.9875    0.82     2235   113  0.2278 0.3201
REMARK   3    18  1.9875 -  1.9500    0.77     2112   113  0.2461 0.3108
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL
REMARK   3   SOLVENT RADIUS     : 1.10
REMARK   3   SHRINKAGE RADIUS   : 0.83
REMARK   3   K_SOL              : 0.39
REMARK   3   B_SOL              : 41.88
REMARK   3
REMARK   3  ERROR ESTIMATES.
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.030
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : 20.13
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 6.92130
REMARK   3    B22 (A**2) : -0.46480
REMARK   3    B33 (A**2) : -6.45640
REMARK   3    B12 (A**2) : 0.60750
REMARK   3    B13 (A**2) : -0.67520
REMARK   3    B23 (A**2) : -3.16900
REMARK   3
REMARK   3  TWINNING INFORMATION.
REMARK   3   FRACTION: NULL
REMARK   3   OPERATOR: NULL
REMARK   3
REMARK   3  DEVIATIONS FROM IDEAL VALUES.
REMARK   3                 RMSD          COUNT
REMARK   3   BOND      :  0.007           5890
REMARK   3   ANGLE     :  0.935           7960
REMARK   3   CHIRALITY :  0.066            865
REMARK   3   PLANARITY :  0.004           1036
REMARK   3   DIHEDRAL  : 12.348           2241
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  NCS DETAILS
REMARK   3   NUMBER OF NCS GROUPS : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3RAU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-APR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064702.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 09-DEC-09
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 5.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 23-ID-D
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332
REMARK 200  MONOCHROMATOR                  : SI(111)
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49890
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2
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) : 1.95
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.5
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2OEW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 44.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH5.5, 16% PEG3350, 0.3M
REMARK 280  MAGNESIUM ACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,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
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 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 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     GLY A    -1
REMARK 465     GLU A     0
REMARK 465     PHE A     1
REMARK 465     GLU A     2
REMARK 465     ALA A     3
REMARK 465     GLY B    -1
REMARK 465     GLU B     0
REMARK 465     PHE B     1
REMARK 465     GLU B     2
REMARK 465     ALA B     3
REMARK 465     VAL B     4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 362
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 363
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 362
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 364
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 363
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 364
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 365
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 366
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 366
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 367
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3R9M   RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE BROX BRO1 DOMAIN
DBREF  3RAU A    2   361  UNP    Q9H3S7   PTN23_HUMAN      2    361
DBREF  3RAU B    2   361  UNP    Q9H3S7   PTN23_HUMAN      2    361
SEQADV 3RAU GLY A   -1  UNP  Q9H3S7              EXPRESSION TAG
SEQADV 3RAU GLU A    0  UNP  Q9H3S7              EXPRESSION TAG
SEQADV 3RAU PHE A    1  UNP  Q9H3S7              EXPRESSION TAG
SEQADV 3RAU GLY B   -1  UNP  Q9H3S7              EXPRESSION TAG
SEQADV 3RAU GLU B    0  UNP  Q9H3S7              EXPRESSION TAG
SEQADV 3RAU PHE B    1  UNP  Q9H3S7              EXPRESSION TAG
SEQRES   1 A  363  GLY GLU PHE GLU ALA VAL PRO ARG MET PRO MET ILE TRP
SEQRES   2 A  363  LEU ASP LEU LYS GLU ALA GLY ASP PHE HIS PHE GLN PRO
SEQRES   3 A  363  ALA VAL LYS LYS PHE VAL LEU LYS ASN TYR GLY GLU ASN
SEQRES   4 A  363  PRO GLU ALA TYR ASN GLU GLU LEU LYS LYS LEU GLU LEU
SEQRES   5 A  363  LEU ARG GLN ASN ALA VAL ARG VAL PRO ARG ASP PHE GLU
SEQRES   6 A  363  GLY CYS SER VAL LEU ARG LYS TYR LEU GLY GLN LEU HIS
SEQRES   7 A  363  TYR LEU GLN SER ARG VAL PRO MET GLY SER GLY GLN GLU
SEQRES   8 A  363  ALA ALA VAL PRO VAL THR TRP THR GLU ILE PHE SER GLY
SEQRES   9 A  363  LYS SER VAL ALA HIS GLU ASP ILE LYS TYR GLU GLN ALA
SEQRES  10 A  363  CYS ILE LEU TYR ASN LEU GLY ALA LEU HIS SER MET LEU
SEQRES  11 A  363  GLY ALA MET ASP LYS ARG VAL SER GLU GLU GLY MET LYS
SEQRES  12 A  363  VAL SER CYS THR HIS PHE GLN CYS ALA ALA GLY ALA PHE
SEQRES  13 A  363  ALA TYR LEU ARG GLU HIS PHE PRO GLN ALA TYR SER VAL
SEQRES  14 A  363  ASP MET SER ARG GLN ILE LEU THR LEU ASN VAL ASN LEU
SEQRES  15 A  363  MET LEU GLY GLN ALA GLN GLU CYS LEU LEU GLU LYS SER
SEQRES  16 A  363  MET LEU ASP ASN ARG LYS SER PHE LEU VAL ALA ARG ILE
SEQRES  17 A  363  SER ALA GLN VAL VAL ASP TYR TYR LYS GLU ALA CYS ARG
SEQRES  18 A  363  ALA LEU GLU ASN PRO ASP THR ALA SER LEU LEU GLY ARG
SEQRES  19 A  363  ILE GLN LYS ASP TRP LYS LYS LEU VAL GLN MET LYS ILE
SEQRES  20 A  363  TYR TYR PHE ALA ALA VAL ALA HIS LEU HIS MET GLY LYS
SEQRES  21 A  363  GLN ALA GLU GLU GLN GLN LYS PHE GLY GLU ARG VAL ALA
SEQRES  22 A  363  TYR PHE GLN SER ALA LEU ASP LYS LEU ASN GLU ALA ILE
SEQRES  23 A  363  LYS LEU ALA LYS GLY GLN PRO ASP THR VAL GLN ASP ALA
SEQRES  24 A  363  LEU ARG PHE THR MET ASP VAL ILE GLY GLY LYS TYR ASN
SEQRES  25 A  363  SER ALA LYS LYS ASP ASN ASP PHE ILE TYR HIS GLU ALA
SEQRES  26 A  363  VAL PRO ALA LEU ASP THR LEU GLN PRO VAL LYS GLY ALA
SEQRES  27 A  363  PRO LEU VAL LYS PRO LEU PRO VAL ASN PRO THR ASP PRO
SEQRES  28 A  363  ALA VAL THR GLY PRO ASP ILE PHE ALA LYS LEU VAL
SEQRES   1 B  363  GLY GLU PHE GLU ALA VAL PRO ARG MET PRO MET ILE TRP
SEQRES   2 B  363  LEU ASP LEU LYS GLU ALA GLY ASP PHE HIS PHE GLN PRO
SEQRES   3 B  363  ALA VAL LYS LYS PHE VAL LEU LYS ASN TYR GLY GLU ASN
SEQRES   4 B  363  PRO GLU ALA TYR ASN GLU GLU LEU LYS LYS LEU GLU LEU
SEQRES   5 B  363  LEU ARG GLN ASN ALA VAL ARG VAL PRO ARG ASP PHE GLU
SEQRES   6 B  363  GLY CYS SER VAL LEU ARG LYS TYR LEU GLY GLN LEU HIS
SEQRES   7 B  363  TYR LEU GLN SER ARG VAL PRO MET GLY SER GLY GLN GLU
SEQRES   8 B  363  ALA ALA VAL PRO VAL THR TRP THR GLU ILE PHE SER GLY
SEQRES   9 B  363  LYS SER VAL ALA HIS GLU ASP ILE LYS TYR GLU GLN ALA
SEQRES  10 B  363  CYS ILE LEU TYR ASN LEU GLY ALA LEU HIS SER MET LEU
SEQRES  11 B  363  GLY ALA MET ASP LYS ARG VAL SER GLU GLU GLY MET LYS
SEQRES  12 B  363  VAL SER CYS THR HIS PHE GLN CYS ALA ALA GLY ALA PHE
SEQRES  13 B  363  ALA TYR LEU ARG GLU HIS PHE PRO GLN ALA TYR SER VAL
SEQRES  14 B  363  ASP MET SER ARG GLN ILE LEU THR LEU ASN VAL ASN LEU
SEQRES  15 B  363  MET LEU GLY GLN ALA GLN GLU CYS LEU LEU GLU LYS SER
SEQRES  16 B  363  MET LEU ASP ASN ARG LYS SER PHE LEU VAL ALA ARG ILE
SEQRES  17 B  363  SER ALA GLN VAL VAL ASP TYR TYR LYS GLU ALA CYS ARG
SEQRES  18 B  363  ALA LEU GLU ASN PRO ASP THR ALA SER LEU LEU GLY ARG
SEQRES  19 B  363  ILE GLN LYS ASP TRP LYS LYS LEU VAL GLN MET LYS ILE
SEQRES  20 B  363  TYR TYR PHE ALA ALA VAL ALA HIS LEU HIS MET GLY LYS
SEQRES  21 B  363  GLN ALA GLU GLU GLN GLN LYS PHE GLY GLU ARG VAL ALA
SEQRES  22 B  363  TYR PHE GLN SER ALA LEU ASP LYS LEU ASN GLU ALA ILE
SEQRES  23 B  363  LYS LEU ALA LYS GLY GLN PRO ASP THR VAL GLN ASP ALA
SEQRES  24 B  363  LEU ARG PHE THR MET ASP VAL ILE GLY GLY LYS TYR ASN
SEQRES  25 B  363  SER ALA LYS LYS ASP ASN ASP PHE ILE TYR HIS GLU ALA
SEQRES  26 B  363  VAL PRO ALA LEU ASP THR LEU GLN PRO VAL LYS GLY ALA
SEQRES  27 B  363  PRO LEU VAL LYS PRO LEU PRO VAL ASN PRO THR ASP PRO
SEQRES  28 B  363  ALA VAL THR GLY PRO ASP ILE PHE ALA LYS LEU VAL
HET    ACT  A 362       4
HET    ACT  A 363       4
HET    ACT  A 364       4
HET    ACT  A 365       4
HET    EDO  A 366       4
HET    EDO  A 367       4
HET    GOL  B 362       6
HET    ACT  B 363       4
HET    ACT  B 364       4
HET    ACT  B 365       4
HET    ACT  B 366       4
HETNAM     ACT ACETATE ION
HETNAM     EDO 1,2-ETHANEDIOL
HETNAM     GOL GLYCEROL
HETSYN     EDO ETHYLENE GLYCOL
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   3  ACT    8(C2 H3 O2 1-)
FORMUL   7  EDO    2(C2 H6 O2)
FORMUL   9  GOL    C3 H8 O3
FORMUL  14  HOH   *299(H2 O)
HELIX    1   1 PHE A   22  ASN A   33  1                                  12
HELIX    2   2 TYR A   41  ARG A   57  1                                  17
HELIX    3   3 ASP A   61  VAL A   82  1                                  22
HELIX    4   4 ASP A  109  ASP A  132  1                                  24
HELIX    5   5 SER A  136  PHE A  161  1                                  26
HELIX    6   6 SER A  166  MET A  169  5                                   4
HELIX    7   7 SER A  170  ASP A  196  1                                  27
HELIX    8   8 LYS A  199  GLU A  222  1                                  24
HELIX    9   9 ASN A  223  GLY A  231  1                                   9
HELIX   10  10 ARG A  232  GLN A  263  1                                  32
HELIX   11  11 LYS A  265  ALA A  287  1                                  23
HELIX   12  12 PRO A  291  ILE A  319  1                                  29
HELIX   13  13 ALA A  326  LEU A  330  5                                   5
HELIX   14  14 ASP A  348  GLY A  353  1                                   6
HELIX   15  15 PHE B   22  TYR B   34  1                                  13
HELIX   16  16 TYR B   41  ARG B   57  1                                  17
HELIX   17  17 ASP B   61  SER B   80  1                                  20
HELIX   18  18 ASP B  109  ASP B  132  1                                  24
HELIX   19  19 SER B  136  PHE B  161  1                                  26
HELIX   20  20 SER B  166  MET B  169  5                                   4
HELIX   21  21 SER B  170  ASP B  196  1                                  27
HELIX   22  22 LYS B  199  GLU B  222  1                                  24
HELIX   23  23 ASN B  223  GLY B  231  1                                   9
HELIX   24  24 GLY B  231  GLN B  263  1                                  33
HELIX   25  25 LYS B  265  ALA B  287  1                                  23
HELIX   26  26 PRO B  291  ILE B  319  1                                  29
HELIX   27  27 ALA B  326  LEU B  330  5                                   5
HELIX   28  28 ASP B  348  GLY B  353  1                                   6
SHEET    1   A 3 ALA A  17  PHE A  20  0
SHEET    2   A 3 VAL A  94  THR A  97 -1  O  THR A  95   N  GLY A  18
SHEET    3   A 3 SER A 104  HIS A 107 -1  O  VAL A 105   N  TRP A  96
SHEET    1   B 2 VAL B  94  THR B  97  0
SHEET    2   B 2 SER B 104  HIS B 107 -1  O  VAL B 105   N  TRP B  96
SITE     1 AC1  7 ALA B 208  ALA B 249  ALA B 252  HIS B 253
SITE     2 AC1  7 VAL B 333  ACT B 365  HOH B 470
SITE     1 AC2  3 LEU B  12  ASP B  13  PHE B 100
SITE     1 AC3  6 LEU A  12  ASP A  13  ILE A  99  TRP A 237
SITE     2 AC3  6 HOH A 508  HOH A 531
SITE     1 AC4  3 GLN B 209  ASP B 212  GLU B 216
SITE     1 AC5  3 GLN A 209  ASP A 212  GLU A 216
SITE     1 AC6  5 LYS B 215  ILE B 245  TYR B 246  LYS B 279
SITE     2 AC6  5 GOL B 362
SITE     1 AC7  4 LYS A 215  ILE A 245  TYR A 246  ALA A 249
SITE     1 AC8  3 ARG A   6  HOH A 375  LYS B 103
SITE     1 AC9  3 HIS B  76  GLN B 114  TYR B 156
SITE     1 BC1  4 GLY A  85  SER A  86  LYS A 111  HOH A 371
SITE     1 BC2  2 LYS A 359  ARG B 198
CRYST1   37.523   61.333   80.582  85.87  81.27  87.99 P 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      0.026650 -0.000936 -0.004039        0.00000
SCALE2      0.000000  0.016314 -0.001103        0.00000
SCALE3      0.000000  0.000000  0.012584        0.00000
      
PROCHECK
Go to PROCHECK summary
 References