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PDBsum entry 2nt2

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Hydrolase PDB id
2nt2
Jmol
Contents
Protein chains
142 a.a.
Ligands
SO4 ×3
Waters ×91
HEADER    HYDROLASE                               06-NOV-06   2NT2
TITLE     CRYSTAL STRUCTURE OF SLINGSHOT PHOSPHATASE 2
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: PROTEIN PHOSPHATASE SLINGSHOT HOMOLOG 2;
COMPND   3 CHAIN: A, B, C;
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 305-449;
COMPND   5 SYNONYM: SLINGSHOT PHOSPHATASE 2, SSH-2L, HSSH-2L;
COMPND   6 EC: 3.1.3.48, 3.1.3.16;
COMPND   7 ENGINEERED: YES;
COMPND   8 MUTATION: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE   3 ORGANISM_COMMON: HUMAN;
SOURCE   4 ORGANISM_TAXID: 9606;
SOURCE   5 GENE: SSH2, KIAA1725, SSH2L;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS    ALPHA/BETA HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    S.K.JUNG,D.G.JEONG,T.S.YOON,J.H.KIM,S.E.RYU,S.J.KIM
REVDAT   2   24-FEB-09 2NT2    1       VERSN
REVDAT   1   05-JUN-07 2NT2    0
JRNL        AUTH   S.K.JUNG,D.G.JEONG,T.S.YOON,J.H.KIM,S.E.RYU,S.J.KIM
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN SLINGSHOT PHOSPHATASE 2.
JRNL        REF    PROTEINS                      V.  68   408 2007
JRNL        REFN                   ISSN 0887-3585
JRNL        PMID   17427953
JRNL        DOI    10.1002/PROT.21399
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : SHELXL-97
REMARK   3   AUTHORS     : G.M.SHELDRICK
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.144
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.144
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.174
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1128
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 22563
REMARK   3
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS      : 3528
REMARK   3   NUCLEIC ACID ATOMS : 0
REMARK   3   HETEROGEN ATOMS    : 15
REMARK   3   SOLVENT ATOMS      : 91
REMARK   3
REMARK   3  MODEL REFINEMENT.
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL
REMARK   3   NUMBER OF RESTRAINTS                     : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK   3   BOND LENGTHS                         (A) : 0.004
REMARK   3   ANGLE DISTANCES                      (A) : 1.370
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.348
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.048
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : NULL
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.021
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED: NULL
REMARK   3
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER
REMARK   3   SPECIAL CASE: NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 2NT2 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-NOV-06.
REMARK 100 THE RCSB ID CODE IS RCSB040266.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-05
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 8.5
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : PAL/PLS
REMARK 200  BEAMLINE                       : 4A
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000
REMARK 200  MONOCHROMATOR                  : MIRROR
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200  DATA SCALING SOFTWARE          : SCALA
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22566
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6
REMARK 200  DATA REDUNDANCY                : 5.600
REMARK 200  R MERGE                    (I) : 0.06900
REMARK 200  R SYM                      (I) : 0.10000
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50
REMARK 200  R MERGE FOR SHELL          (I) : 0.23500
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1VHR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 37.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, PH 8.5, 25% PEG3350,
REMARK 280  8% ETHANOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -Y,X-Y,Z+2/3
REMARK 290       3555   -X+Y,-X,Z+1/3
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 -0.500000 -0.866025  0.000000        0.00000
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       25.84667
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       12.92333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: THE BIOLOGICAL ASSEMBLY IS MONOMER
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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   305
REMARK 465     ASP A   306
REMARK 465     ARG A   449
REMARK 465     MET B   305
REMARK 465     ASP B   306
REMARK 465     ARG B   449
REMARK 465     MET C   305
REMARK 465     ASP C   306
REMARK 465     ARG C   449
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    TRP A 371   CA  -  CB  -  CG  ANGL. DEV. =  15.7 DEGREES
REMARK 500    TRP A 371   CB  -  CG  -  CD2 ANGL. DEV. =   8.4 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    ARG A 335      -13.28   -140.08
REMARK 500    SER A 392     -145.84   -125.44
REMARK 500    SER A 397      -67.49   -123.38
REMARK 500    LYS A 430       80.64   -162.60
REMARK 500    VAL B 340       52.64    -91.24
REMARK 500    SER B 392     -142.76   -130.79
REMARK 500    SER B 397      -65.94   -129.56
REMARK 500    LYS B 430       82.53   -160.43
REMARK 500    VAL C 340       52.68    -94.53
REMARK 500    HIS C 384       30.99    -81.17
REMARK 500    SER C 392     -145.26   -133.74
REMARK 500    SER C 397      -75.96   -126.45
REMARK 500    LYS C 430       82.30   -167.25
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 SO4 A 101
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 101
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 101
DBREF  2NT2 A  305   449  UNP    Q76I76   SSH2_HUMAN     305    449
DBREF  2NT2 B  305   449  UNP    Q76I76   SSH2_HUMAN     305    449
DBREF  2NT2 C  305   449  UNP    Q76I76   SSH2_HUMAN     305    449
SEQADV 2NT2 SER A  392  UNP  Q76I76    CYS   392 ENGINEERED
SEQADV 2NT2 ARG A  449  UNP  Q76I76    SER   449 VARIANT
SEQADV 2NT2 SER B  392  UNP  Q76I76    CYS   392 ENGINEERED
SEQADV 2NT2 ARG B  449  UNP  Q76I76    SER   449 VARIANT
SEQADV 2NT2 SER C  392  UNP  Q76I76    CYS   392 ENGINEERED
SEQADV 2NT2 ARG C  449  UNP  Q76I76    SER   449 VARIANT
SEQRES   1 A  145  MET ASP SER PRO THR GLN ILE PHE GLU HIS VAL PHE LEU
SEQRES   2 A  145  GLY SER GLU TRP ASN ALA SER ASN LEU GLU ASP LEU GLN
SEQRES   3 A  145  ASN ARG GLY VAL ARG TYR ILE LEU ASN VAL THR ARG GLU
SEQRES   4 A  145  ILE ASP ASN PHE PHE PRO GLY VAL PHE GLU TYR HIS ASN
SEQRES   5 A  145  ILE ARG VAL TYR ASP GLU GLU ALA THR ASP LEU LEU ALA
SEQRES   6 A  145  TYR TRP ASN ASP THR TYR LYS PHE ILE SER LYS ALA LYS
SEQRES   7 A  145  LYS HIS GLY SER LYS CYS LEU VAL HIS SER LYS MET GLY
SEQRES   8 A  145  VAL SER ARG SER ALA SER THR VAL ILE ALA TYR ALA MET
SEQRES   9 A  145  LYS GLU TYR GLY TRP ASN LEU ASP ARG ALA TYR ASP TYR
SEQRES  10 A  145  VAL LYS GLU ARG ARG THR VAL THR LYS PRO ASN PRO SER
SEQRES  11 A  145  PHE MET ARG GLN LEU GLU GLU TYR GLN GLY ILE LEU LEU
SEQRES  12 A  145  ALA ARG
SEQRES   1 B  145  MET ASP SER PRO THR GLN ILE PHE GLU HIS VAL PHE LEU
SEQRES   2 B  145  GLY SER GLU TRP ASN ALA SER ASN LEU GLU ASP LEU GLN
SEQRES   3 B  145  ASN ARG GLY VAL ARG TYR ILE LEU ASN VAL THR ARG GLU
SEQRES   4 B  145  ILE ASP ASN PHE PHE PRO GLY VAL PHE GLU TYR HIS ASN
SEQRES   5 B  145  ILE ARG VAL TYR ASP GLU GLU ALA THR ASP LEU LEU ALA
SEQRES   6 B  145  TYR TRP ASN ASP THR TYR LYS PHE ILE SER LYS ALA LYS
SEQRES   7 B  145  LYS HIS GLY SER LYS CYS LEU VAL HIS SER LYS MET GLY
SEQRES   8 B  145  VAL SER ARG SER ALA SER THR VAL ILE ALA TYR ALA MET
SEQRES   9 B  145  LYS GLU TYR GLY TRP ASN LEU ASP ARG ALA TYR ASP TYR
SEQRES  10 B  145  VAL LYS GLU ARG ARG THR VAL THR LYS PRO ASN PRO SER
SEQRES  11 B  145  PHE MET ARG GLN LEU GLU GLU TYR GLN GLY ILE LEU LEU
SEQRES  12 B  145  ALA ARG
SEQRES   1 C  145  MET ASP SER PRO THR GLN ILE PHE GLU HIS VAL PHE LEU
SEQRES   2 C  145  GLY SER GLU TRP ASN ALA SER ASN LEU GLU ASP LEU GLN
SEQRES   3 C  145  ASN ARG GLY VAL ARG TYR ILE LEU ASN VAL THR ARG GLU
SEQRES   4 C  145  ILE ASP ASN PHE PHE PRO GLY VAL PHE GLU TYR HIS ASN
SEQRES   5 C  145  ILE ARG VAL TYR ASP GLU GLU ALA THR ASP LEU LEU ALA
SEQRES   6 C  145  TYR TRP ASN ASP THR TYR LYS PHE ILE SER LYS ALA LYS
SEQRES   7 C  145  LYS HIS GLY SER LYS CYS LEU VAL HIS SER LYS MET GLY
SEQRES   8 C  145  VAL SER ARG SER ALA SER THR VAL ILE ALA TYR ALA MET
SEQRES   9 C  145  LYS GLU TYR GLY TRP ASN LEU ASP ARG ALA TYR ASP TYR
SEQRES  10 C  145  VAL LYS GLU ARG ARG THR VAL THR LYS PRO ASN PRO SER
SEQRES  11 C  145  PHE MET ARG GLN LEU GLU GLU TYR GLN GLY ILE LEU LEU
SEQRES  12 C  145  ALA ARG
HET    SO4  A 101       5
HET    SO4  B 101       5
HET    SO4  C 101       5
HETNAM     SO4 SULFATE ION
FORMUL   4  SO4    3(O4 S 2-)
FORMUL   7  HOH   *91(H2 O)
HELIX    1   1 SER A  319  SER A  324  1                                   6
HELIX    2   2 ASN A  325  ARG A  332  1                                   8
HELIX    3   3 LEU A  367  ALA A  369  5                                   3
HELIX    4   4 TYR A  370  HIS A  384  1                                  15
HELIX    5   5 SER A  397  GLY A  412  1                                  16
HELIX    6   6 ASN A  414  ARG A  426  1                                  13
HELIX    7   7 ASN A  432  ALA A  448  1                                  17
HELIX    8   8 SER B  319  SER B  324  1                                   6
HELIX    9   9 ASN B  325  GLY B  333  1                                   9
HELIX   10  10 LEU B  367  ALA B  369  5                                   3
HELIX   11  11 TYR B  370  HIS B  384  1                                  15
HELIX   12  12 SER B  397  GLY B  412  1                                  16
HELIX   13  13 ASN B  414  ARG B  426  1                                  13
HELIX   14  14 ASN B  432  ALA B  448  1                                  17
HELIX   15  15 SER C  319  SER C  324  1                                   6
HELIX   16  16 ASN C  325  GLY C  333  1                                   9
HELIX   17  17 LEU C  367  ALA C  369  5                                   3
HELIX   18  18 TYR C  370  HIS C  384  1                                  15
HELIX   19  19 SER C  397  GLY C  412  1                                  16
HELIX   20  20 ASN C  414  ARG C  426  1                                  13
HELIX   21  21 ASN C  432  ALA C  448  1                                  17
SHEET    1   A 5 THR A 309  PHE A 312  0
SHEET    2   A 5 VAL A 315  GLY A 318 -1  O  LEU A 317   N  THR A 309
SHEET    3   A 5 LYS A 387  HIS A 391  1  O  VAL A 390   N  PHE A 316
SHEET    4   A 5 VAL A 334  ASN A 339  1  N  LEU A 338   O  HIS A 391
SHEET    5   A 5 GLU A 353  ASN A 356  1  O  GLU A 353   N  ILE A 337
SHEET    1   B 5 THR B 309  PHE B 312  0
SHEET    2   B 5 VAL B 315  GLY B 318 -1  O  LEU B 317   N  THR B 309
SHEET    3   B 5 LYS B 387  HIS B 391  1  O  VAL B 390   N  PHE B 316
SHEET    4   B 5 VAL B 334  ASN B 339  1  N  TYR B 336   O  LEU B 389
SHEET    5   B 5 GLU B 353  ASN B 356  1  O  GLU B 353   N  ILE B 337
SHEET    1   C 5 THR C 309  PHE C 312  0
SHEET    2   C 5 VAL C 315  GLY C 318 -1  O  VAL C 315   N  ILE C 311
SHEET    3   C 5 LYS C 387  HIS C 391  1  O  VAL C 390   N  PHE C 316
SHEET    4   C 5 VAL C 334  ASN C 339  1  N  LEU C 338   O  LEU C 389
SHEET    5   C 5 GLU C 353  ASN C 356  1  O  HIS C 355   N  ASN C 339
SITE     1 AC1  8 ASP A 361  SER A 392  LYS A 393  MET A 394
SITE     2 AC1  8 GLY A 395  VAL A 396  SER A 397  ARG A 398
SITE     1 AC2  8 ASP B 361  SER B 392  LYS B 393  MET B 394
SITE     2 AC2  8 GLY B 395  VAL B 396  SER B 397  ARG B 398
SITE     1 AC3  9 HOH C  66  ASP C 361  SER C 392  LYS C 393
SITE     2 AC3  9 MET C 394  GLY C 395  VAL C 396  SER C 397
SITE     3 AC3  9 ARG C 398
CRYST1   94.580   94.580   38.770  90.00  90.00 120.00 P 32          9
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      0.010573  0.006104  0.000000        0.00000
SCALE2      0.000000  0.012209  0.000000        0.00000
SCALE3      0.000000  0.000000  0.025793        0.00000
      
PROCHECK
Go to PROCHECK summary
 References