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PDBsum entry 2hc1

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Hydrolase PDB id
2hc1
Jmol
Contents
Protein chain
290 a.a.
Ligands
ACT
Metals
_CL ×2
Waters ×362
HEADER    HYDROLASE                               14-JUN-06   2HC1
TITLE     ENGINEERED CATALYTIC DOMAIN OF PROTEIN TYROSINE PHOSPHATASE
TITLE    2 HPTPBETA.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE BETA;
COMPND   3 CHAIN: A;
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;
COMPND   5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE BETA, R-PTP-BETA;
COMPND   6 EC: 3.1.3.48;
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: PTPRB;
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: TOP10;
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHISMBP-DEST
KEYWDS    PROTEIN TYROSINE PHOSPHATASE, WPD-LOOP, SULFAMIC ACID,
KEYWDS   2 PHOSPHATASE, INHIBITOR, DRUG DESIGN, HYDROLASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    A.G.EVDOKIMOV,M.POKROSS,R.WALTER,M.MEKEL
REVDAT   4   09-JUN-09 2HC1    1       REVDAT
REVDAT   3   24-FEB-09 2HC1    1       VERSN
REVDAT   2   02-DEC-08 2HC1    1       JRNL
REVDAT   1   27-JUN-06 2HC1    0
JRNL        AUTH   A.G.EVDOKIMOV,M.POKROSS,R.WALTER,M.MEKEL,B.COX,
JRNL        AUTH 2 C.LI,R.BECHARD,F.GENBAUFFE,R.ANDREWS,C.DIVEN,
JRNL        AUTH 3 B.HOWARD,V.RASTOGI,J.GRAY,M.MAIER,K.G.PETERS
JRNL        TITL   ENGINEERING THE CATALYTIC DOMAIN OF HUMAN PROTEIN
JRNL        TITL 2 TYROSINE PHOSPHATASE BETA FOR STRUCTURE-BASED DRUG
JRNL        TITL 3 DISCOVERY.
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  62  1435 2006
JRNL        REFN                   ISSN 0907-4449
JRNL        PMID   17139078
JRNL        DOI    10.1107/S0907444906037784
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    1.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0005
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.88
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : 72.6
REMARK   3   NUMBER OF REFLECTIONS             : 56897
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 + TEST SET) : 0.136
REMARK   3   R VALUE            (WORKING SET) : 0.134
REMARK   3   FREE R VALUE                     : 0.179
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2998
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.29
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.33
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3437
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 59.74
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2010
REMARK   3   BIN FREE R VALUE SET COUNT          : 174
REMARK   3   BIN FREE R VALUE                    : 0.2880
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 2629
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 6
REMARK   3   SOLVENT ATOMS            : 362
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.49
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : -0.32000
REMARK   3    B22 (A**2) : -0.40000
REMARK   3    B33 (A**2) : 0.72000
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): 0.062
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.060
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.027
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.400
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.963
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2735 ; 0.009 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  2454 ; 0.001 ; 0.020
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3770 ; 1.232 ; 1.950
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5777 ; 0.700 ; 3.000
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   374 ; 8.876 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   149 ;34.657 ;23.691
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   507 ;14.050 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    26 ;15.791 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   405 ; 0.088 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3153 ; 0.006 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):   584 ; 0.002 ; 0.020
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   564 ; 0.250 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2596 ; 0.240 ; 0.200
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1320 ; 0.187 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1516 ; 0.090 ; 0.200
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   246 ; 0.324 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.068 ; 0.200
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    11 ; 0.272 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):    82 ; 0.316 ; 0.200
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    25 ; 0.131 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2136 ; 2.837 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   640 ; 1.224 ; 1.500
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2650 ; 3.291 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1323 ; 4.727 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1078 ; 5.809 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  6342 ; 2.461 ; 3.000
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   364 ;14.431 ; 3.000
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  5087 ; 5.574 ; 3.000
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.20
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 2HC1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-06.
REMARK 100 THE RCSB ID CODE IS RCSB038179.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-05
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : 8.2
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : APS
REMARK 200  BEAMLINE                       : 22-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0
REMARK 200  MONOCHROMATOR                  : SI
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MARGUI
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59896
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.880
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 72.6
REMARK 200  DATA REDUNDANCY                : 1.200
REMARK 200  R MERGE                    (I) : 0.04000
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : 15.3200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.40
REMARK 200  COMPLETENESS FOR SHELL     (%) : 69.2
REMARK 200  DATA REDUNDANCY IN SHELL       : 0.80
REMARK 200  R MERGE FOR SHELL          (I) : 0.35000
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : 2.850
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 2H02
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 49.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 220 MM MGCL2, 1% BME,
REMARK 280  0.1% BOG, 5MM DTT, 180 MM NH4OAC, PH 8.2, VAPOR DIFFUSION,
REMARK 280  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       19.53000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.22750
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.35700
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.22750
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.53000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.35700
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 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     SER A  1675
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   O    HOH A   435     O    HOH A   436              0.00
REMARK 500   O    HOH A   522     O    HOH A   523              0.00
REMARK 500   O    HOH A   462     O    HOH A   585              1.74
REMARK 500   O    HOH A   385     O    HOH A   426              1.93
REMARK 500   NZ   LYS A  1694     O    HOH A   531              2.11
REMARK 500   O    HOH A   463     O    HOH A   477              2.11
REMARK 500   O    HOH A    76     O    HOH A   226              2.12
REMARK 500   O    HOH A   268     O    HOH A   529              2.13
REMARK 500   OD2  ASP A  1938     O    HOH A   441              2.14
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    GLN A1853     -101.34   -124.08
REMARK 500    CYS A1904     -137.02   -113.07
REMARK 500    VAL A1908     -126.52   -136.33
REMARK 500    VAL A1947      107.68     69.40
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 A 516        DISTANCE =  5.73 ANGSTROMS
REMARK 525    HOH A 594        DISTANCE = 11.40 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 601
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 602
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 603
DBREF  2HC1 A 1676  1965  UNP    P23467   PTPRB_HUMAN   1676   1970
SEQADV 2HC1 SER A 1675  UNP  P23467              CLONING ARTIFACT
SEQADV 2HC1     A       UNP  P23467    ASN  1748 DELETION
SEQADV 2HC1     A       UNP  P23467    VAL  1749 DELETION
SEQADV 2HC1     A       UNP  P23467    ASP  1750 DELETION
SEQADV 2HC1     A       UNP  P23467    ASP  1751 DELETION
SEQADV 2HC1     A       UNP  P23467    ASP  1752 DELETION
SEQADV 2HC1 GLY A 1748  UNP  P23467    PRO  1753 ENGINEERED
SEQADV 2HC1 GLY A 1749  UNP  P23467    CYS  1754 ENGINEERED
SEQRES   1 A  291  SER ASN ARG LYS THR SER CYS PRO ILE LYS ILE ASN GLN
SEQRES   2 A  291  PHE GLU GLY HIS PHE MET LYS LEU GLN ALA ASP SER ASN
SEQRES   3 A  291  TYR LEU LEU SER LYS GLU TYR GLU GLU LEU LYS ASP VAL
SEQRES   4 A  291  GLY ARG ASN GLN SER CYS ASP ILE ALA LEU LEU PRO GLU
SEQRES   5 A  291  ASN ARG GLY LYS ASN ARG TYR ASN ASN ILE LEU PRO TYR
SEQRES   6 A  291  ASP ALA THR ARG VAL LYS LEU SER GLY GLY SER ASP TYR
SEQRES   7 A  291  ILE ASN ALA SER TYR ILE PRO GLY ASN ASN PHE ARG ARG
SEQRES   8 A  291  GLU TYR ILE VAL THR GLN GLY PRO LEU PRO GLY THR LYS
SEQRES   9 A  291  ASP ASP PHE TRP LYS MET VAL TRP GLU GLN ASN VAL HIS
SEQRES  10 A  291  ASN ILE VAL MET VAL THR GLN CYS VAL GLU LYS GLY ARG
SEQRES  11 A  291  VAL LYS CYS ASP HIS TYR TRP PRO ALA ASP GLN ASP SER
SEQRES  12 A  291  LEU TYR TYR GLY ASP LEU ILE LEU GLN MET LEU SER GLU
SEQRES  13 A  291  SER VAL LEU PRO GLU TRP THR ILE ARG GLU PHE LYS ILE
SEQRES  14 A  291  CYS GLY GLU GLU GLN LEU ASP ALA HIS ARG LEU ILE ARG
SEQRES  15 A  291  HIS PHE HIS TYR THR VAL TRP PRO ASP HIS GLY VAL PRO
SEQRES  16 A  291  GLU THR THR GLN SER LEU ILE GLN PHE VAL ARG THR VAL
SEQRES  17 A  291  ARG ASP TYR ILE ASN ARG SER PRO GLY ALA GLY PRO THR
SEQRES  18 A  291  VAL VAL HIS CYS SER ALA GLY VAL GLY ARG THR GLY THR
SEQRES  19 A  291  PHE ILE ALA LEU ASP ARG ILE LEU GLN GLN LEU ASP SER
SEQRES  20 A  291  LYS ASP SER VAL ASP ILE TYR GLY ALA VAL HIS ASP LEU
SEQRES  21 A  291  ARG LEU HIS ARG VAL HIS MET VAL GLN THR GLU CYS GLN
SEQRES  22 A  291  TYR VAL TYR LEU HIS GLN CYS VAL ARG ASP VAL LEU ARG
SEQRES  23 A  291  ALA ARG LYS LEU ARG
HET    ACT  A 601       4
HET     CL  A 602       1
HET     CL  A 603       1
HETNAM     ACT ACETATE ION
HETNAM      CL CHLORIDE ION
FORMUL   2  ACT    C2 H3 O2 1-
FORMUL   3   CL    2(CL 1-)
FORMUL   5  HOH   *362(H2 O)
HELIX    1   1 GLN A 1687  LEU A 1710  1                                  24
HELIX    2   2 ASN A 1727  ASN A 1731  5                                   5
HELIX    3   3 TYR A 1739  ALA A 1741  5                                   3
HELIX    4   4 THR A 1782  GLN A 1793  1                                  12
HELIX    5   5 THR A 1876  SER A 1894  1                                  19
HELIX    6   6 VAL A 1908  LYS A 1927  1                                  20
HELIX    7   7 ASP A 1931  LEU A 1941  1                                  11
HELIX    8   8 THR A 1949  LEU A 1969  1                                  21
SHEET    1   A 2 ILE A1683  LYS A1684  0
SHEET    2   A 2 SER A1929  VAL A1930 -1  O  VAL A1930   N  ILE A1683
SHEET    1   B 9 ARG A1743  LYS A1745  0
SHEET    2   B 9 TYR A1757  ILE A1763 -1  O  ALA A1760   N  VAL A1744
SHEET    3   B 9 TYR A1772  THR A1775 -1  O  VAL A1774   N  SER A1761
SHEET    4   B 9 THR A1900  HIS A1903  1  O  VAL A1902   N  ILE A1773
SHEET    5   B 9 ASN A1797  MET A1800  1  N  VAL A1799   O  VAL A1901
SHEET    6   B 9 ARG A1858  TYR A1865  1  O  PHE A1863   N  ILE A1798
SHEET    7   B 9 TRP A1841  CYS A1849 -1  N  THR A1842   O  HIS A1864
SHEET    8   B 9 LEU A1828  VAL A1837 -1  N  LEU A1833   O  GLU A1845
SHEET    9   B 9 LEU A1823  TYR A1825 -1  N  TYR A1825   O  LEU A1828
SHEET    1   C 2 VAL A1805  GLU A1806  0
SHEET    2   C 2 ARG A1809  VAL A1810 -1  O  ARG A1809   N  GLU A1806
LINK         C   GLY A1749                 N   SER A1755     1555   1555  1.33
SITE     1 AC1  3 ARG A1885  ARG A1967  ARG A1970
SITE     1 AC2  6 HOH A 460  GLY A1765  ASN A1766  ASN A1767
SITE     2 AC2  6 PHE A1768  ARG A1970
SITE     1 AC3  3 HOH A 598  PRO A1764  ARG A1770
CRYST1   39.060   70.714  118.455  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      0.025602  0.000000  0.000000        0.00000
SCALE2      0.000000  0.014141  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008442        0.00000
      
PROCHECK
Go to PROCHECK summary
 References