HEADER HYDROLASE 28-MAR-07 2PBN
TITLE CRYSTAL STRUCTURE OF THE HUMAN TYROSINE RECEPTOR PHOSPHATE GAMMA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE GAMMA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TYROSINE-PROTEIN PHOSPHATASE 1;
COMPND 5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE GAMMA, R-PTP-GAMMA;
COMPND 6 EC: 3.1.3.48;
COMPND 7 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: PTPRG;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET26
KEYWDS STRUCTURAL GENOMICS, HYDROLASE, PSI-2, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS, NYSGXRC
EXPDTA X-RAY DIFFRACTION
AUTHOR J.B.BONANNO,J.FREEMAN,K.T.BAIN,C.REYES,L.PELLETIER,X.JIN,D.SMITH,
AUTHOR 2 S.WASSERMAN,J.M.SAUDER,S.K.BURLEY,S.C.ALMO,NEW YORK SGX RESEARCH
AUTHOR 3 CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 5 30-AUG-23 2PBN 1 REMARK
REVDAT 4 03-FEB-21 2PBN 1 AUTHOR JRNL REMARK SEQADV
REVDAT 3 14-NOV-18 2PBN 1 AUTHOR
REVDAT 2 25-MAR-08 2PBN 1 AUTHOR JRNL VERSN
REVDAT 1 03-APR-07 2PBN 0
JRNL AUTH S.C.ALMO,J.B.BONANNO,J.M.SAUDER,S.EMTAGE,T.P.DILORENZO,
JRNL AUTH 2 V.MALASHKEVICH,S.R.WASSERMAN,S.SWAMINATHAN,S.ESWARAMOORTHY,
JRNL AUTH 3 R.AGARWAL,D.KUMARAN,M.MADEGOWDA,S.RAGUMANI,Y.PATSKOVSKY,
JRNL AUTH 4 J.ALVARADO,U.A.RAMAGOPAL,J.FABER-BARATA,M.R.CHANCE,A.SALI,
JRNL AUTH 5 A.FISER,Z.Y.ZHANG,D.S.LAWRENCE,S.K.BURLEY
JRNL TITL STRUCTURAL GENOMICS OF PROTEIN PHOSPHATASES.
JRNL REF J.STRUCT.FUNCT.GENOM. V. 8 121 2007
JRNL REFN ISSN 1345-711X
JRNL PMID 18058037
JRNL DOI 10.1007/S10969-007-9036-1
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 49610
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2485
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3362
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.67
REMARK 3 BIN R VALUE (WORKING SET) : 0.4090
REMARK 3 BIN FREE R VALUE SET COUNT : 160
REMARK 3 BIN FREE R VALUE : 0.4460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2325
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 238
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.63000
REMARK 3 B22 (A**2) : -0.63000
REMARK 3 B33 (A**2) : 0.94000
REMARK 3 B12 (A**2) : -0.31000
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): 0.095
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.095
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.070
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.158
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2389 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3238 ; 1.527 ; 1.935
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 285 ; 5.466 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 121 ;32.267 ;23.802
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 417 ;13.437 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;16.741 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 352 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1820 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1120 ; 0.202 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1653 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 204 ; 0.126 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
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): 34 ; 0.266 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.151 ; 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): 1468 ; 1.283 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2317 ; 1.948 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1061 ; 3.075 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 920 ; 4.865 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2PBN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042197.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-SEP-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.10000
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49677
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 53.683
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 10.20
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : 0.05400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.79
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.64500
REMARK 200 R SYM FOR SHELL (I) : 0.64500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: PDB ENTRY 2HY3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM MES PH 6.5, 22% PEG 8000,
REMARK 280 200MM AMMONIUM SULFATE, VAPOR DIFFUSION, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
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 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 45.17133
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 22.58567
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 22.58567
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 45.17133
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). AUTHORS STATE THAT A MONOMER
REMARK 300 IS PROBABLY THE BIOLOGICAL UNIT OF THIS POLYPEPTIDE.
REMARK 300 SEE REMARK 350 FOR INFORMATION ON GENERATING THE BIOLOGICAL
REMARK 300 MOLECULE(S).
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 818
REMARK 465 LEU A 819
REMARK 465 PRO A 820
REMARK 465 ILE A 821
REMARK 465 PRO A 822
REMARK 465 ASP A 823
REMARK 465 ASP A 824
REMARK 465 MET A 825
REMARK 465 LYS A 1002
REMARK 465 LYS A 1003
REMARK 465 GLY A 1004
REMARK 465 GLN A 1005
REMARK 465 LYS A 1006
REMARK 465 GLY A 1007
REMARK 465 ASN A 1008
REMARK 465 PRO A 1009
REMARK 465 LYS A 1010
REMARK 465 GLY A 1011
REMARK 465 ARG A 1012
REMARK 465 GLN A 1013
REMARK 465 LYS A 1123
REMARK 465 GLU A 1124
REMARK 465 THR A 1125
REMARK 465 GLU A 1126
REMARK 465 VAL A 1127
REMARK 465 SER A 1128
REMARK 465 SER A 1129
REMARK 465 ASN A 1130
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 OH TYR A 841 OD1 ASP A 1114 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 959 NE - CZ - NH2 ANGL. DEV. = -3.2 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 ALA A 866 58.63 -143.10
REMARK 500 LYS A 917 113.84 -162.97
REMARK 500 ASN A 969 -136.18 55.00
REMARK 500 CYS A1060 -122.01 -131.75
REMARK 500 SER A1061 -66.46 -92.61
REMARK 500 VAL A1103 88.20 65.93
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 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-8615A RELATED DB: TARGETDB
REMARK 900 RELATED ID: 2HY3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN TYROSINE RECEPTOR PHOSPHATE GAMMA IN
REMARK 900 COMPLEX WITH VANADATE
DBREF 2PBN A 820 1130 UNP P23470 PTPRG_HUMAN 820 1130
SEQADV 2PBN SER A 818 UNP P23470 CLONING ARTIFACT
SEQADV 2PBN LEU A 819 UNP P23470 CLONING ARTIFACT
SEQRES 1 A 313 SER LEU PRO ILE PRO ASP ASP MET GLU ALA ILE PRO VAL
SEQRES 2 A 313 LYS GLN PHE VAL LYS HIS ILE GLY GLU LEU TYR SER ASN
SEQRES 3 A 313 ASN GLN HIS GLY PHE SER GLU ASP PHE GLU GLU VAL GLN
SEQRES 4 A 313 ARG CYS THR ALA ASP MET ASN ILE THR ALA GLU HIS SER
SEQRES 5 A 313 ASN HIS PRO GLU ASN LYS HIS LYS ASN ARG TYR ILE ASN
SEQRES 6 A 313 ILE LEU ALA TYR ASP HIS SER ARG VAL LYS LEU ARG PRO
SEQRES 7 A 313 LEU PRO GLY LYS ASP SER LYS HIS SER ASP TYR ILE ASN
SEQRES 8 A 313 ALA ASN TYR VAL ASP GLY TYR ASN LYS ALA LYS ALA TYR
SEQRES 9 A 313 ILE ALA THR GLN GLY PRO LEU LYS SER THR PHE GLU ASP
SEQRES 10 A 313 PHE TRP ARG MET ILE TRP GLU GLN ASN THR GLY ILE ILE
SEQRES 11 A 313 VAL MET ILE THR ASN LEU VAL GLU LYS GLY ARG ARG LYS
SEQRES 12 A 313 CYS ASP GLN TYR TRP PRO THR GLU ASN SER GLU GLU TYR
SEQRES 13 A 313 GLY ASN ILE ILE VAL THR LEU LYS SER THR LYS ILE HIS
SEQRES 14 A 313 ALA CYS TYR THR VAL ARG ARG PHE SER ILE ARG ASN THR
SEQRES 15 A 313 LYS VAL LYS LYS GLY GLN LYS GLY ASN PRO LYS GLY ARG
SEQRES 16 A 313 GLN ASN GLU ARG VAL VAL ILE GLN TYR HIS TYR THR GLN
SEQRES 17 A 313 TRP PRO ASP MET GLY VAL PRO GLU TYR ALA LEU PRO VAL
SEQRES 18 A 313 LEU THR PHE VAL ARG ARG SER SER ALA ALA ARG MET PRO
SEQRES 19 A 313 GLU THR GLY PRO VAL LEU VAL HIS CYS SER ALA GLY VAL
SEQRES 20 A 313 GLY ARG THR GLY THR TYR ILE VAL ILE ASP SER MET LEU
SEQRES 21 A 313 GLN GLN ILE LYS ASP LYS SER THR VAL ASN VAL LEU GLY
SEQRES 22 A 313 PHE LEU LYS HIS ILE ARG THR GLN ARG ASN TYR LEU VAL
SEQRES 23 A 313 GLN THR GLU GLU GLN TYR ILE PHE ILE HIS ASP ALA LEU
SEQRES 24 A 313 LEU GLU ALA ILE LEU GLY LYS GLU THR GLU VAL SER SER
SEQRES 25 A 313 ASN
HET SO4 A 301 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 O4 S 2-
FORMUL 3 HOH *238(H2 O)
HELIX 1 1 VAL A 830 CYS A 858 1 29
HELIX 2 2 ALA A 866 HIS A 871 1 6
HELIX 3 3 PRO A 872 ASN A 878 5 7
HELIX 4 4 TYR A 886 HIS A 888 5 3
HELIX 5 5 SER A 901 SER A 904 5 4
HELIX 6 6 LEU A 928 SER A 930 5 3
HELIX 7 7 THR A 931 ASN A 943 1 13
HELIX 8 8 TYR A 1034 ALA A 1048 1 15
HELIX 9 9 VAL A 1064 SER A 1084 1 21
HELIX 10 10 ASN A 1087 ARG A 1096 1 10
HELIX 11 11 THR A 1105 GLY A 1122 1 18
SHEET 1 A 2 ILE A 828 PRO A 829 0
SHEET 2 A 2 THR A1085 VAL A1086 -1 O VAL A1086 N ILE A 828
SHEET 1 B 9 ARG A 890 LYS A 892 0
SHEET 2 B 9 TYR A 906 GLY A 914 -1 O ALA A 909 N VAL A 891
SHEET 3 B 9 LYS A 917 THR A 924 -1 O LYS A 917 N GLY A 914
SHEET 4 B 9 VAL A1056 HIS A1059 1 O VAL A1058 N ILE A 922
SHEET 5 B 9 ILE A 946 MET A 949 1 N VAL A 948 O LEU A1057
SHEET 6 B 9 GLU A1015 TYR A1023 1 O TYR A1021 N ILE A 947
SHEET 7 B 9 TYR A 989 ASN A 998 -1 N THR A 990 O HIS A1022
SHEET 8 B 9 ILE A 976 ILE A 985 -1 N THR A 979 O SER A 995
SHEET 9 B 9 SER A 970 TYR A 973 -1 N TYR A 973 O ILE A 976
SHEET 1 C 2 VAL A 954 GLU A 955 0
SHEET 2 C 2 ARG A 958 ARG A 959 -1 O ARG A 958 N GLU A 955
SITE 1 AC1 8 HOH A 10 HOH A 58 HOH A 89 HOH A 123
SITE 2 AC1 8 GLY A1065 ARG A1066 GLN A1104 GLN A1108
CRYST1 107.338 107.338 67.757 90.00 90.00 120.00 P 32 2 1 6
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 0.009316 0.005379 0.000000 0.00000
SCALE2 0.000000 0.010758 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014759 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
