HEADER HYDROLASE 07-JUL-05 2A8B
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN TYROSINE
TITLE 2 PHOSPHATASE RECEPTOR, TYPE R
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE R;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN RESIDUES 375-655;
COMPND 5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE PCPTP1, NC-PTPCOM1, CH-1PTPASE;
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: PTPRR, ECPTP;
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: PGEX-6P2
KEYWDS PROTEIN TYROSINE PHOSPHATASE, RECEPTOR, HUMAN, STRUCTURAL GENOMICS,
KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, SGC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.UGOCHUKWU,J.ESWARAN,A.BARR,E.LONGMAN,C.ARROWSMITH,A.EDWARDS,
AUTHOR 2 M.SUNDSTROM,F.VON DELFT,S.KNAPP,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 5 23-AUG-23 2A8B 1 REMARK SEQADV
REVDAT 4 13-JUL-11 2A8B 1 VERSN
REVDAT 3 03-FEB-09 2A8B 1 JRNL
REVDAT 2 20-MAY-08 2A8B 1 JRNL VERSN
REVDAT 1 19-JUL-05 2A8B 0
SPRSDE 19-JUL-05 2A8B 1ZEP
JRNL AUTH J.ESWARAN,J.P.VON KRIES,B.MARSDEN,E.LONGMAN,J.E.DEBRECZENI,
JRNL AUTH 2 E.UGOCHUKWU,A.TURNBULL,W.H.LEE,S.KNAPP,A.J.BARR
JRNL TITL CRYSTAL STRUCTURES AND INHIBITOR IDENTIFICATION FOR PTPN5,
JRNL TITL 2 PTPRR AND PTPN7: A FAMILY OF HUMAN MAPK-SPECIFIC PROTEIN
JRNL TITL 3 TYROSINE PHOSPHATASES.
JRNL REF BIOCHEM.J. V. 395 483 2006
JRNL REFN ISSN 0264-6021
JRNL PMID 16441242
JRNL DOI 10.1042/BJ20051931
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 62.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 12390
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 640
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 914
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE SET COUNT : 47
REMARK 3 BIN FREE R VALUE : 0.3130
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2220
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 132
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.55
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.45000
REMARK 3 B22 (A**2) : 2.47000
REMARK 3 B33 (A**2) : -1.02000
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): 0.405
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.264
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.203
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.144
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.895
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2269 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2057 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3082 ; 1.317 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4771 ; 0.976 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 282 ; 6.611 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;35.071 ;23.700
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 387 ;16.064 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;14.749 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 348 ; 0.121 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2510 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 449 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 504 ; 0.188 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2215 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1119 ; 0.171 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1388 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 142 ; 0.180 ; 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): 16 ; 0.154 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 49 ; 0.230 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.205 ; 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): 1462 ; 0.509 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 570 ; 0.088 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2302 ; 0.831 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 935 ; 1.151 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 780 ; 1.824 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A -1 A 655
REMARK 3 ORIGIN FOR THE GROUP (A): 11.8549 17.6100 17.7851
REMARK 3 T TENSOR
REMARK 3 T11: -0.1280 T22: -0.0789
REMARK 3 T33: -0.1083 T12: -0.0070
REMARK 3 T13: 0.0017 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 1.5231 L22: 1.5904
REMARK 3 L33: 1.4891 L12: 0.2840
REMARK 3 L13: 0.1894 L23: -0.3311
REMARK 3 S TENSOR
REMARK 3 S11: -0.0642 S12: 0.1909 S13: -0.0233
REMARK 3 S21: -0.1781 S22: 0.1225 S23: 0.0969
REMARK 3 S31: 0.0631 S32: -0.1926 S33: -0.0583
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2A8B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033613.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAR-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 : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13031
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 62.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
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 <I/SIGMA(I)> 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: 1JLN.PDB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, (NH4)H2PO4, PH 8.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 31.59650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.04900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.59650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.04900
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE A -1 CG1 CG2 CD1
REMARK 470 MET A 398 SD CE
REMARK 470 GLU A 399 CD OE1 OE2
REMARK 470 LYS A 408 CD CE NZ
REMARK 470 GLU A 409 CD OE1 OE2
REMARK 470 LEU A 429 CD1
REMARK 470 LYS A 437 CD CE NZ
REMARK 470 GLU A 459 CD OE1 OE2
REMARK 470 GLU A 507 CD OE1 OE2
REMARK 470 LYS A 508 CE NZ
REMARK 470 LYS A 514 CE NZ
REMARK 470 GLU A 524 CD OE1 OE2
REMARK 470 LYS A 536 NZ
REMARK 470 LYS A 556 CD CE NZ
REMARK 470 GLN A 566 OE1
REMARK 470 LEU A 576 CD1 CD2
REMARK 470 LYS A 609 CD CE NZ
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 376 73.30 -168.30
REMARK 500 SER A 389 59.25 -164.64
REMARK 500 ASP A 411 59.32 -119.95
REMARK 500 ARG A 435 66.64 -119.47
REMARK 500 ILE A 491 70.30 -114.66
REMARK 500 THR A 492 139.71 -174.16
REMARK 500 LYS A 497 -66.55 71.78
REMARK 500 CYS A 588 -110.56 -126.51
REMARK 500 ILE A 592 -36.44 -135.63
REMARK 500 VAL A 631 92.68 67.37
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 CL A 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JLN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF PROTEIN TYROSINE
REMARK 900 PHOSPHATASE PTP-SI/BR7
DBREF 2A8B A 375 655 UNP Q15256 PTPRR_HUMAN 375 655
SEQADV 2A8B ILE A -1 UNP Q15256 CLONING ARTIFACT
SEQADV 2A8B PRO A 0 UNP Q15256 CLONING ARTIFACT
SEQRES 1 A 283 ILE PRO SER ARG ILE LEU THR ARG SER GLN LEU ARG ASP
SEQRES 2 A 283 VAL VAL ALA SER SER HIS LEU LEU GLN SER GLU PHE MET
SEQRES 3 A 283 GLU ILE PRO MET ASN PHE VAL ASP PRO LYS GLU ILE ASP
SEQRES 4 A 283 ILE PRO ARG HIS GLY THR LYS ASN ARG TYR LYS THR ILE
SEQRES 5 A 283 LEU PRO ASN PRO LEU SER ARG VAL CYS LEU ARG PRO LYS
SEQRES 6 A 283 ASN VAL THR ASP SER LEU SER THR TYR ILE ASN ALA ASN
SEQRES 7 A 283 TYR ILE ARG GLY TYR SER GLY LYS GLU LYS ALA PHE ILE
SEQRES 8 A 283 ALA THR GLN GLY PRO MET ILE ASN THR VAL ASP ASP PHE
SEQRES 9 A 283 TRP GLN MET VAL TRP GLN GLU ASP SER PRO VAL ILE VAL
SEQRES 10 A 283 MET ILE THR LYS LEU LYS GLU LYS ASN GLU LYS CYS VAL
SEQRES 11 A 283 LEU TYR TRP PRO GLU LYS ARG GLY ILE TYR GLY LYS VAL
SEQRES 12 A 283 GLU VAL LEU VAL ILE SER VAL ASN GLU CYS ASP ASN TYR
SEQRES 13 A 283 THR ILE ARG ASN LEU VAL LEU LYS GLN GLY SER HIS THR
SEQRES 14 A 283 GLN HIS VAL LYS HIS TYR TRP TYR THR SER TRP PRO ASP
SEQRES 15 A 283 HIS LYS THR PRO ASP SER ALA GLN PRO LEU LEU GLN LEU
SEQRES 16 A 283 MET LEU ASP VAL GLU GLU ASP ARG LEU ALA SER GLN GLY
SEQRES 17 A 283 ARG GLY PRO VAL VAL VAL HIS CYS SER ALA GLY ILE GLY
SEQRES 18 A 283 ARG THR GLY CYS PHE ILE ALA THR SER ILE GLY CYS GLN
SEQRES 19 A 283 GLN LEU LYS GLU GLU GLY VAL VAL ASP ALA LEU SER ILE
SEQRES 20 A 283 VAL CYS GLN LEU ARG MET ASP ARG GLY GLY MET VAL GLN
SEQRES 21 A 283 THR SER GLU GLN TYR GLU PHE VAL HIS HIS ALA LEU CYS
SEQRES 22 A 283 LEU TYR GLU SER ARG LEU SER ALA GLU THR
HET CL A 200 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL CL 1-
FORMUL 3 HOH *132(H2 O)
HELIX 1 1 ARG A 380 VAL A 387 1 8
HELIX 2 2 SER A 389 GLU A 399 1 11
HELIX 3 3 ASP A 406 ILE A 410 5 5
HELIX 4 4 ARG A 414 ASN A 419 5 6
HELIX 5 5 ASN A 427 LEU A 429 5 3
HELIX 6 6 ASP A 441 SER A 444 5 4
HELIX 7 7 GLY A 454 LYS A 458 5 5
HELIX 8 8 MET A 469 ASN A 471 5 3
HELIX 9 9 THR A 472 ASP A 484 1 13
HELIX 10 10 ALA A 561 ALA A 577 1 17
HELIX 11 11 ILE A 592 GLY A 612 1 21
HELIX 12 12 ASP A 615 ARG A 627 1 13
HELIX 13 13 THR A 633 SER A 649 1 17
SHEET 1 A 2 LEU A 378 THR A 379 0
SHEET 2 A 2 VAL A 613 VAL A 614 -1 O VAL A 614 N LEU A 378
SHEET 1 B 9 ARG A 431 CYS A 433 0
SHEET 2 B 9 TYR A 446 ILE A 452 -1 O ALA A 449 N VAL A 432
SHEET 3 B 9 PHE A 462 THR A 465 -1 O PHE A 462 N ILE A 452
SHEET 4 B 9 VAL A 584 HIS A 587 1 O VAL A 586 N ILE A 463
SHEET 5 B 9 VAL A 487 ILE A 491 1 N VAL A 489 O VAL A 585
SHEET 6 B 9 HIS A 540 TYR A 549 1 O LYS A 545 N ILE A 488
SHEET 7 B 9 THR A 529 GLN A 537 -1 N LEU A 535 O GLN A 542
SHEET 8 B 9 VAL A 515 GLU A 524 -1 N ASN A 523 O ILE A 530
SHEET 9 B 9 ARG A 509 TYR A 512 -1 N TYR A 512 O VAL A 515
SITE 1 AC1 3 GLU A 459 GLY A 510 ILE A 511
CRYST1 63.193 74.098 62.328 90.00 90.00 90.00 P 21 21 2 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 0.015825 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013496 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016044 0.00000
(ATOM LINES ARE NOT SHOWN.)
END