HEADER HYDROLASE 21-JUN-07 2QDM
TITLE CRYSTAL STRUCTURE OF THE HEPTP CATALYTIC DOMAIN C270S/D236A/Q314A
TITLE 2 MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 7;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN (RESIDUES 65-360);
COMPND 5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE LC-PTP, HEMATOPOIETIC PROTEIN-
COMPND 6 TYROSINE PHOSPHATASE, HEPTP;
COMPND 7 EC: 3.1.3.48;
COMPND 8 ENGINEERED: YES;
COMPND 9 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: PTPN7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBAD
KEYWDS HEPTP, HUMAN HEMATOPOIETIC TYROSINE PHOSPHATASE CATALYTIC DOMAIN
KEYWDS 2 MUTANT, LC-PTP, PTPN7, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.CRITTON,A.TORTAJADA,R.PAGE
REVDAT 3 13-JUL-11 2QDM 1 VERSN
REVDAT 2 24-FEB-09 2QDM 1 VERSN
REVDAT 1 24-JUN-08 2QDM 0
JRNL AUTH D.A.CRITTON,A.TORTAJADA,G.STETSON,W.PETI,R.PAGE
JRNL TITL STRUCTURAL BASIS OF SUBSTRATE RECOGNITION BY HEMATOPOIETIC
JRNL TITL 2 TYROSINE PHOSPHATASE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 19016
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1023
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1297
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.1590
REMARK 3 BIN FREE R VALUE SET COUNT : 72
REMARK 3 BIN FREE R VALUE : 0.2000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2242
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 186
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) : 22.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.27000
REMARK 3 B22 (A**2) : -0.17000
REMARK 3 B33 (A**2) : -0.07000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.91000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.176
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.156
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.627
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2308 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3145 ; 1.465 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 284 ;10.079 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 103 ;37.790 ;23.495
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 370 ;13.129 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;17.286 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 345 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1769 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 994 ; 0.203 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1537 ; 0.305 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 147 ; 0.156 ; 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): 39 ; 0.158 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.090 ; 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): 1496 ; 1.976 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2316 ; 2.979 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 956 ; 4.692 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 829 ; 6.796 ;11.000
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 45 A 336
REMARK 3 ORIGIN FOR THE GROUP (A): -14.9029 13.4958 -15.2480
REMARK 3 T TENSOR
REMARK 3 T11: -0.0252 T22: -0.0376
REMARK 3 T33: -0.0169 T12: 0.0020
REMARK 3 T13: 0.0051 T23: 0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 0.5573 L22: 0.1444
REMARK 3 L33: 1.0050 L12: 0.0711
REMARK 3 L13: -0.3576 L23: -0.0805
REMARK 3 S TENSOR
REMARK 3 S11: 0.0248 S12: -0.0740 S13: 0.0336
REMARK 3 S21: 0.0022 S22: 0.0073 S23: 0.0389
REMARK 3 S31: -0.0283 S32: 0.0512 S33: -0.0321
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 2QDM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-07.
REMARK 100 THE RCSB ID CODE IS RCSB043465.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-APR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1000
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL CUT MONOCHROMATOR
REMARK 200 OPTICS : SI(111) CHANNEL CUT
REMARK 200 MONOCHROMATOR, TOROIDAL FOCUSING
REMARK 200 MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19884
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.12000
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: PDB ENTRY 1ZC0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM CHLORIDE, 0.1 M SODIUM
REMARK 280 ACETATE, PH 4.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 59.66200
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 19.52050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.66200
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 19.52050
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 MET A -12
REMARK 465 GLY A -11
REMARK 465 SER A -10
REMARK 465 ASP A -9
REMARK 465 LYS A -8
REMARK 465 ILE A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 ASN A 44
REMARK 465 ARG A 177
REMARK 465 GLU A 178
REMARK 465 GLY A 179
REMARK 465 LYS A 180
REMARK 465 GLU A 181
REMARK 465 LYS A 182
REMARK 465 PRO A 337
REMARK 465 SER A 338
REMARK 465 PRO A 339
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 GLN A 112 CG CD OE1 NE2
REMARK 470 SER A 122 OG
REMARK 470 GLN A 123 CG CD OE1 NE2
REMARK 470 GLU A 124 CG CD OE1 OE2
REMARK 470 GLU A 191 CD OE1 OE2
REMARK 470 ARG A 200 NE CZ NH1 NH2
REMARK 470 GLN A 202 CD OE1 NE2
REMARK 470 GLU A 209 CG CD OE1 OE2
REMARK 470 GLU A 221 CG CD OE1 OE2
REMARK 470 GLU A 255 CG CD OE1 OE2
REMARK 470 GLU A 258 CG CD OE1 OE2
REMARK 470 HIS A 262 CG ND1 CD2 CE1 NE2
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 CG GLU A 254 O HOH A 466 2.19
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 A 69 58.24 -143.26
REMARK 500 ASP A 94 74.43 -111.23
REMARK 500 GLU A 190 -55.55 -137.07
REMARK 500 GLN A 220 -121.73 59.13
REMARK 500 ILE A 274 -41.10 -136.73
REMARK 500 ILE A 313 112.77 62.73
REMARK 500 GLU A 335 -148.55 179.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE A 313 ALA A 314 -132.19
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 PO4 A 340
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 341
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZC0 RELATED DB: PDB
REMARK 900 RELATED ID: 2GP0 RELATED DB: PDB
REMARK 900 RELATED ID: 2HVL RELATED DB: PDB
REMARK 900 RELATED ID: 2QDC RELATED DB: PDB
REMARK 900 RELATED ID: 2QDP RELATED DB: PDB
DBREF 2QDM A 44 339 UNP P35236 PTN7_HUMAN 65 360
SEQADV 2QDM MET A -12 UNP P35236 LEADER SEQUENCE
SEQADV 2QDM GLY A -11 UNP P35236 LEADER SEQUENCE
SEQADV 2QDM SER A -10 UNP P35236 LEADER SEQUENCE
SEQADV 2QDM ASP A -9 UNP P35236 LEADER SEQUENCE
SEQADV 2QDM LYS A -8 UNP P35236 LEADER SEQUENCE
SEQADV 2QDM ILE A -7 UNP P35236 LEADER SEQUENCE
SEQADV 2QDM HIS A -6 UNP P35236 LEADER SEQUENCE
SEQADV 2QDM HIS A -5 UNP P35236 LEADER SEQUENCE
SEQADV 2QDM HIS A -4 UNP P35236 LEADER SEQUENCE
SEQADV 2QDM HIS A -3 UNP P35236 LEADER SEQUENCE
SEQADV 2QDM HIS A -2 UNP P35236 LEADER SEQUENCE
SEQADV 2QDM HIS A -1 UNP P35236 LEADER SEQUENCE
SEQADV 2QDM MET A 0 UNP P35236 LEADER SEQUENCE
SEQADV 2QDM ALA A 236 UNP P35236 ASP 257 ENGINEERED
SEQADV 2QDM SER A 270 UNP P35236 CYS 291 ENGINEERED
SEQADV 2QDM ALA A 314 UNP P35236 GLN 335 ENGINEERED
SEQRES 1 A 309 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 A 309 ASN THR PRO ARG GLU VAL THR LEU HIS PHE LEU ARG THR
SEQRES 3 A 309 ALA GLY HIS PRO LEU THR ARG TRP ALA LEU GLN ARG GLN
SEQRES 4 A 309 PRO PRO SER PRO LYS GLN LEU GLU GLU GLU PHE LEU LYS
SEQRES 5 A 309 ILE PRO SER ASN PHE VAL SER PRO GLU ASP LEU ASP ILE
SEQRES 6 A 309 PRO GLY HIS ALA SER LYS ASP ARG TYR LYS THR ILE LEU
SEQRES 7 A 309 PRO ASN PRO GLN SER ARG VAL CYS LEU GLY ARG ALA GLN
SEQRES 8 A 309 SER GLN GLU ASP GLY ASP TYR ILE ASN ALA ASN TYR ILE
SEQRES 9 A 309 ARG GLY TYR ASP GLY LYS GLU LYS VAL TYR ILE ALA THR
SEQRES 10 A 309 GLN GLY PRO MET PRO ASN THR VAL SER ASP PHE TRP GLU
SEQRES 11 A 309 MET VAL TRP GLN GLU GLU VAL SER LEU ILE VAL MET LEU
SEQRES 12 A 309 THR GLN LEU ARG GLU GLY LYS GLU LYS CYS VAL HIS TYR
SEQRES 13 A 309 TRP PRO THR GLU GLU GLU THR TYR GLY PRO PHE GLN ILE
SEQRES 14 A 309 ARG ILE GLN ASP MET LYS GLU CYS PRO GLU TYR THR VAL
SEQRES 15 A 309 ARG GLN LEU THR ILE GLN TYR GLN GLU GLU ARG ARG SER
SEQRES 16 A 309 VAL LYS HIS ILE LEU PHE SER ALA TRP PRO ALA HIS GLN
SEQRES 17 A 309 THR PRO GLU SER ALA GLY PRO LEU LEU ARG LEU VAL ALA
SEQRES 18 A 309 GLU VAL GLU GLU SER PRO GLU THR ALA ALA HIS PRO GLY
SEQRES 19 A 309 PRO ILE VAL VAL HIS SER SER ALA GLY ILE GLY ARG THR
SEQRES 20 A 309 GLY CYS PHE ILE ALA THR ARG ILE GLY CYS GLN GLN LEU
SEQRES 21 A 309 LYS ALA ARG GLY GLU VAL ASP ILE LEU GLY ILE VAL CYS
SEQRES 22 A 309 GLN LEU ARG LEU ASP ARG GLY GLY MET ILE ALA THR ALA
SEQRES 23 A 309 GLU GLN TYR GLN PHE LEU HIS HIS THR LEU ALA LEU TYR
SEQRES 24 A 309 ALA GLY GLN LEU PRO GLU GLU PRO SER PRO
HET PO4 A 340 5
HET PO4 A 341 5
HETNAM PO4 PHOSPHATE ION
FORMUL 2 PO4 2(O4 P 3-)
FORMUL 4 HOH *186(H2 O)
HELIX 1 1 THR A 45 ALA A 57 1 13
HELIX 2 2 ARG A 63 GLN A 69 1 7
HELIX 3 3 SER A 72 ILE A 83 1 12
HELIX 4 4 SER A 89 LEU A 93 5 5
HELIX 5 5 GLY A 97 ASP A 102 5 6
HELIX 6 6 ASN A 110 GLN A 112 5 3
HELIX 7 7 GLY A 136 LYS A 140 5 5
HELIX 8 8 MET A 151 ASN A 153 5 3
HELIX 9 9 THR A 154 GLU A 165 1 12
HELIX 10 10 ALA A 243 SER A 256 1 14
HELIX 11 11 ILE A 274 GLY A 294 1 21
HELIX 12 12 ASP A 297 ARG A 309 1 13
HELIX 13 13 THR A 315 LEU A 333 1 19
SHEET 1 A 2 LEU A 61 THR A 62 0
SHEET 2 A 2 GLU A 295 VAL A 296 -1 O VAL A 296 N LEU A 61
SHEET 1 B 9 ARG A 114 CYS A 116 0
SHEET 2 B 9 TYR A 128 ILE A 134 -1 O ALA A 131 N VAL A 115
SHEET 3 B 9 TYR A 144 GLN A 148 -1 O TYR A 144 N ILE A 134
SHEET 4 B 9 ILE A 266 SER A 270 1 O VAL A 268 N ILE A 145
SHEET 5 B 9 LEU A 169 LEU A 173 1 N VAL A 171 O VAL A 267
SHEET 6 B 9 GLU A 222 PHE A 231 1 O ILE A 229 N MET A 172
SHEET 7 B 9 TYR A 210 TYR A 219 -1 N LEU A 215 O VAL A 226
SHEET 8 B 9 PHE A 197 CYS A 207 -1 N GLN A 202 O GLN A 214
SHEET 9 B 9 GLU A 191 TYR A 194 -1 N GLU A 192 O ILE A 199
SITE 1 AC1 8 SER A 270 SER A 271 ALA A 272 GLY A 273
SITE 2 AC1 8 ILE A 274 GLY A 275 ARG A 276 HOH A 344
SITE 1 AC2 5 THR A 174 GLN A 175 SER A 271 ARG A 276
SITE 2 AC2 5 HOH A 446
CRYST1 119.324 39.041 83.473 90.00 124.53 90.00 C 1 2 1 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 0.008381 0.000000 0.005766 0.00000
SCALE2 0.000000 0.025614 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014542 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
