HEADER HYDROLASE 06-DEC-13 4NWF
TITLE CRYSTAL STRUCTURE OF THE TYROSINE PHOSPHATASE SHP-2 WITH N308D
TITLE 2 MUTATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 11;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-543;
COMPND 5 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE 1D, PTP-1D, PROTEIN-TYROSINE
COMPND 6 PHOSPHATASE 2C, PTP-2C, SH-PTP2, SHP-2, SHP2, SH-PTP3;
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: PTPN11, PTP2C, SHPTP2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.QIU,A.LIN,A.HUTCHINSON,V.ROMANOV,M.RUZANOV,C.THOMPSON,K.LAM,
AUTHOR 2 G.KISSELMAN,K.BATTALIE,N.Y.CHIRGADZE
REVDAT 2 28-FEB-24 4NWF 1 REMARK SEQADV
REVDAT 1 10-DEC-14 4NWF 0
JRNL AUTH W.QIU,A.LIN,A.HUTCHINSON,V.ROMANOV,M.RUZANOV,C.THOMPSON,
JRNL AUTH 2 K.LAM,G.KISSELMAN,K.BATTALIE,N.Y.CHIRGADZE
JRNL TITL CRYSTAL STRUCTURE OF THE TYROSINE PHOSPHATASE SHP-2 WITH
JRNL TITL 2 N308D MUTATION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 64235
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) : 0.267
REMARK 3 R VALUE (WORKING SET) : 0.266
REMARK 3 FREE R VALUE : 0.309
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.490
REMARK 3 FREE R VALUE TEST SET COUNT : 954
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.15
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.96
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4725
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2093
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4658
REMARK 3 BIN R VALUE (WORKING SET) : 0.2093
REMARK 3 BIN FREE R VALUE : 0.2144
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.42
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 67
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7981
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 655
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.31170
REMARK 3 B22 (A**2) : -2.99560
REMARK 3 B33 (A**2) : -1.31610
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.346
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.305
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 8214 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 11065 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3871 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 231 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1173 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8214 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1028 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 9433 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 0.90
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.47
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.08
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|3 - A|533 }
REMARK 3 ORIGIN FOR THE GROUP (A): 81.5570 29.0560 -42.2820
REMARK 3 T TENSOR
REMARK 3 T11: 0.1128 T22: 0.1283
REMARK 3 T33: 0.1752 T12: -0.0223
REMARK 3 T13: -0.0067 T23: -0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 1.6099 L22: 0.4816
REMARK 3 L33: 0.6925 L12: 0.0669
REMARK 3 L13: 0.5826 L23: 0.1244
REMARK 3 S TENSOR
REMARK 3 S11: 0.0942 S12: 0.1179 S13: -0.1013
REMARK 3 S21: 0.0283 S22: -0.0424 S23: 0.0570
REMARK 3 S31: 0.1101 S32: -0.0577 S33: -0.0518
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|3 - B|533 }
REMARK 3 ORIGIN FOR THE GROUP (A): 24.1110 32.6260 -42.4560
REMARK 3 T TENSOR
REMARK 3 T11: 0.1008 T22: 0.1408
REMARK 3 T33: 0.1868 T12: -0.0145
REMARK 3 T13: 0.0099 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 1.4656 L22: 0.5444
REMARK 3 L33: 0.5689 L12: 0.0789
REMARK 3 L13: -0.5334 L23: -0.0969
REMARK 3 S TENSOR
REMARK 3 S11: 0.0659 S12: 0.1257 S13: 0.1584
REMARK 3 S21: -0.0228 S22: -0.0117 S23: -0.0338
REMARK 3 S31: -0.0722 S32: 0.0499 S33: -0.0542
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4NWF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1000083740.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64401
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.930
REMARK 200 R MERGE (I) : 0.09360
REMARK 200 R SYM (I) : 0.05380
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9400
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) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.16
REMARK 200 R MERGE FOR SHELL (I) : 0.43020
REMARK 200 R SYM FOR SHELL (I) : 0.30530
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.190
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG4000, 0.1M TRIS BUFFER, 10%
REMARK 280 GLYCEROL, 0.02M DDT, PH 7.6, VAPOR DIFFUSION, TEMPERATURE 293K
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 105.64000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.81450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.94000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.81450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 105.64000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.94000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 1
REMARK 465 THR A 2
REMARK 465 LYS A 35
REMARK 465 SER A 36
REMARK 465 ASN A 37
REMARK 465 PRO A 38
REMARK 465 LYS A 91
REMARK 465 ASN A 92
REMARK 465 GLY A 93
REMARK 465 ASP A 94
REMARK 465 ASP A 156
REMARK 465 LYS A 157
REMARK 465 GLY A 158
REMARK 465 GLU A 159
REMARK 465 SER A 160
REMARK 465 ASN A 161
REMARK 465 ASP A 162
REMARK 465 GLY A 163
REMARK 465 LYS A 164
REMARK 465 LYS A 235
REMARK 465 LEU A 236
REMARK 465 ALA A 237
REMARK 465 GLU A 238
REMARK 465 THR A 239
REMARK 465 THR A 240
REMARK 465 ASP A 241
REMARK 465 LYS A 242
REMARK 465 VAL A 243
REMARK 465 LYS A 244
REMARK 465 GLN A 245
REMARK 465 ASN A 298
REMARK 465 GLU A 299
REMARK 465 PRO A 300
REMARK 465 PHE A 314
REMARK 465 GLU A 315
REMARK 465 THR A 316
REMARK 465 LYS A 317
REMARK 465 CYS A 318
REMARK 465 ASN A 319
REMARK 465 ASN A 320
REMARK 465 SER A 321
REMARK 465 LYS A 322
REMARK 465 PRO A 323
REMARK 465 LYS A 324
REMARK 465 LYS A 534
REMARK 465 SER A 535
REMARK 465 LYS A 536
REMARK 465 ARG A 537
REMARK 465 LYS A 538
REMARK 465 GLY A 539
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 HIS B 85
REMARK 465 GLU B 90
REMARK 465 LYS B 91
REMARK 465 ASN B 92
REMARK 465 GLY B 93
REMARK 465 ASP B 94
REMARK 465 LYS B 157
REMARK 465 GLY B 158
REMARK 465 GLU B 159
REMARK 465 SER B 160
REMARK 465 ASN B 161
REMARK 465 ASP B 162
REMARK 465 LEU B 236
REMARK 465 ALA B 237
REMARK 465 GLU B 238
REMARK 465 THR B 239
REMARK 465 THR B 240
REMARK 465 ASP B 241
REMARK 465 LYS B 242
REMARK 465 VAL B 243
REMARK 465 LYS B 244
REMARK 465 GLN B 245
REMARK 465 GLU B 299
REMARK 465 PRO B 300
REMARK 465 PHE B 314
REMARK 465 GLU B 315
REMARK 465 THR B 316
REMARK 465 LYS B 317
REMARK 465 CYS B 318
REMARK 465 ASN B 319
REMARK 465 ASN B 320
REMARK 465 SER B 321
REMARK 465 LYS B 322
REMARK 465 PRO B 323
REMARK 465 LYS B 324
REMARK 465 LYS B 534
REMARK 465 SER B 535
REMARK 465 LYS B 536
REMARK 465 ARG B 537
REMARK 465 LYS B 538
REMARK 465 GLY B 539
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 LYS B 235 CG 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 LEU A 177 -6.68 67.57
REMARK 500 GLU A 225 30.42 -98.88
REMARK 500 LEU A 262 59.44 -91.40
REMARK 500 CYS A 459 -121.35 -130.80
REMARK 500 SER A 460 -67.39 -95.47
REMARK 500 ILE A 463 -40.13 -134.39
REMARK 500 VAL A 505 103.58 77.82
REMARK 500 LEU B 177 -5.15 66.40
REMARK 500 LEU B 262 59.11 -91.27
REMARK 500 CYS B 459 -121.38 -130.97
REMARK 500 SER B 460 -67.26 -95.30
REMARK 500 ILE B 463 -39.84 -134.35
REMARK 500 VAL B 505 103.31 77.96
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 EDO A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 603
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NWG RELATED DB: PDB
REMARK 900 RELATED ID: 4NXD RELATED DB: PDB
DBREF 4NWF A 1 539 UNP Q06124 PTN11_HUMAN 1 543
DBREF 4NWF B 1 539 UNP Q06124 PTN11_HUMAN 1 543
SEQADV 4NWF ASP A 308 UNP Q06124 ASN 308 ENGINEERED MUTATION
SEQADV 4NWF A UNP Q06124 GLN 408 DELETION
SEQADV 4NWF A UNP Q06124 ALA 409 DELETION
SEQADV 4NWF A UNP Q06124 LEU 410 DELETION
SEQADV 4NWF A UNP Q06124 LEU 411 DELETION
SEQADV 4NWF ASP B 308 UNP Q06124 ASN 308 ENGINEERED MUTATION
SEQADV 4NWF B UNP Q06124 GLN 408 DELETION
SEQADV 4NWF B UNP Q06124 ALA 409 DELETION
SEQADV 4NWF B UNP Q06124 LEU 410 DELETION
SEQADV 4NWF B UNP Q06124 LEU 411 DELETION
SEQRES 1 A 539 MET THR SER ARG ARG TRP PHE HIS PRO ASN ILE THR GLY
SEQRES 2 A 539 VAL GLU ALA GLU ASN LEU LEU LEU THR ARG GLY VAL ASP
SEQRES 3 A 539 GLY SER PHE LEU ALA ARG PRO SER LYS SER ASN PRO GLY
SEQRES 4 A 539 ASP PHE THR LEU SER VAL ARG ARG ASN GLY ALA VAL THR
SEQRES 5 A 539 HIS ILE LYS ILE GLN ASN THR GLY ASP TYR TYR ASP LEU
SEQRES 6 A 539 TYR GLY GLY GLU LYS PHE ALA THR LEU ALA GLU LEU VAL
SEQRES 7 A 539 GLN TYR TYR MET GLU HIS HIS GLY GLN LEU LYS GLU LYS
SEQRES 8 A 539 ASN GLY ASP VAL ILE GLU LEU LYS TYR PRO LEU ASN CYS
SEQRES 9 A 539 ALA ASP PRO THR SER GLU ARG TRP PHE HIS GLY HIS LEU
SEQRES 10 A 539 SER GLY LYS GLU ALA GLU LYS LEU LEU THR GLU LYS GLY
SEQRES 11 A 539 LYS HIS GLY SER PHE LEU VAL ARG GLU SER GLN SER HIS
SEQRES 12 A 539 PRO GLY ASP PHE VAL LEU SER VAL ARG THR GLY ASP ASP
SEQRES 13 A 539 LYS GLY GLU SER ASN ASP GLY LYS SER LYS VAL THR HIS
SEQRES 14 A 539 VAL MET ILE ARG CYS GLN GLU LEU LYS TYR ASP VAL GLY
SEQRES 15 A 539 GLY GLY GLU ARG PHE ASP SER LEU THR ASP LEU VAL GLU
SEQRES 16 A 539 HIS TYR LYS LYS ASN PRO MET VAL GLU THR LEU GLY THR
SEQRES 17 A 539 VAL LEU GLN LEU LYS GLN PRO LEU ASN THR THR ARG ILE
SEQRES 18 A 539 ASN ALA ALA GLU ILE GLU SER ARG VAL ARG GLU LEU SER
SEQRES 19 A 539 LYS LEU ALA GLU THR THR ASP LYS VAL LYS GLN GLY PHE
SEQRES 20 A 539 TRP GLU GLU PHE GLU THR LEU GLN GLN GLN GLU CYS LYS
SEQRES 21 A 539 LEU LEU TYR SER ARG LYS GLU GLY GLN ARG GLN GLU ASN
SEQRES 22 A 539 LYS ASN LYS ASN ARG TYR LYS ASN ILE LEU PRO PHE ASP
SEQRES 23 A 539 HIS THR ARG VAL VAL LEU HIS ASP GLY ASP PRO ASN GLU
SEQRES 24 A 539 PRO VAL SER ASP TYR ILE ASN ALA ASP ILE ILE MET PRO
SEQRES 25 A 539 GLU PHE GLU THR LYS CYS ASN ASN SER LYS PRO LYS LYS
SEQRES 26 A 539 SER TYR ILE ALA THR GLN GLY CYS LEU GLN ASN THR VAL
SEQRES 27 A 539 ASN ASP PHE TRP ARG MET VAL PHE GLN GLU ASN SER ARG
SEQRES 28 A 539 VAL ILE VAL MET THR THR LYS GLU VAL GLU ARG GLY LYS
SEQRES 29 A 539 SER LYS CYS VAL LYS TYR TRP PRO ASP GLU TYR ALA LEU
SEQRES 30 A 539 LYS GLU TYR GLY VAL MET ARG VAL ARG ASN VAL LYS GLU
SEQRES 31 A 539 SER ALA ALA HIS ASP TYR THR LEU ARG GLU LEU LYS LEU
SEQRES 32 A 539 SER LYS VAL GLY GLN GLY ASN THR GLU ARG THR VAL TRP
SEQRES 33 A 539 GLN TYR HIS PHE ARG THR TRP PRO ASP HIS GLY VAL PRO
SEQRES 34 A 539 SER ASP PRO GLY GLY VAL LEU ASP PHE LEU GLU GLU VAL
SEQRES 35 A 539 HIS HIS LYS GLN GLU SER ILE MET ASP ALA GLY PRO VAL
SEQRES 36 A 539 VAL VAL HIS CYS SER ALA GLY ILE GLY ARG THR GLY THR
SEQRES 37 A 539 PHE ILE VAL ILE ASP ILE LEU ILE ASP ILE ILE ARG GLU
SEQRES 38 A 539 LYS GLY VAL ASP CYS ASP ILE ASP VAL PRO LYS THR ILE
SEQRES 39 A 539 GLN MET VAL ARG SER GLN ARG SER GLY MET VAL GLN THR
SEQRES 40 A 539 GLU ALA GLN TYR ARG PHE ILE TYR MET ALA VAL GLN HIS
SEQRES 41 A 539 TYR ILE GLU THR LEU GLN ARG ARG ILE GLU GLU GLU GLN
SEQRES 42 A 539 LYS SER LYS ARG LYS GLY
SEQRES 1 B 539 MET THR SER ARG ARG TRP PHE HIS PRO ASN ILE THR GLY
SEQRES 2 B 539 VAL GLU ALA GLU ASN LEU LEU LEU THR ARG GLY VAL ASP
SEQRES 3 B 539 GLY SER PHE LEU ALA ARG PRO SER LYS SER ASN PRO GLY
SEQRES 4 B 539 ASP PHE THR LEU SER VAL ARG ARG ASN GLY ALA VAL THR
SEQRES 5 B 539 HIS ILE LYS ILE GLN ASN THR GLY ASP TYR TYR ASP LEU
SEQRES 6 B 539 TYR GLY GLY GLU LYS PHE ALA THR LEU ALA GLU LEU VAL
SEQRES 7 B 539 GLN TYR TYR MET GLU HIS HIS GLY GLN LEU LYS GLU LYS
SEQRES 8 B 539 ASN GLY ASP VAL ILE GLU LEU LYS TYR PRO LEU ASN CYS
SEQRES 9 B 539 ALA ASP PRO THR SER GLU ARG TRP PHE HIS GLY HIS LEU
SEQRES 10 B 539 SER GLY LYS GLU ALA GLU LYS LEU LEU THR GLU LYS GLY
SEQRES 11 B 539 LYS HIS GLY SER PHE LEU VAL ARG GLU SER GLN SER HIS
SEQRES 12 B 539 PRO GLY ASP PHE VAL LEU SER VAL ARG THR GLY ASP ASP
SEQRES 13 B 539 LYS GLY GLU SER ASN ASP GLY LYS SER LYS VAL THR HIS
SEQRES 14 B 539 VAL MET ILE ARG CYS GLN GLU LEU LYS TYR ASP VAL GLY
SEQRES 15 B 539 GLY GLY GLU ARG PHE ASP SER LEU THR ASP LEU VAL GLU
SEQRES 16 B 539 HIS TYR LYS LYS ASN PRO MET VAL GLU THR LEU GLY THR
SEQRES 17 B 539 VAL LEU GLN LEU LYS GLN PRO LEU ASN THR THR ARG ILE
SEQRES 18 B 539 ASN ALA ALA GLU ILE GLU SER ARG VAL ARG GLU LEU SER
SEQRES 19 B 539 LYS LEU ALA GLU THR THR ASP LYS VAL LYS GLN GLY PHE
SEQRES 20 B 539 TRP GLU GLU PHE GLU THR LEU GLN GLN GLN GLU CYS LYS
SEQRES 21 B 539 LEU LEU TYR SER ARG LYS GLU GLY GLN ARG GLN GLU ASN
SEQRES 22 B 539 LYS ASN LYS ASN ARG TYR LYS ASN ILE LEU PRO PHE ASP
SEQRES 23 B 539 HIS THR ARG VAL VAL LEU HIS ASP GLY ASP PRO ASN GLU
SEQRES 24 B 539 PRO VAL SER ASP TYR ILE ASN ALA ASP ILE ILE MET PRO
SEQRES 25 B 539 GLU PHE GLU THR LYS CYS ASN ASN SER LYS PRO LYS LYS
SEQRES 26 B 539 SER TYR ILE ALA THR GLN GLY CYS LEU GLN ASN THR VAL
SEQRES 27 B 539 ASN ASP PHE TRP ARG MET VAL PHE GLN GLU ASN SER ARG
SEQRES 28 B 539 VAL ILE VAL MET THR THR LYS GLU VAL GLU ARG GLY LYS
SEQRES 29 B 539 SER LYS CYS VAL LYS TYR TRP PRO ASP GLU TYR ALA LEU
SEQRES 30 B 539 LYS GLU TYR GLY VAL MET ARG VAL ARG ASN VAL LYS GLU
SEQRES 31 B 539 SER ALA ALA HIS ASP TYR THR LEU ARG GLU LEU LYS LEU
SEQRES 32 B 539 SER LYS VAL GLY GLN GLY ASN THR GLU ARG THR VAL TRP
SEQRES 33 B 539 GLN TYR HIS PHE ARG THR TRP PRO ASP HIS GLY VAL PRO
SEQRES 34 B 539 SER ASP PRO GLY GLY VAL LEU ASP PHE LEU GLU GLU VAL
SEQRES 35 B 539 HIS HIS LYS GLN GLU SER ILE MET ASP ALA GLY PRO VAL
SEQRES 36 B 539 VAL VAL HIS CYS SER ALA GLY ILE GLY ARG THR GLY THR
SEQRES 37 B 539 PHE ILE VAL ILE ASP ILE LEU ILE ASP ILE ILE ARG GLU
SEQRES 38 B 539 LYS GLY VAL ASP CYS ASP ILE ASP VAL PRO LYS THR ILE
SEQRES 39 B 539 GLN MET VAL ARG SER GLN ARG SER GLY MET VAL GLN THR
SEQRES 40 B 539 GLU ALA GLN TYR ARG PHE ILE TYR MET ALA VAL GLN HIS
SEQRES 41 B 539 TYR ILE GLU THR LEU GLN ARG ARG ILE GLU GLU GLU GLN
SEQRES 42 B 539 LYS SER LYS ARG LYS GLY
HET EDO A 601 4
HET GOL A 602 6
HET EDO A 603 4
HET EDO A 604 4
HET EDO A 605 4
HET EDO B 601 4
HET EDO B 602 4
HET EDO B 603 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 EDO 7(C2 H6 O2)
FORMUL 4 GOL C3 H8 O3
FORMUL 11 HOH *655(H2 O)
HELIX 1 1 THR A 12 ARG A 23 1 12
HELIX 2 2 THR A 73 HIS A 84 1 12
HELIX 3 3 SER A 118 LYS A 129 1 12
HELIX 4 4 SER A 189 ASN A 200 1 12
HELIX 5 5 GLU A 225 SER A 234 1 10
HELIX 6 6 PHE A 247 GLN A 256 1 10
HELIX 7 7 GLN A 257 LEU A 261 5 5
HELIX 8 8 ARG A 265 ARG A 270 1 6
HELIX 9 9 GLN A 271 ASN A 277 5 7
HELIX 10 10 LEU A 334 ASN A 336 5 3
HELIX 11 11 THR A 337 GLU A 348 1 12
HELIX 12 12 PRO A 432 SER A 448 1 17
HELIX 13 13 ILE A 463 GLY A 483 1 21
HELIX 14 14 ASP A 489 SER A 499 1 11
HELIX 15 15 THR A 507 GLN A 533 1 27
HELIX 16 16 THR B 12 ARG B 23 1 12
HELIX 17 17 THR B 73 HIS B 84 1 12
HELIX 18 18 SER B 118 LYS B 129 1 12
HELIX 19 19 SER B 189 ASN B 200 1 12
HELIX 20 20 GLU B 225 LYS B 235 1 11
HELIX 21 21 PHE B 247 GLN B 256 1 10
HELIX 22 22 GLN B 257 LEU B 261 5 5
HELIX 23 23 ARG B 265 ARG B 270 1 6
HELIX 24 24 GLN B 271 ASN B 277 5 7
HELIX 25 25 LEU B 334 ASN B 336 5 3
HELIX 26 26 THR B 337 GLU B 348 1 12
HELIX 27 27 PRO B 432 SER B 448 1 17
HELIX 28 28 ILE B 463 GLY B 483 1 21
HELIX 29 29 ASP B 489 SER B 499 1 11
HELIX 30 30 THR B 507 GLN B 533 1 27
SHEET 1 A 6 LYS A 70 PHE A 71 0
SHEET 2 A 6 TYR A 63 LEU A 65 -1 N TYR A 63 O PHE A 71
SHEET 3 A 6 ALA A 50 GLN A 57 -1 N GLN A 57 O ASP A 64
SHEET 4 A 6 ASP A 40 ARG A 47 -1 N PHE A 41 O ILE A 56
SHEET 5 A 6 SER A 28 PRO A 33 -1 N SER A 28 O ARG A 46
SHEET 6 A 6 TYR A 100 PRO A 101 1 O TYR A 100 N PHE A 29
SHEET 1 B 5 PHE A 113 GLY A 115 0
SHEET 2 B 5 SER A 134 GLU A 139 1 O VAL A 137 N HIS A 114
SHEET 3 B 5 PHE A 147 THR A 153 -1 O VAL A 148 N ARG A 138
SHEET 4 B 5 LYS A 166 GLN A 175 -1 O VAL A 170 N LEU A 149
SHEET 5 B 5 LYS A 178 ASP A 180 -1 O LYS A 178 N GLN A 175
SHEET 1 C 3 PHE A 113 GLY A 115 0
SHEET 2 C 3 SER A 134 GLU A 139 1 O VAL A 137 N HIS A 114
SHEET 3 C 3 GLN A 214 PRO A 215 1 O GLN A 214 N PHE A 135
SHEET 1 D 2 MET A 202 VAL A 203 0
SHEET 2 D 2 VAL A 209 LEU A 210 -1 O LEU A 210 N MET A 202
SHEET 1 E 2 ILE A 221 ASN A 222 0
SHEET 2 E 2 ASP A 487 ILE A 488 -1 O ILE A 488 N ILE A 221
SHEET 1 F 8 ALA A 307 ILE A 310 0
SHEET 2 F 8 TYR A 327 THR A 330 -1 O TYR A 327 N ILE A 310
SHEET 3 F 8 VAL A 455 HIS A 458 1 O VAL A 457 N ILE A 328
SHEET 4 F 8 VAL A 352 MET A 355 1 N VAL A 354 O VAL A 456
SHEET 5 F 8 ARG A 413 PHE A 420 1 O TYR A 418 N ILE A 353
SHEET 6 F 8 TYR A 396 LYS A 405 -1 N LEU A 401 O VAL A 415
SHEET 7 F 8 MET A 383 ALA A 392 -1 N SER A 391 O LEU A 398
SHEET 8 F 8 LEU A 377 TYR A 380 -1 N TYR A 380 O MET A 383
SHEET 1 G 2 VAL A 360 GLU A 361 0
SHEET 2 G 2 LYS A 364 SER A 365 -1 O LYS A 364 N GLU A 361
SHEET 1 H 6 LYS B 70 PHE B 71 0
SHEET 2 H 6 TYR B 63 LEU B 65 -1 N TYR B 63 O PHE B 71
SHEET 3 H 6 ALA B 50 GLN B 57 -1 N GLN B 57 O ASP B 64
SHEET 4 H 6 PHE B 41 ARG B 47 -1 N PHE B 41 O ILE B 56
SHEET 5 H 6 SER B 28 PRO B 33 -1 N SER B 28 O ARG B 46
SHEET 6 H 6 TYR B 100 PRO B 101 1 O TYR B 100 N PHE B 29
SHEET 1 I 5 PHE B 113 GLY B 115 0
SHEET 2 I 5 SER B 134 GLU B 139 1 O GLU B 139 N GLY B 115
SHEET 3 I 5 PHE B 147 THR B 153 -1 O ARG B 152 N SER B 134
SHEET 4 I 5 LYS B 166 GLN B 175 -1 O VAL B 170 N LEU B 149
SHEET 5 I 5 LYS B 178 ASP B 180 -1 O LYS B 178 N GLN B 175
SHEET 1 J 3 PHE B 113 GLY B 115 0
SHEET 2 J 3 SER B 134 GLU B 139 1 O GLU B 139 N GLY B 115
SHEET 3 J 3 GLN B 214 PRO B 215 1 O GLN B 214 N PHE B 135
SHEET 1 K 2 MET B 202 VAL B 203 0
SHEET 2 K 2 VAL B 209 LEU B 210 -1 O LEU B 210 N MET B 202
SHEET 1 L 2 ILE B 221 ASN B 222 0
SHEET 2 L 2 ASP B 487 ILE B 488 -1 O ILE B 488 N ILE B 221
SHEET 1 M 8 ALA B 307 ILE B 310 0
SHEET 2 M 8 TYR B 327 THR B 330 -1 O TYR B 327 N ILE B 310
SHEET 3 M 8 VAL B 455 HIS B 458 1 O VAL B 457 N ILE B 328
SHEET 4 M 8 VAL B 352 MET B 355 1 N VAL B 354 O VAL B 456
SHEET 5 M 8 ARG B 413 PHE B 420 1 O TYR B 418 N ILE B 353
SHEET 6 M 8 TYR B 396 LYS B 405 -1 N LEU B 401 O VAL B 415
SHEET 7 M 8 MET B 383 ALA B 392 -1 N SER B 391 O LEU B 398
SHEET 8 M 8 LEU B 377 TYR B 380 -1 N TYR B 380 O MET B 383
SHEET 1 N 2 VAL B 360 GLU B 361 0
SHEET 2 N 2 LYS B 364 SER B 365 -1 O LYS B 364 N GLU B 361
CISPEP 1 LEU B 88 LYS B 89 0 -1.47
SITE 1 AC1 4 TYR A 396 GLY A 407 GLU A 441 HOH A 879
SITE 1 AC2 1 GLY B 363
SITE 1 AC3 6 LYS A 369 TRP A 371 GLU A 390 ARG A 399
SITE 2 AC3 6 HOH A 880 SER B 430
SITE 1 AC4 5 LYS A 358 GLU A 359 VAL A 360 HOH A 944
SITE 2 AC4 5 ASP B 431
SITE 1 AC5 7 ASP A 395 PHE A 420 THR A 422 PRO A 429
SITE 2 AC5 7 ASP A 431 GLY A 434 VAL A 435
SITE 1 AC6 2 ARG B 111 PRO B 215
SITE 1 AC7 3 GLU B 359 ARG B 399 HIS B 419
SITE 1 AC8 1 HOH B 919
CRYST1 211.280 55.880 91.629 90.00 90.00 90.00 P 21 21 21 8
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 0.004733 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017895 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010914 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
