HEADER HYDROLASE/HYDROLASE INHIBITOR 15-NOV-17 6BMU
TITLE NON-RECEPTOR PROTEIN TYROSINE PHOSPHATASE SHP2 IN COMPLEX WITH
TITLE 2 ALLOSTERIC INHIBITORS SHP099 AND SHP244
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 11;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PROTEIN-TYROSINE PHOSPHATASE 1D,PTP-1D,PROTEIN-TYROSINE
COMPND 5 PHOSPHATASE 2C,PTP-2C,SH-PTP2,SHP2,SH-PTP3;
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: PTPN11, PTP2C, SHPTP2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SHP2, PTPN11, PROTEIN TYROSINE PHOSPHATASE, PHOSPHATASE, ALLOSTERIC
KEYWDS 2 INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.STAMS,M.FODOR
REVDAT 3 04-OCT-23 6BMU 1 REMARK
REVDAT 2 28-MAR-18 6BMU 1 JRNL
REVDAT 1 17-JAN-18 6BMU 0
JRNL AUTH M.FODOR,E.PRICE,P.WANG,H.LU,A.ARGINTARU,Z.CHEN,M.GLICK,
JRNL AUTH 2 H.X.HAO,M.KATO,R.KOENIG,J.R.LAROCHELLE,G.LIU,E.MCNEILL,
JRNL AUTH 3 D.MAJUMDAR,G.A.NISHIGUCHI,L.B.PEREZ,G.PARIS,C.M.QUINN,
JRNL AUTH 4 T.RAMSEY,M.SENDZIK,M.D.SHULTZ,S.L.WILLIAMS,T.STAMS,
JRNL AUTH 5 S.C.BLACKLOW,M.G.ACKER,M.J.LAMARCHE
JRNL TITL DUAL ALLOSTERIC INHIBITION OF SHP2 PHOSPHATASE.
JRNL REF ACS CHEM. BIOL. V. 13 647 2018
JRNL REFN ESSN 1554-8937
JRNL PMID 29304282
JRNL DOI 10.1021/ACSCHEMBIO.7B00980
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.7
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) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 58969
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 2895
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) : 2.12
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.17
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.96
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4485
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2066
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4293
REMARK 3 BIN R VALUE (WORKING SET) : 0.2058
REMARK 3 BIN FREE R VALUE : 0.2245
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.28
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 192
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 : 7731
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 136
REMARK 3 SOLVENT ATOMS : 487
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.84
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -12.24860
REMARK 3 B22 (A**2) : 6.30680
REMARK 3 B33 (A**2) : 5.94180
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.56060
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.250
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.220
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.179
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.221
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.181
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 : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 8048 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 10864 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2840 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 212 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1142 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 8048 ; 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 : 995 ; 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 : 9346 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.21
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.19
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6BMU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1000231140.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59399
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.116
REMARK 200 RESOLUTION RANGE LOW (A) : 213.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : 0.10800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.76000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: BUSTER
REMARK 200 STARTING MODEL: 6BMR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.73
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG3350, 200MM AMMONIUM PHOSPHATE,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 106.72500
REMARK 290 SMTRY3 2 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 SER A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 LYS A 35
REMARK 465 SER A 36
REMARK 465 GLU A 90
REMARK 465 LYS A 91
REMARK 465 ASN A 92
REMARK 465 SER A 118
REMARK 465 GLY A 119
REMARK 465 LYS A 120
REMARK 465 GLU A 121
REMARK 465 ALA A 122
REMARK 465 GLN A 141
REMARK 465 SER A 142
REMARK 465 HIS A 143
REMARK 465 ASP A 155
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 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 ASN A 298
REMARK 465 GLU A 299
REMARK 465 GLU A 313
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 SER B 0
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 SER B 3
REMARK 465 LYS B 89
REMARK 465 GLU B 90
REMARK 465 LYS B 91
REMARK 465 ASN B 92
REMARK 465 GLY B 93
REMARK 465 LYS B 120
REMARK 465 GLU B 121
REMARK 465 SER B 140
REMARK 465 GLN B 141
REMARK 465 SER B 142
REMARK 465 HIS B 143
REMARK 465 GLY B 154
REMARK 465 ASP B 155
REMARK 465 ASP B 156
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 GLY B 163
REMARK 465 LYS B 164
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 ASP B 294
REMARK 465 GLY B 295
REMARK 465 ASP B 296
REMARK 465 PRO B 297
REMARK 465 ASN B 298
REMARK 465 GLU B 299
REMARK 465 PRO B 300
REMARK 465 GLU B 313
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 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 VAL A 301 76.05 -152.81
REMARK 500 LYS A 325 42.62 -109.19
REMARK 500 TYR A 375 -5.61 73.59
REMARK 500 CYS A 459 -121.77 -130.90
REMARK 500 SER A 460 -72.53 -91.59
REMARK 500 VAL A 505 102.80 76.23
REMARK 500 HIS B 84 77.30 -112.91
REMARK 500 VAL B 181 34.10 -98.07
REMARK 500 LEU B 212 69.89 -101.04
REMARK 500 TYR B 375 -10.37 72.20
REMARK 500 CYS B 459 -127.65 -138.65
REMARK 500 SER B 460 -72.90 -92.13
REMARK 500 VAL B 505 103.95 82.44
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 941 DISTANCE = 7.38 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5OD A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DZV A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5OD B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DZV B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 605
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6BMR RELATED DB: PDB
DBREF 6BMU A 1 525 UNP Q06124 PTN11_HUMAN 1 525
DBREF 6BMU B 1 525 UNP Q06124 PTN11_HUMAN 1 525
SEQADV 6BMU SER A 0 UNP Q06124 EXPRESSION TAG
SEQADV 6BMU SER B 0 UNP Q06124 EXPRESSION TAG
SEQRES 1 A 526 SER MET THR SER ARG ARG TRP PHE HIS PRO ASN ILE THR
SEQRES 2 A 526 GLY VAL GLU ALA GLU ASN LEU LEU LEU THR ARG GLY VAL
SEQRES 3 A 526 ASP GLY SER PHE LEU ALA ARG PRO SER LYS SER ASN PRO
SEQRES 4 A 526 GLY ASP PHE THR LEU SER VAL ARG ARG ASN GLY ALA VAL
SEQRES 5 A 526 THR HIS ILE LYS ILE GLN ASN THR GLY ASP TYR TYR ASP
SEQRES 6 A 526 LEU TYR GLY GLY GLU LYS PHE ALA THR LEU ALA GLU LEU
SEQRES 7 A 526 VAL GLN TYR TYR MET GLU HIS HIS GLY GLN LEU LYS GLU
SEQRES 8 A 526 LYS ASN GLY ASP VAL ILE GLU LEU LYS TYR PRO LEU ASN
SEQRES 9 A 526 CYS ALA ASP PRO THR SER GLU ARG TRP PHE HIS GLY HIS
SEQRES 10 A 526 LEU SER GLY LYS GLU ALA GLU LYS LEU LEU THR GLU LYS
SEQRES 11 A 526 GLY LYS HIS GLY SER PHE LEU VAL ARG GLU SER GLN SER
SEQRES 12 A 526 HIS PRO GLY ASP PHE VAL LEU SER VAL ARG THR GLY ASP
SEQRES 13 A 526 ASP LYS GLY GLU SER ASN ASP GLY LYS SER LYS VAL THR
SEQRES 14 A 526 HIS VAL MET ILE ARG CYS GLN GLU LEU LYS TYR ASP VAL
SEQRES 15 A 526 GLY GLY GLY GLU ARG PHE ASP SER LEU THR ASP LEU VAL
SEQRES 16 A 526 GLU HIS TYR LYS LYS ASN PRO MET VAL GLU THR LEU GLY
SEQRES 17 A 526 THR VAL LEU GLN LEU LYS GLN PRO LEU ASN THR THR ARG
SEQRES 18 A 526 ILE ASN ALA ALA GLU ILE GLU SER ARG VAL ARG GLU LEU
SEQRES 19 A 526 SER LYS LEU ALA GLU THR THR ASP LYS VAL LYS GLN GLY
SEQRES 20 A 526 PHE TRP GLU GLU PHE GLU THR LEU GLN GLN GLN GLU CYS
SEQRES 21 A 526 LYS LEU LEU TYR SER ARG LYS GLU GLY GLN ARG GLN GLU
SEQRES 22 A 526 ASN LYS ASN LYS ASN ARG TYR LYS ASN ILE LEU PRO PHE
SEQRES 23 A 526 ASP HIS THR ARG VAL VAL LEU HIS ASP GLY ASP PRO ASN
SEQRES 24 A 526 GLU PRO VAL SER ASP TYR ILE ASN ALA ASN ILE ILE MET
SEQRES 25 A 526 PRO GLU PHE GLU THR LYS CYS ASN ASN SER LYS PRO LYS
SEQRES 26 A 526 LYS SER TYR ILE ALA THR GLN GLY CYS LEU GLN ASN THR
SEQRES 27 A 526 VAL ASN ASP PHE TRP ARG MET VAL PHE GLN GLU ASN SER
SEQRES 28 A 526 ARG VAL ILE VAL MET THR THR LYS GLU VAL GLU ARG GLY
SEQRES 29 A 526 LYS SER LYS CYS VAL LYS TYR TRP PRO ASP GLU TYR ALA
SEQRES 30 A 526 LEU LYS GLU TYR GLY VAL MET ARG VAL ARG ASN VAL LYS
SEQRES 31 A 526 GLU SER ALA ALA HIS ASP TYR THR LEU ARG GLU LEU LYS
SEQRES 32 A 526 LEU SER LYS VAL GLY GLN GLY ASN THR GLU ARG THR VAL
SEQRES 33 A 526 TRP GLN TYR HIS PHE ARG THR TRP PRO ASP HIS GLY VAL
SEQRES 34 A 526 PRO SER ASP PRO GLY GLY VAL LEU ASP PHE LEU GLU GLU
SEQRES 35 A 526 VAL HIS HIS LYS GLN GLU SER ILE MET ASP ALA GLY PRO
SEQRES 36 A 526 VAL VAL VAL HIS CYS SER ALA GLY ILE GLY ARG THR GLY
SEQRES 37 A 526 THR PHE ILE VAL ILE ASP ILE LEU ILE ASP ILE ILE ARG
SEQRES 38 A 526 GLU LYS GLY VAL ASP CYS ASP ILE ASP VAL PRO LYS THR
SEQRES 39 A 526 ILE GLN MET VAL ARG SER GLN ARG SER GLY MET VAL GLN
SEQRES 40 A 526 THR GLU ALA GLN TYR ARG PHE ILE TYR MET ALA VAL GLN
SEQRES 41 A 526 HIS TYR ILE GLU THR LEU
SEQRES 1 B 526 SER MET THR SER ARG ARG TRP PHE HIS PRO ASN ILE THR
SEQRES 2 B 526 GLY VAL GLU ALA GLU ASN LEU LEU LEU THR ARG GLY VAL
SEQRES 3 B 526 ASP GLY SER PHE LEU ALA ARG PRO SER LYS SER ASN PRO
SEQRES 4 B 526 GLY ASP PHE THR LEU SER VAL ARG ARG ASN GLY ALA VAL
SEQRES 5 B 526 THR HIS ILE LYS ILE GLN ASN THR GLY ASP TYR TYR ASP
SEQRES 6 B 526 LEU TYR GLY GLY GLU LYS PHE ALA THR LEU ALA GLU LEU
SEQRES 7 B 526 VAL GLN TYR TYR MET GLU HIS HIS GLY GLN LEU LYS GLU
SEQRES 8 B 526 LYS ASN GLY ASP VAL ILE GLU LEU LYS TYR PRO LEU ASN
SEQRES 9 B 526 CYS ALA ASP PRO THR SER GLU ARG TRP PHE HIS GLY HIS
SEQRES 10 B 526 LEU SER GLY LYS GLU ALA GLU LYS LEU LEU THR GLU LYS
SEQRES 11 B 526 GLY LYS HIS GLY SER PHE LEU VAL ARG GLU SER GLN SER
SEQRES 12 B 526 HIS PRO GLY ASP PHE VAL LEU SER VAL ARG THR GLY ASP
SEQRES 13 B 526 ASP LYS GLY GLU SER ASN ASP GLY LYS SER LYS VAL THR
SEQRES 14 B 526 HIS VAL MET ILE ARG CYS GLN GLU LEU LYS TYR ASP VAL
SEQRES 15 B 526 GLY GLY GLY GLU ARG PHE ASP SER LEU THR ASP LEU VAL
SEQRES 16 B 526 GLU HIS TYR LYS LYS ASN PRO MET VAL GLU THR LEU GLY
SEQRES 17 B 526 THR VAL LEU GLN LEU LYS GLN PRO LEU ASN THR THR ARG
SEQRES 18 B 526 ILE ASN ALA ALA GLU ILE GLU SER ARG VAL ARG GLU LEU
SEQRES 19 B 526 SER LYS LEU ALA GLU THR THR ASP LYS VAL LYS GLN GLY
SEQRES 20 B 526 PHE TRP GLU GLU PHE GLU THR LEU GLN GLN GLN GLU CYS
SEQRES 21 B 526 LYS LEU LEU TYR SER ARG LYS GLU GLY GLN ARG GLN GLU
SEQRES 22 B 526 ASN LYS ASN LYS ASN ARG TYR LYS ASN ILE LEU PRO PHE
SEQRES 23 B 526 ASP HIS THR ARG VAL VAL LEU HIS ASP GLY ASP PRO ASN
SEQRES 24 B 526 GLU PRO VAL SER ASP TYR ILE ASN ALA ASN ILE ILE MET
SEQRES 25 B 526 PRO GLU PHE GLU THR LYS CYS ASN ASN SER LYS PRO LYS
SEQRES 26 B 526 LYS SER TYR ILE ALA THR GLN GLY CYS LEU GLN ASN THR
SEQRES 27 B 526 VAL ASN ASP PHE TRP ARG MET VAL PHE GLN GLU ASN SER
SEQRES 28 B 526 ARG VAL ILE VAL MET THR THR LYS GLU VAL GLU ARG GLY
SEQRES 29 B 526 LYS SER LYS CYS VAL LYS TYR TRP PRO ASP GLU TYR ALA
SEQRES 30 B 526 LEU LYS GLU TYR GLY VAL MET ARG VAL ARG ASN VAL LYS
SEQRES 31 B 526 GLU SER ALA ALA HIS ASP TYR THR LEU ARG GLU LEU LYS
SEQRES 32 B 526 LEU SER LYS VAL GLY GLN GLY ASN THR GLU ARG THR VAL
SEQRES 33 B 526 TRP GLN TYR HIS PHE ARG THR TRP PRO ASP HIS GLY VAL
SEQRES 34 B 526 PRO SER ASP PRO GLY GLY VAL LEU ASP PHE LEU GLU GLU
SEQRES 35 B 526 VAL HIS HIS LYS GLN GLU SER ILE MET ASP ALA GLY PRO
SEQRES 36 B 526 VAL VAL VAL HIS CYS SER ALA GLY ILE GLY ARG THR GLY
SEQRES 37 B 526 THR PHE ILE VAL ILE ASP ILE LEU ILE ASP ILE ILE ARG
SEQRES 38 B 526 GLU LYS GLY VAL ASP CYS ASP ILE ASP VAL PRO LYS THR
SEQRES 39 B 526 ILE GLN MET VAL ARG SER GLN ARG SER GLY MET VAL GLN
SEQRES 40 B 526 THR GLU ALA GLN TYR ARG PHE ILE TYR MET ALA VAL GLN
SEQRES 41 B 526 HIS TYR ILE GLU THR LEU
HET 5OD A 601 23
HET DZV A 602 31
HET PO4 A 603 5
HET GOL A 604 6
HET 5OD B 601 23
HET DZV B 602 31
HET PO4 B 603 5
HET GOL B 604 6
HET GOL B 605 6
HETNAM 5OD 6-(4-AZANYL-4-METHYL-PIPERIDIN-1-YL)-3-[2,3-
HETNAM 2 5OD BIS(CHLORANYL)PHENYL]PYRAZIN-2-AMINE
HETNAM DZV 4-[(2-CHLOROPHENYL)METHYL]-1-(2-HYDROXY-3-
HETNAM 2 DZV METHOXYPHENYL)[1,2,4]TRIAZOLO[4,3-A]QUINAZOLIN-5(4H)-
HETNAM 3 DZV ONE
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETSYN 5OD SHP099
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 5OD 2(C16 H19 CL2 N5)
FORMUL 4 DZV 2(C23 H17 CL N4 O3)
FORMUL 5 PO4 2(O4 P 3-)
FORMUL 6 GOL 3(C3 H8 O3)
FORMUL 12 HOH *487(H2 O)
HELIX 1 AA1 THR A 12 GLY A 24 1 13
HELIX 2 AA2 THR A 73 MET A 82 1 10
HELIX 3 AA3 LYS A 124 LYS A 129 1 6
HELIX 4 AA4 SER A 189 ASN A 200 1 12
HELIX 5 AA5 GLU A 225 LYS A 235 1 11
HELIX 6 AA6 GLY A 246 GLN A 257 1 12
HELIX 7 AA7 GLU A 258 LEU A 261 5 4
HELIX 8 AA8 LYS A 266 ASN A 277 5 12
HELIX 9 AA9 LEU A 334 ASN A 336 5 3
HELIX 10 AB1 THR A 337 ASN A 349 1 13
HELIX 11 AB2 PRO A 432 ILE A 449 1 18
HELIX 12 AB3 ILE A 463 GLY A 483 1 21
HELIX 13 AB4 ASP A 489 SER A 499 1 11
HELIX 14 AB5 THR A 507 THR A 524 1 18
HELIX 15 AB6 THR B 12 ARG B 23 1 12
HELIX 16 AB7 THR B 73 HIS B 84 1 12
HELIX 17 AB8 GLU B 123 LYS B 129 1 7
HELIX 18 AB9 SER B 189 ASN B 200 1 12
HELIX 19 AC1 GLU B 225 LYS B 235 1 11
HELIX 20 AC2 GLY B 246 GLN B 257 1 12
HELIX 21 AC3 GLU B 258 LEU B 262 5 5
HELIX 22 AC4 LYS B 266 ASN B 277 5 12
HELIX 23 AC5 LEU B 334 ASN B 336 5 3
HELIX 24 AC6 THR B 337 GLU B 348 1 12
HELIX 25 AC7 PRO B 432 ILE B 449 1 18
HELIX 26 AC8 GLY B 464 GLY B 483 1 20
HELIX 27 AC9 ASP B 489 SER B 499 1 11
HELIX 28 AD1 THR B 507 THR B 524 1 18
SHEET 1 AA1 6 LYS A 70 PHE A 71 0
SHEET 2 AA1 6 TYR A 63 LEU A 65 -1 N TYR A 63 O PHE A 71
SHEET 3 AA1 6 ALA A 50 GLN A 57 -1 N GLN A 57 O ASP A 64
SHEET 4 AA1 6 PHE A 41 ARG A 47 -1 N VAL A 45 O THR A 52
SHEET 5 AA1 6 SER A 28 PRO A 33 -1 N SER A 28 O ARG A 46
SHEET 6 AA1 6 TYR A 100 PRO A 101 1 O TYR A 100 N PHE A 29
SHEET 1 AA2 5 LYS A 178 ASP A 180 0
SHEET 2 AA2 5 LYS A 166 GLN A 175 -1 N GLN A 175 O LYS A 178
SHEET 3 AA2 5 PHE A 147 THR A 153 -1 N PHE A 147 O ILE A 172
SHEET 4 AA2 5 SER A 134 GLU A 139 -1 N SER A 134 O ARG A 152
SHEET 5 AA2 5 GLN A 214 PRO A 215 1 O GLN A 214 N PHE A 135
SHEET 1 AA3 2 MET A 202 VAL A 203 0
SHEET 2 AA3 2 VAL A 209 LEU A 210 -1 O LEU A 210 N MET A 202
SHEET 1 AA4 2 ILE A 221 ASN A 222 0
SHEET 2 AA4 2 ASP A 487 ILE A 488 -1 O ILE A 488 N ILE A 221
SHEET 1 AA5 8 ALA A 307 ILE A 310 0
SHEET 2 AA5 8 TYR A 327 THR A 330 -1 O TYR A 327 N ILE A 310
SHEET 3 AA5 8 VAL A 455 HIS A 458 1 O VAL A 457 N ILE A 328
SHEET 4 AA5 8 VAL A 352 MET A 355 1 N VAL A 354 O VAL A 456
SHEET 5 AA5 8 GLN A 408 PHE A 420 1 O TYR A 418 N ILE A 353
SHEET 6 AA5 8 TYR A 396 LYS A 405 -1 N THR A 397 O HIS A 419
SHEET 7 AA5 8 MET A 383 ALA A 392 -1 N LYS A 389 O GLU A 400
SHEET 8 AA5 8 LEU A 377 TYR A 380 -1 N TYR A 380 O MET A 383
SHEET 1 AA6 2 VAL A 360 GLU A 361 0
SHEET 2 AA6 2 LYS A 364 SER A 365 -1 O LYS A 364 N GLU A 361
SHEET 1 AA7 6 LYS B 70 PHE B 71 0
SHEET 2 AA7 6 TYR B 63 LEU B 65 -1 N TYR B 63 O PHE B 71
SHEET 3 AA7 6 ALA B 50 GLN B 57 -1 N GLN B 57 O ASP B 64
SHEET 4 AA7 6 PHE B 41 ARG B 47 -1 N PHE B 41 O ILE B 56
SHEET 5 AA7 6 SER B 28 PRO B 33 -1 N SER B 28 O ARG B 46
SHEET 6 AA7 6 TYR B 100 PRO B 101 1 O TYR B 100 N PHE B 29
SHEET 1 AA8 5 LYS B 178 ASP B 180 0
SHEET 2 AA8 5 VAL B 167 GLN B 175 -1 N GLN B 175 O LYS B 178
SHEET 3 AA8 5 PHE B 147 ARG B 152 -1 N PHE B 147 O ILE B 172
SHEET 4 AA8 5 SER B 134 ARG B 138 -1 N LEU B 136 O SER B 150
SHEET 5 AA8 5 GLN B 214 PRO B 215 1 O GLN B 214 N PHE B 135
SHEET 1 AA9 2 MET B 202 VAL B 203 0
SHEET 2 AA9 2 VAL B 209 LEU B 210 -1 O LEU B 210 N MET B 202
SHEET 1 AB1 2 ILE B 221 ASN B 222 0
SHEET 2 AB1 2 ASP B 487 ILE B 488 -1 O ILE B 488 N ILE B 221
SHEET 1 AB2 9 ARG B 289 VAL B 291 0
SHEET 2 AB2 9 TYR B 304 ILE B 310 -1 O ALA B 307 N VAL B 290
SHEET 3 AB2 9 TYR B 327 THR B 330 -1 O TYR B 327 N ILE B 310
SHEET 4 AB2 9 VAL B 455 HIS B 458 1 O VAL B 457 N ILE B 328
SHEET 5 AB2 9 VAL B 352 MET B 355 1 N VAL B 354 O VAL B 456
SHEET 6 AB2 9 GLN B 408 PHE B 420 1 O TYR B 418 N ILE B 353
SHEET 7 AB2 9 TYR B 396 LYS B 405 -1 N THR B 397 O HIS B 419
SHEET 8 AB2 9 MET B 383 ALA B 392 -1 N ARG B 384 O SER B 404
SHEET 9 AB2 9 LEU B 377 TYR B 380 -1 N TYR B 380 O MET B 383
SHEET 1 AB3 2 VAL B 360 GLU B 361 0
SHEET 2 AB3 2 LYS B 364 SER B 365 -1 O LYS B 364 N GLU B 361
SITE 1 AC1 15 THR A 108 GLU A 110 ARG A 111 PHE A 113
SITE 2 AC1 15 HIS A 114 THR A 218 THR A 219 GLU A 249
SITE 3 AC1 15 GLU A 250 THR A 253 LEU A 254 GLN A 257
SITE 4 AC1 15 PRO A 491 LYS A 492 GLN A 495
SITE 1 AC2 12 GLN A 79 TYR A 80 GLU A 83 HIS A 84
SITE 2 AC2 12 LEU A 262 TYR A 263 SER A 264 ARG A 265
SITE 3 AC2 12 GLN A 269 ASN A 281 HOH A 804 HOH A 866
SITE 1 AC3 3 ARG A 32 SER A 34 THR A 42
SITE 1 AC4 7 GLU A 110 GLU A 195 LYS A 198 GLN A 257
SITE 2 AC4 7 LYS A 260 HOH A 731 HOH A 763
SITE 1 AC5 16 THR B 108 GLU B 110 ARG B 111 PHE B 113
SITE 2 AC5 16 THR B 218 THR B 219 GLU B 249 GLU B 250
SITE 3 AC5 16 THR B 253 LEU B 254 GLN B 257 PRO B 491
SITE 4 AC5 16 LYS B 492 GLN B 495 HOH B 712 HOH B 847
SITE 1 AC6 14 GLN B 79 TYR B 80 GLU B 83 HIS B 84
SITE 2 AC6 14 LEU B 262 TYR B 263 SER B 264 ARG B 265
SITE 3 AC6 14 GLN B 269 ASN B 281 LEU B 283 HOH B 767
SITE 4 AC6 14 HOH B 876 HOH B 879
SITE 1 AC7 6 ARG B 32 SER B 34 LYS B 35 SER B 36
SITE 2 AC7 6 THR B 42 HOH B 825
SITE 1 AC8 6 ARG B 111 LYS B 198 GLN B 256 GLN B 257
SITE 2 AC8 6 LYS B 260 HOH B 764
SITE 1 AC9 5 SER A 391 TYR A 396 LEU A 398 HOH A 717
SITE 2 AC9 5 GLY B 407
CRYST1 46.130 213.450 55.940 90.00 96.75 90.00 P 1 21 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 0.021678 0.000000 0.002566 0.00000
SCALE2 0.000000 0.004685 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018001 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
