HEADER OXIDOREDUCTASE 24-OCT-16 5TQH
TITLE IDH1 R132H MUTANT IN COMPLEX WITH IDH889
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOCITRATE DEHYDROGENASE [NADP] CYTOPLASMIC;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: IDH,CYTOSOLIC NADP-ISOCITRATE DEHYDROGENASE,IDP,NADP(+)-
COMPND 5 SPECIFIC ICDH,OXALOSUCCINATE DECARBOXYLASE;
COMPND 6 EC: 1.1.1.42;
COMPND 7 ENGINEERED: YES;
COMPND 8 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: IDH1, PICD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ISOCITRATE DEHYDROGENASE, ROSSMANN FOLD, NADPH, INHIBITOR,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.XIE,R.KULATHILA
REVDAT 3 06-MAR-24 5TQH 1 REMARK
REVDAT 2 01-MAR-17 5TQH 1 JRNL
REVDAT 1 25-JAN-17 5TQH 0
JRNL AUTH J.R.LEVELL,T.CAFERRO,G.CHENAIL,I.DIX,J.DOOLEY,B.FIRESTONE,
JRNL AUTH 2 P.D.FORTIN,J.GIRALDES,T.GOULD,J.D.GROWNEY,M.D.JONES,
JRNL AUTH 3 R.KULATHILA,F.LIN,G.LIU,A.MUELLER,S.VAN DER PLAS,K.SLOCUM,
JRNL AUTH 4 T.SMITH,R.TERRANOVA,B.B.TOURE,V.TYAGI,T.WAGNER,X.XIE,M.XU,
JRNL AUTH 5 F.S.YANG,L.X.ZHOU,R.PAGLIARINI,Y.S.CHO
JRNL TITL OPTIMIZATION OF 3-PYRIMIDIN-4-YL-OXAZOLIDIN-2-ONES AS
JRNL TITL 2 ALLOSTERIC AND MUTANT SPECIFIC INHIBITORS OF IDH1.
JRNL REF ACS MED CHEM LETT V. 8 151 2017
JRNL REFN ISSN 1948-5875
JRNL PMID 28197303
JRNL DOI 10.1021/ACSMEDCHEMLETT.6B00334
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT 2.11.6
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 112.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 106033
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 5295
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.26
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.41
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 7720
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2119
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 7322
REMARK 3 BIN R VALUE (WORKING SET) : 0.2107
REMARK 3 BIN FREE R VALUE : 0.2329
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.16
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 398
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 : 12822
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 372
REMARK 3 SOLVENT ATOMS : 634
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.45
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.91960
REMARK 3 B22 (A**2) : 1.25490
REMARK 3 B33 (A**2) : -0.33530
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) : 0.280
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.219
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.178
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.215
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.178
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 : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 13525 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 18291 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 4814 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 349 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1917 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 13525 ; 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 : 1752 ; 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 : 15864 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.09
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.17
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.05
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 5TQH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-16.
REMARK 100 THE DEPOSITION ID IS D_1000224644.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100.0
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 106133
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 163.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.49500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
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 (%): 37.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CO-CRYSTALLIZATION WITH PROTEIN
REMARK 280 CONCENTRATION AT 10MG/ML AND COMPOUND AT 250UM; RESERVOIR
REMARK 280 SOLUTION CONTAINS 1.6M TRI-AMMONIUM CITRATE AND 0.1M BIS-TRIS
REMARK 280 (PH5.5), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
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 40.86550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.52400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 77.87250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.52400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.86550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 77.87250
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8480 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 GLY A -2
REMARK 465 PRO A -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 TYR A 135
REMARK 465 GLY A 136
REMARK 465 ASP A 137
REMARK 465 TYR A 272
REMARK 465 ASP A 273
REMARK 465 GLY A 274
REMARK 465 ASP A 275
REMARK 465 VAL A 276
REMARK 465 GLN A 277
REMARK 465 LYS A 413
REMARK 465 LEU A 414
REMARK 465 GLY B -2
REMARK 465 PRO B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ALA B 134
REMARK 465 TYR B 135
REMARK 465 GLY B 136
REMARK 465 LYS B 413
REMARK 465 LEU B 414
REMARK 465 GLY C -2
REMARK 465 PRO C -1
REMARK 465 GLY C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 ALA C 134
REMARK 465 TYR C 135
REMARK 465 GLY C 136
REMARK 465 ASP C 137
REMARK 465 GLY D -2
REMARK 465 PRO D -1
REMARK 465 GLY D 0
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 LYS D 3
REMARK 465 ASN D 271
REMARK 465 TYR D 272
REMARK 465 ASP D 273
REMARK 465 GLY D 274
REMARK 465 ASP D 275
REMARK 465 VAL D 276
REMARK 465 GLN D 277
REMARK 465 LYS D 413
REMARK 465 LEU D 414
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 GLU A 17 -128.09 44.62
REMARK 500 ILE A 31 -65.04 -95.88
REMARK 500 ASN A 68 -12.09 69.66
REMARK 500 HIS A 170 141.22 -172.19
REMARK 500 LYS A 212 53.97 -112.17
REMARK 500 GLU B 17 -133.09 50.40
REMARK 500 ILE B 31 -65.49 -100.74
REMARK 500 ASN B 68 -8.36 70.60
REMARK 500 ASN B 271 59.63 -93.52
REMARK 500 VAL B 276 -64.97 -93.10
REMARK 500 GLU C 17 -134.16 48.56
REMARK 500 ILE C 31 -68.44 -92.47
REMARK 500 ASN C 68 -16.51 79.34
REMARK 500 GLN C 90 145.53 -172.37
REMARK 500 ILE C 215 -63.51 -96.00
REMARK 500 LYS C 270 -70.61 -66.36
REMARK 500 GLU D 17 -132.27 44.82
REMARK 500 ILE D 31 -70.43 -92.22
REMARK 500 ASN D 68 -22.37 68.17
REMARK 500 ASP D 137 -122.43 52.37
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 FLC A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7J2 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7J2 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7J2 C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7J2 D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP D 503
DBREF 5TQH A 1 414 UNP O75874 IDHC_HUMAN 1 414
DBREF 5TQH B 1 414 UNP O75874 IDHC_HUMAN 1 414
DBREF 5TQH C 1 414 UNP O75874 IDHC_HUMAN 1 414
DBREF 5TQH D 1 414 UNP O75874 IDHC_HUMAN 1 414
SEQADV 5TQH GLY A -2 UNP O75874 EXPRESSION TAG
SEQADV 5TQH PRO A -1 UNP O75874 EXPRESSION TAG
SEQADV 5TQH GLY A 0 UNP O75874 EXPRESSION TAG
SEQADV 5TQH HIS A 132 UNP O75874 ARG 132 ENGINEERED MUTATION
SEQADV 5TQH GLY B -2 UNP O75874 EXPRESSION TAG
SEQADV 5TQH PRO B -1 UNP O75874 EXPRESSION TAG
SEQADV 5TQH GLY B 0 UNP O75874 EXPRESSION TAG
SEQADV 5TQH HIS B 132 UNP O75874 ARG 132 ENGINEERED MUTATION
SEQADV 5TQH GLY C -2 UNP O75874 EXPRESSION TAG
SEQADV 5TQH PRO C -1 UNP O75874 EXPRESSION TAG
SEQADV 5TQH GLY C 0 UNP O75874 EXPRESSION TAG
SEQADV 5TQH HIS C 132 UNP O75874 ARG 132 ENGINEERED MUTATION
SEQADV 5TQH GLY D -2 UNP O75874 EXPRESSION TAG
SEQADV 5TQH PRO D -1 UNP O75874 EXPRESSION TAG
SEQADV 5TQH GLY D 0 UNP O75874 EXPRESSION TAG
SEQADV 5TQH HIS D 132 UNP O75874 ARG 132 ENGINEERED MUTATION
SEQRES 1 A 417 GLY PRO GLY MET SER LYS LYS ILE SER GLY GLY SER VAL
SEQRES 2 A 417 VAL GLU MET GLN GLY ASP GLU MET THR ARG ILE ILE TRP
SEQRES 3 A 417 GLU LEU ILE LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU
SEQRES 4 A 417 LEU ASP LEU HIS SER TYR ASP LEU GLY ILE GLU ASN ARG
SEQRES 5 A 417 ASP ALA THR ASN ASP GLN VAL THR LYS ASP ALA ALA GLU
SEQRES 6 A 417 ALA ILE LYS LYS HIS ASN VAL GLY VAL LYS CYS ALA THR
SEQRES 7 A 417 ILE THR PRO ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU
SEQRES 8 A 417 LYS GLN MET TRP LYS SER PRO ASN GLY THR ILE ARG ASN
SEQRES 9 A 417 ILE LEU GLY GLY THR VAL PHE ARG GLU ALA ILE ILE CYS
SEQRES 10 A 417 LYS ASN ILE PRO ARG LEU VAL SER GLY TRP VAL LYS PRO
SEQRES 11 A 417 ILE ILE ILE GLY HIS HIS ALA TYR GLY ASP GLN TYR ARG
SEQRES 12 A 417 ALA THR ASP PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU
SEQRES 13 A 417 ILE THR TYR THR PRO SER ASP GLY THR GLN LYS VAL THR
SEQRES 14 A 417 TYR LEU VAL HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA
SEQRES 15 A 417 MET GLY MET TYR ASN GLN ASP LYS SER ILE GLU ASP PHE
SEQRES 16 A 417 ALA HIS SER SER PHE GLN MET ALA LEU SER LYS GLY TRP
SEQRES 17 A 417 PRO LEU TYR LEU SER THR LYS ASN THR ILE LEU LYS LYS
SEQRES 18 A 417 TYR ASP GLY ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR
SEQRES 19 A 417 ASP LYS GLN TYR LYS SER GLN PHE GLU ALA GLN LYS ILE
SEQRES 20 A 417 TRP TYR GLU HIS ARG LEU ILE ASP ASP MET VAL ALA GLN
SEQRES 21 A 417 ALA MET LYS SER GLU GLY GLY PHE ILE TRP ALA CYS LYS
SEQRES 22 A 417 ASN TYR ASP GLY ASP VAL GLN SER ASP SER VAL ALA GLN
SEQRES 23 A 417 GLY TYR GLY SER LEU GLY MET MET THR SER VAL LEU VAL
SEQRES 24 A 417 CYS PRO ASP GLY LYS THR VAL GLU ALA GLU ALA ALA HIS
SEQRES 25 A 417 GLY THR VAL THR ARG HIS TYR ARG MET TYR GLN LYS GLY
SEQRES 26 A 417 GLN GLU THR SER THR ASN PRO ILE ALA SER ILE PHE ALA
SEQRES 27 A 417 TRP THR ARG GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN
SEQRES 28 A 417 ASN LYS GLU LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU
SEQRES 29 A 417 VAL SER ILE GLU THR ILE GLU ALA GLY PHE MET THR LYS
SEQRES 30 A 417 ASP LEU ALA ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN
SEQRES 31 A 417 ARG SER ASP TYR LEU ASN THR PHE GLU PHE MET ASP LYS
SEQRES 32 A 417 LEU GLY GLU ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS
SEQRES 33 A 417 LEU
SEQRES 1 B 417 GLY PRO GLY MET SER LYS LYS ILE SER GLY GLY SER VAL
SEQRES 2 B 417 VAL GLU MET GLN GLY ASP GLU MET THR ARG ILE ILE TRP
SEQRES 3 B 417 GLU LEU ILE LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU
SEQRES 4 B 417 LEU ASP LEU HIS SER TYR ASP LEU GLY ILE GLU ASN ARG
SEQRES 5 B 417 ASP ALA THR ASN ASP GLN VAL THR LYS ASP ALA ALA GLU
SEQRES 6 B 417 ALA ILE LYS LYS HIS ASN VAL GLY VAL LYS CYS ALA THR
SEQRES 7 B 417 ILE THR PRO ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU
SEQRES 8 B 417 LYS GLN MET TRP LYS SER PRO ASN GLY THR ILE ARG ASN
SEQRES 9 B 417 ILE LEU GLY GLY THR VAL PHE ARG GLU ALA ILE ILE CYS
SEQRES 10 B 417 LYS ASN ILE PRO ARG LEU VAL SER GLY TRP VAL LYS PRO
SEQRES 11 B 417 ILE ILE ILE GLY HIS HIS ALA TYR GLY ASP GLN TYR ARG
SEQRES 12 B 417 ALA THR ASP PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU
SEQRES 13 B 417 ILE THR TYR THR PRO SER ASP GLY THR GLN LYS VAL THR
SEQRES 14 B 417 TYR LEU VAL HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA
SEQRES 15 B 417 MET GLY MET TYR ASN GLN ASP LYS SER ILE GLU ASP PHE
SEQRES 16 B 417 ALA HIS SER SER PHE GLN MET ALA LEU SER LYS GLY TRP
SEQRES 17 B 417 PRO LEU TYR LEU SER THR LYS ASN THR ILE LEU LYS LYS
SEQRES 18 B 417 TYR ASP GLY ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR
SEQRES 19 B 417 ASP LYS GLN TYR LYS SER GLN PHE GLU ALA GLN LYS ILE
SEQRES 20 B 417 TRP TYR GLU HIS ARG LEU ILE ASP ASP MET VAL ALA GLN
SEQRES 21 B 417 ALA MET LYS SER GLU GLY GLY PHE ILE TRP ALA CYS LYS
SEQRES 22 B 417 ASN TYR ASP GLY ASP VAL GLN SER ASP SER VAL ALA GLN
SEQRES 23 B 417 GLY TYR GLY SER LEU GLY MET MET THR SER VAL LEU VAL
SEQRES 24 B 417 CYS PRO ASP GLY LYS THR VAL GLU ALA GLU ALA ALA HIS
SEQRES 25 B 417 GLY THR VAL THR ARG HIS TYR ARG MET TYR GLN LYS GLY
SEQRES 26 B 417 GLN GLU THR SER THR ASN PRO ILE ALA SER ILE PHE ALA
SEQRES 27 B 417 TRP THR ARG GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN
SEQRES 28 B 417 ASN LYS GLU LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU
SEQRES 29 B 417 VAL SER ILE GLU THR ILE GLU ALA GLY PHE MET THR LYS
SEQRES 30 B 417 ASP LEU ALA ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN
SEQRES 31 B 417 ARG SER ASP TYR LEU ASN THR PHE GLU PHE MET ASP LYS
SEQRES 32 B 417 LEU GLY GLU ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS
SEQRES 33 B 417 LEU
SEQRES 1 C 417 GLY PRO GLY MET SER LYS LYS ILE SER GLY GLY SER VAL
SEQRES 2 C 417 VAL GLU MET GLN GLY ASP GLU MET THR ARG ILE ILE TRP
SEQRES 3 C 417 GLU LEU ILE LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU
SEQRES 4 C 417 LEU ASP LEU HIS SER TYR ASP LEU GLY ILE GLU ASN ARG
SEQRES 5 C 417 ASP ALA THR ASN ASP GLN VAL THR LYS ASP ALA ALA GLU
SEQRES 6 C 417 ALA ILE LYS LYS HIS ASN VAL GLY VAL LYS CYS ALA THR
SEQRES 7 C 417 ILE THR PRO ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU
SEQRES 8 C 417 LYS GLN MET TRP LYS SER PRO ASN GLY THR ILE ARG ASN
SEQRES 9 C 417 ILE LEU GLY GLY THR VAL PHE ARG GLU ALA ILE ILE CYS
SEQRES 10 C 417 LYS ASN ILE PRO ARG LEU VAL SER GLY TRP VAL LYS PRO
SEQRES 11 C 417 ILE ILE ILE GLY HIS HIS ALA TYR GLY ASP GLN TYR ARG
SEQRES 12 C 417 ALA THR ASP PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU
SEQRES 13 C 417 ILE THR TYR THR PRO SER ASP GLY THR GLN LYS VAL THR
SEQRES 14 C 417 TYR LEU VAL HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA
SEQRES 15 C 417 MET GLY MET TYR ASN GLN ASP LYS SER ILE GLU ASP PHE
SEQRES 16 C 417 ALA HIS SER SER PHE GLN MET ALA LEU SER LYS GLY TRP
SEQRES 17 C 417 PRO LEU TYR LEU SER THR LYS ASN THR ILE LEU LYS LYS
SEQRES 18 C 417 TYR ASP GLY ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR
SEQRES 19 C 417 ASP LYS GLN TYR LYS SER GLN PHE GLU ALA GLN LYS ILE
SEQRES 20 C 417 TRP TYR GLU HIS ARG LEU ILE ASP ASP MET VAL ALA GLN
SEQRES 21 C 417 ALA MET LYS SER GLU GLY GLY PHE ILE TRP ALA CYS LYS
SEQRES 22 C 417 ASN TYR ASP GLY ASP VAL GLN SER ASP SER VAL ALA GLN
SEQRES 23 C 417 GLY TYR GLY SER LEU GLY MET MET THR SER VAL LEU VAL
SEQRES 24 C 417 CYS PRO ASP GLY LYS THR VAL GLU ALA GLU ALA ALA HIS
SEQRES 25 C 417 GLY THR VAL THR ARG HIS TYR ARG MET TYR GLN LYS GLY
SEQRES 26 C 417 GLN GLU THR SER THR ASN PRO ILE ALA SER ILE PHE ALA
SEQRES 27 C 417 TRP THR ARG GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN
SEQRES 28 C 417 ASN LYS GLU LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU
SEQRES 29 C 417 VAL SER ILE GLU THR ILE GLU ALA GLY PHE MET THR LYS
SEQRES 30 C 417 ASP LEU ALA ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN
SEQRES 31 C 417 ARG SER ASP TYR LEU ASN THR PHE GLU PHE MET ASP LYS
SEQRES 32 C 417 LEU GLY GLU ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS
SEQRES 33 C 417 LEU
SEQRES 1 D 417 GLY PRO GLY MET SER LYS LYS ILE SER GLY GLY SER VAL
SEQRES 2 D 417 VAL GLU MET GLN GLY ASP GLU MET THR ARG ILE ILE TRP
SEQRES 3 D 417 GLU LEU ILE LYS GLU LYS LEU ILE PHE PRO TYR VAL GLU
SEQRES 4 D 417 LEU ASP LEU HIS SER TYR ASP LEU GLY ILE GLU ASN ARG
SEQRES 5 D 417 ASP ALA THR ASN ASP GLN VAL THR LYS ASP ALA ALA GLU
SEQRES 6 D 417 ALA ILE LYS LYS HIS ASN VAL GLY VAL LYS CYS ALA THR
SEQRES 7 D 417 ILE THR PRO ASP GLU LYS ARG VAL GLU GLU PHE LYS LEU
SEQRES 8 D 417 LYS GLN MET TRP LYS SER PRO ASN GLY THR ILE ARG ASN
SEQRES 9 D 417 ILE LEU GLY GLY THR VAL PHE ARG GLU ALA ILE ILE CYS
SEQRES 10 D 417 LYS ASN ILE PRO ARG LEU VAL SER GLY TRP VAL LYS PRO
SEQRES 11 D 417 ILE ILE ILE GLY HIS HIS ALA TYR GLY ASP GLN TYR ARG
SEQRES 12 D 417 ALA THR ASP PHE VAL VAL PRO GLY PRO GLY LYS VAL GLU
SEQRES 13 D 417 ILE THR TYR THR PRO SER ASP GLY THR GLN LYS VAL THR
SEQRES 14 D 417 TYR LEU VAL HIS ASN PHE GLU GLU GLY GLY GLY VAL ALA
SEQRES 15 D 417 MET GLY MET TYR ASN GLN ASP LYS SER ILE GLU ASP PHE
SEQRES 16 D 417 ALA HIS SER SER PHE GLN MET ALA LEU SER LYS GLY TRP
SEQRES 17 D 417 PRO LEU TYR LEU SER THR LYS ASN THR ILE LEU LYS LYS
SEQRES 18 D 417 TYR ASP GLY ARG PHE LYS ASP ILE PHE GLN GLU ILE TYR
SEQRES 19 D 417 ASP LYS GLN TYR LYS SER GLN PHE GLU ALA GLN LYS ILE
SEQRES 20 D 417 TRP TYR GLU HIS ARG LEU ILE ASP ASP MET VAL ALA GLN
SEQRES 21 D 417 ALA MET LYS SER GLU GLY GLY PHE ILE TRP ALA CYS LYS
SEQRES 22 D 417 ASN TYR ASP GLY ASP VAL GLN SER ASP SER VAL ALA GLN
SEQRES 23 D 417 GLY TYR GLY SER LEU GLY MET MET THR SER VAL LEU VAL
SEQRES 24 D 417 CYS PRO ASP GLY LYS THR VAL GLU ALA GLU ALA ALA HIS
SEQRES 25 D 417 GLY THR VAL THR ARG HIS TYR ARG MET TYR GLN LYS GLY
SEQRES 26 D 417 GLN GLU THR SER THR ASN PRO ILE ALA SER ILE PHE ALA
SEQRES 27 D 417 TRP THR ARG GLY LEU ALA HIS ARG ALA LYS LEU ASP ASN
SEQRES 28 D 417 ASN LYS GLU LEU ALA PHE PHE ALA ASN ALA LEU GLU GLU
SEQRES 29 D 417 VAL SER ILE GLU THR ILE GLU ALA GLY PHE MET THR LYS
SEQRES 30 D 417 ASP LEU ALA ALA CYS ILE LYS GLY LEU PRO ASN VAL GLN
SEQRES 31 D 417 ARG SER ASP TYR LEU ASN THR PHE GLU PHE MET ASP LYS
SEQRES 32 D 417 LEU GLY GLU ASN LEU LYS ILE LYS LEU ALA GLN ALA LYS
SEQRES 33 D 417 LEU
HET FLC A 501 13
HET 7J2 A 502 32
HET NDP A 503 48
HET 7J2 B 501 32
HET FLC B 502 13
HET NDP B 503 48
HET 7J2 C 501 32
HET FLC C 502 13
HET NDP C 503 48
HET 7J2 D 501 32
HET FLC D 502 13
HET NDP D 503 48
HETNAM FLC CITRATE ANION
HETNAM 7J2 (4S)-3-[2-({(1S)-1-[5-(4-FLUORO-3-METHYLPHENYL)
HETNAM 2 7J2 PYRIMIDIN-2-YL]ETHYL}AMINO)PYRIMIDIN-4-YL]-4-(PROPAN-
HETNAM 3 7J2 2-YL)-1,3-OXAZOLIDIN-2-ONE
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
FORMUL 5 FLC 4(C6 H5 O7 3-)
FORMUL 6 7J2 4(C23 H25 F N6 O2)
FORMUL 7 NDP 4(C21 H30 N7 O17 P3)
FORMUL 17 HOH *634(H2 O)
HELIX 1 AA1 ASP A 16 LEU A 30 1 15
HELIX 2 AA2 GLY A 45 THR A 52 1 8
HELIX 3 AA3 ASP A 54 ASN A 68 1 15
HELIX 4 AA4 ASP A 79 LYS A 87 1 9
HELIX 5 AA5 SER A 94 GLY A 104 1 11
HELIX 6 AA6 ASP A 186 GLY A 204 1 19
HELIX 7 AA7 LYS A 218 TYR A 235 1 18
HELIX 8 AA8 TYR A 235 GLN A 242 1 8
HELIX 9 AA9 ILE A 251 LYS A 260 1 10
HELIX 10 AB1 ASP A 279 GLY A 286 1 8
HELIX 11 AB2 SER A 287 GLY A 289 5 3
HELIX 12 AB3 VAL A 312 LYS A 321 1 10
HELIX 13 AB4 PRO A 329 ASN A 348 1 20
HELIX 14 AB5 ASN A 349 ALA A 369 1 21
HELIX 15 AB6 THR A 373 GLY A 382 1 10
HELIX 16 AB7 LEU A 383 VAL A 386 5 4
HELIX 17 AB8 GLN A 387 TYR A 391 5 5
HELIX 18 AB9 ASN A 393 GLN A 411 1 19
HELIX 19 AC1 ASP B 16 ILE B 31 1 16
HELIX 20 AC2 GLY B 45 THR B 52 1 8
HELIX 21 AC3 ASP B 54 ASN B 68 1 15
HELIX 22 AC4 ASP B 79 LYS B 87 1 9
HELIX 23 AC5 SER B 94 GLY B 104 1 11
HELIX 24 AC6 ASP B 137 ALA B 141 5 5
HELIX 25 AC7 ASP B 186 GLY B 204 1 19
HELIX 26 AC8 LYS B 218 TYR B 235 1 18
HELIX 27 AC9 TYR B 235 GLN B 242 1 8
HELIX 28 AD1 ILE B 251 SER B 261 1 11
HELIX 29 AD2 ASP B 273 SER B 278 1 6
HELIX 30 AD3 SER B 278 GLY B 286 1 9
HELIX 31 AD4 SER B 287 GLY B 289 5 3
HELIX 32 AD5 VAL B 312 LYS B 321 1 10
HELIX 33 AD6 PRO B 329 ASN B 348 1 20
HELIX 34 AD7 ASN B 349 ALA B 369 1 21
HELIX 35 AD8 THR B 373 GLY B 382 1 10
HELIX 36 AD9 LEU B 383 VAL B 386 5 4
HELIX 37 AE1 GLN B 387 TYR B 391 5 5
HELIX 38 AE2 ASN B 393 GLN B 411 1 19
HELIX 39 AE3 ASP C 16 LEU C 30 1 15
HELIX 40 AE4 GLY C 45 ASP C 50 1 6
HELIX 41 AE5 ASP C 54 ASN C 68 1 15
HELIX 42 AE6 ASP C 79 LYS C 87 1 9
HELIX 43 AE7 SER C 94 GLY C 104 1 11
HELIX 44 AE8 ASP C 186 GLY C 204 1 19
HELIX 45 AE9 ASP C 220 TYR C 235 1 16
HELIX 46 AF1 TYR C 235 ALA C 241 1 7
HELIX 47 AF2 ILE C 251 SER C 261 1 11
HELIX 48 AF3 ASP C 273 SER C 278 1 6
HELIX 49 AF4 SER C 278 GLY C 286 1 9
HELIX 50 AF5 SER C 287 GLY C 289 5 3
HELIX 51 AF6 VAL C 312 LYS C 321 1 10
HELIX 52 AF7 PRO C 329 ASN C 348 1 20
HELIX 53 AF8 ASN C 349 ALA C 369 1 21
HELIX 54 AF9 THR C 373 GLY C 382 1 10
HELIX 55 AG1 GLN C 387 TYR C 391 5 5
HELIX 56 AG2 ASN C 393 GLN C 411 1 19
HELIX 57 AG3 ASP D 16 LEU D 30 1 15
HELIX 58 AG4 GLY D 45 THR D 52 1 8
HELIX 59 AG5 ASP D 54 ASN D 68 1 15
HELIX 60 AG6 ASP D 79 LYS D 87 1 9
HELIX 61 AG7 SER D 94 GLY D 104 1 11
HELIX 62 AG8 GLY D 136 ARG D 140 5 5
HELIX 63 AG9 ASP D 186 GLY D 204 1 19
HELIX 64 AH1 LYS D 218 TYR D 235 1 18
HELIX 65 AH2 TYR D 235 GLN D 242 1 8
HELIX 66 AH3 ILE D 251 LYS D 260 1 10
HELIX 67 AH4 ASP D 279 GLY D 286 1 8
HELIX 68 AH5 SER D 287 GLY D 289 5 3
HELIX 69 AH6 VAL D 312 LYS D 321 1 10
HELIX 70 AH7 PRO D 329 ASN D 348 1 20
HELIX 71 AH8 ASN D 349 ALA D 369 1 21
HELIX 72 AH9 THR D 373 GLY D 382 1 10
HELIX 73 AI1 LEU D 383 VAL D 386 5 4
HELIX 74 AI2 GLN D 387 TYR D 391 5 5
HELIX 75 AI3 ASN D 393 GLN D 411 1 19
SHEET 1 AA110 VAL A 35 ASP A 43 0
SHEET 2 AA110 ILE A 5 GLN A 14 1 N ILE A 5 O GLU A 36
SHEET 3 AA110 VAL A 69 LYS A 72 1 O VAL A 69 N VAL A 11
SHEET 4 AA110 VAL A 303 ALA A 307 1 O ALA A 305 N GLY A 70
SHEET 5 AA110 MET A 291 VAL A 296 -1 N LEU A 295 O GLU A 304
SHEET 6 AA110 THR A 106 ALA A 111 -1 N THR A 106 O VAL A 296
SHEET 7 AA110 ILE A 128 HIS A 132 -1 O ILE A 130 N ARG A 109
SHEET 8 AA110 PHE A 265 CYS A 269 1 O CYS A 269 N GLY A 131
SHEET 9 AA110 LEU A 207 THR A 211 1 N TYR A 208 O ALA A 268
SHEET 10 AA110 TYR A 246 LEU A 250 1 O ARG A 249 N LEU A 209
SHEET 1 AA2 4 THR A 142 VAL A 146 0
SHEET 2 AA2 4 GLY A 177 GLN A 185 -1 O ALA A 179 N PHE A 144
SHEET 3 AA2 4 GLY C 177 GLN C 185 -1 O ASN C 184 N VAL A 178
SHEET 4 AA2 4 THR C 142 VAL C 146 -1 N VAL C 146 O GLY C 177
SHEET 1 AA3 4 VAL A 165 PHE A 172 0
SHEET 2 AA3 4 GLY A 150 PRO A 158 -1 N ILE A 154 O TYR A 167
SHEET 3 AA3 4 GLY C 150 PRO C 158 -1 O GLU C 153 N THR A 155
SHEET 4 AA3 4 VAL C 165 PHE C 172 -1 O PHE C 172 N GLY C 150
SHEET 1 AA410 VAL B 35 ASP B 43 0
SHEET 2 AA410 ILE B 5 GLN B 14 1 N ILE B 5 O GLU B 36
SHEET 3 AA410 VAL B 69 LYS B 72 1 O VAL B 71 N MET B 13
SHEET 4 AA410 VAL B 303 ALA B 307 1 O ALA B 305 N GLY B 70
SHEET 5 AA410 MET B 291 VAL B 296 -1 N LEU B 295 O GLU B 304
SHEET 6 AA410 THR B 106 ALA B 111 -1 N THR B 106 O VAL B 296
SHEET 7 AA410 ILE B 128 HIS B 132 -1 O HIS B 132 N VAL B 107
SHEET 8 AA410 PHE B 265 CYS B 269 1 O TRP B 267 N GLY B 131
SHEET 9 AA410 LEU B 207 THR B 211 1 N TYR B 208 O ALA B 268
SHEET 10 AA410 TYR B 246 LEU B 250 1 O ARG B 249 N LEU B 209
SHEET 1 AA5 4 THR B 142 VAL B 146 0
SHEET 2 AA5 4 GLY B 177 GLN B 185 -1 O GLY B 177 N VAL B 146
SHEET 3 AA5 4 GLY D 177 GLN D 185 -1 O VAL D 178 N ASN B 184
SHEET 4 AA5 4 THR D 142 VAL D 146 -1 N THR D 142 O GLY D 181
SHEET 1 AA6 4 VAL B 165 PHE B 172 0
SHEET 2 AA6 4 GLY B 150 PRO B 158 -1 N GLY B 150 O PHE B 172
SHEET 3 AA6 4 GLY D 150 PRO D 158 -1 O GLU D 153 N THR B 155
SHEET 4 AA6 4 VAL D 165 PHE D 172 -1 O PHE D 172 N GLY D 150
SHEET 1 AA710 VAL C 35 ASP C 43 0
SHEET 2 AA710 ILE C 5 GLN C 14 1 N GLY C 8 O ASP C 38
SHEET 3 AA710 VAL C 69 LYS C 72 1 O VAL C 69 N VAL C 11
SHEET 4 AA710 VAL C 303 ALA C 307 1 O ALA C 305 N GLY C 70
SHEET 5 AA710 MET C 291 VAL C 296 -1 N LEU C 295 O GLU C 304
SHEET 6 AA710 THR C 106 ALA C 111 -1 N THR C 106 O VAL C 296
SHEET 7 AA710 ILE C 129 HIS C 132 -1 O ILE C 130 N ARG C 109
SHEET 8 AA710 ILE C 266 CYS C 269 1 O CYS C 269 N GLY C 131
SHEET 9 AA710 LEU C 207 THR C 211 1 N TYR C 208 O ALA C 268
SHEET 10 AA710 TYR C 246 LEU C 250 1 O ARG C 249 N LEU C 209
SHEET 1 AA810 VAL D 35 ASP D 43 0
SHEET 2 AA810 ILE D 5 GLN D 14 1 N VAL D 10 O HIS D 40
SHEET 3 AA810 VAL D 69 LYS D 72 1 O VAL D 71 N VAL D 11
SHEET 4 AA810 VAL D 303 ALA D 307 1 O ALA D 305 N LYS D 72
SHEET 5 AA810 MET D 291 VAL D 296 -1 N LEU D 295 O GLU D 304
SHEET 6 AA810 THR D 106 ALA D 111 -1 N THR D 106 O VAL D 296
SHEET 7 AA810 ILE D 128 HIS D 132 -1 O ILE D 130 N ARG D 109
SHEET 8 AA810 PHE D 265 CYS D 269 1 O TRP D 267 N GLY D 131
SHEET 9 AA810 LEU D 207 THR D 211 1 N TYR D 208 O ALA D 268
SHEET 10 AA810 TYR D 246 LEU D 250 1 O ARG D 249 N LEU D 209
SITE 1 AC1 5 THR A 77 SER A 94 ASN A 96 ARG A 100
SITE 2 AC1 5 NDP A 503
SITE 1 AC2 14 ARG A 109 ALA A 111 ARG A 119 LEU A 120
SITE 2 AC2 14 TRP A 124 PRO A 127 ILE A 128 ILE A 130
SITE 3 AC2 14 MET A 259 SER A 278 ALA A 282 TYR A 285
SITE 4 AC2 14 SER A 287 MET A 291
SITE 1 AC3 23 LYS A 72 ALA A 74 THR A 75 THR A 77
SITE 2 AC3 23 ARG A 82 ASN A 96 GLN A 283 LEU A 288
SITE 3 AC3 23 GLU A 306 HIS A 309 GLY A 310 THR A 311
SITE 4 AC3 23 VAL A 312 THR A 313 ARG A 314 HIS A 315
SITE 5 AC3 23 THR A 327 ASN A 328 FLC A 501 HOH A 640
SITE 6 AC3 23 HOH A 646 HOH A 655 HOH A 743
SITE 1 AC4 15 ARG B 109 ALA B 111 ILE B 113 ARG B 119
SITE 2 AC4 15 LEU B 120 TRP B 124 ILE B 128 ILE B 130
SITE 3 AC4 15 VAL B 255 MET B 259 TYR B 272 GLN B 277
SITE 4 AC4 15 SER B 278 TYR B 285 SER B 287
SITE 1 AC5 7 THR B 77 SER B 94 ASN B 96 ARG B 100
SITE 2 AC5 7 NDP B 503 HOH B 734 HOH B 776
SITE 1 AC6 27 LYS B 72 ALA B 74 THR B 75 THR B 77
SITE 2 AC6 27 ARG B 82 ASN B 96 GLN B 283 LEU B 288
SITE 3 AC6 27 HIS B 309 GLY B 310 THR B 311 VAL B 312
SITE 4 AC6 27 THR B 313 ARG B 314 HIS B 315 ASN B 328
SITE 5 AC6 27 FLC B 502 HOH B 607 HOH B 617 HOH B 623
SITE 6 AC6 27 HOH B 657 HOH B 667 HOH B 698 HOH B 739
SITE 7 AC6 27 HOH B 766 HOH B 781 LYS D 260
SITE 1 AC7 15 ARG C 109 ALA C 111 ARG C 119 LEU C 120
SITE 2 AC7 15 TRP C 124 ILE C 128 ILE C 130 VAL C 255
SITE 3 AC7 15 MET C 259 TRP C 267 GLN C 277 SER C 278
SITE 4 AC7 15 TYR C 285 SER C 287 MET C 291
SITE 1 AC8 5 THR C 77 SER C 94 ASN C 96 ARG C 100
SITE 2 AC8 5 NDP C 503
SITE 1 AC9 19 LYS C 72 ALA C 74 THR C 75 ILE C 76
SITE 2 AC9 19 THR C 77 ARG C 82 ASN C 96 LEU C 288
SITE 3 AC9 19 GLU C 306 HIS C 309 GLY C 310 THR C 311
SITE 4 AC9 19 VAL C 312 THR C 313 ARG C 314 HIS C 315
SITE 5 AC9 19 THR C 327 ASN C 328 FLC C 502
SITE 1 AD1 14 VAL B 281 ARG D 109 ALA D 111 ILE D 113
SITE 2 AD1 14 ARG D 119 LEU D 120 TRP D 124 ILE D 128
SITE 3 AD1 14 ILE D 130 MET D 259 ALA D 282 TYR D 285
SITE 4 AD1 14 SER D 287 MET D 291
SITE 1 AD2 5 THR D 77 SER D 94 ASN D 96 ARG D 100
SITE 2 AD2 5 NDP D 503
SITE 1 AD3 19 LYS D 72 ALA D 74 THR D 75 ILE D 76
SITE 2 AD3 19 THR D 77 ARG D 82 ASN D 96 LEU D 288
SITE 3 AD3 19 GLY D 289 GLU D 306 HIS D 309 GLY D 310
SITE 4 AD3 19 THR D 311 VAL D 312 THR D 313 ARG D 314
SITE 5 AD3 19 HIS D 315 ASN D 328 FLC D 502
CRYST1 81.731 155.745 163.048 90.00 90.00 90.00 P 21 21 21 16
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 0.012235 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006421 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006133 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
