HEADER OXIDOREDUCTASE 15-SEP-17 6B0Z
TITLE IDH1 R132H MUTANT IN COMPLEX WITH IDH305
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOCITRATE DEHYDROGENASE [NADP] CYTOPLASMIC;
COMPND 3 CHAIN: A, C, B, 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 2 06-MAR-24 6B0Z 1 REMARK
REVDAT 1 08-NOV-17 6B0Z 0
JRNL AUTH Y.S.CHO,J.R.LEVELL,G.LIU,T.CAFERRO,J.SUTTON,C.M.SHAFER,
JRNL AUTH 2 A.COSTALES,J.R.MANNING,Q.ZHAO,M.SENDZIK,M.SHULTZ,G.CHENAIL,
JRNL AUTH 3 J.DOOLEY,B.VILLALBA,A.FARSIDJANI,J.CHEN,R.KULATHILA,X.XIE,
JRNL AUTH 4 S.DODD,T.GOULD,G.LIANG,T.HEIMBACH,K.SLOCUM,B.FIRESTONE,M.PU,
JRNL AUTH 5 R.PAGLIARINI,J.D.GROWNEY
JRNL TITL DISCOVERY AND EVALUATION OF CLINICAL CANDIDATE IDH305, A
JRNL TITL 2 BRAIN PENETRANT MUTANT IDH1 INHIBITOR.
JRNL REF ACS MED CHEM LETT V. 8 1116 2017
JRNL REFN ISSN 1948-5875
JRNL PMID 29057061
JRNL DOI 10.1021/ACSMEDCHEMLETT.7B00342
REMARK 2
REMARK 2 RESOLUTION. 2.33 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 88623
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4444
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.7113 - 7.2404 0.99 3012 167 0.1650 0.1789
REMARK 3 2 7.2404 - 5.7511 1.00 2915 143 0.1827 0.2171
REMARK 3 3 5.7511 - 5.0253 1.00 2867 137 0.1662 0.1941
REMARK 3 4 5.0253 - 4.5664 1.00 2857 146 0.1439 0.1768
REMARK 3 5 4.5664 - 4.2394 1.00 2830 147 0.1476 0.1977
REMARK 3 6 4.2394 - 3.9896 1.00 2809 168 0.1583 0.2185
REMARK 3 7 3.9896 - 3.7899 1.00 2809 157 0.1621 0.2126
REMARK 3 8 3.7899 - 3.6250 1.00 2797 167 0.1726 0.2167
REMARK 3 9 3.6250 - 3.4855 1.00 2834 143 0.1828 0.2489
REMARK 3 10 3.4855 - 3.3653 1.00 2765 151 0.1938 0.2399
REMARK 3 11 3.3653 - 3.2601 1.00 2784 161 0.2062 0.2580
REMARK 3 12 3.2601 - 3.1669 1.00 2787 150 0.2139 0.2651
REMARK 3 13 3.1669 - 3.0836 1.00 2815 149 0.2210 0.2844
REMARK 3 14 3.0836 - 3.0084 1.00 2792 142 0.2254 0.2756
REMARK 3 15 3.0084 - 2.9400 1.00 2813 142 0.2246 0.2681
REMARK 3 16 2.9400 - 2.8774 1.00 2782 150 0.2315 0.2856
REMARK 3 17 2.8774 - 2.8199 1.00 2778 149 0.2273 0.2669
REMARK 3 18 2.8199 - 2.7667 1.00 2811 140 0.2268 0.3029
REMARK 3 19 2.7667 - 2.7173 1.00 2746 142 0.2196 0.2961
REMARK 3 20 2.7173 - 2.6712 1.00 2817 152 0.2223 0.2614
REMARK 3 21 2.6712 - 2.6282 1.00 2728 137 0.2226 0.2631
REMARK 3 22 2.6282 - 2.5877 1.00 2813 129 0.2233 0.2749
REMARK 3 23 2.5877 - 2.5497 1.00 2771 139 0.2279 0.2697
REMARK 3 24 2.5497 - 2.5138 1.00 2857 134 0.2312 0.3192
REMARK 3 25 2.5138 - 2.4798 1.00 2738 149 0.2346 0.3334
REMARK 3 26 2.4798 - 2.4476 1.00 2761 149 0.2287 0.3014
REMARK 3 27 2.4476 - 2.4170 1.00 2772 143 0.2350 0.3105
REMARK 3 28 2.4170 - 2.3879 1.00 2747 178 0.2404 0.2984
REMARK 3 29 2.3879 - 2.3601 1.00 2797 119 0.2437 0.2906
REMARK 3 30 2.3601 - 2.3336 1.00 2775 164 0.2433 0.2892
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 13583
REMARK 3 ANGLE : 0.708 18386
REMARK 3 CHIRALITY : 0.047 1976
REMARK 3 PLANARITY : 0.004 2311
REMARK 3 DIHEDRAL : 13.760 10342
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6B0Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1000230113.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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 PILATUS3 X 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 584723
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.334
REMARK 200 RESOLUTION RANGE LOW (A) : 163.054
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 55.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CO-CRYSTALLIZATION OF PROTEIN (20
REMARK 280 -24MG/ML) /COMPOUND COMPLEX AT 1/1.5 MOLAR RATIO; RESERVOIR
REMARK 280 SOLUTION: 1.5-1.8M TRI AMMONIUM CITRATE, 0.1M BIS-TRIS PH6.5,
REMARK 280 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 40.74750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.52700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 77.65600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 81.52700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.74750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 77.65600
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: 8590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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: 34260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 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 GLN A 138
REMARK 465 TYR A 139
REMARK 465 ARG A 140
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 LYS A 413
REMARK 465 LEU A 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 TYR C 135
REMARK 465 GLY C 136
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 TYR B 135
REMARK 465 GLY B 136
REMARK 465 LEU B 414
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 TYR D 135
REMARK 465 GLY D 136
REMARK 465 ASP D 137
REMARK 465 GLN D 138
REMARK 465 TYR D 139
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 ALA D 412
REMARK 465 LYS D 413
REMARK 465 LEU D 414
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 NZ LYS C 212 OD1 ASN C 271 1.97
REMARK 500 OG1 THR B 77 OB2 FLC B 503 2.16
REMARK 500 OG1 THR C 77 OB2 FLC C 503 2.17
REMARK 500 OG1 THR A 77 OB1 FLC A 503 2.17
REMARK 500 NE2 GLN D 55 OD1 ASP D 59 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG D 314 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
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 GLU A 17 -131.05 53.11
REMARK 500 ILE A 31 -66.79 -97.51
REMARK 500 ASN A 68 -5.86 70.39
REMARK 500 TRP A 124 94.12 -69.22
REMARK 500 LYS A 212 52.25 -112.96
REMARK 500 PRO A 384 2.83 -65.07
REMARK 500 GLN A 411 45.03 -73.33
REMARK 500 GLU C 17 -130.49 55.50
REMARK 500 ILE C 31 -65.80 -97.83
REMARK 500 ASN C 68 -4.15 78.75
REMARK 500 LYS C 87 57.43 33.31
REMARK 500 ARG C 140 63.44 -110.09
REMARK 500 TYR C 235 -25.25 -142.98
REMARK 500 LYS C 413 45.90 -86.22
REMARK 500 GLU B 17 -134.74 52.24
REMARK 500 ILE B 31 -62.24 -101.77
REMARK 500 ASN B 68 -6.68 73.43
REMARK 500 ASP B 79 -167.75 -127.89
REMARK 500 LYS B 212 48.43 -102.53
REMARK 500 LYS B 301 -30.42 -132.82
REMARK 500 GLU D 17 -134.92 49.50
REMARK 500 ILE D 31 -65.19 -103.89
REMARK 500 ASN D 68 -15.36 80.41
REMARK 500 TYR D 235 -23.16 -146.82
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 B 808 DISTANCE = 6.29 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue C81 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue C81 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue C81 C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC C 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue C81 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue C81 D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FLC D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue C81 D 504
DBREF 6B0Z A 1 414 UNP O75874 IDHC_HUMAN 1 414
DBREF 6B0Z C 1 414 UNP O75874 IDHC_HUMAN 1 414
DBREF 6B0Z B 1 414 UNP O75874 IDHC_HUMAN 1 414
DBREF 6B0Z D 1 414 UNP O75874 IDHC_HUMAN 1 414
SEQADV 6B0Z GLY A -2 UNP O75874 EXPRESSION TAG
SEQADV 6B0Z PRO A -1 UNP O75874 EXPRESSION TAG
SEQADV 6B0Z GLY A 0 UNP O75874 EXPRESSION TAG
SEQADV 6B0Z HIS A 132 UNP O75874 ARG 132 ENGINEERED MUTATION
SEQADV 6B0Z GLY C -2 UNP O75874 EXPRESSION TAG
SEQADV 6B0Z PRO C -1 UNP O75874 EXPRESSION TAG
SEQADV 6B0Z GLY C 0 UNP O75874 EXPRESSION TAG
SEQADV 6B0Z HIS C 132 UNP O75874 ARG 132 ENGINEERED MUTATION
SEQADV 6B0Z GLY B -2 UNP O75874 EXPRESSION TAG
SEQADV 6B0Z PRO B -1 UNP O75874 EXPRESSION TAG
SEQADV 6B0Z GLY B 0 UNP O75874 EXPRESSION TAG
SEQADV 6B0Z HIS B 132 UNP O75874 ARG 132 ENGINEERED MUTATION
SEQADV 6B0Z GLY D -2 UNP O75874 EXPRESSION TAG
SEQADV 6B0Z PRO D -1 UNP O75874 EXPRESSION TAG
SEQADV 6B0Z GLY D 0 UNP O75874 EXPRESSION TAG
SEQADV 6B0Z 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 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 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 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 NDP A 501 48
HET C81 A 502 35
HET FLC A 503 13
HET C81 A 504 35
HET NDP C 501 48
HET C81 C 502 35
HET FLC C 503 13
HET NDP B 501 48
HET C81 B 502 35
HET FLC B 503 13
HET NDP D 501 48
HET C81 D 502 35
HET FLC D 503 13
HET C81 D 504 35
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM C81 (4R)-4-[(1S)-1-FLUOROETHYL]-3-[2-({(1S)-1-[4-METHYL-2'-
HETNAM 2 C81 (TRIFLUOROMETHYL)[3,4'-BIPYRIDIN]-6-YL]ETHYL}AMINO)
HETNAM 3 C81 PYRIMIDIN-4-YL]-1,3-OXAZOLIDIN-2-ONE
HETNAM FLC CITRATE ANION
FORMUL 5 NDP 4(C21 H30 N7 O17 P3)
FORMUL 6 C81 6(C23 H22 F4 N6 O2)
FORMUL 7 FLC 4(C6 H5 O7 3-)
FORMUL 19 HOH *511(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 SER A 278 GLY A 286 1 9
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 C 16 LEU C 30 1 15
HELIX 20 AC2 GLY C 45 THR C 52 1 8
HELIX 21 AC3 ASP C 54 ASN C 68 1 15
HELIX 22 AC4 ASP C 79 LYS C 87 1 9
HELIX 23 AC5 SER C 94 GLY C 104 1 11
HELIX 24 AC6 ASP C 186 GLY C 204 1 19
HELIX 25 AC7 LYS C 218 TYR C 235 1 18
HELIX 26 AC8 TYR C 235 GLN C 242 1 8
HELIX 27 AC9 ILE C 251 SER C 261 1 11
HELIX 28 AD1 ASP C 273 SER C 278 1 6
HELIX 29 AD2 SER C 278 GLY C 286 1 9
HELIX 30 AD3 SER C 287 GLY C 289 5 3
HELIX 31 AD4 VAL C 312 LYS C 321 1 10
HELIX 32 AD5 PRO C 329 ASN C 348 1 20
HELIX 33 AD6 ASN C 349 ALA C 369 1 21
HELIX 34 AD7 THR C 373 GLY C 382 1 10
HELIX 35 AD8 GLN C 387 TYR C 391 5 5
HELIX 36 AD9 ASN C 393 ALA C 412 1 20
HELIX 37 AE1 ASP B 16 LEU B 30 1 15
HELIX 38 AE2 GLY B 45 THR B 52 1 8
HELIX 39 AE3 ASP B 54 ASN B 68 1 15
HELIX 40 AE4 ASP B 79 LYS B 87 1 9
HELIX 41 AE5 SER B 94 GLY B 104 1 11
HELIX 42 AE6 ASP B 137 ALA B 141 5 5
HELIX 43 AE7 ASP B 186 GLY B 204 1 19
HELIX 44 AE8 LYS B 218 TYR B 235 1 18
HELIX 45 AE9 TYR B 235 GLN B 242 1 8
HELIX 46 AF1 ILE B 251 SER B 261 1 11
HELIX 47 AF2 ASP B 273 SER B 278 1 6
HELIX 48 AF3 SER B 278 GLY B 286 1 9
HELIX 49 AF4 SER B 287 GLY B 289 5 3
HELIX 50 AF5 VAL B 312 LYS B 321 1 10
HELIX 51 AF6 PRO B 329 ASN B 348 1 20
HELIX 52 AF7 ASN B 349 ALA B 369 1 21
HELIX 53 AF8 THR B 373 GLY B 382 1 10
HELIX 54 AF9 LEU B 383 VAL B 386 5 4
HELIX 55 AG1 GLN B 387 TYR B 391 5 5
HELIX 56 AG2 ASN B 393 ALA B 412 1 20
HELIX 57 AG3 ASP D 16 LEU D 30 1 15
HELIX 58 AG4 GLY D 45 ASP D 50 1 6
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 ASP D 186 GLY D 204 1 19
HELIX 63 AG9 LYS D 218 TYR D 235 1 18
HELIX 64 AH1 TYR D 235 GLN D 242 1 8
HELIX 65 AH2 ILE D 251 LYS D 260 1 10
HELIX 66 AH3 SER D 278 GLY D 286 1 9
HELIX 67 AH4 SER D 287 GLY D 289 5 3
HELIX 68 AH5 VAL D 312 LYS D 321 1 10
HELIX 69 AH6 PRO D 329 ASP D 347 1 19
HELIX 70 AH7 ASN D 349 ALA D 369 1 21
HELIX 71 AH8 THR D 373 GLY D 382 1 10
HELIX 72 AH9 LEU D 383 VAL D 386 5 4
HELIX 73 AI1 GLN D 387 TYR D 391 5 5
HELIX 74 AI2 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 GLY A 177 N VAL A 146
SHEET 3 AA2 4 GLY C 177 GLN C 185 -1 O ASN C 184 N VAL A 178
SHEET 4 AA2 4 ALA C 141 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 THR C 155 N GLU A 153
SHEET 4 AA3 4 VAL C 165 PHE C 172 -1 O TYR C 167 N ILE C 154
SHEET 1 AA410 VAL C 35 ASP C 43 0
SHEET 2 AA410 ILE C 5 GLN C 14 1 N GLY C 7 O GLU C 36
SHEET 3 AA410 VAL C 69 LYS C 72 1 O VAL C 69 N VAL C 11
SHEET 4 AA410 VAL C 303 ALA C 307 1 O ALA C 305 N GLY C 70
SHEET 5 AA410 MET C 291 VAL C 296 -1 N LEU C 295 O GLU C 304
SHEET 6 AA410 THR C 106 ALA C 111 -1 N THR C 106 O VAL C 296
SHEET 7 AA410 ILE C 129 HIS C 133 -1 O ILE C 130 N ARG C 109
SHEET 8 AA410 ILE C 266 CYS C 269 1 O TRP C 267 N GLY C 131
SHEET 9 AA410 LEU C 207 THR C 211 1 N TYR C 208 O ALA C 268
SHEET 10 AA410 TYR C 246 LEU C 250 1 O ARG C 249 N LEU C 209
SHEET 1 AA510 VAL B 35 ASP B 43 0
SHEET 2 AA510 ILE B 5 GLN B 14 1 N VAL B 10 O HIS B 40
SHEET 3 AA510 VAL B 69 LYS B 72 1 O VAL B 69 N VAL B 11
SHEET 4 AA510 VAL B 303 ALA B 307 1 O ALA B 305 N GLY B 70
SHEET 5 AA510 MET B 291 VAL B 296 -1 N LEU B 295 O GLU B 304
SHEET 6 AA510 THR B 106 ALA B 111 -1 N THR B 106 O VAL B 296
SHEET 7 AA510 ILE B 129 HIS B 133 -1 O HIS B 132 N VAL B 107
SHEET 8 AA510 ILE B 266 CYS B 269 1 O CYS B 269 N GLY B 131
SHEET 9 AA510 LEU B 207 THR B 211 1 N TYR B 208 O ALA B 268
SHEET 10 AA510 TYR B 246 LEU B 250 1 O ARG B 249 N LEU B 209
SHEET 1 AA6 4 THR B 142 VAL B 146 0
SHEET 2 AA6 4 GLY B 177 GLN B 185 -1 O GLY B 177 N VAL B 146
SHEET 3 AA6 4 GLY D 177 GLN D 185 -1 O ASN D 184 N VAL B 178
SHEET 4 AA6 4 ALA D 141 VAL D 146 -1 N VAL D 146 O GLY D 177
SHEET 1 AA7 4 VAL B 165 PHE B 172 0
SHEET 2 AA7 4 GLY B 150 PRO B 158 -1 N ILE B 154 O TYR B 167
SHEET 3 AA7 4 GLY D 150 PRO D 158 -1 O GLU D 153 N THR B 155
SHEET 4 AA7 4 VAL D 165 PHE D 172 -1 O TYR D 167 N ILE D 154
SHEET 1 AA810 VAL D 35 ASP D 43 0
SHEET 2 AA810 ILE D 5 GLN D 14 1 N GLY D 8 O ASP D 38
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 GLY D 70
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 CYS D 269 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 22 LYS A 72 ALA A 74 THR A 75 THR A 77
SITE 2 AC1 22 ARG A 82 ASN A 96 LEU A 288 HIS A 309
SITE 3 AC1 22 GLY A 310 THR A 311 VAL A 312 THR A 313
SITE 4 AC1 22 ARG A 314 HIS A 315 THR A 327 ASN A 328
SITE 5 AC1 22 FLC A 503 HOH A 601 HOH A 613 HOH A 660
SITE 6 AC1 22 HOH A 702 HOH A 729
SITE 1 AC2 15 ARG A 109 ALA A 111 ARG A 119 LEU A 120
SITE 2 AC2 15 TRP A 124 ILE A 128 ILE A 130 VAL A 255
SITE 3 AC2 15 MET A 259 SER A 278 ALA A 282 TYR A 285
SITE 4 AC2 15 SER A 287 MET A 291 C81 A 504
SITE 1 AC3 5 THR A 77 SER A 94 ASN A 96 ARG A 100
SITE 2 AC3 5 NDP A 501
SITE 1 AC4 13 LEU A 120 HIS A 132 ILE A 251 CYS A 269
SITE 2 AC4 13 ASN A 271 GLN A 277 SER A 278 VAL A 281
SITE 3 AC4 13 C81 A 502 LEU C 120 GLN C 277 VAL C 281
SITE 4 AC4 13 C81 C 502
SITE 1 AC5 16 LYS C 72 THR C 75 THR C 77 ARG C 82
SITE 2 AC5 16 ASN C 96 LEU C 288 GLU C 306 HIS C 309
SITE 3 AC5 16 GLY C 310 THR C 311 VAL C 312 THR C 313
SITE 4 AC5 16 ARG C 314 HIS C 315 ASN C 328 FLC C 503
SITE 1 AC6 13 C81 A 504 ARG C 109 ALA C 111 ARG C 119
SITE 2 AC6 13 LEU C 120 ILE C 128 VAL C 255 TYR C 272
SITE 3 AC6 13 GLN C 277 SER C 278 TYR C 285 SER C 287
SITE 4 AC6 13 MET C 291
SITE 1 AC7 5 THR C 77 SER C 94 ASN C 96 ARG C 100
SITE 2 AC7 5 NDP C 501
SITE 1 AC8 27 LYS B 72 ALA B 74 THR B 75 THR B 77
SITE 2 AC8 27 ARG B 82 ASN B 96 GLN B 283 LEU B 288
SITE 3 AC8 27 GLU B 306 HIS B 309 GLY B 310 THR B 311
SITE 4 AC8 27 VAL B 312 THR B 313 ARG B 314 HIS B 315
SITE 5 AC8 27 ASN B 328 FLC B 503 HOH B 605 HOH B 609
SITE 6 AC8 27 HOH B 612 HOH B 634 HOH B 701 HOH B 716
SITE 7 AC8 27 HOH B 742 HOH B 745 LYS D 260
SITE 1 AC9 14 ARG B 109 ALA B 111 ILE B 113 ARG B 119
SITE 2 AC9 14 LEU B 120 TRP B 124 ILE B 128 ILE B 130
SITE 3 AC9 14 VAL B 255 GLN B 277 SER B 278 VAL B 281
SITE 4 AC9 14 SER B 287 C81 D 504
SITE 1 AD1 6 THR B 77 SER B 94 ASN B 96 ARG B 100
SITE 2 AD1 6 NDP B 501 HOH B 621
SITE 1 AD2 18 LYS D 72 ALA D 74 THR D 75 THR D 77
SITE 2 AD2 18 ARG D 82 ASN D 96 LEU D 288 GLU D 306
SITE 3 AD2 18 HIS D 309 GLY D 310 THR D 311 VAL D 312
SITE 4 AD2 18 THR D 313 ARG D 314 HIS D 315 THR D 327
SITE 5 AD2 18 ASN D 328 FLC D 503
SITE 1 AD3 15 ARG D 109 ALA D 111 ILE D 113 ARG D 119
SITE 2 AD3 15 LEU D 120 TRP D 124 ILE D 128 ILE D 130
SITE 3 AD3 15 VAL D 255 MET D 259 ALA D 282 TYR D 285
SITE 4 AD3 15 SER D 287 MET D 291 C81 D 504
SITE 1 AD4 4 THR D 77 SER D 94 ASN D 96 NDP D 501
SITE 1 AD5 11 LEU B 120 GLN B 277 VAL B 281 C81 B 502
SITE 2 AD5 11 LEU D 120 HIS D 132 CYS D 269 GLN D 277
SITE 3 AD5 11 SER D 278 VAL D 281 C81 D 502
CRYST1 81.495 155.312 163.054 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 0.012271 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006439 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006133 0.00000
(ATOM LINES ARE NOT SHOWN.)
END