HEADER OXIDOREDUCTASE 06-AUG-16 5SVO
TITLE STRUCTURE OF IDH2 MUTANT R140Q
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ISOCITRATE DEHYDROGENASE [NADP], MITOCHONDRIAL;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: IDH,ICD-M,IDP,NADP(+)-SPECIFIC ICDH,OXALOSUCCINATE
COMPND 5 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: IDH2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INHIBITOR, ISOCITRATE DEHYDROGENASE, MITOCHONDRIAL, NADPH,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.XIE,R.KULATHILA
REVDAT 3 06-MAR-24 5SVO 1 REMARK
REVDAT 2 22-MAR-17 5SVO 1 JRNL
REVDAT 1 08-FEB-17 5SVO 0
JRNL AUTH X.XIE,D.BAIRD,K.BOWEN,V.CAPKA,J.CHEN,G.CHENAIL,Y.CHO,
JRNL AUTH 2 J.DOOLEY,A.FARSIDJANI,P.FORTIN,D.KOHLS,R.KULATHILA,F.LIN,
JRNL AUTH 3 D.MCKAY,L.RODRIGUES,D.SAGE,B.B.TOURE,S.VAN DER PLAS,
JRNL AUTH 4 K.WRIGHT,M.XU,H.YIN,J.LEVELL,R.A.PAGLIARINI
JRNL TITL ALLOSTERIC MUTANT IDH1 INHIBITORS REVEAL MECHANISMS FOR IDH1
JRNL TITL 2 MUTANT AND ISOFORM SELECTIVITY.
JRNL REF STRUCTURE V. 25 506 2017
JRNL REFN ISSN 1878-4186
JRNL PMID 28132785
JRNL DOI 10.1016/J.STR.2016.12.017
REMARK 2
REMARK 2 RESOLUTION. 1.87 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
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) : 1.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 87.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 74609
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 3763
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) : 1.87
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.92
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5475
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2166
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5233
REMARK 3 BIN R VALUE (WORKING SET) : 0.2159
REMARK 3 BIN FREE R VALUE : 0.2327
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.42
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 242
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 : 6335
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 111
REMARK 3 SOLVENT ATOMS : 413
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.61390
REMARK 3 B22 (A**2) : 3.43190
REMARK 3 B33 (A**2) : 5.18200
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) : 0.235
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.139
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.125
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.135
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.123
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 : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6617 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 8966 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2342 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 160 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 947 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6617 ; 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 : 870 ; 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 : 8050 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.02
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.27
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.26
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4741 10.2523 9.2580
REMARK 3 T TENSOR
REMARK 3 T11: -0.0964 T22: -0.0976
REMARK 3 T33: -0.0681 T12: 0.0270
REMARK 3 T13: 0.0421 T23: -0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 0.5604 L22: 1.6216
REMARK 3 L33: 1.0496 L12: -0.2206
REMARK 3 L13: 0.1738 L23: -0.3982
REMARK 3 S TENSOR
REMARK 3 S11: 0.1002 S12: 0.1273 S13: 0.0002
REMARK 3 S21: -0.0701 S22: -0.1400 S23: 0.2179
REMARK 3 S31: 0.0849 S32: 0.0474 S33: 0.0398
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 41.4510 14.1940 40.7132
REMARK 3 T TENSOR
REMARK 3 T11: -0.0697 T22: -0.1417
REMARK 3 T33: -0.1811 T12: -0.0661
REMARK 3 T13: -0.0353 T23: 0.0498
REMARK 3 L TENSOR
REMARK 3 L11: 0.6176 L22: 1.3090
REMARK 3 L33: 2.4528 L12: 0.0129
REMARK 3 L13: 0.2524 L23: -0.0836
REMARK 3 S TENSOR
REMARK 3 S11: -0.0461 S12: -0.0508 S13: 0.1142
REMARK 3 S21: 0.3050 S22: -0.1380 S23: -0.0494
REMARK 3 S31: -0.3191 S32: 0.3436 S33: 0.1840
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5SVO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1000223216.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-OCT-13
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 PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 75021
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.870
REMARK 200 RESOLUTION RANGE LOW (A) : 127.500
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) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87
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 (%): 46.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH7.5, 0.2M NACL, 25% (W/V)
REMARK 280 PEG3350, VAPOR DIFFUSION, TEMPERATURE 277K
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 29.33050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.74800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 59.60350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.74800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.33050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 59.60350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 ALA A 40
REMARK 465 ASP A 41
REMARK 465 GLN A 452
REMARK 465 SER A 453
REMARK 465 LEU A 454
REMARK 465 GLU A 455
REMARK 465 HIS A 456
REMARK 465 HIS A 457
REMARK 465 HIS A 458
REMARK 465 HIS A 459
REMARK 465 HIS A 460
REMARK 465 HIS A 461
REMARK 465 HIS A 462
REMARK 465 HIS A 463
REMARK 465 ALA B 40
REMARK 465 ASP B 41
REMARK 465 LYS B 42
REMARK 465 PRO B 118
REMARK 465 ASP B 119
REMARK 465 GLU B 120
REMARK 465 ALA B 121
REMARK 465 ARG B 122
REMARK 465 VAL B 123
REMARK 465 GLU B 124
REMARK 465 GLU B 125
REMARK 465 PHE B 126
REMARK 465 LYS B 127
REMARK 465 LEU B 128
REMARK 465 LYS B 129
REMARK 465 LYS B 130
REMARK 465 MET B 131
REMARK 465 LYS B 360
REMARK 465 GLY B 361
REMARK 465 ARG B 362
REMARK 465 PRO B 363
REMARK 465 THR B 364
REMARK 465 ARG B 451
REMARK 465 GLN B 452
REMARK 465 SER B 453
REMARK 465 LEU B 454
REMARK 465 GLU B 455
REMARK 465 HIS B 456
REMARK 465 HIS B 457
REMARK 465 HIS B 458
REMARK 465 HIS B 459
REMARK 465 HIS B 460
REMARK 465 HIS B 461
REMARK 465 HIS B 462
REMARK 465 HIS B 463
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 57 -132.51 47.71
REMARK 500 ILE A 71 -68.02 -102.87
REMARK 500 SER A 108 -12.00 72.15
REMARK 500 ASP A 177 -136.56 60.32
REMARK 500 GLU B 57 -132.97 50.15
REMARK 500 ILE B 71 -70.17 -97.21
REMARK 500 ASP B 94 -0.78 76.83
REMARK 500 SER B 108 -12.88 70.14
REMARK 500 ALA B 174 57.16 -93.12
REMARK 500 ASP B 177 -134.79 56.65
REMARK 500 LYS B 180 35.86 -142.03
REMARK 500 ALA B 214 -169.60 -161.02
REMARK 500 ASN B 428 12.51 53.45
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 NAP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAP B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5SUN RELATED DB: PDB
REMARK 900 5SUN CONTAINS A DIFFERENT ISOFORM OF THE PROTEIN
REMARK 900 RELATED ID: 5SVN RELATED DB: PDB
REMARK 900 RELATED ID: 5SVF RELATED DB: PDB
DBREF 5SVO A 40 452 UNP P48735 IDHP_HUMAN 40 452
DBREF 5SVO B 40 452 UNP P48735 IDHP_HUMAN 40 452
SEQADV 5SVO GLN A 140 UNP P48735 ARG 140 ENGINEERED MUTATION
SEQADV 5SVO SER A 453 UNP P48735 EXPRESSION TAG
SEQADV 5SVO LEU A 454 UNP P48735 EXPRESSION TAG
SEQADV 5SVO GLU A 455 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS A 456 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS A 457 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS A 458 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS A 459 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS A 460 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS A 461 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS A 462 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS A 463 UNP P48735 EXPRESSION TAG
SEQADV 5SVO GLN B 140 UNP P48735 ARG 140 ENGINEERED MUTATION
SEQADV 5SVO SER B 453 UNP P48735 EXPRESSION TAG
SEQADV 5SVO LEU B 454 UNP P48735 EXPRESSION TAG
SEQADV 5SVO GLU B 455 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS B 456 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS B 457 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS B 458 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS B 459 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS B 460 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS B 461 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS B 462 UNP P48735 EXPRESSION TAG
SEQADV 5SVO HIS B 463 UNP P48735 EXPRESSION TAG
SEQRES 1 A 424 ALA ASP LYS ARG ILE LYS VAL ALA LYS PRO VAL VAL GLU
SEQRES 2 A 424 MET ASP GLY ASP GLU MET THR ARG ILE ILE TRP GLN PHE
SEQRES 3 A 424 ILE LYS GLU LYS LEU ILE LEU PRO HIS VAL ASP ILE GLN
SEQRES 4 A 424 LEU LYS TYR PHE ASP LEU GLY LEU PRO ASN ARG ASP GLN
SEQRES 5 A 424 THR ASP ASP GLN VAL THR ILE ASP SER ALA LEU ALA THR
SEQRES 6 A 424 GLN LYS TYR SER VAL ALA VAL LYS CYS ALA THR ILE THR
SEQRES 7 A 424 PRO ASP GLU ALA ARG VAL GLU GLU PHE LYS LEU LYS LYS
SEQRES 8 A 424 MET TRP LYS SER PRO ASN GLY THR ILE GLN ASN ILE LEU
SEQRES 9 A 424 GLY GLY THR VAL PHE ARG GLU PRO ILE ILE CYS LYS ASN
SEQRES 10 A 424 ILE PRO ARG LEU VAL PRO GLY TRP THR LYS PRO ILE THR
SEQRES 11 A 424 ILE GLY ARG HIS ALA HIS GLY ASP GLN TYR LYS ALA THR
SEQRES 12 A 424 ASP PHE VAL ALA ASP ARG ALA GLY THR PHE LYS MET VAL
SEQRES 13 A 424 PHE THR PRO LYS ASP GLY SER GLY VAL LYS GLU TRP GLU
SEQRES 14 A 424 VAL TYR ASN PHE PRO ALA GLY GLY VAL GLY MET GLY MET
SEQRES 15 A 424 TYR ASN THR ASP GLU SER ILE SER GLY PHE ALA HIS SER
SEQRES 16 A 424 CYS PHE GLN TYR ALA ILE GLN LYS LYS TRP PRO LEU TYR
SEQRES 17 A 424 MET SER THR LYS ASN THR ILE LEU LYS ALA TYR ASP GLY
SEQRES 18 A 424 ARG PHE LYS ASP ILE PHE GLN GLU ILE PHE ASP LYS HIS
SEQRES 19 A 424 TYR LYS THR ASP PHE ASP LYS ASN LYS ILE TRP TYR GLU
SEQRES 20 A 424 HIS ARG LEU ILE ASP ASP MET VAL ALA GLN VAL LEU LYS
SEQRES 21 A 424 SER SER GLY GLY PHE VAL TRP ALA CYS LYS ASN TYR ASP
SEQRES 22 A 424 GLY ASP VAL GLN SER ASP ILE LEU ALA GLN GLY PHE GLY
SEQRES 23 A 424 SER LEU GLY LEU MET THR SER VAL LEU VAL CYS PRO ASP
SEQRES 24 A 424 GLY LYS THR ILE GLU ALA GLU ALA ALA HIS GLY THR VAL
SEQRES 25 A 424 THR ARG HIS TYR ARG GLU HIS GLN LYS GLY ARG PRO THR
SEQRES 26 A 424 SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG
SEQRES 27 A 424 GLY LEU GLU HIS ARG GLY LYS LEU ASP GLY ASN GLN ASP
SEQRES 28 A 424 LEU ILE ARG PHE ALA GLN MET LEU GLU LYS VAL CYS VAL
SEQRES 29 A 424 GLU THR VAL GLU SER GLY ALA MET THR LYS ASP LEU ALA
SEQRES 30 A 424 GLY CYS ILE HIS GLY LEU SER ASN VAL LYS LEU ASN GLU
SEQRES 31 A 424 HIS PHE LEU ASN THR THR ASP PHE LEU ASP THR ILE LYS
SEQRES 32 A 424 SER ASN LEU ASP ARG ALA LEU GLY ARG GLN SER LEU GLU
SEQRES 33 A 424 HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 1 B 424 ALA ASP LYS ARG ILE LYS VAL ALA LYS PRO VAL VAL GLU
SEQRES 2 B 424 MET ASP GLY ASP GLU MET THR ARG ILE ILE TRP GLN PHE
SEQRES 3 B 424 ILE LYS GLU LYS LEU ILE LEU PRO HIS VAL ASP ILE GLN
SEQRES 4 B 424 LEU LYS TYR PHE ASP LEU GLY LEU PRO ASN ARG ASP GLN
SEQRES 5 B 424 THR ASP ASP GLN VAL THR ILE ASP SER ALA LEU ALA THR
SEQRES 6 B 424 GLN LYS TYR SER VAL ALA VAL LYS CYS ALA THR ILE THR
SEQRES 7 B 424 PRO ASP GLU ALA ARG VAL GLU GLU PHE LYS LEU LYS LYS
SEQRES 8 B 424 MET TRP LYS SER PRO ASN GLY THR ILE GLN ASN ILE LEU
SEQRES 9 B 424 GLY GLY THR VAL PHE ARG GLU PRO ILE ILE CYS LYS ASN
SEQRES 10 B 424 ILE PRO ARG LEU VAL PRO GLY TRP THR LYS PRO ILE THR
SEQRES 11 B 424 ILE GLY ARG HIS ALA HIS GLY ASP GLN TYR LYS ALA THR
SEQRES 12 B 424 ASP PHE VAL ALA ASP ARG ALA GLY THR PHE LYS MET VAL
SEQRES 13 B 424 PHE THR PRO LYS ASP GLY SER GLY VAL LYS GLU TRP GLU
SEQRES 14 B 424 VAL TYR ASN PHE PRO ALA GLY GLY VAL GLY MET GLY MET
SEQRES 15 B 424 TYR ASN THR ASP GLU SER ILE SER GLY PHE ALA HIS SER
SEQRES 16 B 424 CYS PHE GLN TYR ALA ILE GLN LYS LYS TRP PRO LEU TYR
SEQRES 17 B 424 MET SER THR LYS ASN THR ILE LEU LYS ALA TYR ASP GLY
SEQRES 18 B 424 ARG PHE LYS ASP ILE PHE GLN GLU ILE PHE ASP LYS HIS
SEQRES 19 B 424 TYR LYS THR ASP PHE ASP LYS ASN LYS ILE TRP TYR GLU
SEQRES 20 B 424 HIS ARG LEU ILE ASP ASP MET VAL ALA GLN VAL LEU LYS
SEQRES 21 B 424 SER SER GLY GLY PHE VAL TRP ALA CYS LYS ASN TYR ASP
SEQRES 22 B 424 GLY ASP VAL GLN SER ASP ILE LEU ALA GLN GLY PHE GLY
SEQRES 23 B 424 SER LEU GLY LEU MET THR SER VAL LEU VAL CYS PRO ASP
SEQRES 24 B 424 GLY LYS THR ILE GLU ALA GLU ALA ALA HIS GLY THR VAL
SEQRES 25 B 424 THR ARG HIS TYR ARG GLU HIS GLN LYS GLY ARG PRO THR
SEQRES 26 B 424 SER THR ASN PRO ILE ALA SER ILE PHE ALA TRP THR ARG
SEQRES 27 B 424 GLY LEU GLU HIS ARG GLY LYS LEU ASP GLY ASN GLN ASP
SEQRES 28 B 424 LEU ILE ARG PHE ALA GLN MET LEU GLU LYS VAL CYS VAL
SEQRES 29 B 424 GLU THR VAL GLU SER GLY ALA MET THR LYS ASP LEU ALA
SEQRES 30 B 424 GLY CYS ILE HIS GLY LEU SER ASN VAL LYS LEU ASN GLU
SEQRES 31 B 424 HIS PHE LEU ASN THR THR ASP PHE LEU ASP THR ILE LYS
SEQRES 32 B 424 SER ASN LEU ASP ARG ALA LEU GLY ARG GLN SER LEU GLU
SEQRES 33 B 424 HIS HIS HIS HIS HIS HIS HIS HIS
HET NAP A 501 48
HET EPE A 502 15
HET NAP B 501 48
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
HETSYN EPE HEPES
FORMUL 3 NAP 2(C21 H28 N7 O17 P3)
FORMUL 4 EPE C8 H18 N2 O4 S
FORMUL 6 HOH *413(H2 O)
HELIX 1 AA1 ASP A 56 LEU A 70 1 15
HELIX 2 AA2 GLY A 85 THR A 92 1 8
HELIX 3 AA3 ASP A 94 SER A 108 1 15
HELIX 4 AA4 ASP A 119 LYS A 127 1 9
HELIX 5 AA5 SER A 134 GLY A 144 1 11
HELIX 6 AA6 GLY A 176 ALA A 181 5 6
HELIX 7 AA7 ASP A 225 LYS A 243 1 19
HELIX 8 AA8 ALA A 257 TYR A 274 1 18
HELIX 9 AA9 TYR A 274 ASN A 281 1 8
HELIX 10 AB1 ILE A 290 SER A 300 1 11
HELIX 11 AB2 LYS A 309 PHE A 324 1 16
HELIX 12 AB3 SER A 326 GLY A 328 5 3
HELIX 13 AB4 VAL A 351 LYS A 360 1 10
HELIX 14 AB5 PRO A 368 GLY A 387 1 20
HELIX 15 AB6 ASN A 388 SER A 408 1 21
HELIX 16 AB7 THR A 412 GLY A 421 1 10
HELIX 17 AB8 ASN A 433 ARG A 451 1 19
HELIX 18 AB9 ASP B 56 LEU B 70 1 15
HELIX 19 AC1 GLY B 85 THR B 92 1 8
HELIX 20 AC2 ASP B 94 SER B 108 1 15
HELIX 21 AC3 SER B 134 GLY B 144 1 11
HELIX 22 AC4 GLY B 176 ALA B 181 5 6
HELIX 23 AC5 ASP B 225 LYS B 243 1 19
HELIX 24 AC6 ALA B 257 TYR B 274 1 18
HELIX 25 AC7 TYR B 274 ASN B 281 1 8
HELIX 26 AC8 ILE B 290 SER B 300 1 11
HELIX 27 AC9 LYS B 309 GLY B 325 1 17
HELIX 28 AD1 SER B 326 GLY B 328 5 3
HELIX 29 AD2 VAL B 351 GLN B 359 1 9
HELIX 30 AD3 PRO B 368 GLY B 387 1 20
HELIX 31 AD4 ASN B 388 GLY B 409 1 22
HELIX 32 AD5 THR B 412 GLY B 421 1 10
HELIX 33 AD6 ASN B 433 GLY B 450 1 18
SHEET 1 AA1 2 ILE A 44 LYS A 45 0
SHEET 2 AA1 2 VAL A 75 ASP A 76 1 O ASP A 76 N ILE A 44
SHEET 1 AA210 LEU A 79 ASP A 83 0
SHEET 2 AA210 VAL A 50 ASP A 54 1 N GLU A 52 O LYS A 80
SHEET 3 AA210 VAL A 109 LYS A 112 1 O VAL A 109 N VAL A 51
SHEET 4 AA210 ILE A 342 ALA A 346 1 O ALA A 344 N ALA A 110
SHEET 5 AA210 MET A 330 VAL A 335 -1 N LEU A 334 O GLU A 343
SHEET 6 AA210 THR A 146 PRO A 151 -1 N THR A 146 O VAL A 335
SHEET 7 AA210 ILE A 168 ARG A 172 -1 O ILE A 170 N ARG A 149
SHEET 8 AA210 PHE A 304 CYS A 308 1 O CYS A 308 N GLY A 171
SHEET 9 AA210 LEU A 246 THR A 250 1 N TYR A 247 O ALA A 307
SHEET 10 AA210 TYR A 285 LEU A 289 1 O ARG A 288 N MET A 248
SHEET 1 AA3 4 THR A 182 ALA A 186 0
SHEET 2 AA3 4 GLY A 216 THR A 224 -1 O GLY A 216 N ALA A 186
SHEET 3 AA3 4 GLY B 216 THR B 224 -1 O MET B 221 N MET A 219
SHEET 4 AA3 4 THR B 182 ALA B 186 -1 N ALA B 186 O GLY B 216
SHEET 1 AA4 4 LYS A 205 PHE A 212 0
SHEET 2 AA4 4 GLY A 190 PRO A 198 -1 N PHE A 192 O TYR A 210
SHEET 3 AA4 4 GLY B 190 PRO B 198 -1 O LYS B 193 N VAL A 195
SHEET 4 AA4 4 LYS B 205 PHE B 212 -1 O TYR B 210 N PHE B 192
SHEET 1 AA5 2 ILE B 44 LYS B 45 0
SHEET 2 AA5 2 VAL B 75 ASP B 76 1 O ASP B 76 N ILE B 44
SHEET 1 AA610 LEU B 79 ASP B 83 0
SHEET 2 AA610 VAL B 50 ASP B 54 1 N GLU B 52 O LYS B 80
SHEET 3 AA610 VAL B 109 LYS B 112 1 O VAL B 109 N VAL B 51
SHEET 4 AA610 ILE B 342 ALA B 346 1 O ALA B 344 N LYS B 112
SHEET 5 AA610 MET B 330 VAL B 335 -1 N LEU B 334 O GLU B 343
SHEET 6 AA610 THR B 146 PRO B 151 -1 N THR B 146 O VAL B 335
SHEET 7 AA610 ILE B 168 ARG B 172 -1 O ILE B 170 N ARG B 149
SHEET 8 AA610 PHE B 304 CYS B 308 1 O CYS B 308 N GLY B 171
SHEET 9 AA610 LEU B 246 THR B 250 1 N TYR B 247 O ALA B 307
SHEET 10 AA610 TYR B 285 LEU B 289 1 O ARG B 288 N MET B 248
SITE 1 AC1 22 LYS A 112 ALA A 114 THR A 115 THR A 117
SITE 2 AC1 22 ARG A 122 ASN A 136 HIS A 348 GLY A 349
SITE 3 AC1 22 THR A 350 VAL A 351 THR A 352 ARG A 353
SITE 4 AC1 22 HIS A 354 THR A 366 ASN A 367 HOH A 630
SITE 5 AC1 22 HOH A 641 HOH A 647 HOH A 670 HOH A 673
SITE 6 AC1 22 HOH A 742 HOH A 749
SITE 1 AC2 6 HIS A 233 GLN A 237 HIS A 273 TYR A 274
SITE 2 AC2 6 PRO A 337 HOH A 612
SITE 1 AC3 17 LYS B 112 ALA B 114 THR B 115 THR B 117
SITE 2 AC3 17 ASN B 136 GLU B 345 HIS B 348 GLY B 349
SITE 3 AC3 17 THR B 350 VAL B 351 THR B 352 ARG B 353
SITE 4 AC3 17 HIS B 354 ASN B 367 HOH B 626 HOH B 645
SITE 5 AC3 17 HOH B 658
CRYST1 58.661 119.207 127.496 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017047 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008389 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007843 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
