HEADER OXIDOREDUCTASE 20-JAN-15 4XRB
TITLE CRYSTAL STRUCTURE OF RV2671 FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RV2671;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: ATCC 25618 / H37RV;
SOURCE 5 GENE: RIBD, RV2671, RVBD_2671, LH57_14640, P425_02787;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS REDUCTASE, STRUCTURAL GENOMICS, TB STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 2 TBSGC, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.S.CHENG,J.C.SACCHETTINI,TB STRUCTURAL GENOMICS CONSORTIUM (TBSGC)
REVDAT 5 27-SEP-23 4XRB 1 REMARK
REVDAT 4 11-DEC-19 4XRB 1 REMARK
REVDAT 3 27-SEP-17 4XRB 1 JRNL REMARK
REVDAT 2 09-MAR-16 4XRB 1 JRNL
REVDAT 1 24-FEB-16 4XRB 0
JRNL AUTH Y.S.CHENG,J.C.SACCHETTINI
JRNL TITL STRUCTURAL INSIGHTS INTO MYCOBACTERIUM TUBERCULOSIS RV2671
JRNL TITL 2 PROTEIN AS A DIHYDROFOLATE REDUCTASE FUNCTIONAL ANALOGUE
JRNL TITL 3 CONTRIBUTING TO PARA-AMINOSALICYLIC ACID RESISTANCE.
JRNL REF BIOCHEMISTRY V. 55 1107 2016
JRNL REFN ISSN 0006-2960
JRNL PMID 26848874
JRNL DOI 10.1021/ACS.BIOCHEM.5B00993
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 20993
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1077
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 27.3613 - 3.7820 0.95 2518 119 0.1729 0.1797
REMARK 3 2 3.7820 - 3.0031 1.00 2544 124 0.1687 0.1807
REMARK 3 3 3.0031 - 2.6238 1.00 2496 155 0.1818 0.2149
REMARK 3 4 2.6238 - 2.3841 1.00 2514 126 0.1792 0.2522
REMARK 3 5 2.3841 - 2.2133 1.00 2477 130 0.1768 0.1964
REMARK 3 6 2.2133 - 2.0828 1.00 2467 145 0.1726 0.2210
REMARK 3 7 2.0828 - 1.9786 1.00 2487 141 0.1850 0.2169
REMARK 3 8 1.9786 - 1.8924 0.99 2413 137 0.2005 0.2480
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.45
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.43
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 : 0.018 1935
REMARK 3 ANGLE : 1.956 2640
REMARK 3 CHIRALITY : 0.137 316
REMARK 3 PLANARITY : 0.007 339
REMARK 3 DIHEDRAL : 15.408 715
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8749 27.2598 12.5363
REMARK 3 T TENSOR
REMARK 3 T11: 0.1724 T22: 0.1755
REMARK 3 T33: 0.1346 T12: -0.0119
REMARK 3 T13: 0.0090 T23: 0.0348
REMARK 3 L TENSOR
REMARK 3 L11: 1.8934 L22: 1.5735
REMARK 3 L33: 0.6441 L12: 0.5920
REMARK 3 L13: 0.4057 L23: 0.2536
REMARK 3 S TENSOR
REMARK 3 S11: -0.0620 S12: -0.0469 S13: 0.0568
REMARK 3 S21: -0.1754 S22: 0.0710 S23: 0.1430
REMARK 3 S31: -0.0103 S32: -0.1410 S33: -0.0006
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 4XRB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000206065.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUL-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 : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21013
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.29000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2P4G
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.2M SODIUM CHLORIDE,
REMARK 280 0.1M BIS(2-HYDROXYETHYL)-AMINO-TRIS(HYDROXYMETHYL)-METHANE)
REMARK 280 PH6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.76250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.76250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 35.67750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.30400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.67750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.30400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 37.76250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.67750
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.30400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 37.76250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.67750
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.30400
REMARK 290 SMTRY3 8 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: 9390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 71.35500
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 37.76250
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 428 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 ASP A 3
REMARK 465 SER A 4
REMARK 465 GLY A 5
REMARK 465 GLN A 6
REMARK 465 LEU A 7
REMARK 465 GLY A 8
REMARK 465 ALA A 9
REMARK 465 ILE A 90
REMARK 465 GLU A 91
REMARK 465 GLY A 92
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 97 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 122 CG CD NE CZ NH1 NH2
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 NH2 ARG A 103 OE2 GLU A 137 2.04
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 ARG A 135 79.24 -105.02
REMARK 500 LEU A 187 69.61 -101.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 NDP A 301
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TB-RV2671 RELATED DB: TARGETTRACK
REMARK 900 RELATED ID: 4XT5 RELATED DB: PDB
REMARK 900 RELATED ID: 4XT8 RELATED DB: PDB
REMARK 900 RELATED ID: 4XT6 RELATED DB: PDB
REMARK 900 RELATED ID: 4XT7 RELATED DB: PDB
REMARK 900 RELATED ID: 4XT4 RELATED DB: PDB
DBREF 4XRB A 1 258 UNP P71968 P71968_MYCTU 1 258
SEQRES 1 A 258 MET PRO ASP SER GLY GLN LEU GLY ALA ALA ASP THR PRO
SEQRES 2 A 258 LEU ARG LEU LEU SER SER VAL HIS TYR LEU THR ASP GLY
SEQRES 3 A 258 GLU LEU PRO GLN LEU TYR ASP TYR PRO ASP ASP GLY THR
SEQRES 4 A 258 TRP LEU ARG ALA ASN PHE ILE SER SER LEU ASP GLY GLY
SEQRES 5 A 258 ALA THR VAL ASP GLY THR SER GLY ALA MET ALA GLY PRO
SEQRES 6 A 258 GLY ASP ARG PHE VAL PHE ASN LEU LEU ARG GLU LEU ALA
SEQRES 7 A 258 ASP VAL ILE VAL VAL GLY VAL GLY THR VAL ARG ILE GLU
SEQRES 8 A 258 GLY TYR SER GLY VAL ARG MET GLY VAL VAL GLN ARG GLN
SEQRES 9 A 258 HIS ARG GLN ALA ARG GLY GLN SER GLU VAL PRO GLN LEU
SEQRES 10 A 258 ALA ILE VAL THR ARG SER GLY ARG LEU ASP ARG ASP MET
SEQRES 11 A 258 ALA VAL PHE THR ARG THR GLU MET ALA PRO LEU VAL LEU
SEQRES 12 A 258 THR THR THR ALA VAL ALA ASP ASP THR ARG GLN ARG LEU
SEQRES 13 A 258 ALA GLY LEU ALA GLU VAL ILE ALA CYS SER GLY ASP ASP
SEQRES 14 A 258 PRO GLY THR VAL ASP GLU ALA VAL LEU VAL SER GLN LEU
SEQRES 15 A 258 ALA ALA ARG GLY LEU ARG ARG ILE LEU THR GLU GLY GLY
SEQRES 16 A 258 PRO THR LEU LEU GLY THR PHE VAL GLU ARG ASP VAL LEU
SEQRES 17 A 258 ASP GLU LEU CYS LEU THR ILE ALA PRO TYR VAL VAL GLY
SEQRES 18 A 258 GLY LEU ALA ARG ARG ILE VAL THR GLY PRO GLY GLN VAL
SEQRES 19 A 258 LEU THR ARG MET ARG CYS ALA HIS VAL LEU THR ASP ASP
SEQRES 20 A 258 SER GLY TYR LEU TYR THR ARG TYR VAL LYS THR
HET NDP A 301 48
HET PEG A 302 7
HETNAM NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NDP PHOSPHATE
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 2 NDP C21 H30 N7 O17 P3
FORMUL 3 PEG C4 H10 O3
FORMUL 4 HOH *68(H2 O)
HELIX 1 AA1 GLU A 27 ASP A 33 1 7
HELIX 2 AA2 SER A 59 ALA A 63 5 5
HELIX 3 AA3 GLY A 66 ALA A 78 1 13
HELIX 4 AA4 VAL A 85 ARG A 89 1 5
HELIX 5 AA5 GLY A 99 ARG A 109 1 11
HELIX 6 AA6 MET A 130 ARG A 135 1 6
HELIX 7 AA7 VAL A 148 LEU A 156 1 9
HELIX 8 AA8 ASP A 174 ALA A 184 1 11
HELIX 9 AA9 GLY A 195 ARG A 205 1 11
SHEET 1 AA1 9 GLU A 161 ALA A 164 0
SHEET 2 AA1 9 LEU A 141 THR A 144 1 N VAL A 142 O ILE A 163
SHEET 3 AA1 9 GLN A 116 VAL A 120 1 N LEU A 117 O LEU A 141
SHEET 4 AA1 9 VAL A 80 GLY A 84 1 N VAL A 83 O ALA A 118
SHEET 5 AA1 9 ARG A 189 GLY A 194 1 O LEU A 191 N VAL A 82
SHEET 6 AA1 9 TRP A 40 SER A 48 1 N TRP A 40 O ILE A 190
SHEET 7 AA1 9 GLU A 210 ALA A 216 1 O CYS A 212 N ALA A 43
SHEET 8 AA1 9 LEU A 251 LYS A 257 -1 O LEU A 251 N ILE A 215
SHEET 9 AA1 9 MET A 238 THR A 245 -1 N ARG A 239 O VAL A 256
CISPEP 1 GLY A 194 GLY A 195 0 -2.39
SITE 1 AC1 25 PHE A 45 ILE A 46 ALA A 53 GLY A 57
SITE 2 AC1 25 THR A 58 SER A 59 GLY A 84 VAL A 85
SITE 3 AC1 25 GLY A 86 THR A 87 VAL A 120 THR A 121
SITE 4 AC1 25 ARG A 122 SER A 123 VAL A 173 GLU A 175
SITE 5 AC1 25 GLU A 193 GLY A 194 GLY A 195 PRO A 196
SITE 6 AC1 25 THR A 197 LEU A 198 THR A 201 ARG A 225
SITE 7 AC1 25 HOH A 440
SITE 1 AC2 4 ASP A 79 ARG A 106 SER A 112 GLY A 186
CRYST1 71.355 96.608 75.525 90.00 90.00 90.00 C 2 2 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 0.014014 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010351 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013241 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
