HEADER OXIDOREDUCTASE 11-JUL-14 4U0K
TITLE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ENOYL REDUCTASE
TITLE 2 COMPLEXED WITH N-(5-CHLORO-2-METHYLPHENYL)-1-CYCLOHEXYL-5-
TITLE 3 OXOPYRROLIDINE-3-CARBOXAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH];
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: NADH-DEPENDENT ENOYL-ACP REDUCTASE;
COMPND 5 EC: 1.3.1.9;
COMPND 6 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: INHA, RV1484, MTCY277.05;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS OXIDOREDUCTASE, PYRROLIDINE CARBOXAMIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.HE,A.ALIAN,R.M.STROUD,P.R.ORTIZ DE MONTELLANO
REVDAT 4 27-SEP-23 4U0K 1 REMARK
REVDAT 3 25-DEC-19 4U0K 1 REMARK
REVDAT 2 20-SEP-17 4U0K 1 SOURCE JRNL REMARK
REVDAT 1 30-JUL-14 4U0K 0
SPRSDE 30-JUL-14 4U0K 2H7N
JRNL AUTH X.HE,A.ALIAN,R.M.STROUD,P.R.ORTIZ DE MONTELLANO
JRNL TITL PYRROLIDINE CARBOXAMIDES AS A NOVEL CLASS OF INHIBITORS OF
JRNL TITL 2 ENOYL ACYL CARRIER PROTEIN REDUCTASE FROM MYCOBACTERIUM
JRNL TITL 3 TUBERCULOSIS
JRNL REF J. MED. CHEM. 6308 2006
JRNL REFN ISSN 0022-2623
JRNL PMID 17034137
JRNL DOI 10.1021/JM060715Y
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
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) : 40.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 30665
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.144
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.610
REMARK 3 FREE R VALUE TEST SET COUNT : 2335
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 40.9033 - 4.8832 0.97 1871 130 0.1661 0.1816
REMARK 3 2 4.8832 - 3.8769 0.99 1789 124 0.1247 0.1506
REMARK 3 3 3.8769 - 3.3871 1.00 1739 150 0.1354 0.1567
REMARK 3 4 3.3871 - 3.0775 0.99 1682 168 0.1520 0.1378
REMARK 3 5 3.0775 - 2.8570 0.99 1677 145 0.1488 0.2265
REMARK 3 6 2.8570 - 2.6886 0.98 1670 152 0.1409 0.1803
REMARK 3 7 2.6886 - 2.5540 0.98 1648 133 0.1398 0.1885
REMARK 3 8 2.5540 - 2.4428 0.98 1662 138 0.1465 0.1673
REMARK 3 9 2.4428 - 2.3488 0.97 1651 132 0.1312 0.1798
REMARK 3 10 2.3488 - 2.2677 0.97 1637 143 0.1330 0.1724
REMARK 3 11 2.2677 - 2.1968 0.97 1605 148 0.1360 0.1532
REMARK 3 12 2.1968 - 2.1340 0.97 1641 130 0.1445 0.1855
REMARK 3 13 2.1340 - 2.0779 0.97 1627 126 0.1483 0.1874
REMARK 3 14 2.0779 - 2.0272 0.97 1613 137 0.1499 0.1977
REMARK 3 15 2.0272 - 1.9811 0.98 1633 124 0.1594 0.1895
REMARK 3 16 1.9811 - 1.9389 0.96 1613 122 0.1553 0.2321
REMARK 3 17 1.9389 - 1.9000 0.94 1572 133 0.1661 0.1948
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.600
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.011 2127
REMARK 3 ANGLE : 1.258 2902
REMARK 3 CHIRALITY : 0.052 328
REMARK 3 PLANARITY : 0.007 393
REMARK 3 DIHEDRAL : 12.781 794
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): 45.5857 47.9713 52.1419
REMARK 3 T TENSOR
REMARK 3 T11: 0.1060 T22: 0.1745
REMARK 3 T33: 0.1419 T12: -0.0039
REMARK 3 T13: -0.0104 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.2332 L22: 0.4566
REMARK 3 L33: 0.4661 L12: -0.0288
REMARK 3 L13: 0.1955 L23: -0.0114
REMARK 3 S TENSOR
REMARK 3 S11: -0.0246 S12: -0.0049 S13: 0.0289
REMARK 3 S21: 0.0227 S22: -0.0064 S23: -0.0661
REMARK 3 S31: -0.0430 S32: 0.1302 S33: 0.0325
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 4U0K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-14.
REMARK 100 THE DEPOSITION ID IS D_1000202608.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7 - 8
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1159
REMARK 200 MONOCHROMATOR : DOUBLE FLAT, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30670
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 41.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.6000
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) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.44900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB 1P45
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% MPD, 50 MM NA CITRATE PH 6.5, 100MM
REMARK 280 HEPES PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+2/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.61400
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.80700
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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 93.61400
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 46.80700
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 93.61400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 46.80700
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 93.61400
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 46.80700
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -132.0 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 48.52850
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 84.05383
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 93.61400
REMARK 350 BIOMT1 4 0.500000 -0.866025 0.000000 48.52850
REMARK 350 BIOMT2 4 -0.866025 -0.500000 0.000000 84.05383
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 93.61400
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 636 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 THR A 2
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 HE21 GLN A 48 O HOH A 774 1.53
REMARK 500 O HOH A 844 O HOH A 848 2.11
REMARK 500 O HOH A 821 O HOH A 845 2.12
REMARK 500 O HOH A 784 O HOH A 809 2.19
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 ASP A 42 -58.15 76.83
REMARK 500 ALA A 124 -56.73 -126.94
REMARK 500 ALA A 157 -33.20 70.99
REMARK 500 ASN A 159 -115.24 38.99
REMARK 500 ALA A 260 74.08 -109.86
REMARK 500 ASP A 261 16.20 -140.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 778 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH A 827 DISTANCE = 6.28 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 744 A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TRJ RELATED DB: PDB
REMARK 900 RELATED ID: 4TZK RELATED DB: PDB
REMARK 900 RELATED ID: 4TZT RELATED DB: PDB
REMARK 900 RELATED ID: 4U0J RELATED DB: PDB
DBREF 4U0K A 1 269 UNP P9WGR1 INHA_MYCTU 1 269
SEQRES 1 A 269 MET THR GLY LEU LEU ASP GLY LYS ARG ILE LEU VAL SER
SEQRES 2 A 269 GLY ILE ILE THR ASP SER SER ILE ALA PHE HIS ILE ALA
SEQRES 3 A 269 ARG VAL ALA GLN GLU GLN GLY ALA GLN LEU VAL LEU THR
SEQRES 4 A 269 GLY PHE ASP ARG LEU ARG LEU ILE GLN ARG ILE THR ASP
SEQRES 5 A 269 ARG LEU PRO ALA LYS ALA PRO LEU LEU GLU LEU ASP VAL
SEQRES 6 A 269 GLN ASN GLU GLU HIS LEU ALA SER LEU ALA GLY ARG VAL
SEQRES 7 A 269 THR GLU ALA ILE GLY ALA GLY ASN LYS LEU ASP GLY VAL
SEQRES 8 A 269 VAL HIS SER ILE GLY PHE MET PRO GLN THR GLY MET GLY
SEQRES 9 A 269 ILE ASN PRO PHE PHE ASP ALA PRO TYR ALA ASP VAL SER
SEQRES 10 A 269 LYS GLY ILE HIS ILE SER ALA TYR SER TYR ALA SER MET
SEQRES 11 A 269 ALA LYS ALA LEU LEU PRO ILE MET ASN PRO GLY GLY SER
SEQRES 12 A 269 ILE VAL GLY MET ASP PHE ASP PRO SER ARG ALA MET PRO
SEQRES 13 A 269 ALA TYR ASN TRP MET THR VAL ALA LYS SER ALA LEU GLU
SEQRES 14 A 269 SER VAL ASN ARG PHE VAL ALA ARG GLU ALA GLY LYS TYR
SEQRES 15 A 269 GLY VAL ARG SER ASN LEU VAL ALA ALA GLY PRO ILE ARG
SEQRES 16 A 269 THR LEU ALA MET SER ALA ILE VAL GLY GLY ALA LEU GLY
SEQRES 17 A 269 GLU GLU ALA GLY ALA GLN ILE GLN LEU LEU GLU GLU GLY
SEQRES 18 A 269 TRP ASP GLN ARG ALA PRO ILE GLY TRP ASN MET LYS ASP
SEQRES 19 A 269 ALA THR PRO VAL ALA LYS THR VAL CYS ALA LEU LEU SER
SEQRES 20 A 269 ASP TRP LEU PRO ALA THR THR GLY ASP ILE ILE TYR ALA
SEQRES 21 A 269 ASP GLY GLY ALA HIS THR GLN LEU LEU
HET NAD A 500 70
HET 744 A 501 46
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 744 (3S)-N-(5-CHLORO-2-METHYLPHENYL)-1-CYCLOHEXYL-5-
HETNAM 2 744 OXOPYRROLIDINE-3-CARBOXAMIDE
FORMUL 2 NAD C21 H27 N7 O14 P2
FORMUL 3 744 C18 H23 CL N2 O2
FORMUL 4 HOH *269(H2 O)
HELIX 1 AA1 SER A 20 GLN A 32 1 13
HELIX 2 AA2 ARG A 43 ASP A 52 1 10
HELIX 3 AA3 ASN A 67 GLY A 83 1 17
HELIX 4 AA4 PRO A 99 MET A 103 5 5
HELIX 5 AA5 PRO A 107 ALA A 111 5 5
HELIX 6 AA6 PRO A 112 ALA A 124 1 13
HELIX 7 AA7 ALA A 124 LEU A 135 1 12
HELIX 8 AA8 TYR A 158 LYS A 181 1 24
HELIX 9 AA9 THR A 196 GLY A 204 1 9
HELIX 10 AB1 GLY A 208 ALA A 226 1 19
HELIX 11 AB2 ALA A 235 SER A 247 1 13
HELIX 12 AB3 GLY A 263 GLN A 267 5 5
SHEET 1 AA1 7 LEU A 60 GLU A 62 0
SHEET 2 AA1 7 GLN A 35 GLY A 40 1 N LEU A 38 O LEU A 61
SHEET 3 AA1 7 ARG A 9 SER A 13 1 N VAL A 12 O VAL A 37
SHEET 4 AA1 7 LEU A 88 HIS A 93 1 O ASP A 89 N ARG A 9
SHEET 5 AA1 7 MET A 138 ASP A 148 1 O VAL A 145 N HIS A 93
SHEET 6 AA1 7 ARG A 185 ALA A 191 1 O VAL A 189 N ASP A 148
SHEET 7 AA1 7 ASP A 256 ALA A 260 1 O ILE A 258 N LEU A 188
SITE 1 AC1 32 GLY A 14 ILE A 15 ILE A 16 SER A 20
SITE 2 AC1 32 ILE A 21 PHE A 41 LEU A 63 ASP A 64
SITE 3 AC1 32 VAL A 65 SER A 94 ILE A 95 GLY A 96
SITE 4 AC1 32 ILE A 122 MET A 147 ASP A 148 PHE A 149
SITE 5 AC1 32 LYS A 165 GLY A 192 PRO A 193 ILE A 194
SITE 6 AC1 32 THR A 196 744 A 501 HOH A 680 HOH A 688
SITE 7 AC1 32 HOH A 689 HOH A 696 HOH A 704 HOH A 714
SITE 8 AC1 32 HOH A 768 HOH A 776 HOH A 780 HOH A 828
SITE 1 AC2 11 GLY A 96 MET A 103 PHE A 149 PRO A 156
SITE 2 AC2 11 ALA A 157 TYR A 158 MET A 161 MET A 199
SITE 3 AC2 11 ILE A 215 LEU A 218 NAD A 500
CRYST1 97.057 97.057 140.421 90.00 90.00 120.00 P 62 2 2 12
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 0.010303 0.005949 0.000000 0.00000
SCALE2 0.000000 0.011897 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007121 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
