HEADER OXIDOREDUCTASE 10-JUL-14 4TZT
TITLE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ENOYL REDUCTASE (INHA)
TITLE 2 COMPLEXED WITH N-(3-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-DEC-23 4TZT 1 REMARK
REVDAT 3 25-DEC-19 4TZT 1 REMARK
REVDAT 2 20-SEP-17 4TZT 1 SOURCE REMARK
REVDAT 1 20-AUG-14 4TZT 0
SPRSDE 20-AUG-14 4TZT 2H7P
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. 1.86 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) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.34
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 33284
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.141
REMARK 3 R VALUE (WORKING SET) : 0.140
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.850
REMARK 3 FREE R VALUE TEST SET COUNT : 1910
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 42.3518 - 5.5064 0.99 2273 138 0.1477 0.1500
REMARK 3 2 5.5064 - 4.3720 1.00 2304 145 0.1239 0.1417
REMARK 3 3 4.3720 - 3.8198 1.00 2294 143 0.1273 0.1455
REMARK 3 4 3.8198 - 3.4707 1.00 2304 146 0.1343 0.1608
REMARK 3 5 3.4707 - 3.2220 1.00 2293 142 0.1423 0.1730
REMARK 3 6 3.2220 - 3.0321 1.00 2285 148 0.1410 0.1753
REMARK 3 7 3.0321 - 2.8803 1.00 2292 139 0.1340 0.1682
REMARK 3 8 2.8803 - 2.7550 1.00 2303 145 0.1343 0.1697
REMARK 3 9 2.7550 - 2.6489 1.00 2291 140 0.1309 0.1789
REMARK 3 10 2.6489 - 2.5575 1.00 2312 139 0.1344 0.1954
REMARK 3 11 2.5575 - 2.4776 1.00 2308 143 0.1406 0.1861
REMARK 3 12 2.4776 - 2.4067 1.00 2298 146 0.1289 0.1889
REMARK 3 13 2.4067 - 2.3434 1.00 2281 138 0.1257 0.1843
REMARK 3 14 2.3434 - 2.2862 1.00 2273 145 0.1273 0.1573
REMARK 3 15 2.2862 - 2.2343 1.00 2308 135 0.1290 0.1497
REMARK 3 16 2.2343 - 2.1867 1.00 2318 143 0.1377 0.1782
REMARK 3 17 2.1867 - 2.1430 1.00 2289 144 0.1457 0.1564
REMARK 3 18 2.1430 - 2.1025 1.00 2303 140 0.1474 0.1622
REMARK 3 19 2.1025 - 2.0650 1.00 2293 141 0.1503 0.1667
REMARK 3 20 2.0650 - 2.0300 1.00 2292 147 0.1562 0.1903
REMARK 3 21 2.0300 - 1.9972 1.00 2265 137 0.1595 0.2196
REMARK 3 22 1.9972 - 1.9665 1.00 2326 144 0.1617 0.1740
REMARK 3 23 1.9665 - 1.9376 1.00 2292 148 0.1694 0.1850
REMARK 3 24 1.9376 - 1.9103 1.00 2282 148 0.1809 0.2323
REMARK 3 25 1.9103 - 1.8845 1.00 2277 139 0.1989 0.2166
REMARK 3 26 1.8845 - 1.8600 1.00 2313 144 0.2265 0.2341
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.480
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 : 0.012 2131
REMARK 3 ANGLE : 1.316 2908
REMARK 3 CHIRALITY : 0.057 330
REMARK 3 PLANARITY : 0.007 394
REMARK 3 DIHEDRAL : 12.705 797
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): 45.5974 48.1684 52.5347
REMARK 3 T TENSOR
REMARK 3 T11: 0.1277 T22: 0.2186
REMARK 3 T33: 0.1636 T12: -0.0043
REMARK 3 T13: -0.0111 T23: 0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.2450 L22: 0.2795
REMARK 3 L33: 0.4400 L12: -0.0682
REMARK 3 L13: 0.1397 L23: 0.0045
REMARK 3 S TENSOR
REMARK 3 S11: -0.0224 S12: -0.0121 S13: 0.0305
REMARK 3 S21: 0.0235 S22: -0.0122 S23: -0.0291
REMARK 3 S31: -0.0533 S32: 0.1409 S33: -0.0140
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 4TZT 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_1000202578.
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 : NULL
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 : 33284
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 42.341
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.12900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.42000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% MPD, 50MM NA CITRATE PH 6.5, 100
REMARK 280 MM HEPES PH 7.2, 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 94.08333
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 47.04167
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 94.08333
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 47.04167
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 94.08333
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 47.04167
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 94.08333
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 47.04167
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: 22210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -138.0 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 48.89100
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 84.68170
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 94.08333
REMARK 350 BIOMT1 4 0.500000 -0.866025 0.000000 48.89100
REMARK 350 BIOMT2 4 -0.866025 -0.500000 0.000000 84.68170
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 94.08333
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 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 THR A 2 OG1 CG2
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 HE22 GLN A 48 O HOH A 797 1.58
REMARK 500 O HOH A 838 O HOH A 854 2.02
REMARK 500 O HOH A 849 O HOH A 873 2.12
REMARK 500 O HOH A 822 O HOH A 843 2.18
REMARK 500 O HOH A 805 O HOH A 836 2.18
REMARK 500 O HOH A 809 O HOH A 842 2.19
REMARK 500 O HOH A 847 O HOH A 882 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 667 O HOH A 667 10665 2.05
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 ILE A 16 -32.41 -136.62
REMARK 500 ASP A 42 -60.23 72.54
REMARK 500 ALA A 124 -56.55 -125.39
REMARK 500 ALA A 157 -33.63 73.52
REMARK 500 ASN A 159 -116.42 44.00
REMARK 500 ALA A 260 75.37 -111.35
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 802 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH A 803 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH A 816 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH A 845 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A 861 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH A 863 DISTANCE = 8.32 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 468 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: 4U0J RELATED DB: PDB
REMARK 900 RELATED ID: 4U0K RELATED DB: PDB
DBREF 4TZT 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 69
HET 468 A 501 46
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 468 (3S)-N-(3-CHLORO-2-METHYLPHENYL)-1-CYCLOHEXYL-5-
HETNAM 2 468 OXOPYRROLIDINE-3-CARBOXAMIDE
FORMUL 2 NAD C21 H27 N7 O14 P2
FORMUL 3 468 C18 H23 CL N2 O2
FORMUL 4 HOH *282(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 35 GLY A 14 ILE A 15 ILE A 16 SER A 20
SITE 2 AC1 35 ILE A 21 PHE A 41 LEU A 63 ASP A 64
SITE 3 AC1 35 VAL A 65 SER A 94 ILE A 95 GLY A 96
SITE 4 AC1 35 ILE A 122 MET A 147 ASP A 148 PHE A 149
SITE 5 AC1 35 LYS A 165 GLY A 192 PRO A 193 ILE A 194
SITE 6 AC1 35 THR A 196 468 A 501 HOH A 682 HOH A 690
SITE 7 AC1 35 HOH A 691 HOH A 698 HOH A 707 HOH A 717
SITE 8 AC1 35 HOH A 723 HOH A 788 HOH A 790 HOH A 798
SITE 9 AC1 35 HOH A 800 HOH A 804 HOH A 848
SITE 1 AC2 10 GLY A 96 MET A 103 PHE A 149 PRO A 156
SITE 2 AC2 10 ALA A 157 TYR A 158 MET A 199 ILE A 215
SITE 3 AC2 10 NAD A 500 HOH A 723
CRYST1 97.782 97.782 141.125 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 0.010227 0.005904 0.000000 0.00000
SCALE2 0.000000 0.011809 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007086 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
