HEADER OXIDOREDUCTASE 19-SEP-05 2B36
TITLE CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS ENOYL REDUCTASE (INHA)
TITLE 2 INHIBITED BY 5-PENTYL-2-PHENOXYPHENOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH];
COMPND 3 CHAIN: A, B, C, D, E, F;
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: 1773;
SOURCE 4 GENE: INHA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ENOYL REDUCTASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.J.SULLIVAN,J.J.TRUGLIO,P.NOVICHENOK,C.STRATTON,X.ZHANG,T.KAUR,
AUTHOR 2 F.JOHNSON,M.S.BOYNE,A.AMIN
REVDAT 4 14-FEB-24 2B36 1 REMARK
REVDAT 3 11-OCT-17 2B36 1 REMARK
REVDAT 2 24-FEB-09 2B36 1 VERSN
REVDAT 1 07-MAR-06 2B36 0
JRNL AUTH T.J.SULLIVAN,J.J.TRUGLIO,M.E.BOYNE,P.NOVICHENOK,X.ZHANG,
JRNL AUTH 2 C.STRATTON,H.J.LI,T.KAUR,A.AMIN,F.JOHNSON,R.A.SLAYDEN,
JRNL AUTH 3 C.KISKER,P.J.TONGE
JRNL TITL HIGH AFFINITY INHA INHIBITORS WITH ACTIVITY AGAINST
JRNL TITL 2 DRUG-RESISTANT STRAINS OF MYCOBACTERIUM TUBERCULOSIS
JRNL REF ACS CHEM.BIOL. V. 1 43 2006
JRNL REFN ISSN 1554-8929
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 34274
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) : 0.245
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1872
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2262
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.2860
REMARK 3 BIN FREE R VALUE SET COUNT : 120
REMARK 3 BIN FREE R VALUE : 0.3490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11463
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 378
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.87000
REMARK 3 B22 (A**2) : -0.69000
REMARK 3 B33 (A**2) : 1.32000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.20000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.496
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.355
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.311
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.854
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.777
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12094 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 11272 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16460 ; 1.480 ; 2.003
REMARK 3 BOND ANGLES OTHERS (DEGREES): 26137 ; 1.112 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1517 ; 4.234 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 461 ;37.423 ;23.753
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1898 ;16.720 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 78 ;23.208 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1889 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13315 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2285 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3095 ; 0.222 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 12589 ; 0.208 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6032 ; 0.183 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 6957 ; 0.090 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 320 ; 0.168 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 3 ; 0.053 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 43 ; 0.272 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 166 ; 0.318 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.330 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): 1 ; 0.012 ; 0.200
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 9666 ; 2.544 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3141 ; 0.506 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12075 ; 3.326 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5173 ; 2.043 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4385 ; 3.041 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2B36 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034618.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34274
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 10.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, DMSO, AMMONIUM ACETATE,
REMARK 280 NAD+, ADA , PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 49.97750
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.91350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 49.97750
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.91350
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A TETRAMER.
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 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 21600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -137.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F
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 MET A 1
REMARK 465 MET B 1
REMARK 465 LEU B 197
REMARK 465 ALA B 198
REMARK 465 MET B 199
REMARK 465 SER B 200
REMARK 465 ALA B 201
REMARK 465 ILE B 202
REMARK 465 VAL B 203
REMARK 465 GLY B 204
REMARK 465 GLY B 205
REMARK 465 MET C 1
REMARK 465 LEU C 197
REMARK 465 ALA C 198
REMARK 465 MET C 199
REMARK 465 SER C 200
REMARK 465 ALA C 201
REMARK 465 ILE C 202
REMARK 465 VAL C 203
REMARK 465 GLY C 204
REMARK 465 GLY C 205
REMARK 465 ALA C 206
REMARK 465 LEU C 207
REMARK 465 GLY C 208
REMARK 465 GLU C 209
REMARK 465 GLU C 210
REMARK 465 ALA C 211
REMARK 465 GLY C 212
REMARK 465 ALA C 213
REMARK 465 GLN C 214
REMARK 465 ILE C 215
REMARK 465 GLN C 216
REMARK 465 MET D 1
REMARK 465 SER D 200
REMARK 465 ALA D 201
REMARK 465 ILE D 202
REMARK 465 VAL D 203
REMARK 465 GLY D 204
REMARK 465 GLY D 205
REMARK 465 ALA D 206
REMARK 465 LEU D 207
REMARK 465 GLY D 208
REMARK 465 GLU D 209
REMARK 465 GLU D 210
REMARK 465 ALA D 211
REMARK 465 GLY D 212
REMARK 465 ALA D 213
REMARK 465 GLN D 214
REMARK 465 ILE D 215
REMARK 465 GLN D 216
REMARK 465 LEU D 217
REMARK 465 LEU D 218
REMARK 465 GLU D 219
REMARK 465 MET E 1
REMARK 465 LEU E 197
REMARK 465 ALA E 198
REMARK 465 MET E 199
REMARK 465 SER E 200
REMARK 465 ALA E 201
REMARK 465 ILE E 202
REMARK 465 VAL E 203
REMARK 465 GLY E 204
REMARK 465 GLY E 205
REMARK 465 ALA E 206
REMARK 465 LEU E 207
REMARK 465 GLY E 208
REMARK 465 GLU E 209
REMARK 465 GLU E 210
REMARK 465 MET F 1
REMARK 465 LEU F 197
REMARK 465 ALA F 198
REMARK 465 MET F 199
REMARK 465 SER F 200
REMARK 465 ALA F 201
REMARK 465 ILE F 202
REMARK 465 VAL F 203
REMARK 465 GLY F 204
REMARK 465 GLY F 205
REMARK 465 ALA F 206
REMARK 465 LEU F 207
REMARK 465 GLY F 208
REMARK 465 GLU F 209
REMARK 465 GLU F 210
REMARK 465 ALA F 211
REMARK 465 GLY F 212
REMARK 465 ALA F 213
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 O THR D 101 ND2 ASN D 106 2.16
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 NH1 ARG A 153 O HIS A 265 2555 2.18
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 -42.02 -130.42
REMARK 500 ASP A 42 -59.44 -126.94
REMARK 500 ALA A 84 132.81 -28.89
REMARK 500 ALA A 124 -61.03 -121.26
REMARK 500 ASP A 150 109.85 -43.45
REMARK 500 ALA A 157 -51.89 69.24
REMARK 500 ASN A 159 -112.63 37.28
REMARK 500 THR A 196 -91.46 -120.54
REMARK 500 LEU A 197 -68.18 -129.90
REMARK 500 VAL A 203 -75.62 -45.49
REMARK 500 ALA A 211 -158.57 -58.61
REMARK 500 GLN A 214 -62.47 -90.70
REMARK 500 SER A 247 -165.67 -74.07
REMARK 500 LEU A 250 51.60 -146.48
REMARK 500 ALA A 260 75.79 -101.97
REMARK 500 ASP A 261 18.12 -140.37
REMARK 500 HIS A 265 -3.56 -58.23
REMARK 500 ILE B 16 -31.03 -143.65
REMARK 500 PHE B 41 -68.02 -93.44
REMARK 500 SER B 94 50.90 -140.99
REMARK 500 MET B 98 117.27 -175.29
REMARK 500 MET B 103 127.31 -173.56
REMARK 500 ASP B 150 109.52 -36.97
REMARK 500 ALA B 157 -48.41 69.41
REMARK 500 ASN B 159 -111.82 38.41
REMARK 500 SER B 247 -162.46 -68.63
REMARK 500 LEU B 250 58.61 -154.28
REMARK 500 ALA B 260 79.68 -106.59
REMARK 500 ASP B 261 15.75 -140.39
REMARK 500 HIS B 265 2.31 -65.30
REMARK 500 ILE C 16 -37.83 -138.79
REMARK 500 PHE C 41 -70.47 -95.99
REMARK 500 ALA C 124 -61.85 -108.77
REMARK 500 ILE C 137 40.65 -96.51
REMARK 500 ALA C 157 -52.16 61.95
REMARK 500 ASN C 159 -119.87 39.06
REMARK 500 SER C 247 -169.42 -72.49
REMARK 500 LEU C 250 51.92 -150.50
REMARK 500 ALA C 260 79.77 -116.67
REMARK 500 ASP C 261 18.00 -140.45
REMARK 500 LEU C 268 -61.08 -91.59
REMARK 500 ILE D 16 -34.79 -139.54
REMARK 500 PHE D 41 -67.14 -101.17
REMARK 500 VAL D 65 -12.62 -47.54
REMARK 500 ALA D 124 -68.39 -102.01
REMARK 500 ASP D 150 109.90 -40.81
REMARK 500 ALA D 157 -53.61 71.29
REMARK 500 ASN D 159 -106.75 25.79
REMARK 500 THR D 196 -79.57 -124.29
REMARK 500 LEU D 197 -123.85 -121.22
REMARK 500
REMARK 500 THIS ENTRY HAS 79 RAMACHANDRAN OUTLIERS.
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 5PP A 290
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5PP B 291
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5PP C 292
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5PP D 293
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5PP E 294
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD E 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5PP F 295
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD F 306
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BVR RELATED DB: PDB
REMARK 900 RELATED ID: 1ENZ RELATED DB: PDB
REMARK 900 RELATED ID: 1ENY RELATED DB: PDB
REMARK 900 RELATED ID: 1ZID RELATED DB: PDB
REMARK 900 RELATED ID: 1P44 RELATED DB: PDB
REMARK 900 RELATED ID: 1P45 RELATED DB: PDB
DBREF 2B36 A 1 269 UNP P0A5Y6 INHA_MYCTU 1 269
DBREF 2B36 B 1 269 UNP P0A5Y6 INHA_MYCTU 1 269
DBREF 2B36 C 1 269 UNP P0A5Y6 INHA_MYCTU 1 269
DBREF 2B36 D 1 269 UNP P0A5Y6 INHA_MYCTU 1 269
DBREF 2B36 E 1 269 UNP P0A5Y6 INHA_MYCTU 1 269
DBREF 2B36 F 1 269 UNP P0A5Y6 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
SEQRES 1 B 269 MET THR GLY LEU LEU ASP GLY LYS ARG ILE LEU VAL SER
SEQRES 2 B 269 GLY ILE ILE THR ASP SER SER ILE ALA PHE HIS ILE ALA
SEQRES 3 B 269 ARG VAL ALA GLN GLU GLN GLY ALA GLN LEU VAL LEU THR
SEQRES 4 B 269 GLY PHE ASP ARG LEU ARG LEU ILE GLN ARG ILE THR ASP
SEQRES 5 B 269 ARG LEU PRO ALA LYS ALA PRO LEU LEU GLU LEU ASP VAL
SEQRES 6 B 269 GLN ASN GLU GLU HIS LEU ALA SER LEU ALA GLY ARG VAL
SEQRES 7 B 269 THR GLU ALA ILE GLY ALA GLY ASN LYS LEU ASP GLY VAL
SEQRES 8 B 269 VAL HIS SER ILE GLY PHE MET PRO GLN THR GLY MET GLY
SEQRES 9 B 269 ILE ASN PRO PHE PHE ASP ALA PRO TYR ALA ASP VAL SER
SEQRES 10 B 269 LYS GLY ILE HIS ILE SER ALA TYR SER TYR ALA SER MET
SEQRES 11 B 269 ALA LYS ALA LEU LEU PRO ILE MET ASN PRO GLY GLY SER
SEQRES 12 B 269 ILE VAL GLY MET ASP PHE ASP PRO SER ARG ALA MET PRO
SEQRES 13 B 269 ALA TYR ASN TRP MET THR VAL ALA LYS SER ALA LEU GLU
SEQRES 14 B 269 SER VAL ASN ARG PHE VAL ALA ARG GLU ALA GLY LYS TYR
SEQRES 15 B 269 GLY VAL ARG SER ASN LEU VAL ALA ALA GLY PRO ILE ARG
SEQRES 16 B 269 THR LEU ALA MET SER ALA ILE VAL GLY GLY ALA LEU GLY
SEQRES 17 B 269 GLU GLU ALA GLY ALA GLN ILE GLN LEU LEU GLU GLU GLY
SEQRES 18 B 269 TRP ASP GLN ARG ALA PRO ILE GLY TRP ASN MET LYS ASP
SEQRES 19 B 269 ALA THR PRO VAL ALA LYS THR VAL CYS ALA LEU LEU SER
SEQRES 20 B 269 ASP TRP LEU PRO ALA THR THR GLY ASP ILE ILE TYR ALA
SEQRES 21 B 269 ASP GLY GLY ALA HIS THR GLN LEU LEU
SEQRES 1 C 269 MET THR GLY LEU LEU ASP GLY LYS ARG ILE LEU VAL SER
SEQRES 2 C 269 GLY ILE ILE THR ASP SER SER ILE ALA PHE HIS ILE ALA
SEQRES 3 C 269 ARG VAL ALA GLN GLU GLN GLY ALA GLN LEU VAL LEU THR
SEQRES 4 C 269 GLY PHE ASP ARG LEU ARG LEU ILE GLN ARG ILE THR ASP
SEQRES 5 C 269 ARG LEU PRO ALA LYS ALA PRO LEU LEU GLU LEU ASP VAL
SEQRES 6 C 269 GLN ASN GLU GLU HIS LEU ALA SER LEU ALA GLY ARG VAL
SEQRES 7 C 269 THR GLU ALA ILE GLY ALA GLY ASN LYS LEU ASP GLY VAL
SEQRES 8 C 269 VAL HIS SER ILE GLY PHE MET PRO GLN THR GLY MET GLY
SEQRES 9 C 269 ILE ASN PRO PHE PHE ASP ALA PRO TYR ALA ASP VAL SER
SEQRES 10 C 269 LYS GLY ILE HIS ILE SER ALA TYR SER TYR ALA SER MET
SEQRES 11 C 269 ALA LYS ALA LEU LEU PRO ILE MET ASN PRO GLY GLY SER
SEQRES 12 C 269 ILE VAL GLY MET ASP PHE ASP PRO SER ARG ALA MET PRO
SEQRES 13 C 269 ALA TYR ASN TRP MET THR VAL ALA LYS SER ALA LEU GLU
SEQRES 14 C 269 SER VAL ASN ARG PHE VAL ALA ARG GLU ALA GLY LYS TYR
SEQRES 15 C 269 GLY VAL ARG SER ASN LEU VAL ALA ALA GLY PRO ILE ARG
SEQRES 16 C 269 THR LEU ALA MET SER ALA ILE VAL GLY GLY ALA LEU GLY
SEQRES 17 C 269 GLU GLU ALA GLY ALA GLN ILE GLN LEU LEU GLU GLU GLY
SEQRES 18 C 269 TRP ASP GLN ARG ALA PRO ILE GLY TRP ASN MET LYS ASP
SEQRES 19 C 269 ALA THR PRO VAL ALA LYS THR VAL CYS ALA LEU LEU SER
SEQRES 20 C 269 ASP TRP LEU PRO ALA THR THR GLY ASP ILE ILE TYR ALA
SEQRES 21 C 269 ASP GLY GLY ALA HIS THR GLN LEU LEU
SEQRES 1 D 269 MET THR GLY LEU LEU ASP GLY LYS ARG ILE LEU VAL SER
SEQRES 2 D 269 GLY ILE ILE THR ASP SER SER ILE ALA PHE HIS ILE ALA
SEQRES 3 D 269 ARG VAL ALA GLN GLU GLN GLY ALA GLN LEU VAL LEU THR
SEQRES 4 D 269 GLY PHE ASP ARG LEU ARG LEU ILE GLN ARG ILE THR ASP
SEQRES 5 D 269 ARG LEU PRO ALA LYS ALA PRO LEU LEU GLU LEU ASP VAL
SEQRES 6 D 269 GLN ASN GLU GLU HIS LEU ALA SER LEU ALA GLY ARG VAL
SEQRES 7 D 269 THR GLU ALA ILE GLY ALA GLY ASN LYS LEU ASP GLY VAL
SEQRES 8 D 269 VAL HIS SER ILE GLY PHE MET PRO GLN THR GLY MET GLY
SEQRES 9 D 269 ILE ASN PRO PHE PHE ASP ALA PRO TYR ALA ASP VAL SER
SEQRES 10 D 269 LYS GLY ILE HIS ILE SER ALA TYR SER TYR ALA SER MET
SEQRES 11 D 269 ALA LYS ALA LEU LEU PRO ILE MET ASN PRO GLY GLY SER
SEQRES 12 D 269 ILE VAL GLY MET ASP PHE ASP PRO SER ARG ALA MET PRO
SEQRES 13 D 269 ALA TYR ASN TRP MET THR VAL ALA LYS SER ALA LEU GLU
SEQRES 14 D 269 SER VAL ASN ARG PHE VAL ALA ARG GLU ALA GLY LYS TYR
SEQRES 15 D 269 GLY VAL ARG SER ASN LEU VAL ALA ALA GLY PRO ILE ARG
SEQRES 16 D 269 THR LEU ALA MET SER ALA ILE VAL GLY GLY ALA LEU GLY
SEQRES 17 D 269 GLU GLU ALA GLY ALA GLN ILE GLN LEU LEU GLU GLU GLY
SEQRES 18 D 269 TRP ASP GLN ARG ALA PRO ILE GLY TRP ASN MET LYS ASP
SEQRES 19 D 269 ALA THR PRO VAL ALA LYS THR VAL CYS ALA LEU LEU SER
SEQRES 20 D 269 ASP TRP LEU PRO ALA THR THR GLY ASP ILE ILE TYR ALA
SEQRES 21 D 269 ASP GLY GLY ALA HIS THR GLN LEU LEU
SEQRES 1 E 269 MET THR GLY LEU LEU ASP GLY LYS ARG ILE LEU VAL SER
SEQRES 2 E 269 GLY ILE ILE THR ASP SER SER ILE ALA PHE HIS ILE ALA
SEQRES 3 E 269 ARG VAL ALA GLN GLU GLN GLY ALA GLN LEU VAL LEU THR
SEQRES 4 E 269 GLY PHE ASP ARG LEU ARG LEU ILE GLN ARG ILE THR ASP
SEQRES 5 E 269 ARG LEU PRO ALA LYS ALA PRO LEU LEU GLU LEU ASP VAL
SEQRES 6 E 269 GLN ASN GLU GLU HIS LEU ALA SER LEU ALA GLY ARG VAL
SEQRES 7 E 269 THR GLU ALA ILE GLY ALA GLY ASN LYS LEU ASP GLY VAL
SEQRES 8 E 269 VAL HIS SER ILE GLY PHE MET PRO GLN THR GLY MET GLY
SEQRES 9 E 269 ILE ASN PRO PHE PHE ASP ALA PRO TYR ALA ASP VAL SER
SEQRES 10 E 269 LYS GLY ILE HIS ILE SER ALA TYR SER TYR ALA SER MET
SEQRES 11 E 269 ALA LYS ALA LEU LEU PRO ILE MET ASN PRO GLY GLY SER
SEQRES 12 E 269 ILE VAL GLY MET ASP PHE ASP PRO SER ARG ALA MET PRO
SEQRES 13 E 269 ALA TYR ASN TRP MET THR VAL ALA LYS SER ALA LEU GLU
SEQRES 14 E 269 SER VAL ASN ARG PHE VAL ALA ARG GLU ALA GLY LYS TYR
SEQRES 15 E 269 GLY VAL ARG SER ASN LEU VAL ALA ALA GLY PRO ILE ARG
SEQRES 16 E 269 THR LEU ALA MET SER ALA ILE VAL GLY GLY ALA LEU GLY
SEQRES 17 E 269 GLU GLU ALA GLY ALA GLN ILE GLN LEU LEU GLU GLU GLY
SEQRES 18 E 269 TRP ASP GLN ARG ALA PRO ILE GLY TRP ASN MET LYS ASP
SEQRES 19 E 269 ALA THR PRO VAL ALA LYS THR VAL CYS ALA LEU LEU SER
SEQRES 20 E 269 ASP TRP LEU PRO ALA THR THR GLY ASP ILE ILE TYR ALA
SEQRES 21 E 269 ASP GLY GLY ALA HIS THR GLN LEU LEU
SEQRES 1 F 269 MET THR GLY LEU LEU ASP GLY LYS ARG ILE LEU VAL SER
SEQRES 2 F 269 GLY ILE ILE THR ASP SER SER ILE ALA PHE HIS ILE ALA
SEQRES 3 F 269 ARG VAL ALA GLN GLU GLN GLY ALA GLN LEU VAL LEU THR
SEQRES 4 F 269 GLY PHE ASP ARG LEU ARG LEU ILE GLN ARG ILE THR ASP
SEQRES 5 F 269 ARG LEU PRO ALA LYS ALA PRO LEU LEU GLU LEU ASP VAL
SEQRES 6 F 269 GLN ASN GLU GLU HIS LEU ALA SER LEU ALA GLY ARG VAL
SEQRES 7 F 269 THR GLU ALA ILE GLY ALA GLY ASN LYS LEU ASP GLY VAL
SEQRES 8 F 269 VAL HIS SER ILE GLY PHE MET PRO GLN THR GLY MET GLY
SEQRES 9 F 269 ILE ASN PRO PHE PHE ASP ALA PRO TYR ALA ASP VAL SER
SEQRES 10 F 269 LYS GLY ILE HIS ILE SER ALA TYR SER TYR ALA SER MET
SEQRES 11 F 269 ALA LYS ALA LEU LEU PRO ILE MET ASN PRO GLY GLY SER
SEQRES 12 F 269 ILE VAL GLY MET ASP PHE ASP PRO SER ARG ALA MET PRO
SEQRES 13 F 269 ALA TYR ASN TRP MET THR VAL ALA LYS SER ALA LEU GLU
SEQRES 14 F 269 SER VAL ASN ARG PHE VAL ALA ARG GLU ALA GLY LYS TYR
SEQRES 15 F 269 GLY VAL ARG SER ASN LEU VAL ALA ALA GLY PRO ILE ARG
SEQRES 16 F 269 THR LEU ALA MET SER ALA ILE VAL GLY GLY ALA LEU GLY
SEQRES 17 F 269 GLU GLU ALA GLY ALA GLN ILE GLN LEU LEU GLU GLU GLY
SEQRES 18 F 269 TRP ASP GLN ARG ALA PRO ILE GLY TRP ASN MET LYS ASP
SEQRES 19 F 269 ALA THR PRO VAL ALA LYS THR VAL CYS ALA LEU LEU SER
SEQRES 20 F 269 ASP TRP LEU PRO ALA THR THR GLY ASP ILE ILE TYR ALA
SEQRES 21 F 269 ASP GLY GLY ALA HIS THR GLN LEU LEU
HET 5PP A 290 19
HET NAD A 301 44
HET 5PP B 291 19
HET NAD B 302 44
HET 5PP C 292 19
HET NAD C 303 44
HET 5PP D 293 19
HET NAD D 304 44
HET 5PP E 294 19
HET NAD E 305 44
HET 5PP F 295 19
HET NAD F 306 44
HETNAM 5PP 5-PENTYL-2-PHENOXYPHENOL
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
FORMUL 7 5PP 6(C17 H20 O2)
FORMUL 8 NAD 6(C21 H27 N7 O14 P2)
HELIX 1 1 SER A 20 GLN A 32 1 13
HELIX 2 2 ARG A 43 ASP A 52 1 10
HELIX 3 3 ASN A 67 GLY A 83 1 17
HELIX 4 4 PRO A 99 MET A 103 5 5
HELIX 5 5 PRO A 107 ALA A 111 5 5
HELIX 6 6 PRO A 112 ALA A 124 1 13
HELIX 7 7 ALA A 124 LEU A 135 1 12
HELIX 8 8 TYR A 158 LYS A 181 1 24
HELIX 9 9 GLN A 214 ALA A 226 1 13
HELIX 10 10 ALA A 235 SER A 247 1 13
HELIX 11 11 GLY A 263 GLN A 267 5 5
HELIX 12 12 SER B 20 GLN B 32 1 13
HELIX 13 13 ARG B 43 ASP B 52 1 10
HELIX 14 14 ASN B 67 GLY B 83 1 17
HELIX 15 15 PRO B 99 MET B 103 5 5
HELIX 16 16 PRO B 107 ALA B 111 5 5
HELIX 17 17 PRO B 112 ALA B 124 1 13
HELIX 18 18 ALA B 124 LEU B 135 1 12
HELIX 19 19 TYR B 158 LYS B 181 1 24
HELIX 20 20 GLY B 208 ALA B 226 1 19
HELIX 21 21 ALA B 235 SER B 247 1 13
HELIX 22 22 GLY B 263 GLN B 267 5 5
HELIX 23 23 SER C 20 GLN C 32 1 13
HELIX 24 24 ARG C 43 ASP C 52 1 10
HELIX 25 25 ASN C 67 GLY C 83 1 17
HELIX 26 26 PRO C 99 MET C 103 5 5
HELIX 27 27 PRO C 107 ALA C 111 5 5
HELIX 28 28 PRO C 112 ALA C 124 1 13
HELIX 29 29 ALA C 124 LEU C 135 1 12
HELIX 30 30 TYR C 158 LYS C 181 1 24
HELIX 31 31 LEU C 217 ALA C 226 1 10
HELIX 32 32 ALA C 235 SER C 247 1 13
HELIX 33 33 GLY C 263 GLN C 267 5 5
HELIX 34 34 SER D 20 GLN D 32 1 13
HELIX 35 35 ARG D 43 ASP D 52 1 10
HELIX 36 36 ASN D 67 GLY D 83 1 17
HELIX 37 37 PRO D 99 MET D 103 5 5
HELIX 38 38 PRO D 107 ALA D 111 5 5
HELIX 39 39 PRO D 112 ALA D 124 1 13
HELIX 40 40 TYR D 125 LEU D 135 1 11
HELIX 41 41 TYR D 158 LYS D 181 1 24
HELIX 42 42 GLU D 220 ALA D 226 1 7
HELIX 43 43 ALA D 235 SER D 247 1 13
HELIX 44 44 GLY D 263 GLN D 267 5 5
HELIX 45 45 SER E 20 GLN E 32 1 13
HELIX 46 46 ARG E 43 ASP E 52 1 10
HELIX 47 47 ASN E 67 GLY E 83 1 17
HELIX 48 48 PRO E 99 MET E 103 5 5
HELIX 49 49 PRO E 107 ALA E 111 5 5
HELIX 50 50 PRO E 112 ALA E 124 1 13
HELIX 51 51 ALA E 124 LEU E 135 1 12
HELIX 52 52 TYR E 158 LYS E 181 1 24
HELIX 53 53 ALA E 211 ALA E 226 1 16
HELIX 54 54 ALA E 235 SER E 247 1 13
HELIX 55 55 GLY E 263 GLN E 267 5 5
HELIX 56 56 SER F 20 GLN F 32 1 13
HELIX 57 57 ARG F 43 ASP F 52 1 10
HELIX 58 58 ASN F 67 GLY F 83 1 17
HELIX 59 59 PRO F 99 MET F 103 5 5
HELIX 60 60 PRO F 107 ALA F 111 5 5
HELIX 61 61 PRO F 112 ALA F 124 1 13
HELIX 62 62 ALA F 124 LEU F 135 1 12
HELIX 63 63 TYR F 158 LYS F 181 1 24
HELIX 64 64 LEU F 217 ALA F 226 1 10
HELIX 65 65 ALA F 235 SER F 247 1 13
HELIX 66 66 GLY F 263 GLN F 267 5 5
SHEET 1 A 7 LEU A 60 GLU A 62 0
SHEET 2 A 7 GLN A 35 GLY A 40 1 N GLY A 40 O LEU A 61
SHEET 3 A 7 ARG A 9 VAL A 12 1 N VAL A 12 O VAL A 37
SHEET 4 A 7 LEU A 88 HIS A 93 1 O ASP A 89 N ARG A 9
SHEET 5 A 7 MET A 138 ASP A 148 1 O ASN A 139 N LEU A 88
SHEET 6 A 7 ARG A 185 ALA A 191 1 O VAL A 189 N GLY A 146
SHEET 7 A 7 ASP A 256 ALA A 260 1 O ILE A 258 N LEU A 188
SHEET 1 B 7 LEU B 60 GLU B 62 0
SHEET 2 B 7 GLN B 35 GLY B 40 1 N GLY B 40 O LEU B 61
SHEET 3 B 7 ARG B 9 SER B 13 1 N ILE B 10 O GLN B 35
SHEET 4 B 7 LEU B 88 HIS B 93 1 O ASP B 89 N ARG B 9
SHEET 5 B 7 MET B 138 ASP B 148 1 O ASN B 139 N LEU B 88
SHEET 6 B 7 ARG B 185 ALA B 191 1 O VAL B 189 N GLY B 146
SHEET 7 B 7 ASP B 256 ALA B 260 1 O ILE B 258 N LEU B 188
SHEET 1 C 7 LEU C 60 GLU C 62 0
SHEET 2 C 7 GLN C 35 GLY C 40 1 N LEU C 38 O LEU C 61
SHEET 3 C 7 ARG C 9 VAL C 12 1 N ILE C 10 O GLN C 35
SHEET 4 C 7 LEU C 88 HIS C 93 1 O ASP C 89 N ARG C 9
SHEET 5 C 7 MET C 138 ASP C 148 1 O ASN C 139 N LEU C 88
SHEET 6 C 7 ARG C 185 ALA C 191 1 O VAL C 189 N GLY C 146
SHEET 7 C 7 ASP C 256 ALA C 260 1 O ILE C 258 N ALA C 190
SHEET 1 D 7 LEU D 60 GLU D 62 0
SHEET 2 D 7 GLN D 35 GLY D 40 1 N GLY D 40 O LEU D 61
SHEET 3 D 7 ARG D 9 VAL D 12 1 N VAL D 12 O VAL D 37
SHEET 4 D 7 LEU D 88 HIS D 93 1 O VAL D 92 N LEU D 11
SHEET 5 D 7 MET D 138 ASP D 148 1 O ASN D 139 N LEU D 88
SHEET 6 D 7 ARG D 185 ALA D 191 1 O VAL D 189 N ASP D 148
SHEET 7 D 7 ASP D 256 ALA D 260 1 O ILE D 258 N LEU D 188
SHEET 1 E 7 LEU E 60 GLU E 62 0
SHEET 2 E 7 GLN E 35 GLY E 40 1 N LEU E 38 O LEU E 61
SHEET 3 E 7 ARG E 9 VAL E 12 1 N ILE E 10 O GLN E 35
SHEET 4 E 7 LEU E 88 HIS E 93 1 O ASP E 89 N ARG E 9
SHEET 5 E 7 MET E 138 ASP E 148 1 O ASN E 139 N LEU E 88
SHEET 6 E 7 ARG E 185 ALA E 191 1 O VAL E 189 N ASP E 148
SHEET 7 E 7 ASP E 256 ALA E 260 1 O ILE E 258 N LEU E 188
SHEET 1 F 7 LEU F 60 GLU F 62 0
SHEET 2 F 7 GLN F 35 GLY F 40 1 N LEU F 38 O LEU F 61
SHEET 3 F 7 ARG F 9 VAL F 12 1 N VAL F 12 O VAL F 37
SHEET 4 F 7 LEU F 88 HIS F 93 1 O ASP F 89 N ARG F 9
SHEET 5 F 7 MET F 138 ASP F 148 1 O ASN F 139 N LEU F 88
SHEET 6 F 7 VAL F 184 ALA F 191 1 O VAL F 189 N ASP F 148
SHEET 7 F 7 ASP F 256 ALA F 260 1 O ILE F 258 N LEU F 188
SITE 1 AC1 5 GLY A 96 PHE A 149 TYR A 158 MET A 199
SITE 2 AC1 5 NAD A 301
SITE 1 AC2 22 GLY A 14 ILE A 16 SER A 20 ILE A 21
SITE 2 AC2 22 PHE A 41 LEU A 63 ASP A 64 VAL A 65
SITE 3 AC2 22 SER A 94 ILE A 95 GLY A 96 ILE A 122
SITE 4 AC2 22 MET A 147 ASP A 148 PHE A 149 LYS A 165
SITE 5 AC2 22 ALA A 191 GLY A 192 PRO A 193 ILE A 194
SITE 6 AC2 22 THR A 196 5PP A 290
SITE 1 AC3 5 GLY B 96 PHE B 149 TYR B 158 MET B 161
SITE 2 AC3 5 NAD B 302
SITE 1 AC4 21 GLY B 14 ILE B 15 ILE B 16 SER B 20
SITE 2 AC4 21 ILE B 21 PHE B 41 LEU B 63 ASP B 64
SITE 3 AC4 21 VAL B 65 SER B 94 ILE B 95 GLY B 96
SITE 4 AC4 21 ILE B 122 MET B 147 ASP B 148 LYS B 165
SITE 5 AC4 21 ALA B 191 PRO B 193 ILE B 194 THR B 196
SITE 6 AC4 21 5PP B 291
SITE 1 AC5 6 GLY C 96 PHE C 97 MET C 103 PHE C 149
SITE 2 AC5 6 TYR C 158 NAD C 303
SITE 1 AC6 22 GLY C 14 ILE C 15 ILE C 16 SER C 20
SITE 2 AC6 22 ILE C 21 PHE C 41 LEU C 63 ASP C 64
SITE 3 AC6 22 VAL C 65 SER C 94 ILE C 95 GLY C 96
SITE 4 AC6 22 ILE C 122 MET C 147 ASP C 148 LYS C 165
SITE 5 AC6 22 ALA C 191 GLY C 192 PRO C 193 ILE C 194
SITE 6 AC6 22 THR C 196 5PP C 292
SITE 1 AC7 5 MET D 103 PHE D 149 TYR D 158 MET D 199
SITE 2 AC7 5 NAD D 304
SITE 1 AC8 23 GLY D 14 ILE D 15 ILE D 16 SER D 20
SITE 2 AC8 23 ILE D 21 PHE D 41 LEU D 63 ASP D 64
SITE 3 AC8 23 VAL D 65 SER D 94 ILE D 95 GLY D 96
SITE 4 AC8 23 ILE D 122 MET D 147 ASP D 148 PHE D 149
SITE 5 AC8 23 LYS D 165 ALA D 191 PRO D 193 ILE D 194
SITE 6 AC8 23 THR D 196 LEU D 197 5PP D 293
SITE 1 AC9 3 TYR E 158 ILE E 215 NAD E 305
SITE 1 BC1 20 GLY E 14 ILE E 16 SER E 20 ILE E 21
SITE 2 BC1 20 PHE E 41 LEU E 63 ASP E 64 VAL E 65
SITE 3 BC1 20 SER E 94 ILE E 95 GLY E 96 ILE E 122
SITE 4 BC1 20 MET E 147 ASP E 148 PHE E 149 LYS E 165
SITE 5 BC1 20 GLY E 192 ILE E 194 THR E 196 5PP E 294
SITE 1 BC2 5 PHE F 97 MET F 103 TYR F 158 MET F 161
SITE 2 BC2 5 NAD F 306
SITE 1 BC3 20 GLY F 14 ILE F 15 ILE F 16 SER F 20
SITE 2 BC3 20 ILE F 21 PHE F 41 LEU F 63 ASP F 64
SITE 3 BC3 20 VAL F 65 SER F 94 ILE F 95 GLY F 96
SITE 4 BC3 20 ILE F 122 MET F 147 ASP F 148 PHE F 149
SITE 5 BC3 20 LYS F 165 ILE F 194 THR F 196 5PP F 295
CRYST1 99.955 81.827 188.656 90.00 95.69 90.00 C 1 2 1 24
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 0.010005 0.000000 0.000997 0.00000
SCALE2 0.000000 0.012221 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005327 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
