HEADER OXIDOREDUCTASE 22-MAR-14 4CV3
TITLE CRYSTAL STRUCTURE OF E. COLI FABI IN COMPLEX WITH NADH AND PT166
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADH];
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ENOYL-ACP REDUCTASE;
COMPND 5 EC: 1.3.1.9;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 469008;
SOURCE 4 STRAIN: BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET23B
KEYWDS SHORT-CHAIN DEHYDROGENASE/REDUCTASE SUPERFAMILY, FATTY ACID
KEYWDS 2 BIOSYNTHESIS, LIPID SYNTHESIS, ECFABI, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.ELTSCHKNER,J.SCHIEBEL,A.CHANG,S.SHAH,P.J.TONGE,C.KISKER
REVDAT 4 20-DEC-23 4CV3 1 REMARK
REVDAT 3 13-AUG-14 4CV3 1 JRNL
REVDAT 2 30-APR-14 4CV3 1 JRNL
REVDAT 1 16-APR-14 4CV3 0
JRNL AUTH J.SCHIEBEL,A.CHANG,S.SHAH,Y.LU,L.LIU,P.PAN,M.W.HIRSCHBECK,
JRNL AUTH 2 M.TAREILUS,S.ELTSCHKNER,W.YU,J.E.CUMMINGS,S.E.KNUDSON,
JRNL AUTH 3 G.R.BOMMINENI,S.G.WALKER,R.A.SLAYDEN,C.A.SOTRIFFER,
JRNL AUTH 4 P.J.TONGE,C.KISKER
JRNL TITL RATIONAL DESIGN OF BROAD SPECTRUM ANTIBACTERIAL ACTIVITY
JRNL TITL 2 BASED ON A CLINICALLY RELEVANT ENOYL-ACYL CARRIER PROTEIN
JRNL TITL 3 (ACP) REDUCTASE INHIBITOR.
JRNL REF J.BIOL.CHEM. V. 289 15987 2014
JRNL REFN ISSN 0021-9258
JRNL PMID 24739388
JRNL DOI 10.1074/JBC.M113.532804
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 43820
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2338
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3092
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE SET COUNT : 173
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3536
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 132
REMARK 3 SOLVENT ATOMS : 246
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : 0.08000
REMARK 3 B33 (A**2) : -0.13000
REMARK 3 B12 (A**2) : 0.04000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.131
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.127
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.090
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.621
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3768 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5115 ; 1.774 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 484 ; 7.275 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 151 ;35.382 ;24.172
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 587 ;14.146 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;15.616 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 574 ; 0.109 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3067 ; 0.015 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
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): 2379 ; 1.732 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3781 ; 2.586 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1389 ; 4.161 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1329 ; 6.145 ; 4.500
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 : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 147
REMARK 3 ORIGIN FOR THE GROUP (A): -20.5812 30.2118 -13.9927
REMARK 3 T TENSOR
REMARK 3 T11: 0.0165 T22: 0.1583
REMARK 3 T33: 0.0826 T12: 0.0145
REMARK 3 T13: 0.0004 T23: -0.0511
REMARK 3 L TENSOR
REMARK 3 L11: 0.4277 L22: 0.1154
REMARK 3 L33: 0.3690 L12: -0.0467
REMARK 3 L13: 0.1938 L23: 0.1474
REMARK 3 S TENSOR
REMARK 3 S11: 0.0050 S12: -0.0289 S13: 0.0126
REMARK 3 S21: -0.0045 S22: 0.0575 S23: -0.0214
REMARK 3 S31: -0.0062 S32: 0.1115 S33: -0.0625
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 148 A 192
REMARK 3 ORIGIN FOR THE GROUP (A): -33.5074 29.7573 -20.8187
REMARK 3 T TENSOR
REMARK 3 T11: 0.0505 T22: 0.1283
REMARK 3 T33: 0.0798 T12: 0.0335
REMARK 3 T13: -0.0075 T23: -0.0237
REMARK 3 L TENSOR
REMARK 3 L11: 0.4085 L22: 0.2464
REMARK 3 L33: 0.6258 L12: 0.2369
REMARK 3 L13: -0.1465 L23: 0.1562
REMARK 3 S TENSOR
REMARK 3 S11: 0.0056 S12: -0.0542 S13: 0.0501
REMARK 3 S21: -0.0236 S22: -0.0113 S23: 0.0447
REMARK 3 S31: -0.0200 S32: 0.0551 S33: 0.0057
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 210 A 223
REMARK 3 ORIGIN FOR THE GROUP (A): -36.1388 10.2008 -13.1766
REMARK 3 T TENSOR
REMARK 3 T11: 0.1213 T22: 0.0907
REMARK 3 T33: 0.0294 T12: 0.0245
REMARK 3 T13: 0.0286 T23: 0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 7.4063 L22: 1.3935
REMARK 3 L33: 2.3473 L12: 0.9144
REMARK 3 L13: 1.5336 L23: 0.5931
REMARK 3 S TENSOR
REMARK 3 S11: -0.0250 S12: -0.5510 S13: -0.2162
REMARK 3 S21: 0.2645 S22: -0.0848 S23: 0.0968
REMARK 3 S31: 0.2881 S32: -0.0674 S33: 0.1097
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 224 A 257
REMARK 3 ORIGIN FOR THE GROUP (A): -31.5915 18.1272 -23.8174
REMARK 3 T TENSOR
REMARK 3 T11: 0.0455 T22: 0.1232
REMARK 3 T33: 0.1099 T12: 0.0523
REMARK 3 T13: -0.0058 T23: -0.0405
REMARK 3 L TENSOR
REMARK 3 L11: 0.1953 L22: 0.6092
REMARK 3 L33: 0.6573 L12: 0.3349
REMARK 3 L13: 0.3206 L23: 0.6163
REMARK 3 S TENSOR
REMARK 3 S11: 0.0323 S12: -0.0107 S13: 0.0443
REMARK 3 S21: 0.0533 S22: 0.0059 S23: 0.0181
REMARK 3 S31: 0.0666 S32: 0.0398 S33: -0.0382
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 147
REMARK 3 ORIGIN FOR THE GROUP (A): -51.4756 50.6117 -17.4572
REMARK 3 T TENSOR
REMARK 3 T11: 0.1258 T22: 0.0926
REMARK 3 T33: 0.1074 T12: 0.0794
REMARK 3 T13: -0.0506 T23: -0.0507
REMARK 3 L TENSOR
REMARK 3 L11: 0.5152 L22: 0.5563
REMARK 3 L33: 0.4482 L12: -0.3769
REMARK 3 L13: 0.0007 L23: 0.3489
REMARK 3 S TENSOR
REMARK 3 S11: -0.0386 S12: -0.0629 S13: 0.0367
REMARK 3 S21: -0.1538 S22: -0.0476 S23: 0.0192
REMARK 3 S31: -0.2293 S32: -0.1117 S33: 0.0862
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 148 B 192
REMARK 3 ORIGIN FOR THE GROUP (A): -46.0090 37.6233 -21.6431
REMARK 3 T TENSOR
REMARK 3 T11: 0.0699 T22: 0.1169
REMARK 3 T33: 0.0992 T12: 0.0470
REMARK 3 T13: -0.0143 T23: -0.0359
REMARK 3 L TENSOR
REMARK 3 L11: 0.5971 L22: 0.0574
REMARK 3 L33: 0.2458 L12: 0.0460
REMARK 3 L13: -0.0865 L23: 0.0793
REMARK 3 S TENSOR
REMARK 3 S11: -0.0216 S12: -0.0645 S13: 0.0108
REMARK 3 S21: -0.0585 S22: -0.0684 S23: 0.0256
REMARK 3 S31: -0.1014 S32: -0.0397 S33: 0.0900
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 210 B 223
REMARK 3 ORIGIN FOR THE GROUP (A): -52.3590 41.8944 -41.1495
REMARK 3 T TENSOR
REMARK 3 T11: 0.1833 T22: 0.0608
REMARK 3 T33: 0.1357 T12: 0.0603
REMARK 3 T13: -0.0822 T23: -0.0398
REMARK 3 L TENSOR
REMARK 3 L11: 2.2552 L22: 5.4509
REMARK 3 L33: 4.6333 L12: -0.9557
REMARK 3 L13: -1.9228 L23: 4.6799
REMARK 3 S TENSOR
REMARK 3 S11: 0.1424 S12: 0.2878 S13: 0.0150
REMARK 3 S21: -0.6471 S22: -0.0696 S23: -0.1829
REMARK 3 S31: -0.6218 S32: -0.2366 S33: -0.0728
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 224 B 257
REMARK 3 ORIGIN FOR THE GROUP (A): -55.2518 36.0472 -29.2533
REMARK 3 T TENSOR
REMARK 3 T11: 0.0846 T22: 0.1095
REMARK 3 T33: 0.1143 T12: 0.0727
REMARK 3 T13: -0.0346 T23: -0.0451
REMARK 3 L TENSOR
REMARK 3 L11: 0.3867 L22: 0.7107
REMARK 3 L33: 0.4771 L12: 0.2586
REMARK 3 L13: 0.3155 L23: 0.5530
REMARK 3 S TENSOR
REMARK 3 S11: -0.0353 S12: -0.0785 S13: 0.0019
REMARK 3 S21: -0.1691 S22: -0.0497 S23: 0.0934
REMARK 3 S31: -0.1233 S32: -0.0703 S33: 0.0850
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 : 1.40
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. DUE TO VERY WEAK ELECTRON DENSITY, THE LOOP REGION
REMARK 3 193-209 WAS NOT MODELED
REMARK 4
REMARK 4 4CV3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-MAR-14.
REMARK 100 THE DEPOSITION ID IS D_1290057034.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0644
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46243
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 47.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.65000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1QSG
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA-CITRATE PH 5.6, 0.2 M NH4AC,
REMARK 280 10% PEG 8000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 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+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 110.05000
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 220.10000
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 165.07500
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 275.12500
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 55.02500
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 110.05000
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 220.10000
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 275.12500
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 165.07500
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 55.02500
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: 21360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.5 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 350 BIOMT1 2 0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -55.02500
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 B2098 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 ARG A 193
REMARK 465 THR A 194
REMARK 465 LEU A 195
REMARK 465 ALA A 196
REMARK 465 ALA A 197
REMARK 465 SER A 198
REMARK 465 GLY A 199
REMARK 465 ILE A 200
REMARK 465 LYS A 201
REMARK 465 ASP A 202
REMARK 465 PHE A 203
REMARK 465 ARG A 204
REMARK 465 LYS A 205
REMARK 465 MET A 206
REMARK 465 LEU A 207
REMARK 465 ALA A 208
REMARK 465 HIS A 209
REMARK 465 GLU A 258
REMARK 465 LEU A 259
REMARK 465 GLU A 260
REMARK 465 LEU A 261
REMARK 465 LYS A 262
REMARK 465 LEU A 263
REMARK 465 GLU A 264
REMARK 465 HIS A 265
REMARK 465 HIS A 266
REMARK 465 HIS A 267
REMARK 465 HIS A 268
REMARK 465 HIS A 269
REMARK 465 HIS A 270
REMARK 465 MET B 1
REMARK 465 ARG B 193
REMARK 465 THR B 194
REMARK 465 LEU B 195
REMARK 465 ALA B 196
REMARK 465 ALA B 197
REMARK 465 SER B 198
REMARK 465 GLY B 199
REMARK 465 ILE B 200
REMARK 465 LYS B 201
REMARK 465 ASP B 202
REMARK 465 PHE B 203
REMARK 465 ARG B 204
REMARK 465 LYS B 205
REMARK 465 MET B 206
REMARK 465 LEU B 207
REMARK 465 ALA B 208
REMARK 465 HIS B 209
REMARK 465 GLU B 258
REMARK 465 LEU B 259
REMARK 465 GLU B 260
REMARK 465 LEU B 261
REMARK 465 LYS B 262
REMARK 465 LEU B 263
REMARK 465 GLU B 264
REMARK 465 HIS B 265
REMARK 465 HIS B 266
REMARK 465 HIS B 267
REMARK 465 HIS B 268
REMARK 465 HIS B 269
REMARK 465 HIS B 270
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 98 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 MET A 159 CG - SD - CE ANGL. DEV. = -18.6 DEGREES
REMARK 500 ARG B 171 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
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 ASN A 155 -27.57 67.58
REMARK 500 ASN A 157 -126.69 48.44
REMARK 500 VAL A 247 70.62 -110.06
REMARK 500 MET A 256 42.86 77.75
REMARK 500 ASP B 103 124.33 -36.12
REMARK 500 ASN B 155 -36.93 77.04
REMARK 500 ASN B 157 -129.07 51.37
REMARK 500 VAL B 247 64.35 -112.95
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 VT4 A 1258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VT4 B 1258
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI A 1259
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAI B 1259
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CUZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S. AUREUS FABI IN COMPLEX WITH NADPH AND PT173
REMARK 900 RELATED ID: 4CV0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S. AUREUS FABI IN COMPLEX WITH NADPH AND
REMARK 900 CG400549 (SMALL UNIT CELL)
REMARK 900 RELATED ID: 4CV1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF S. AUREUS FABI IN COMPLEX WITH NADPH AND
REMARK 900 CG400549
REMARK 900 RELATED ID: 4CV2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E. COLI FABI IN COMPLEX WITH NADH AND CG400549
DBREF 4CV3 A 1 262 UNP C6EFU4 C6EFU4_ECOBD 1 262
DBREF 4CV3 B 1 262 UNP C6EFU4 C6EFU4_ECOBD 1 262
SEQADV 4CV3 LEU A 263 UNP C6EFU4 EXPRESSION TAG
SEQADV 4CV3 GLU A 264 UNP C6EFU4 EXPRESSION TAG
SEQADV 4CV3 HIS A 265 UNP C6EFU4 EXPRESSION TAG
SEQADV 4CV3 HIS A 266 UNP C6EFU4 EXPRESSION TAG
SEQADV 4CV3 HIS A 267 UNP C6EFU4 EXPRESSION TAG
SEQADV 4CV3 HIS A 268 UNP C6EFU4 EXPRESSION TAG
SEQADV 4CV3 HIS A 269 UNP C6EFU4 EXPRESSION TAG
SEQADV 4CV3 HIS A 270 UNP C6EFU4 EXPRESSION TAG
SEQADV 4CV3 LEU B 263 UNP C6EFU4 EXPRESSION TAG
SEQADV 4CV3 GLU B 264 UNP C6EFU4 EXPRESSION TAG
SEQADV 4CV3 HIS B 265 UNP C6EFU4 EXPRESSION TAG
SEQADV 4CV3 HIS B 266 UNP C6EFU4 EXPRESSION TAG
SEQADV 4CV3 HIS B 267 UNP C6EFU4 EXPRESSION TAG
SEQADV 4CV3 HIS B 268 UNP C6EFU4 EXPRESSION TAG
SEQADV 4CV3 HIS B 269 UNP C6EFU4 EXPRESSION TAG
SEQADV 4CV3 HIS B 270 UNP C6EFU4 EXPRESSION TAG
SEQRES 1 A 270 MET GLY PHE LEU SER GLY LYS ARG ILE LEU VAL THR GLY
SEQRES 2 A 270 VAL ALA SER LYS LEU SER ILE ALA TYR GLY ILE ALA GLN
SEQRES 3 A 270 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 A 270 GLN ASN ASP LYS LEU LYS GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 A 270 ALA GLN LEU GLY SER ASP ILE VAL LEU GLN CYS ASP VAL
SEQRES 6 A 270 ALA GLU ASP ALA SER ILE ASP THR MET PHE ALA GLU LEU
SEQRES 7 A 270 GLY LYS VAL TRP PRO LYS PHE ASP GLY PHE VAL HIS SER
SEQRES 8 A 270 ILE GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY ASP TYR
SEQRES 9 A 270 VAL ASN ALA VAL THR ARG GLU GLY PHE LYS ILE ALA HIS
SEQRES 10 A 270 ASP ILE SER SER TYR SER PHE VAL ALA MET ALA LYS ALA
SEQRES 11 A 270 CYS ARG SER MET LEU ASN PRO GLY SER ALA LEU LEU THR
SEQRES 12 A 270 LEU SER TYR LEU GLY ALA GLU ARG ALA ILE PRO ASN TYR
SEQRES 13 A 270 ASN VAL MET GLY LEU ALA LYS ALA SER LEU GLU ALA ASN
SEQRES 14 A 270 VAL ARG TYR MET ALA ASN ALA MET GLY PRO GLU GLY VAL
SEQRES 15 A 270 ARG VAL ASN ALA ILE SER ALA GLY PRO ILE ARG THR LEU
SEQRES 16 A 270 ALA ALA SER GLY ILE LYS ASP PHE ARG LYS MET LEU ALA
SEQRES 17 A 270 HIS CYS GLU ALA VAL THR PRO ILE ARG ARG THR VAL THR
SEQRES 18 A 270 ILE GLU ASP VAL GLY ASN SER ALA ALA PHE LEU CYS SER
SEQRES 19 A 270 ASP LEU SER ALA GLY ILE SER GLY GLU VAL VAL HIS VAL
SEQRES 20 A 270 ASP GLY GLY PHE SER ILE ALA ALA MET ASN GLU LEU GLU
SEQRES 21 A 270 LEU LYS LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 270 MET GLY PHE LEU SER GLY LYS ARG ILE LEU VAL THR GLY
SEQRES 2 B 270 VAL ALA SER LYS LEU SER ILE ALA TYR GLY ILE ALA GLN
SEQRES 3 B 270 ALA MET HIS ARG GLU GLY ALA GLU LEU ALA PHE THR TYR
SEQRES 4 B 270 GLN ASN ASP LYS LEU LYS GLY ARG VAL GLU GLU PHE ALA
SEQRES 5 B 270 ALA GLN LEU GLY SER ASP ILE VAL LEU GLN CYS ASP VAL
SEQRES 6 B 270 ALA GLU ASP ALA SER ILE ASP THR MET PHE ALA GLU LEU
SEQRES 7 B 270 GLY LYS VAL TRP PRO LYS PHE ASP GLY PHE VAL HIS SER
SEQRES 8 B 270 ILE GLY PHE ALA PRO GLY ASP GLN LEU ASP GLY ASP TYR
SEQRES 9 B 270 VAL ASN ALA VAL THR ARG GLU GLY PHE LYS ILE ALA HIS
SEQRES 10 B 270 ASP ILE SER SER TYR SER PHE VAL ALA MET ALA LYS ALA
SEQRES 11 B 270 CYS ARG SER MET LEU ASN PRO GLY SER ALA LEU LEU THR
SEQRES 12 B 270 LEU SER TYR LEU GLY ALA GLU ARG ALA ILE PRO ASN TYR
SEQRES 13 B 270 ASN VAL MET GLY LEU ALA LYS ALA SER LEU GLU ALA ASN
SEQRES 14 B 270 VAL ARG TYR MET ALA ASN ALA MET GLY PRO GLU GLY VAL
SEQRES 15 B 270 ARG VAL ASN ALA ILE SER ALA GLY PRO ILE ARG THR LEU
SEQRES 16 B 270 ALA ALA SER GLY ILE LYS ASP PHE ARG LYS MET LEU ALA
SEQRES 17 B 270 HIS CYS GLU ALA VAL THR PRO ILE ARG ARG THR VAL THR
SEQRES 18 B 270 ILE GLU ASP VAL GLY ASN SER ALA ALA PHE LEU CYS SER
SEQRES 19 B 270 ASP LEU SER ALA GLY ILE SER GLY GLU VAL VAL HIS VAL
SEQRES 20 B 270 ASP GLY GLY PHE SER ILE ALA ALA MET ASN GLU LEU GLU
SEQRES 21 B 270 LEU LYS LEU GLU HIS HIS HIS HIS HIS HIS
HET VT4 A1258 22
HET NAI A1259 44
HET VT4 B1258 22
HET NAI B1259 44
HETNAM VT4 2-HEXYL-1-METHYL-5-(2-METHYLPHENOXY)PYRIDIN-4(1H)-ONE
HETNAM NAI 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE
HETSYN NAI NADH
FORMUL 3 VT4 2(C19 H25 N O2)
FORMUL 4 NAI 2(C21 H29 N7 O14 P2)
FORMUL 7 HOH *246(H2 O)
HELIX 1 1 SER A 19 GLU A 31 1 13
HELIX 2 2 LEU A 44 LEU A 55 1 12
HELIX 3 3 GLU A 67 TRP A 82 1 16
HELIX 4 4 PRO A 96 ASP A 101 5 6
HELIX 5 5 ASP A 103 VAL A 108 1 6
HELIX 6 6 THR A 109 SER A 121 1 13
HELIX 7 7 SER A 121 ARG A 132 1 12
HELIX 8 8 TYR A 146 GLU A 150 5 5
HELIX 9 9 ASN A 157 GLY A 178 1 22
HELIX 10 10 THR A 221 CYS A 233 1 13
HELIX 11 11 SER A 234 ALA A 238 5 5
HELIX 12 12 GLY A 250 ALA A 254 5 5
HELIX 13 13 SER B 19 GLU B 31 1 13
HELIX 14 14 LEU B 44 LEU B 55 1 12
HELIX 15 15 GLU B 67 TRP B 82 1 16
HELIX 16 16 PRO B 96 ASP B 101 5 6
HELIX 17 17 ASP B 103 VAL B 108 1 6
HELIX 18 18 THR B 109 SER B 121 1 13
HELIX 19 19 SER B 121 ARG B 132 1 12
HELIX 20 20 TYR B 146 GLU B 150 5 5
HELIX 21 21 ASN B 157 GLY B 178 1 22
HELIX 22 22 THR B 221 CYS B 233 1 13
HELIX 23 23 SER B 234 ALA B 238 5 5
HELIX 24 24 GLY B 250 ALA B 254 5 5
SHEET 1 AA 7 VAL A 60 GLN A 62 0
SHEET 2 AA 7 GLU A 34 TYR A 39 1 O PHE A 37 N LEU A 61
SHEET 3 AA 7 ARG A 8 VAL A 11 1 O ILE A 9 N ALA A 36
SHEET 4 AA 7 PHE A 85 HIS A 90 1 N ASP A 86 O ARG A 8
SHEET 5 AA 7 LEU A 135 SER A 145 1 N ASN A 136 O PHE A 85
SHEET 6 AA 7 VAL A 182 ALA A 189 1 O ARG A 183 N LEU A 141
SHEET 7 AA 7 VAL A 244 VAL A 247 1 O VAL A 245 N SER A 188
SHEET 1 BA 7 VAL B 60 GLN B 62 0
SHEET 2 BA 7 GLU B 34 TYR B 39 1 O PHE B 37 N LEU B 61
SHEET 3 BA 7 ARG B 8 VAL B 11 1 O ILE B 9 N ALA B 36
SHEET 4 BA 7 PHE B 88 HIS B 90 1 N VAL B 89 O LEU B 10
SHEET 5 BA 7 SER B 139 SER B 145 1 O LEU B 142 N HIS B 90
SHEET 6 BA 7 VAL B 182 ALA B 189 1 O ARG B 183 N LEU B 141
SHEET 7 BA 7 VAL B 244 VAL B 247 1 O VAL B 245 N SER B 188
SITE 1 AC1 5 GLY A 93 TYR A 146 TYR A 156 NAI A1259
SITE 2 AC1 5 MET B 256
SITE 1 AC2 5 GLY B 93 ILE B 153 TYR B 156 NAI B1259
SITE 2 AC2 5 HOH B2081
SITE 1 AC3 25 GLY A 13 ALA A 15 SER A 19 ILE A 20
SITE 2 AC3 25 GLN A 40 LEU A 44 CYS A 63 ASP A 64
SITE 3 AC3 25 VAL A 65 SER A 91 ILE A 92 LEU A 144
SITE 4 AC3 25 SER A 145 LYS A 163 ALA A 189 PRO A 191
SITE 5 AC3 25 ILE A 192 VT4 A1258 HOH A2010 HOH A2011
SITE 6 AC3 25 HOH A2012 HOH A2030 HOH A2068 HOH A2143
SITE 7 AC3 25 HOH A2145
SITE 1 AC4 25 GLY B 13 ALA B 15 SER B 19 ILE B 20
SITE 2 AC4 25 GLN B 40 CYS B 63 ASP B 64 VAL B 65
SITE 3 AC4 25 SER B 91 ILE B 92 GLY B 93 LEU B 144
SITE 4 AC4 25 SER B 145 TYR B 146 LYS B 163 ALA B 189
SITE 5 AC4 25 PRO B 191 ILE B 192 VT4 B1258 HOH B2007
SITE 6 AC4 25 HOH B2008 HOH B2011 HOH B2023 HOH B2024
SITE 7 AC4 25 HOH B2051
CRYST1 79.678 79.678 330.150 90.00 90.00 120.00 P 61 2 2 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 0.012551 0.007246 0.000000 0.00000
SCALE2 0.000000 0.014492 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003029 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
