HEADER OXIDOREDUCTASE 12-FEB-08 3C8N
TITLE CRYSTAL STRUCTURE OF APO-FGD1 FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE F420-DEPENDENT GLUCOSE-6-PHOSPHATE DEHYDROGENASE
COMPND 3 FGD1;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 SYNONYM: GLUCOSE-6-PHOSPHATE DEHYDROGENASE, F420-DEPENDENT;
COMPND 6 EC: 1.-.-.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 ATCC: 25618;
SOURCE 6 GENE: FGD1, FGD, MT0420, RV0407;
SOURCE 7 EXPRESSION_SYSTEM: MYCOBACTERIUM SMEGMATIS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 1772;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: MC(2) 4517;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PYUB1049
KEYWDS TIM BARREL, NON-PROLYL CIS-PEPTIDE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.BASHIRI,C.J.SQUIRE,N.J.MORELAND,E.N.BAKER
REVDAT 5 20-OCT-21 3C8N 1 SEQADV LINK
REVDAT 4 13-JUL-11 3C8N 1 VERSN
REVDAT 3 22-SEP-09 3C8N 1 JRNL
REVDAT 2 24-FEB-09 3C8N 1 VERSN
REVDAT 1 22-APR-08 3C8N 0
JRNL AUTH G.BASHIRI,C.J.SQUIRE,N.J.MORELAND,E.N.BAKER
JRNL TITL CRYSTAL STRUCTURES OF F420-DEPENDENT GLUCOSE-6-PHOSPHATE
JRNL TITL 2 DEHYDROGENASE FGD1 INVOLVED IN THE ACTIVATION OF THE
JRNL TITL 3 ANTI-TUBERCULOSIS DRUG CANDIDATE PA-824 REVEAL THE BASIS OF
JRNL TITL 4 COENZYME AND SUBSTRATE BINDING.
JRNL REF J.BIOL.CHEM. V. 283 17531 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18434308
JRNL DOI 10.1074/JBC.M801854200
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0008
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 101282
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) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5077
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6883
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.24
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE SET COUNT : 348
REMARK 3 BIN FREE R VALUE : 0.3990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10324
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 371
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.07000
REMARK 3 B22 (A**2) : 0.12000
REMARK 3 B33 (A**2) : -0.19000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.05000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.184
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.165
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.126
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.379
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10651 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14472 ; 1.541 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1342 ; 6.833 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 497 ;36.103 ;22.998
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1642 ;15.082 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 88 ;15.641 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1537 ; 0.105 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8328 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5249 ; 0.202 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 7078 ; 0.300 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 545 ; 0.159 ; 0.200
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): 71 ; 0.226 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.125 ; 0.200
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): 6843 ; 0.894 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10599 ; 1.241 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4406 ; 2.129 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3866 ; 2.948 ; 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 : 4
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 147 A 334
REMARK 3 ORIGIN FOR THE GROUP (A): 36.3890 42.7550 93.2370
REMARK 3 T TENSOR
REMARK 3 T11: -0.0526 T22: -0.0905
REMARK 3 T33: 0.0533 T12: 0.0023
REMARK 3 T13: -0.0435 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 0.5227 L22: 1.1028
REMARK 3 L33: 0.7435 L12: -0.1190
REMARK 3 L13: -0.0242 L23: 0.1641
REMARK 3 S TENSOR
REMARK 3 S11: -0.0572 S12: 0.0501 S13: 0.0100
REMARK 3 S21: -0.1043 S22: 0.0410 S23: 0.1964
REMARK 3 S31: -0.0693 S32: -0.1641 S33: 0.0162
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 43
REMARK 3 RESIDUE RANGE : A 6 A 34
REMARK 3 ORIGIN FOR THE GROUP (A): 69.4110 26.5740 100.6430
REMARK 3 T TENSOR
REMARK 3 T11: -0.0024 T22: -0.1078
REMARK 3 T33: 0.0371 T12: 0.0137
REMARK 3 T13: 0.0175 T23: -0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 2.1463 L22: 0.8602
REMARK 3 L33: 1.5206 L12: -0.6198
REMARK 3 L13: 0.9245 L23: -0.1177
REMARK 3 S TENSOR
REMARK 3 S11: -0.0367 S12: -0.0401 S13: -0.0264
REMARK 3 S21: -0.0721 S22: 0.0901 S23: -0.0599
REMARK 3 S31: 0.1029 S32: 0.0894 S33: -0.0534
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 : C 3 C 334
REMARK 3 ORIGIN FOR THE GROUP (A): 41.0460 25.5560 132.2610
REMARK 3 T TENSOR
REMARK 3 T11: -0.0561 T22: 0.0118
REMARK 3 T33: -0.0081 T12: 0.0286
REMARK 3 T13: 0.0242 T23: -0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 1.1103 L22: 0.6826
REMARK 3 L33: 0.9504 L12: 0.3291
REMARK 3 L13: 0.2052 L23: 0.2839
REMARK 3 S TENSOR
REMARK 3 S11: -0.0304 S12: -0.3156 S13: 0.0820
REMARK 3 S21: 0.0642 S22: -0.0028 S23: 0.0821
REMARK 3 S31: 0.1022 S32: -0.1376 S33: 0.0332
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 : D 3 D 334
REMARK 3 ORIGIN FOR THE GROUP (A): 73.1520 38.7640 133.8980
REMARK 3 T TENSOR
REMARK 3 T11: -0.0679 T22: 0.0409
REMARK 3 T33: -0.0030 T12: 0.0332
REMARK 3 T13: -0.0443 T23: -0.0964
REMARK 3 L TENSOR
REMARK 3 L11: 0.8876 L22: 0.7599
REMARK 3 L33: 1.1565 L12: 0.2945
REMARK 3 L13: -0.0316 L23: -0.0392
REMARK 3 S TENSOR
REMARK 3 S11: -0.0208 S12: -0.2573 S13: 0.0756
REMARK 3 S21: 0.0820 S22: 0.0500 S23: -0.0751
REMARK 3 S31: -0.0890 S32: 0.2045 S33: -0.0292
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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
REMARK 4
REMARK 4 3C8N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-FEB-08.
REMARK 100 THE DEPOSITION ID IS D_1000046479.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-07; 15-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 110; NULL
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; N
REMARK 200 RADIATION SOURCE : SSRL; ROTATING ANODE
REMARK 200 BEAMLINE : BL9-2; NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL; RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97929, 0.91162, 0.97941;
REMARK 200 1.5418
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : MIRRORS; OSMIC
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD; MAR
REMARK 200 SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101311
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 40.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.55200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M TRI-SODIUM CITRATE, 0.1%
REMARK 280 DIOXANE, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 44.56650
REMARK 290 SMTRY3 2 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 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4330 ANGSTROM**2
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4300 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 MSE A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 ALA A 2
REMARK 465 GLY A 145
REMARK 465 LEU A 335
REMARK 465 GLY A 336
REMARK 465 MSE B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 TRP B 44
REMARK 465 ARG B 45
REMARK 465 LEU B 335
REMARK 465 GLY B 336
REMARK 465 MSE C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MSE C 1
REMARK 465 ALA C 2
REMARK 465 LEU C 335
REMARK 465 GLY C 336
REMARK 465 MSE D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MSE D 1
REMARK 465 ALA D 2
REMARK 465 GLU D 119
REMARK 465 GLY D 145
REMARK 465 LEU D 335
REMARK 465 GLY D 336
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 GLU A 119 CG CD OE1 OE2
REMARK 470 SER A 144 OG
REMARK 470 ASP A 146 CG OD1 OD2
REMARK 470 LYS A 198 CG CD CE NZ
REMARK 470 MSE B 1 CG SE CE
REMARK 470 GLU B 201 CG CD OE1 OE2
REMARK 470 GLU C 3 CG CD OE1 OE2
REMARK 470 LYS C 126 CG CD CE NZ
REMARK 470 GLU C 201 CG CD OE1 OE2
REMARK 470 LYS C 206 CG CD CE NZ
REMARK 470 GLU C 240 CG CD OE1 OE2
REMARK 470 GLU C 257 CG CD OE1 OE2
REMARK 470 LYS C 282 CG CD CE NZ
REMARK 470 GLU C 322 CG CD OE1 OE2
REMARK 470 GLU D 3 CG CD OE1 OE2
REMARK 470 GLN D 47 CG CD OE1 NE2
REMARK 470 GLU D 124 CG CD OE1 OE2
REMARK 470 LYS D 126 CG CD CE NZ
REMARK 470 ASP D 167 CG OD1 OD2
REMARK 470 GLU D 201 CG CD OE1 OE2
REMARK 470 GLU D 257 CG CD OE1 OE2
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 GLU B 119 O HOH B 427 2.15
REMARK 500 O GLN D 141 OG SER D 144 2.19
REMARK 500 O TRP A 284 O HOH A 437 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 ARG C 100 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG C 140 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 140 NE - CZ - NH2 ANGL. DEV. = -3.1 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 ALA A 51 72.78 -156.59
REMARK 500 PHE A 79 -87.49 -121.39
REMARK 500 LYS A 206 -70.81 -101.94
REMARK 500 ALA B 51 70.52 -159.82
REMARK 500 PHE B 79 -84.89 -121.98
REMARK 500 LYS B 206 -62.28 -105.41
REMARK 500 SER B 234 75.89 -118.98
REMARK 500 ALA C 51 65.46 -159.03
REMARK 500 PHE C 79 -76.89 -120.37
REMARK 500 LYS C 206 -62.17 -121.57
REMARK 500 ASP C 219 27.95 46.13
REMARK 500 ALA D 51 63.05 -154.45
REMARK 500 PRO D 77 36.17 -89.85
REMARK 500 PHE D 79 -90.57 -121.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3B4Y RELATED DB: PDB
REMARK 900 FGD1 (RV0407) FROM MYCOBACTERIUM TUBERCULOSIS WITH F420 AND CITRATE
REMARK 900 BOUND
DBREF 3C8N A 1 336 UNP P96253 P96253_MYCTU 1 336
DBREF 3C8N B 1 336 UNP P96253 P96253_MYCTU 1 336
DBREF 3C8N C 1 336 UNP P96253 P96253_MYCTU 1 336
DBREF 3C8N D 1 336 UNP P96253 P96253_MYCTU 1 336
SEQADV 3C8N MSE A -19 UNP P96253 EXPRESSION TAG
SEQADV 3C8N GLY A -18 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER A -17 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER A -16 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS A -15 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS A -14 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS A -13 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS A -12 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS A -11 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS A -10 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER A -9 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER A -8 UNP P96253 EXPRESSION TAG
SEQADV 3C8N GLY A -7 UNP P96253 EXPRESSION TAG
SEQADV 3C8N LEU A -6 UNP P96253 EXPRESSION TAG
SEQADV 3C8N VAL A -5 UNP P96253 EXPRESSION TAG
SEQADV 3C8N PRO A -4 UNP P96253 EXPRESSION TAG
SEQADV 3C8N ARG A -3 UNP P96253 EXPRESSION TAG
SEQADV 3C8N GLY A -2 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER A -1 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS A 0 UNP P96253 EXPRESSION TAG
SEQADV 3C8N MSE A 243 UNP P96253 LEU 243 ENGINEERED MUTATION
SEQADV 3C8N MSE B -19 UNP P96253 EXPRESSION TAG
SEQADV 3C8N GLY B -18 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER B -17 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER B -16 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS B -15 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS B -14 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS B -13 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS B -12 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS B -11 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS B -10 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER B -9 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER B -8 UNP P96253 EXPRESSION TAG
SEQADV 3C8N GLY B -7 UNP P96253 EXPRESSION TAG
SEQADV 3C8N LEU B -6 UNP P96253 EXPRESSION TAG
SEQADV 3C8N VAL B -5 UNP P96253 EXPRESSION TAG
SEQADV 3C8N PRO B -4 UNP P96253 EXPRESSION TAG
SEQADV 3C8N ARG B -3 UNP P96253 EXPRESSION TAG
SEQADV 3C8N GLY B -2 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER B -1 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS B 0 UNP P96253 EXPRESSION TAG
SEQADV 3C8N MSE B 243 UNP P96253 LEU 243 ENGINEERED MUTATION
SEQADV 3C8N MSE C -19 UNP P96253 EXPRESSION TAG
SEQADV 3C8N GLY C -18 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER C -17 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER C -16 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS C -15 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS C -14 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS C -13 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS C -12 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS C -11 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS C -10 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER C -9 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER C -8 UNP P96253 EXPRESSION TAG
SEQADV 3C8N GLY C -7 UNP P96253 EXPRESSION TAG
SEQADV 3C8N LEU C -6 UNP P96253 EXPRESSION TAG
SEQADV 3C8N VAL C -5 UNP P96253 EXPRESSION TAG
SEQADV 3C8N PRO C -4 UNP P96253 EXPRESSION TAG
SEQADV 3C8N ARG C -3 UNP P96253 EXPRESSION TAG
SEQADV 3C8N GLY C -2 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER C -1 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS C 0 UNP P96253 EXPRESSION TAG
SEQADV 3C8N MSE C 243 UNP P96253 LEU 243 ENGINEERED MUTATION
SEQADV 3C8N MSE D -19 UNP P96253 EXPRESSION TAG
SEQADV 3C8N GLY D -18 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER D -17 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER D -16 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS D -15 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS D -14 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS D -13 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS D -12 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS D -11 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS D -10 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER D -9 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER D -8 UNP P96253 EXPRESSION TAG
SEQADV 3C8N GLY D -7 UNP P96253 EXPRESSION TAG
SEQADV 3C8N LEU D -6 UNP P96253 EXPRESSION TAG
SEQADV 3C8N VAL D -5 UNP P96253 EXPRESSION TAG
SEQADV 3C8N PRO D -4 UNP P96253 EXPRESSION TAG
SEQADV 3C8N ARG D -3 UNP P96253 EXPRESSION TAG
SEQADV 3C8N GLY D -2 UNP P96253 EXPRESSION TAG
SEQADV 3C8N SER D -1 UNP P96253 EXPRESSION TAG
SEQADV 3C8N HIS D 0 UNP P96253 EXPRESSION TAG
SEQADV 3C8N MSE D 243 UNP P96253 LEU 243 ENGINEERED MUTATION
SEQRES 1 A 356 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 356 LEU VAL PRO ARG GLY SER HIS MSE ALA GLU LEU LYS LEU
SEQRES 3 A 356 GLY TYR LYS ALA SER ALA GLU GLN PHE ALA PRO ARG GLU
SEQRES 4 A 356 LEU VAL GLU LEU ALA VAL ALA ALA GLU ALA HIS GLY MSE
SEQRES 5 A 356 ASP SER ALA THR VAL SER ASP HIS PHE GLN PRO TRP ARG
SEQRES 6 A 356 HIS GLN GLY GLY HIS ALA PRO PHE SER LEU SER TRP MSE
SEQRES 7 A 356 THR ALA VAL GLY GLU ARG THR ASN ARG LEU LEU LEU GLY
SEQRES 8 A 356 THR SER VAL LEU THR PRO THR PHE ARG TYR ASN PRO ALA
SEQRES 9 A 356 VAL ILE ALA GLN ALA PHE ALA THR MSE GLY CYS LEU TYR
SEQRES 10 A 356 PRO ASN ARG VAL PHE LEU GLY VAL GLY THR GLY GLU ALA
SEQRES 11 A 356 LEU ASN GLU ILE ALA THR GLY TYR GLU GLY ALA TRP PRO
SEQRES 12 A 356 GLU PHE LYS GLU ARG PHE ALA ARG LEU ARG GLU SER VAL
SEQRES 13 A 356 GLY LEU MSE ARG GLN LEU TRP SER GLY ASP ARG VAL ASP
SEQRES 14 A 356 PHE ASP GLY ASP TYR TYR ARG LEU LYS GLY ALA SER ILE
SEQRES 15 A 356 TYR ASP VAL PRO ASP GLY GLY VAL PRO VAL TYR ILE ALA
SEQRES 16 A 356 ALA GLY GLY PRO ALA VAL ALA LYS TYR ALA GLY ARG ALA
SEQRES 17 A 356 GLY ASP GLY PHE ILE CYS THR SER GLY LYS GLY GLU GLU
SEQRES 18 A 356 LEU TYR THR GLU LYS LEU MSE PRO ALA VAL ARG GLU GLY
SEQRES 19 A 356 ALA ALA ALA ALA ASP ARG SER VAL ASP GLY ILE ASP LYS
SEQRES 20 A 356 MSE ILE GLU ILE LYS ILE SER TYR ASP PRO ASP PRO GLU
SEQRES 21 A 356 LEU ALA MSE ASN ASN THR ARG PHE TRP ALA PRO LEU SER
SEQRES 22 A 356 LEU THR ALA GLU GLN LYS HIS SER ILE ASP ASP PRO ILE
SEQRES 23 A 356 GLU MSE GLU LYS ALA ALA ASP ALA LEU PRO ILE GLU GLN
SEQRES 24 A 356 ILE ALA LYS ARG TRP ILE VAL ALA SER ASP PRO ASP GLU
SEQRES 25 A 356 ALA VAL GLU LYS VAL GLY GLN TYR VAL THR TRP GLY LEU
SEQRES 26 A 356 ASN HIS LEU VAL PHE HIS ALA PRO GLY HIS ASP GLN ARG
SEQRES 27 A 356 ARG PHE LEU GLU LEU PHE GLN SER ASP LEU ALA PRO ARG
SEQRES 28 A 356 LEU ARG ARG LEU GLY
SEQRES 1 B 356 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 356 LEU VAL PRO ARG GLY SER HIS MSE ALA GLU LEU LYS LEU
SEQRES 3 B 356 GLY TYR LYS ALA SER ALA GLU GLN PHE ALA PRO ARG GLU
SEQRES 4 B 356 LEU VAL GLU LEU ALA VAL ALA ALA GLU ALA HIS GLY MSE
SEQRES 5 B 356 ASP SER ALA THR VAL SER ASP HIS PHE GLN PRO TRP ARG
SEQRES 6 B 356 HIS GLN GLY GLY HIS ALA PRO PHE SER LEU SER TRP MSE
SEQRES 7 B 356 THR ALA VAL GLY GLU ARG THR ASN ARG LEU LEU LEU GLY
SEQRES 8 B 356 THR SER VAL LEU THR PRO THR PHE ARG TYR ASN PRO ALA
SEQRES 9 B 356 VAL ILE ALA GLN ALA PHE ALA THR MSE GLY CYS LEU TYR
SEQRES 10 B 356 PRO ASN ARG VAL PHE LEU GLY VAL GLY THR GLY GLU ALA
SEQRES 11 B 356 LEU ASN GLU ILE ALA THR GLY TYR GLU GLY ALA TRP PRO
SEQRES 12 B 356 GLU PHE LYS GLU ARG PHE ALA ARG LEU ARG GLU SER VAL
SEQRES 13 B 356 GLY LEU MSE ARG GLN LEU TRP SER GLY ASP ARG VAL ASP
SEQRES 14 B 356 PHE ASP GLY ASP TYR TYR ARG LEU LYS GLY ALA SER ILE
SEQRES 15 B 356 TYR ASP VAL PRO ASP GLY GLY VAL PRO VAL TYR ILE ALA
SEQRES 16 B 356 ALA GLY GLY PRO ALA VAL ALA LYS TYR ALA GLY ARG ALA
SEQRES 17 B 356 GLY ASP GLY PHE ILE CYS THR SER GLY LYS GLY GLU GLU
SEQRES 18 B 356 LEU TYR THR GLU LYS LEU MSE PRO ALA VAL ARG GLU GLY
SEQRES 19 B 356 ALA ALA ALA ALA ASP ARG SER VAL ASP GLY ILE ASP LYS
SEQRES 20 B 356 MSE ILE GLU ILE LYS ILE SER TYR ASP PRO ASP PRO GLU
SEQRES 21 B 356 LEU ALA MSE ASN ASN THR ARG PHE TRP ALA PRO LEU SER
SEQRES 22 B 356 LEU THR ALA GLU GLN LYS HIS SER ILE ASP ASP PRO ILE
SEQRES 23 B 356 GLU MSE GLU LYS ALA ALA ASP ALA LEU PRO ILE GLU GLN
SEQRES 24 B 356 ILE ALA LYS ARG TRP ILE VAL ALA SER ASP PRO ASP GLU
SEQRES 25 B 356 ALA VAL GLU LYS VAL GLY GLN TYR VAL THR TRP GLY LEU
SEQRES 26 B 356 ASN HIS LEU VAL PHE HIS ALA PRO GLY HIS ASP GLN ARG
SEQRES 27 B 356 ARG PHE LEU GLU LEU PHE GLN SER ASP LEU ALA PRO ARG
SEQRES 28 B 356 LEU ARG ARG LEU GLY
SEQRES 1 C 356 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 356 LEU VAL PRO ARG GLY SER HIS MSE ALA GLU LEU LYS LEU
SEQRES 3 C 356 GLY TYR LYS ALA SER ALA GLU GLN PHE ALA PRO ARG GLU
SEQRES 4 C 356 LEU VAL GLU LEU ALA VAL ALA ALA GLU ALA HIS GLY MSE
SEQRES 5 C 356 ASP SER ALA THR VAL SER ASP HIS PHE GLN PRO TRP ARG
SEQRES 6 C 356 HIS GLN GLY GLY HIS ALA PRO PHE SER LEU SER TRP MSE
SEQRES 7 C 356 THR ALA VAL GLY GLU ARG THR ASN ARG LEU LEU LEU GLY
SEQRES 8 C 356 THR SER VAL LEU THR PRO THR PHE ARG TYR ASN PRO ALA
SEQRES 9 C 356 VAL ILE ALA GLN ALA PHE ALA THR MSE GLY CYS LEU TYR
SEQRES 10 C 356 PRO ASN ARG VAL PHE LEU GLY VAL GLY THR GLY GLU ALA
SEQRES 11 C 356 LEU ASN GLU ILE ALA THR GLY TYR GLU GLY ALA TRP PRO
SEQRES 12 C 356 GLU PHE LYS GLU ARG PHE ALA ARG LEU ARG GLU SER VAL
SEQRES 13 C 356 GLY LEU MSE ARG GLN LEU TRP SER GLY ASP ARG VAL ASP
SEQRES 14 C 356 PHE ASP GLY ASP TYR TYR ARG LEU LYS GLY ALA SER ILE
SEQRES 15 C 356 TYR ASP VAL PRO ASP GLY GLY VAL PRO VAL TYR ILE ALA
SEQRES 16 C 356 ALA GLY GLY PRO ALA VAL ALA LYS TYR ALA GLY ARG ALA
SEQRES 17 C 356 GLY ASP GLY PHE ILE CYS THR SER GLY LYS GLY GLU GLU
SEQRES 18 C 356 LEU TYR THR GLU LYS LEU MSE PRO ALA VAL ARG GLU GLY
SEQRES 19 C 356 ALA ALA ALA ALA ASP ARG SER VAL ASP GLY ILE ASP LYS
SEQRES 20 C 356 MSE ILE GLU ILE LYS ILE SER TYR ASP PRO ASP PRO GLU
SEQRES 21 C 356 LEU ALA MSE ASN ASN THR ARG PHE TRP ALA PRO LEU SER
SEQRES 22 C 356 LEU THR ALA GLU GLN LYS HIS SER ILE ASP ASP PRO ILE
SEQRES 23 C 356 GLU MSE GLU LYS ALA ALA ASP ALA LEU PRO ILE GLU GLN
SEQRES 24 C 356 ILE ALA LYS ARG TRP ILE VAL ALA SER ASP PRO ASP GLU
SEQRES 25 C 356 ALA VAL GLU LYS VAL GLY GLN TYR VAL THR TRP GLY LEU
SEQRES 26 C 356 ASN HIS LEU VAL PHE HIS ALA PRO GLY HIS ASP GLN ARG
SEQRES 27 C 356 ARG PHE LEU GLU LEU PHE GLN SER ASP LEU ALA PRO ARG
SEQRES 28 C 356 LEU ARG ARG LEU GLY
SEQRES 1 D 356 MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 356 LEU VAL PRO ARG GLY SER HIS MSE ALA GLU LEU LYS LEU
SEQRES 3 D 356 GLY TYR LYS ALA SER ALA GLU GLN PHE ALA PRO ARG GLU
SEQRES 4 D 356 LEU VAL GLU LEU ALA VAL ALA ALA GLU ALA HIS GLY MSE
SEQRES 5 D 356 ASP SER ALA THR VAL SER ASP HIS PHE GLN PRO TRP ARG
SEQRES 6 D 356 HIS GLN GLY GLY HIS ALA PRO PHE SER LEU SER TRP MSE
SEQRES 7 D 356 THR ALA VAL GLY GLU ARG THR ASN ARG LEU LEU LEU GLY
SEQRES 8 D 356 THR SER VAL LEU THR PRO THR PHE ARG TYR ASN PRO ALA
SEQRES 9 D 356 VAL ILE ALA GLN ALA PHE ALA THR MSE GLY CYS LEU TYR
SEQRES 10 D 356 PRO ASN ARG VAL PHE LEU GLY VAL GLY THR GLY GLU ALA
SEQRES 11 D 356 LEU ASN GLU ILE ALA THR GLY TYR GLU GLY ALA TRP PRO
SEQRES 12 D 356 GLU PHE LYS GLU ARG PHE ALA ARG LEU ARG GLU SER VAL
SEQRES 13 D 356 GLY LEU MSE ARG GLN LEU TRP SER GLY ASP ARG VAL ASP
SEQRES 14 D 356 PHE ASP GLY ASP TYR TYR ARG LEU LYS GLY ALA SER ILE
SEQRES 15 D 356 TYR ASP VAL PRO ASP GLY GLY VAL PRO VAL TYR ILE ALA
SEQRES 16 D 356 ALA GLY GLY PRO ALA VAL ALA LYS TYR ALA GLY ARG ALA
SEQRES 17 D 356 GLY ASP GLY PHE ILE CYS THR SER GLY LYS GLY GLU GLU
SEQRES 18 D 356 LEU TYR THR GLU LYS LEU MSE PRO ALA VAL ARG GLU GLY
SEQRES 19 D 356 ALA ALA ALA ALA ASP ARG SER VAL ASP GLY ILE ASP LYS
SEQRES 20 D 356 MSE ILE GLU ILE LYS ILE SER TYR ASP PRO ASP PRO GLU
SEQRES 21 D 356 LEU ALA MSE ASN ASN THR ARG PHE TRP ALA PRO LEU SER
SEQRES 22 D 356 LEU THR ALA GLU GLN LYS HIS SER ILE ASP ASP PRO ILE
SEQRES 23 D 356 GLU MSE GLU LYS ALA ALA ASP ALA LEU PRO ILE GLU GLN
SEQRES 24 D 356 ILE ALA LYS ARG TRP ILE VAL ALA SER ASP PRO ASP GLU
SEQRES 25 D 356 ALA VAL GLU LYS VAL GLY GLN TYR VAL THR TRP GLY LEU
SEQRES 26 D 356 ASN HIS LEU VAL PHE HIS ALA PRO GLY HIS ASP GLN ARG
SEQRES 27 D 356 ARG PHE LEU GLU LEU PHE GLN SER ASP LEU ALA PRO ARG
SEQRES 28 D 356 LEU ARG ARG LEU GLY
MODRES 3C8N MSE A 1 MET SELENOMETHIONINE
MODRES 3C8N MSE A 32 MET SELENOMETHIONINE
MODRES 3C8N MSE A 58 MET SELENOMETHIONINE
MODRES 3C8N MSE A 93 MET SELENOMETHIONINE
MODRES 3C8N MSE A 139 MET SELENOMETHIONINE
MODRES 3C8N MSE A 208 MET SELENOMETHIONINE
MODRES 3C8N MSE A 228 MET SELENOMETHIONINE
MODRES 3C8N MSE A 243 MET SELENOMETHIONINE
MODRES 3C8N MSE A 268 MET SELENOMETHIONINE
MODRES 3C8N MSE B 1 MET SELENOMETHIONINE
MODRES 3C8N MSE B 32 MET SELENOMETHIONINE
MODRES 3C8N MSE B 58 MET SELENOMETHIONINE
MODRES 3C8N MSE B 93 MET SELENOMETHIONINE
MODRES 3C8N MSE B 139 MET SELENOMETHIONINE
MODRES 3C8N MSE B 208 MET SELENOMETHIONINE
MODRES 3C8N MSE B 228 MET SELENOMETHIONINE
MODRES 3C8N MSE B 243 MET SELENOMETHIONINE
MODRES 3C8N MSE B 268 MET SELENOMETHIONINE
MODRES 3C8N MSE C 32 MET SELENOMETHIONINE
MODRES 3C8N MSE C 58 MET SELENOMETHIONINE
MODRES 3C8N MSE C 93 MET SELENOMETHIONINE
MODRES 3C8N MSE C 139 MET SELENOMETHIONINE
MODRES 3C8N MSE C 208 MET SELENOMETHIONINE
MODRES 3C8N MSE C 228 MET SELENOMETHIONINE
MODRES 3C8N MSE C 243 MET SELENOMETHIONINE
MODRES 3C8N MSE C 268 MET SELENOMETHIONINE
MODRES 3C8N MSE D 32 MET SELENOMETHIONINE
MODRES 3C8N MSE D 58 MET SELENOMETHIONINE
MODRES 3C8N MSE D 93 MET SELENOMETHIONINE
MODRES 3C8N MSE D 139 MET SELENOMETHIONINE
MODRES 3C8N MSE D 208 MET SELENOMETHIONINE
MODRES 3C8N MSE D 228 MET SELENOMETHIONINE
MODRES 3C8N MSE D 243 MET SELENOMETHIONINE
MODRES 3C8N MSE D 268 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 32 8
HET MSE A 58 8
HET MSE A 93 8
HET MSE A 139 8
HET MSE A 208 8
HET MSE A 228 8
HET MSE A 243 8
HET MSE A 268 8
HET MSE B 1 5
HET MSE B 32 8
HET MSE B 58 8
HET MSE B 93 8
HET MSE B 139 8
HET MSE B 208 8
HET MSE B 228 8
HET MSE B 243 8
HET MSE B 268 8
HET MSE C 32 8
HET MSE C 58 8
HET MSE C 93 8
HET MSE C 139 8
HET MSE C 208 8
HET MSE C 228 8
HET MSE C 243 8
HET MSE C 268 8
HET MSE D 32 8
HET MSE D 58 8
HET MSE D 93 8
HET MSE D 139 8
HET MSE D 208 8
HET MSE D 228 8
HET MSE D 243 8
HET MSE D 268 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 34(C5 H11 N O2 SE)
FORMUL 5 HOH *371(H2 O)
HELIX 1 1 ALA A 16 HIS A 30 1 15
HELIX 2 2 PHE A 53 THR A 65 1 13
HELIX 3 3 ASN A 82 TYR A 97 1 16
HELIX 4 4 GLU A 109 ILE A 114 1 6
HELIX 5 5 GLU A 124 TRP A 143 1 20
HELIX 6 6 GLY A 178 GLY A 189 1 12
HELIX 7 7 GLY A 199 LYS A 206 1 8
HELIX 8 8 LYS A 206 ALA A 218 1 13
HELIX 9 9 SER A 221 ILE A 225 5 5
HELIX 10 10 ASP A 238 ASN A 245 1 8
HELIX 11 11 THR A 246 LEU A 254 5 9
HELIX 12 12 THR A 255 ILE A 262 1 8
HELIX 13 13 ASP A 264 ALA A 274 1 11
HELIX 14 14 PRO A 276 LYS A 282 1 7
HELIX 15 15 ASP A 289 TRP A 303 1 15
HELIX 16 16 ASP A 316 LEU A 328 1 13
HELIX 17 17 LEU A 328 ARG A 334 1 7
HELIX 18 18 ALA B 16 HIS B 30 1 15
HELIX 19 19 PHE B 53 THR B 65 1 13
HELIX 20 20 ASN B 82 TYR B 97 1 16
HELIX 21 21 GLU B 109 THR B 116 1 8
HELIX 22 22 GLU B 124 TRP B 143 1 20
HELIX 23 23 GLY B 178 GLY B 189 1 12
HELIX 24 24 GLY B 199 LYS B 206 1 8
HELIX 25 25 LYS B 206 ALA B 218 1 13
HELIX 26 26 SER B 221 ILE B 225 5 5
HELIX 27 27 ASP B 238 ASN B 245 1 8
HELIX 28 28 THR B 246 LEU B 254 5 9
HELIX 29 29 THR B 255 ILE B 262 1 8
HELIX 30 30 ASP B 264 ALA B 274 1 11
HELIX 31 31 PRO B 276 LYS B 282 1 7
HELIX 32 32 ASP B 289 TRP B 303 1 15
HELIX 33 33 ASP B 316 LEU B 328 1 13
HELIX 34 34 LEU B 328 ARG B 334 1 7
HELIX 35 35 ALA C 16 HIS C 30 1 15
HELIX 36 36 PHE C 53 THR C 65 1 13
HELIX 37 37 ASN C 82 TYR C 97 1 16
HELIX 38 38 GLU C 109 THR C 116 1 8
HELIX 39 39 GLU C 124 TRP C 143 1 20
HELIX 40 40 GLY C 178 GLY C 189 1 12
HELIX 41 41 GLY C 199 GLU C 205 1 7
HELIX 42 42 LYS C 206 ALA C 218 1 13
HELIX 43 43 SER C 221 ILE C 225 5 5
HELIX 44 44 ASP C 238 ASN C 245 1 8
HELIX 45 45 THR C 246 LEU C 254 5 9
HELIX 46 46 THR C 255 ILE C 262 1 8
HELIX 47 47 ASP C 264 ALA C 274 1 11
HELIX 48 48 PRO C 276 ALA C 281 1 6
HELIX 49 49 LYS C 282 TRP C 284 5 3
HELIX 50 50 ASP C 289 TRP C 303 1 15
HELIX 51 51 ASP C 316 ASP C 327 1 12
HELIX 52 52 ASP C 327 ARG C 334 1 8
HELIX 53 53 ALA D 16 HIS D 30 1 15
HELIX 54 54 PHE D 53 THR D 65 1 13
HELIX 55 55 ASN D 82 TYR D 97 1 16
HELIX 56 56 GLU D 109 THR D 116 1 8
HELIX 57 57 GLU D 124 TRP D 143 1 20
HELIX 58 58 GLY D 178 GLY D 189 1 12
HELIX 59 59 GLY D 199 LYS D 206 1 8
HELIX 60 60 LYS D 206 ASP D 219 1 14
HELIX 61 61 SER D 221 ILE D 225 5 5
HELIX 62 62 ASP D 238 ASN D 245 1 8
HELIX 63 63 THR D 246 LEU D 254 5 9
HELIX 64 64 THR D 255 ILE D 262 1 8
HELIX 65 65 ASP D 264 ALA D 274 1 11
HELIX 66 66 PRO D 276 LYS D 282 1 7
HELIX 67 67 ASP D 289 TRP D 303 1 15
HELIX 68 68 ASP D 316 ASP D 327 1 12
HELIX 69 69 LEU D 328 ARG D 334 1 7
SHEET 1 A10 ILE A 285 ALA A 287 0
SHEET 2 A10 ASP A 226 TYR A 235 1 N SER A 234 O ILE A 285
SHEET 3 A10 HIS A 307 HIS A 311 1 O HIS A 311 N ILE A 231
SHEET 4 A10 LYS A 5 ALA A 10 1 N GLY A 7 O LEU A 308
SHEET 5 A10 SER A 34 VAL A 37 1 O THR A 36 N ALA A 10
SHEET 6 A10 LEU A 69 THR A 72 1 O LEU A 69 N ALA A 35
SHEET 7 A10 VAL A 101 VAL A 105 1 O PHE A 102 N LEU A 70
SHEET 8 A10 VAL A 172 ALA A 175 1 O TYR A 173 N VAL A 105
SHEET 9 A10 GLY A 191 THR A 195 1 O ILE A 193 N ILE A 174
SHEET 10 A10 ASP A 226 TYR A 235 1 O GLU A 230 N CYS A 194
SHEET 1 B 2 VAL A 148 ASP A 151 0
SHEET 2 B 2 ARG A 156 ALA A 160 -1 O ALA A 160 N VAL A 148
SHEET 1 C10 ILE B 285 ALA B 287 0
SHEET 2 C10 ASP B 226 TYR B 235 1 N SER B 234 O ILE B 285
SHEET 3 C10 HIS B 307 HIS B 311 1 O VAL B 309 N ILE B 229
SHEET 4 C10 LYS B 5 ALA B 10 1 N LYS B 5 O LEU B 308
SHEET 5 C10 SER B 34 VAL B 37 1 O THR B 36 N ALA B 10
SHEET 6 C10 LEU B 69 THR B 72 1 O LEU B 69 N ALA B 35
SHEET 7 C10 VAL B 101 VAL B 105 1 O PHE B 102 N LEU B 70
SHEET 8 C10 VAL B 172 ALA B 175 1 O TYR B 173 N LEU B 103
SHEET 9 C10 GLY B 191 THR B 195 1 O GLY B 191 N ILE B 174
SHEET 10 C10 ASP B 226 TYR B 235 1 O MSE B 228 N PHE B 192
SHEET 1 D 2 VAL B 148 ASP B 151 0
SHEET 2 D 2 ARG B 156 ALA B 160 -1 O ALA B 160 N VAL B 148
SHEET 1 E10 ILE C 285 ALA C 287 0
SHEET 2 E10 ASP C 226 TYR C 235 1 N SER C 234 O ILE C 285
SHEET 3 E10 HIS C 307 HIS C 311 1 O VAL C 309 N ILE C 229
SHEET 4 E10 LYS C 5 ALA C 10 1 N GLY C 7 O PHE C 310
SHEET 5 E10 SER C 34 VAL C 37 1 O THR C 36 N ALA C 10
SHEET 6 E10 LEU C 69 THR C 72 1 O LEU C 69 N ALA C 35
SHEET 7 E10 VAL C 101 VAL C 105 1 O PHE C 102 N LEU C 70
SHEET 8 E10 VAL C 172 ALA C 175 1 O TYR C 173 N LEU C 103
SHEET 9 E10 GLY C 191 THR C 195 1 O ILE C 193 N ILE C 174
SHEET 10 E10 ASP C 226 TYR C 235 1 O GLU C 230 N CYS C 194
SHEET 1 F 2 VAL C 148 ASP C 151 0
SHEET 2 F 2 ARG C 156 ALA C 160 -1 O ALA C 160 N VAL C 148
SHEET 1 G10 ILE D 285 ALA D 287 0
SHEET 2 G10 ASP D 226 TYR D 235 1 N LYS D 232 O ILE D 285
SHEET 3 G10 HIS D 307 HIS D 311 1 O VAL D 309 N ILE D 229
SHEET 4 G10 LYS D 5 ALA D 10 1 N GLY D 7 O LEU D 308
SHEET 5 G10 SER D 34 VAL D 37 1 O THR D 36 N ALA D 10
SHEET 6 G10 LEU D 69 THR D 72 1 O LEU D 69 N ALA D 35
SHEET 7 G10 VAL D 101 VAL D 105 1 O PHE D 102 N LEU D 70
SHEET 8 G10 VAL D 172 ALA D 175 1 O TYR D 173 N LEU D 103
SHEET 9 G10 GLY D 191 THR D 195 1 O GLY D 191 N ILE D 174
SHEET 10 G10 ASP D 226 TYR D 235 1 O MSE D 228 N PHE D 192
SHEET 1 H 2 VAL D 148 ASP D 151 0
SHEET 2 H 2 ARG D 156 ALA D 160 -1 O LEU D 157 N PHE D 150
LINK C GLY A 31 N MSE A 32 1555 1555 1.35
LINK C MSE A 32 N ASP A 33 1555 1555 1.32
LINK C TRP A 57 N MSE A 58 1555 1555 1.33
LINK C MSE A 58 N THR A 59 1555 1555 1.33
LINK C THR A 92 N MSE A 93 1555 1555 1.34
LINK C MSE A 93 N GLY A 94 1555 1555 1.33
LINK C LEU A 138 N MSE A 139 1555 1555 1.34
LINK C MSE A 139 N ARG A 140 1555 1555 1.33
LINK C LEU A 207 N MSE A 208 1555 1555 1.34
LINK C MSE A 208 N PRO A 209 1555 1555 1.36
LINK C LYS A 227 N MSE A 228 1555 1555 1.33
LINK C MSE A 228 N ILE A 229 1555 1555 1.32
LINK C ALA A 242 N MSE A 243 1555 1555 1.34
LINK C MSE A 243 N ASN A 244 1555 1555 1.34
LINK C GLU A 267 N MSE A 268 1555 1555 1.34
LINK C MSE A 268 N GLU A 269 1555 1555 1.34
LINK C MSE B 1 N ALA B 2 1555 1555 1.34
LINK C GLY B 31 N MSE B 32 1555 1555 1.34
LINK C MSE B 32 N ASP B 33 1555 1555 1.33
LINK C TRP B 57 N MSE B 58 1555 1555 1.31
LINK C MSE B 58 N THR B 59 1555 1555 1.34
LINK C THR B 92 N MSE B 93 1555 1555 1.34
LINK C MSE B 93 N GLY B 94 1555 1555 1.31
LINK C LEU B 138 N MSE B 139 1555 1555 1.34
LINK C MSE B 139 N ARG B 140 1555 1555 1.32
LINK C LEU B 207 N MSE B 208 1555 1555 1.33
LINK C MSE B 208 N PRO B 209 1555 1555 1.37
LINK C LYS B 227 N MSE B 228 1555 1555 1.32
LINK C MSE B 228 N ILE B 229 1555 1555 1.32
LINK C ALA B 242 N MSE B 243 1555 1555 1.33
LINK C MSE B 243 N ASN B 244 1555 1555 1.34
LINK C GLU B 267 N MSE B 268 1555 1555 1.34
LINK C MSE B 268 N GLU B 269 1555 1555 1.33
LINK C GLY C 31 N MSE C 32 1555 1555 1.33
LINK C MSE C 32 N ASP C 33 1555 1555 1.33
LINK C TRP C 57 N MSE C 58 1555 1555 1.33
LINK C MSE C 58 N THR C 59 1555 1555 1.34
LINK C THR C 92 N MSE C 93 1555 1555 1.32
LINK C MSE C 93 N GLY C 94 1555 1555 1.34
LINK C LEU C 138 N MSE C 139 1555 1555 1.34
LINK C MSE C 139 N ARG C 140 1555 1555 1.34
LINK C LEU C 207 N MSE C 208 1555 1555 1.33
LINK C MSE C 208 N PRO C 209 1555 1555 1.36
LINK C LYS C 227 N MSE C 228 1555 1555 1.32
LINK C MSE C 228 N ILE C 229 1555 1555 1.33
LINK C ALA C 242 N MSE C 243 1555 1555 1.33
LINK C MSE C 243 N ASN C 244 1555 1555 1.33
LINK C GLU C 267 N MSE C 268 1555 1555 1.33
LINK C MSE C 268 N GLU C 269 1555 1555 1.33
LINK C GLY D 31 N MSE D 32 1555 1555 1.33
LINK C MSE D 32 N ASP D 33 1555 1555 1.33
LINK C TRP D 57 N MSE D 58 1555 1555 1.32
LINK C MSE D 58 N THR D 59 1555 1555 1.33
LINK C THR D 92 N MSE D 93 1555 1555 1.34
LINK C MSE D 93 N GLY D 94 1555 1555 1.34
LINK C LEU D 138 N MSE D 139 1555 1555 1.33
LINK C MSE D 139 N ARG D 140 1555 1555 1.33
LINK C LEU D 207 N MSE D 208 1555 1555 1.33
LINK C MSE D 208 N PRO D 209 1555 1555 1.36
LINK C LYS D 227 N MSE D 228 1555 1555 1.33
LINK C MSE D 228 N ILE D 229 1555 1555 1.32
LINK C ALA D 242 N MSE D 243 1555 1555 1.34
LINK C MSE D 243 N ASN D 244 1555 1555 1.33
LINK C GLU D 267 N MSE D 268 1555 1555 1.34
LINK C MSE D 268 N GLU D 269 1555 1555 1.33
CISPEP 1 SER A 73 VAL A 74 0 0.14
CISPEP 2 SER B 73 VAL B 74 0 -11.25
CISPEP 3 SER C 73 VAL C 74 0 -9.14
CISPEP 4 SER D 73 VAL D 74 0 -3.14
CRYST1 80.954 89.133 90.859 90.00 91.64 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012353 0.000000 0.000354 0.00000
SCALE2 0.000000 0.011219 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011011 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
