HEADER OXIDOREDUCTASE 17-AUG-06 2I3A
TITLE CRYSTAL STRUCTURE OF N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE
TITLE 2 (RV1652) FROM MYCOBACTERIUM TUBERCULOSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: AGPR, N-ACETYL-GLUTAMATE SEMIALDEHYDE DEHYDROGENASE, NAGSA
COMPND 5 DEHYDROGENASE;
COMPND 6 EC: 1.2.1.38;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 83332;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: ARGC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PDEST15-1652
KEYWDS DIMER INTERFACE BETA SANDWICH, TETRAMER, ROSSMANN FOLD, STRUCTURAL
KEYWDS 2 GENOMICS, MYCOBACTERIUM TUBERCULOSIS STRUCTURAL PROTEOMICS PROJECT,
KEYWDS 3 XMTB, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.T.CHERNEY,M.M.CHERNEY,C.R.GAREN,F.MORAIDIN,M.N.G.JAMES,
AUTHOR 2 MYCOBACTERIUM TUBERCULOSIS STRUCTURAL PROTEOMICS PROJECT (XMTB)
REVDAT 6 21-FEB-24 2I3A 1 REMARK
REVDAT 5 13-JUL-11 2I3A 1 VERSN
REVDAT 4 24-FEB-09 2I3A 1 VERSN
REVDAT 3 10-APR-07 2I3A 1 REMARK MASTER
REVDAT 2 03-APR-07 2I3A 1 JRNL
REVDAT 1 29-AUG-06 2I3A 0
JRNL AUTH L.T.CHERNEY,M.M.CHERNEY,C.R.GAREN,C.NIU,F.MORADIAN,
JRNL AUTH 2 M.N.G.JAMES
JRNL TITL CRYSTAL STRUCTURE OF N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE
JRNL TITL 2 REDUCTASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH
JRNL TITL 3 NADP(+).
JRNL REF J.MOL.BIOL. V. 367 1357 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17316682
JRNL DOI 10.1016/J.JMB.2007.01.033
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 66273
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3532
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4291
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.88
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE SET COUNT : 256
REMARK 3 BIN FREE R VALUE : 0.3120
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10017
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 916
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.77000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : -0.92000
REMARK 3 B12 (A**2) : 0.00000
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): 0.249
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.201
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.140
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.412
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10293 ; 0.020 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14094 ; 1.798 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1377 ; 6.732 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 374 ;34.236 ;22.299
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1419 ;15.098 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 80 ;19.955 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1670 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7856 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4809 ; 0.209 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6969 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 860 ; 0.164 ; 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): 56 ; 0.241 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.212 ; 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): 6998 ; 1.072 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10931 ; 1.726 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3658 ; 2.747 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3163 ; 4.324 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 10 A 352 4
REMARK 3 1 B 10 B 352 4
REMARK 3 1 C 10 C 352 4
REMARK 3 1 D 10 D 352 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2491 ; 0.64 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 2491 ; 0.59 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 2491 ; 0.51 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 2491 ; 0.53 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2491 ; 1.58 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 2491 ; 1.21 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 2491 ; 1.23 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 2491 ; 1.87 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 2I3A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-AUG-06.
REMARK 100 THE DEPOSITION ID IS D_1000039082.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11587
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69868
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
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) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.3
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG MME 5000, 0.1M BIS-TRIS, PH
REMARK 280 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 44.84750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.21750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.01550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.21750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.84750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.01550
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, 3, 4
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 BIOLOGYCAL ASSEMBLY IS A DIMER. THERE ARE TWO DIMERS IN
REMARK 300 THE ASYMMETRIC UNIT.
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: 4090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 4090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 52.01550
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -69.21750
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 GLN A 2
REMARK 465 ASN A 3
REMARK 465 ARG A 4
REMARK 465 GLN A 5
REMARK 465 VAL A 6
REMARK 465 ALA A 7
REMARK 465 ASN A 8
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 ASN B 3
REMARK 465 ARG B 4
REMARK 465 GLN B 5
REMARK 465 VAL B 6
REMARK 465 MET C 1
REMARK 465 GLN C 2
REMARK 465 ASN C 3
REMARK 465 ARG C 4
REMARK 465 GLN C 5
REMARK 465 VAL C 6
REMARK 465 ALA C 7
REMARK 465 ASN C 8
REMARK 465 MET D 1
REMARK 465 GLN D 2
REMARK 465 ASN D 3
REMARK 465 ARG D 4
REMARK 465 GLN D 5
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 198 CB - CG - OD1 ANGL. DEV. = 5.7 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 87 63.44 -108.98
REMARK 500 HIS A 92 81.14 -150.36
REMARK 500 GLN A 99 47.26 -101.42
REMARK 500 PRO A 102 -0.97 -59.84
REMARK 500 PRO A 134 119.13 -38.89
REMARK 500 ALA A 195 77.12 -68.71
REMARK 500 GLU A 284 111.29 -13.98
REMARK 500 VAL A 322 -90.11 -100.09
REMARK 500 THR A 325 -91.58 -151.01
REMARK 500 SER B 50 24.63 -157.68
REMARK 500 LEU B 62 58.52 -96.86
REMARK 500 VAL B 322 -86.42 -104.38
REMARK 500 THR B 325 -87.87 -150.16
REMARK 500 ALA C 48 -81.93 -50.61
REMARK 500 LEU C 62 48.61 -93.18
REMARK 500 ALA C 87 64.99 -116.05
REMARK 500 HIS C 90 140.38 -38.93
REMARK 500 ALA C 191 -5.94 -59.09
REMARK 500 GLU C 284 123.83 -35.81
REMARK 500 VAL C 322 -86.98 -109.59
REMARK 500 THR C 325 -88.84 -149.57
REMARK 500 ALA D 9 141.58 174.91
REMARK 500 SER D 50 51.49 31.98
REMARK 500 PRO D 178 23.55 -76.82
REMARK 500 VAL D 322 -81.66 -108.74
REMARK 500 THR D 325 -87.69 -153.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR C 49 SER C 50 -141.26
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 BTB A 1400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB B 1500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB C 1600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTB D 1700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV1652 RELATED DB: TARGETDB
DBREF 2I3A A 1 352 UNP P63562 ARGC_MYCTU 1 352
DBREF 2I3A B 1 352 UNP P63562 ARGC_MYCTU 1 352
DBREF 2I3A C 1 352 UNP P63562 ARGC_MYCTU 1 352
DBREF 2I3A D 1 352 UNP P63562 ARGC_MYCTU 1 352
SEQRES 1 A 352 MET GLN ASN ARG GLN VAL ALA ASN ALA THR LYS VAL ALA
SEQRES 2 A 352 VAL ALA GLY ALA SER GLY TYR ALA GLY GLY GLU ILE LEU
SEQRES 3 A 352 ARG LEU LEU LEU GLY HIS PRO ALA TYR ALA ASP GLY ARG
SEQRES 4 A 352 LEU ARG ILE GLY ALA LEU THR ALA ALA THR SER ALA GLY
SEQRES 5 A 352 SER THR LEU GLY GLU HIS HIS PRO HIS LEU THR PRO LEU
SEQRES 6 A 352 ALA HIS ARG VAL VAL GLU PRO THR GLU ALA ALA VAL LEU
SEQRES 7 A 352 GLY GLY HIS ASP ALA VAL PHE LEU ALA LEU PRO HIS GLY
SEQRES 8 A 352 HIS SER ALA VAL LEU ALA GLN GLN LEU SER PRO GLU THR
SEQRES 9 A 352 LEU ILE ILE ASP CYS GLY ALA ASP PHE ARG LEU THR ASP
SEQRES 10 A 352 ALA ALA VAL TRP GLU ARG PHE TYR GLY SER SER HIS ALA
SEQRES 11 A 352 GLY SER TRP PRO TYR GLY LEU PRO GLU LEU PRO GLY ALA
SEQRES 12 A 352 ARG ASP GLN LEU ARG GLY THR ARG ARG ILE ALA VAL PRO
SEQRES 13 A 352 GLY CYS TYR PRO THR ALA ALA LEU LEU ALA LEU PHE PRO
SEQRES 14 A 352 ALA LEU ALA ALA ASP LEU ILE GLU PRO ALA VAL THR VAL
SEQRES 15 A 352 VAL ALA VAL SER GLY THR SER GLY ALA GLY ARG ALA ALA
SEQRES 16 A 352 THR THR ASP LEU LEU GLY ALA GLU VAL ILE GLY SER ALA
SEQRES 17 A 352 ARG ALA TYR ASN ILE ALA GLY VAL HIS ARG HIS THR PRO
SEQRES 18 A 352 GLU ILE ALA GLN GLY LEU ARG ALA VAL THR ASP ARG ASP
SEQRES 19 A 352 VAL SER VAL SER PHE THR PRO VAL LEU ILE PRO ALA SER
SEQRES 20 A 352 ARG GLY ILE LEU ALA THR CYS THR ALA ARG THR ARG SER
SEQRES 21 A 352 PRO LEU SER GLN LEU ARG ALA ALA TYR GLU LYS ALA TYR
SEQRES 22 A 352 HIS ALA GLU PRO PHE ILE TYR LEU MET PRO GLU GLY GLN
SEQRES 23 A 352 LEU PRO ARG THR GLY ALA VAL ILE GLY SER ASN ALA ALA
SEQRES 24 A 352 HIS ILE ALA VAL ALA VAL ASP GLU ASP ALA GLN THR PHE
SEQRES 25 A 352 VAL ALA ILE ALA ALA ILE ASP ASN LEU VAL LYS GLY THR
SEQRES 26 A 352 ALA GLY ALA ALA VAL GLN SER MET ASN LEU ALA LEU GLY
SEQRES 27 A 352 TRP PRO GLU THR ASP GLY LEU SER VAL VAL GLY VAL ALA
SEQRES 28 A 352 PRO
SEQRES 1 B 352 MET GLN ASN ARG GLN VAL ALA ASN ALA THR LYS VAL ALA
SEQRES 2 B 352 VAL ALA GLY ALA SER GLY TYR ALA GLY GLY GLU ILE LEU
SEQRES 3 B 352 ARG LEU LEU LEU GLY HIS PRO ALA TYR ALA ASP GLY ARG
SEQRES 4 B 352 LEU ARG ILE GLY ALA LEU THR ALA ALA THR SER ALA GLY
SEQRES 5 B 352 SER THR LEU GLY GLU HIS HIS PRO HIS LEU THR PRO LEU
SEQRES 6 B 352 ALA HIS ARG VAL VAL GLU PRO THR GLU ALA ALA VAL LEU
SEQRES 7 B 352 GLY GLY HIS ASP ALA VAL PHE LEU ALA LEU PRO HIS GLY
SEQRES 8 B 352 HIS SER ALA VAL LEU ALA GLN GLN LEU SER PRO GLU THR
SEQRES 9 B 352 LEU ILE ILE ASP CYS GLY ALA ASP PHE ARG LEU THR ASP
SEQRES 10 B 352 ALA ALA VAL TRP GLU ARG PHE TYR GLY SER SER HIS ALA
SEQRES 11 B 352 GLY SER TRP PRO TYR GLY LEU PRO GLU LEU PRO GLY ALA
SEQRES 12 B 352 ARG ASP GLN LEU ARG GLY THR ARG ARG ILE ALA VAL PRO
SEQRES 13 B 352 GLY CYS TYR PRO THR ALA ALA LEU LEU ALA LEU PHE PRO
SEQRES 14 B 352 ALA LEU ALA ALA ASP LEU ILE GLU PRO ALA VAL THR VAL
SEQRES 15 B 352 VAL ALA VAL SER GLY THR SER GLY ALA GLY ARG ALA ALA
SEQRES 16 B 352 THR THR ASP LEU LEU GLY ALA GLU VAL ILE GLY SER ALA
SEQRES 17 B 352 ARG ALA TYR ASN ILE ALA GLY VAL HIS ARG HIS THR PRO
SEQRES 18 B 352 GLU ILE ALA GLN GLY LEU ARG ALA VAL THR ASP ARG ASP
SEQRES 19 B 352 VAL SER VAL SER PHE THR PRO VAL LEU ILE PRO ALA SER
SEQRES 20 B 352 ARG GLY ILE LEU ALA THR CYS THR ALA ARG THR ARG SER
SEQRES 21 B 352 PRO LEU SER GLN LEU ARG ALA ALA TYR GLU LYS ALA TYR
SEQRES 22 B 352 HIS ALA GLU PRO PHE ILE TYR LEU MET PRO GLU GLY GLN
SEQRES 23 B 352 LEU PRO ARG THR GLY ALA VAL ILE GLY SER ASN ALA ALA
SEQRES 24 B 352 HIS ILE ALA VAL ALA VAL ASP GLU ASP ALA GLN THR PHE
SEQRES 25 B 352 VAL ALA ILE ALA ALA ILE ASP ASN LEU VAL LYS GLY THR
SEQRES 26 B 352 ALA GLY ALA ALA VAL GLN SER MET ASN LEU ALA LEU GLY
SEQRES 27 B 352 TRP PRO GLU THR ASP GLY LEU SER VAL VAL GLY VAL ALA
SEQRES 28 B 352 PRO
SEQRES 1 C 352 MET GLN ASN ARG GLN VAL ALA ASN ALA THR LYS VAL ALA
SEQRES 2 C 352 VAL ALA GLY ALA SER GLY TYR ALA GLY GLY GLU ILE LEU
SEQRES 3 C 352 ARG LEU LEU LEU GLY HIS PRO ALA TYR ALA ASP GLY ARG
SEQRES 4 C 352 LEU ARG ILE GLY ALA LEU THR ALA ALA THR SER ALA GLY
SEQRES 5 C 352 SER THR LEU GLY GLU HIS HIS PRO HIS LEU THR PRO LEU
SEQRES 6 C 352 ALA HIS ARG VAL VAL GLU PRO THR GLU ALA ALA VAL LEU
SEQRES 7 C 352 GLY GLY HIS ASP ALA VAL PHE LEU ALA LEU PRO HIS GLY
SEQRES 8 C 352 HIS SER ALA VAL LEU ALA GLN GLN LEU SER PRO GLU THR
SEQRES 9 C 352 LEU ILE ILE ASP CYS GLY ALA ASP PHE ARG LEU THR ASP
SEQRES 10 C 352 ALA ALA VAL TRP GLU ARG PHE TYR GLY SER SER HIS ALA
SEQRES 11 C 352 GLY SER TRP PRO TYR GLY LEU PRO GLU LEU PRO GLY ALA
SEQRES 12 C 352 ARG ASP GLN LEU ARG GLY THR ARG ARG ILE ALA VAL PRO
SEQRES 13 C 352 GLY CYS TYR PRO THR ALA ALA LEU LEU ALA LEU PHE PRO
SEQRES 14 C 352 ALA LEU ALA ALA ASP LEU ILE GLU PRO ALA VAL THR VAL
SEQRES 15 C 352 VAL ALA VAL SER GLY THR SER GLY ALA GLY ARG ALA ALA
SEQRES 16 C 352 THR THR ASP LEU LEU GLY ALA GLU VAL ILE GLY SER ALA
SEQRES 17 C 352 ARG ALA TYR ASN ILE ALA GLY VAL HIS ARG HIS THR PRO
SEQRES 18 C 352 GLU ILE ALA GLN GLY LEU ARG ALA VAL THR ASP ARG ASP
SEQRES 19 C 352 VAL SER VAL SER PHE THR PRO VAL LEU ILE PRO ALA SER
SEQRES 20 C 352 ARG GLY ILE LEU ALA THR CYS THR ALA ARG THR ARG SER
SEQRES 21 C 352 PRO LEU SER GLN LEU ARG ALA ALA TYR GLU LYS ALA TYR
SEQRES 22 C 352 HIS ALA GLU PRO PHE ILE TYR LEU MET PRO GLU GLY GLN
SEQRES 23 C 352 LEU PRO ARG THR GLY ALA VAL ILE GLY SER ASN ALA ALA
SEQRES 24 C 352 HIS ILE ALA VAL ALA VAL ASP GLU ASP ALA GLN THR PHE
SEQRES 25 C 352 VAL ALA ILE ALA ALA ILE ASP ASN LEU VAL LYS GLY THR
SEQRES 26 C 352 ALA GLY ALA ALA VAL GLN SER MET ASN LEU ALA LEU GLY
SEQRES 27 C 352 TRP PRO GLU THR ASP GLY LEU SER VAL VAL GLY VAL ALA
SEQRES 28 C 352 PRO
SEQRES 1 D 352 MET GLN ASN ARG GLN VAL ALA ASN ALA THR LYS VAL ALA
SEQRES 2 D 352 VAL ALA GLY ALA SER GLY TYR ALA GLY GLY GLU ILE LEU
SEQRES 3 D 352 ARG LEU LEU LEU GLY HIS PRO ALA TYR ALA ASP GLY ARG
SEQRES 4 D 352 LEU ARG ILE GLY ALA LEU THR ALA ALA THR SER ALA GLY
SEQRES 5 D 352 SER THR LEU GLY GLU HIS HIS PRO HIS LEU THR PRO LEU
SEQRES 6 D 352 ALA HIS ARG VAL VAL GLU PRO THR GLU ALA ALA VAL LEU
SEQRES 7 D 352 GLY GLY HIS ASP ALA VAL PHE LEU ALA LEU PRO HIS GLY
SEQRES 8 D 352 HIS SER ALA VAL LEU ALA GLN GLN LEU SER PRO GLU THR
SEQRES 9 D 352 LEU ILE ILE ASP CYS GLY ALA ASP PHE ARG LEU THR ASP
SEQRES 10 D 352 ALA ALA VAL TRP GLU ARG PHE TYR GLY SER SER HIS ALA
SEQRES 11 D 352 GLY SER TRP PRO TYR GLY LEU PRO GLU LEU PRO GLY ALA
SEQRES 12 D 352 ARG ASP GLN LEU ARG GLY THR ARG ARG ILE ALA VAL PRO
SEQRES 13 D 352 GLY CYS TYR PRO THR ALA ALA LEU LEU ALA LEU PHE PRO
SEQRES 14 D 352 ALA LEU ALA ALA ASP LEU ILE GLU PRO ALA VAL THR VAL
SEQRES 15 D 352 VAL ALA VAL SER GLY THR SER GLY ALA GLY ARG ALA ALA
SEQRES 16 D 352 THR THR ASP LEU LEU GLY ALA GLU VAL ILE GLY SER ALA
SEQRES 17 D 352 ARG ALA TYR ASN ILE ALA GLY VAL HIS ARG HIS THR PRO
SEQRES 18 D 352 GLU ILE ALA GLN GLY LEU ARG ALA VAL THR ASP ARG ASP
SEQRES 19 D 352 VAL SER VAL SER PHE THR PRO VAL LEU ILE PRO ALA SER
SEQRES 20 D 352 ARG GLY ILE LEU ALA THR CYS THR ALA ARG THR ARG SER
SEQRES 21 D 352 PRO LEU SER GLN LEU ARG ALA ALA TYR GLU LYS ALA TYR
SEQRES 22 D 352 HIS ALA GLU PRO PHE ILE TYR LEU MET PRO GLU GLY GLN
SEQRES 23 D 352 LEU PRO ARG THR GLY ALA VAL ILE GLY SER ASN ALA ALA
SEQRES 24 D 352 HIS ILE ALA VAL ALA VAL ASP GLU ASP ALA GLN THR PHE
SEQRES 25 D 352 VAL ALA ILE ALA ALA ILE ASP ASN LEU VAL LYS GLY THR
SEQRES 26 D 352 ALA GLY ALA ALA VAL GLN SER MET ASN LEU ALA LEU GLY
SEQRES 27 D 352 TRP PRO GLU THR ASP GLY LEU SER VAL VAL GLY VAL ALA
SEQRES 28 D 352 PRO
HET BTB A1400 14
HET BTB B1500 14
HET BTB C1600 14
HET BTB D1700 14
HETNAM BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-
HETNAM 2 BTB PROPANE-1,3-DIOL
HETSYN BTB BIS-TRIS BUFFER
FORMUL 5 BTB 4(C8 H19 N O5)
FORMUL 9 HOH *916(H2 O)
HELIX 1 1 GLY A 19 GLY A 31 1 13
HELIX 2 2 HIS A 32 ASP A 37 1 6
HELIX 3 3 THR A 54 HIS A 58 5 5
HELIX 4 4 LEU A 62 ALA A 66 5 5
HELIX 5 5 GLU A 74 GLY A 79 1 6
HELIX 6 6 SER A 93 GLN A 99 1 7
HELIX 7 7 ASP A 117 GLY A 126 1 10
HELIX 8 8 GLY A 142 ARG A 148 1 7
HELIX 9 9 GLY A 157 ALA A 173 1 17
HELIX 10 10 THR A 188 GLY A 192 5 5
HELIX 11 11 THR A 196 LEU A 199 5 4
HELIX 12 12 LEU A 200 ILE A 205 1 6
HELIX 13 13 ARG A 218 ALA A 229 1 12
HELIX 14 14 PRO A 261 HIS A 274 1 14
HELIX 15 15 ARG A 289 VAL A 293 5 5
HELIX 16 16 THR A 325 LEU A 337 1 13
HELIX 17 17 GLY B 19 HIS B 32 1 14
HELIX 18 18 HIS B 32 ASP B 37 1 6
HELIX 19 19 THR B 54 HIS B 58 5 5
HELIX 20 20 LEU B 62 ALA B 66 5 5
HELIX 21 21 GLU B 74 GLY B 79 1 6
HELIX 22 22 HIS B 92 GLN B 99 1 8
HELIX 23 23 ASP B 117 GLY B 126 1 10
HELIX 24 24 GLY B 142 ARG B 148 1 7
HELIX 25 25 GLY B 157 ALA B 173 1 17
HELIX 26 26 THR B 188 GLY B 192 5 5
HELIX 27 27 THR B 196 LEU B 199 5 4
HELIX 28 28 LEU B 200 ILE B 205 1 6
HELIX 29 29 HIS B 219 ALA B 229 1 11
HELIX 30 30 PRO B 261 HIS B 274 1 14
HELIX 31 31 ARG B 289 VAL B 293 5 5
HELIX 32 32 THR B 325 GLY B 338 1 14
HELIX 33 33 GLY C 19 GLY C 31 1 13
HELIX 34 34 HIS C 32 ASP C 37 1 6
HELIX 35 35 THR C 54 HIS C 59 1 6
HELIX 36 36 LEU C 62 ALA C 66 5 5
HELIX 37 37 GLU C 74 GLY C 79 1 6
HELIX 38 38 GLY C 91 LEU C 100 1 10
HELIX 39 39 ASP C 117 GLY C 126 1 10
HELIX 40 40 GLY C 142 ARG C 148 1 7
HELIX 41 41 GLY C 157 ALA C 173 1 17
HELIX 42 42 THR C 188 GLY C 192 5 5
HELIX 43 43 THR C 196 LEU C 199 5 4
HELIX 44 44 LEU C 200 ILE C 205 1 6
HELIX 45 45 HIS C 219 ALA C 229 1 11
HELIX 46 46 PRO C 261 HIS C 274 1 14
HELIX 47 47 ARG C 289 VAL C 293 5 5
HELIX 48 48 THR C 325 GLY C 338 1 14
HELIX 49 49 GLY D 19 GLY D 31 1 13
HELIX 50 50 HIS D 32 ASP D 37 1 6
HELIX 51 51 THR D 54 HIS D 58 5 5
HELIX 52 52 LEU D 62 ALA D 66 5 5
HELIX 53 53 GLU D 74 GLY D 79 1 6
HELIX 54 54 GLY D 91 LEU D 100 1 10
HELIX 55 55 ASP D 117 GLY D 126 1 10
HELIX 56 56 GLY D 142 ARG D 148 1 7
HELIX 57 57 GLY D 157 ALA D 173 1 17
HELIX 58 58 THR D 188 GLY D 192 5 5
HELIX 59 59 THR D 196 LEU D 199 5 4
HELIX 60 60 LEU D 200 ILE D 205 1 6
HELIX 61 61 HIS D 219 ALA D 229 1 11
HELIX 62 62 PRO D 261 HIS D 274 1 14
HELIX 63 63 ARG D 289 ILE D 294 1 6
HELIX 64 64 THR D 325 GLY D 338 1 14
SHEET 1 A 6 GLU A 71 PRO A 72 0
SHEET 2 A 6 LEU A 40 ALA A 47 1 N LEU A 45 O GLU A 71
SHEET 3 A 6 THR A 10 ALA A 15 1 N VAL A 12 O GLY A 43
SHEET 4 A 6 ALA A 83 LEU A 86 1 O PHE A 85 N ALA A 15
SHEET 5 A 6 LEU A 105 ASP A 108 1 O LEU A 105 N VAL A 84
SHEET 6 A 6 ARG A 152 ALA A 154 1 O ILE A 153 N ASP A 108
SHEET 1 B 7 ARG A 209 ALA A 210 0
SHEET 2 B 7 SER A 236 LEU A 243 -1 O LEU A 243 N ARG A 209
SHEET 3 B 7 ALA A 179 SER A 186 1 N VAL A 182 O SER A 238
SHEET 4 B 7 ILE A 250 ARG A 257 -1 O LEU A 251 N VAL A 185
SHEET 5 B 7 THR A 311 ILE A 318 -1 O PHE A 312 N ALA A 256
SHEET 6 B 7 ALA A 299 ASP A 306 -1 N ASP A 306 O THR A 311
SHEET 7 B 7 ILE A 279 LEU A 281 1 N TYR A 280 O ALA A 299
SHEET 1 C 6 GLU B 71 PRO B 72 0
SHEET 2 C 6 LEU B 40 ALA B 47 1 N LEU B 45 O GLU B 71
SHEET 3 C 6 THR B 10 ALA B 15 1 N VAL B 12 O ARG B 41
SHEET 4 C 6 ALA B 83 LEU B 86 1 O PHE B 85 N ALA B 15
SHEET 5 C 6 LEU B 105 ASP B 108 1 O ILE B 107 N VAL B 84
SHEET 6 C 6 ARG B 152 ALA B 154 1 O ILE B 153 N ASP B 108
SHEET 1 D 7 ARG B 209 ALA B 210 0
SHEET 2 D 7 SER B 236 LEU B 243 -1 O LEU B 243 N ARG B 209
SHEET 3 D 7 ALA B 179 SER B 186 1 N VAL B 182 O SER B 238
SHEET 4 D 7 ILE B 250 ARG B 257 -1 O THR B 255 N THR B 181
SHEET 5 D 7 THR B 311 ILE B 318 -1 O ALA B 314 N CYS B 254
SHEET 6 D 7 ALA B 299 ASP B 306 -1 N ASP B 306 O THR B 311
SHEET 7 D 7 ILE B 279 LEU B 281 1 N TYR B 280 O ALA B 299
SHEET 1 E 5 LEU C 40 THR C 46 0
SHEET 2 E 5 THR C 10 ALA C 15 1 N VAL C 12 O GLY C 43
SHEET 3 E 5 ALA C 83 LEU C 86 1 O PHE C 85 N ALA C 15
SHEET 4 E 5 LEU C 105 ASP C 108 1 O ILE C 107 N VAL C 84
SHEET 5 E 5 ARG C 152 ALA C 154 1 O ILE C 153 N ASP C 108
SHEET 1 F 7 ARG C 209 ALA C 210 0
SHEET 2 F 7 SER C 236 LEU C 243 -1 O LEU C 243 N ARG C 209
SHEET 3 F 7 ALA C 179 SER C 186 1 N VAL C 182 O SER C 238
SHEET 4 F 7 ILE C 250 ARG C 257 -1 O THR C 253 N VAL C 183
SHEET 5 F 7 THR C 311 ILE C 318 -1 O PHE C 312 N ALA C 256
SHEET 6 F 7 ALA C 299 ASP C 306 -1 N ASP C 306 O THR C 311
SHEET 7 F 7 ILE C 279 LEU C 281 1 N TYR C 280 O ILE C 301
SHEET 1 G 5 LEU D 40 THR D 46 0
SHEET 2 G 5 THR D 10 ALA D 15 1 N VAL D 12 O GLY D 43
SHEET 3 G 5 ALA D 83 LEU D 86 1 O PHE D 85 N ALA D 15
SHEET 4 G 5 LEU D 105 ASP D 108 1 O LEU D 105 N VAL D 84
SHEET 5 G 5 ARG D 152 ALA D 154 1 O ILE D 153 N ASP D 108
SHEET 1 H 7 ARG D 209 ALA D 210 0
SHEET 2 H 7 SER D 236 LEU D 243 -1 O LEU D 243 N ARG D 209
SHEET 3 H 7 ALA D 179 SER D 186 1 N VAL D 182 O THR D 240
SHEET 4 H 7 ILE D 250 ARG D 257 -1 O THR D 253 N VAL D 183
SHEET 5 H 7 THR D 311 ILE D 318 -1 O PHE D 312 N ALA D 256
SHEET 6 H 7 ALA D 299 ASP D 306 -1 N ASP D 306 O THR D 311
SHEET 7 H 7 ILE D 279 LEU D 281 1 N TYR D 280 O ALA D 299
CISPEP 1 ALA A 351 PRO A 352 0 -7.84
CISPEP 2 ALA B 351 PRO B 352 0 1.14
CISPEP 3 ALA C 351 PRO C 352 0 -3.99
CISPEP 4 ALA D 351 PRO D 352 0 -3.39
SITE 1 AC1 7 HIS A 32 ALA A 34 ASP A 37 ARG A 39
SITE 2 AC1 7 TRP A 339 PRO A 340 ASP A 343
SITE 1 AC2 7 HIS B 32 ALA B 34 ASP B 37 ARG B 39
SITE 2 AC2 7 TRP B 339 PRO B 340 ASP B 343
SITE 1 AC3 6 HIS C 32 ALA C 34 ASP C 37 ARG C 39
SITE 2 AC3 6 TRP C 339 ASP C 343
SITE 1 AC4 5 HIS D 32 ALA D 34 ASP D 37 ARG D 39
SITE 2 AC4 5 ASP D 343
CRYST1 89.695 104.031 138.435 90.00 90.00 90.00 P 21 21 21 16
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 0.011149 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009613 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007224 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
