HEADER OXIDOREDUCTASE 03-JUL-08 3DOC
TITLE CRYSTAL STRUCTURE OF TRKA GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE
TITLE 2 FROM BRUCELLA MELITENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BRUCELLA MELITENSIS BIOVAR ABORTUS 2308;
SOURCE 3 ORGANISM_TAXID: 359391;
SOURCE 4 STRAIN: BIOVAR ABORTUS 2308;
SOURCE 5 GENE: TRKA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PBADSMT
KEYWDS SSGCID, BRUCELLA, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS
KEYWDS 3 DISEASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 4 30-AUG-23 3DOC 1 REMARK
REVDAT 3 25-OCT-17 3DOC 1 REMARK
REVDAT 2 24-FEB-09 3DOC 1 VERSN
REVDAT 1 29-JUL-08 3DOC 0
JRNL AUTH SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE
JRNL AUTH 2 (SSGCID)
JRNL TITL CRYSTAL STRUCTURE OF TRKA GLYCERALDEHYDE-3-PHOSPHATE
JRNL TITL 2 DEHYDROGENASE FROM BRUCELLA MELITENSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.4.0067
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 49077
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2471
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.47
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3018
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 163
REMARK 3 BIN FREE R VALUE : 0.2760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10164
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 176
REMARK 3 SOLVENT ATOMS : 521
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.44000
REMARK 3 B22 (A**2) : 0.24000
REMARK 3 B33 (A**2) : -0.67000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.848
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.268
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.179
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.786
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10528 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14349 ; 1.467 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1335 ; 6.232 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 435 ;38.003 ;24.023
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1723 ;19.308 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 72 ;19.712 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1707 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7812 ; 0.005 ; 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): 6639 ; 0.524 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10736 ; 0.998 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3889 ; 1.578 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3613 ; 2.561 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3DOC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048286.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9774
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49106
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.15000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.44400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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: 1OBF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: JCSG+ SCREEN WELL B2, 20% PEG 3350,
REMARK 280 0.2 M SODIUM ISOTHIOCYANATE, , PH 6.9, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 289K
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 53.16650
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, 3, 4, 5
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -136.0 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: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 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 D 1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 143 CG CD CE NZ
REMARK 470 GLU B 61 CG CD OE1 OE2
REMARK 470 LYS B 88 CG CD CE NZ
REMARK 470 LYS B 143 CG CD CE NZ
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 NH2 ARG B 105 OD1 ASP B 129 1.33
REMARK 500 NH2 ARG A 198 NH1 ARG A 234 1.88
REMARK 500 OE1 GLN A 163 NH2 ARG A 269 1.96
REMARK 500 OE1 GLN B 163 NH2 ARG B 269 2.02
REMARK 500 NH2 ARG B 105 CG ASP B 129 2.10
REMARK 500 O HOH A 905 O HOH D 975 2.11
REMARK 500 O ALA C 63 OG1 THR C 66 2.12
REMARK 500 CG2 VAL B 3 O HOH B 975 2.18
REMARK 500 N ILE A 13 O2N NAD A 901 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 90 CB GLU A 90 CG -0.149
REMARK 500 GLU A 97 CD GLU A 97 OE1 -0.079
REMARK 500 ASN A 138 CB ASN A 138 CG -0.155
REMARK 500 TYR A 197 CD1 TYR A 197 CE1 -0.093
REMARK 500 ILE A 335 C ILE A 335 OXT -0.274
REMARK 500 GLU B 317 CD GLU B 317 OE2 -0.068
REMARK 500 VAL C 240 CB VAL C 240 CG1 -0.129
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 LEU A 219 CA - CB - CG ANGL. DEV. = 21.3 DEGREES
REMARK 500 ARG B 105 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG C 19 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP D 68 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP D 244 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 ASP A 65 37.61 -80.36
REMARK 500 TYR A 71 19.77 -141.16
REMARK 500 PRO A 82 0.68 -67.24
REMARK 500 SER A 122 33.78 -91.17
REMARK 500 ALA A 151 -148.02 63.63
REMARK 500 MET A 192 130.49 -32.57
REMARK 500 PRO A 236 62.55 -65.75
REMARK 500 VAL A 240 127.45 89.70
REMARK 500 HIS A 288 30.83 72.53
REMARK 500 PHE B 10 55.16 -96.16
REMARK 500 ASP B 36 -156.27 -159.52
REMARK 500 PRO B 57 20.66 -74.65
REMARK 500 ALA B 78 51.20 -147.76
REMARK 500 PRO B 86 45.40 -86.21
REMARK 500 SER B 122 35.89 -82.06
REMARK 500 ASN B 137 22.94 -141.38
REMARK 500 ALA B 151 -160.43 66.52
REMARK 500 LYS B 173 137.94 -177.27
REMARK 500 THR B 191 156.43 179.57
REMARK 500 MET B 192 129.72 -31.30
REMARK 500 PRO B 236 57.01 -69.12
REMARK 500 VAL B 240 130.31 89.02
REMARK 500 HIS B 288 14.65 80.35
REMARK 500 PHE C 10 52.52 -106.05
REMARK 500 ASP C 36 -158.09 -150.72
REMARK 500 ASP C 65 41.41 -101.68
REMARK 500 SER C 122 40.26 -79.40
REMARK 500 VAL C 136 -50.82 -121.25
REMARK 500 ALA C 151 -160.73 64.74
REMARK 500 VAL C 240 131.89 86.49
REMARK 500 SER C 293 122.97 -173.94
REMARK 500 ASP D 36 -156.34 -147.80
REMARK 500 TYR D 71 41.92 -144.87
REMARK 500 PRO D 86 49.12 -84.56
REMARK 500 ASN D 91 64.13 60.40
REMARK 500 SER D 122 49.14 -85.36
REMARK 500 ALA D 123 170.40 176.18
REMARK 500 ASN D 137 18.31 -144.43
REMARK 500 ALA D 151 -167.15 64.80
REMARK 500 LYS D 173 133.05 -175.80
REMARK 500 MET D 192 126.51 -35.78
REMARK 500 PRO D 236 66.99 -66.77
REMARK 500 VAL D 240 131.12 97.70
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 NAD A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 901
DBREF 3DOC A 1 335 PDB 3DOC 3DOC 1 335
DBREF 3DOC B 1 335 PDB 3DOC 3DOC 1 335
DBREF 3DOC C 1 335 PDB 3DOC 3DOC 1 335
DBREF 3DOC D 1 335 PDB 3DOC 3DOC 1 335
SEQRES 1 A 335 MET ALA VAL ARG VAL ALA ILE ASN GLY PHE GLY ARG ILE
SEQRES 2 A 335 GLY ARG ASN ILE LEU ARG ALA ILE VAL GLU SER GLY ARG
SEQRES 3 A 335 THR ASP ILE GLN VAL VAL ALA ILE ASN ASP LEU GLY PRO
SEQRES 4 A 335 VAL GLU THR ASN ALA HIS LEU LEU ARG TYR ASP SER VAL
SEQRES 5 A 335 HIS GLY ARG PHE PRO LYS GLU VAL GLU VAL ALA GLY ASP
SEQRES 6 A 335 THR ILE ASP VAL GLY TYR GLY PRO ILE LYS VAL HIS ALA
SEQRES 7 A 335 VAL ARG ASN PRO ALA GLU LEU PRO TRP LYS GLU GLU ASN
SEQRES 8 A 335 VAL ASP ILE ALA LEU GLU CYS THR GLY ILE PHE THR SER
SEQRES 9 A 335 ARG ASP LYS ALA ALA LEU HIS LEU GLU ALA GLY ALA LYS
SEQRES 10 A 335 ARG VAL ILE VAL SER ALA PRO ALA ASP GLY ALA ASP LEU
SEQRES 11 A 335 THR VAL VAL TYR GLY VAL ASN ASN ASP LYS LEU THR LYS
SEQRES 12 A 335 ASP HIS LEU VAL ILE SER ASN ALA SER CYS THR THR ASN
SEQRES 13 A 335 CYS LEU ALA PRO VAL ALA GLN VAL LEU ASN ASP THR ILE
SEQRES 14 A 335 GLY ILE GLU LYS GLY PHE MET THR THR ILE HIS SER TYR
SEQRES 15 A 335 THR GLY ASP GLN PRO THR LEU ASP THR MET HIS LYS ASP
SEQRES 16 A 335 LEU TYR ARG ALA ARG ALA ALA ALA LEU SER MET ILE PRO
SEQRES 17 A 335 THR SER THR GLY ALA ALA LYS ALA VAL GLY LEU VAL LEU
SEQRES 18 A 335 PRO GLU LEU LYS GLY LYS LEU ASP GLY VAL ALA ILE ARG
SEQRES 19 A 335 VAL PRO THR PRO ASN VAL SER VAL VAL ASP LEU THR PHE
SEQRES 20 A 335 ILE ALA LYS ARG GLU THR THR VAL GLU GLU VAL ASN ASN
SEQRES 21 A 335 ALA ILE ARG GLU ALA ALA ASN GLY ARG LEU LYS GLY ILE
SEQRES 22 A 335 LEU GLY TYR THR ASP GLU LYS LEU VAL SER HIS ASP PHE
SEQRES 23 A 335 ASN HIS ASP SER HIS SER SER VAL PHE HIS THR ASP GLN
SEQRES 24 A 335 THR LYS VAL MET ASP GLY THR MET VAL ARG ILE LEU SER
SEQRES 25 A 335 TRP TYR ASP ASN GLU TRP GLY PHE SER SER ARG MET SER
SEQRES 26 A 335 ASP THR ALA VAL ALA LEU GLY LYS LEU ILE
SEQRES 1 B 335 MET ALA VAL ARG VAL ALA ILE ASN GLY PHE GLY ARG ILE
SEQRES 2 B 335 GLY ARG ASN ILE LEU ARG ALA ILE VAL GLU SER GLY ARG
SEQRES 3 B 335 THR ASP ILE GLN VAL VAL ALA ILE ASN ASP LEU GLY PRO
SEQRES 4 B 335 VAL GLU THR ASN ALA HIS LEU LEU ARG TYR ASP SER VAL
SEQRES 5 B 335 HIS GLY ARG PHE PRO LYS GLU VAL GLU VAL ALA GLY ASP
SEQRES 6 B 335 THR ILE ASP VAL GLY TYR GLY PRO ILE LYS VAL HIS ALA
SEQRES 7 B 335 VAL ARG ASN PRO ALA GLU LEU PRO TRP LYS GLU GLU ASN
SEQRES 8 B 335 VAL ASP ILE ALA LEU GLU CYS THR GLY ILE PHE THR SER
SEQRES 9 B 335 ARG ASP LYS ALA ALA LEU HIS LEU GLU ALA GLY ALA LYS
SEQRES 10 B 335 ARG VAL ILE VAL SER ALA PRO ALA ASP GLY ALA ASP LEU
SEQRES 11 B 335 THR VAL VAL TYR GLY VAL ASN ASN ASP LYS LEU THR LYS
SEQRES 12 B 335 ASP HIS LEU VAL ILE SER ASN ALA SER CYS THR THR ASN
SEQRES 13 B 335 CYS LEU ALA PRO VAL ALA GLN VAL LEU ASN ASP THR ILE
SEQRES 14 B 335 GLY ILE GLU LYS GLY PHE MET THR THR ILE HIS SER TYR
SEQRES 15 B 335 THR GLY ASP GLN PRO THR LEU ASP THR MET HIS LYS ASP
SEQRES 16 B 335 LEU TYR ARG ALA ARG ALA ALA ALA LEU SER MET ILE PRO
SEQRES 17 B 335 THR SER THR GLY ALA ALA LYS ALA VAL GLY LEU VAL LEU
SEQRES 18 B 335 PRO GLU LEU LYS GLY LYS LEU ASP GLY VAL ALA ILE ARG
SEQRES 19 B 335 VAL PRO THR PRO ASN VAL SER VAL VAL ASP LEU THR PHE
SEQRES 20 B 335 ILE ALA LYS ARG GLU THR THR VAL GLU GLU VAL ASN ASN
SEQRES 21 B 335 ALA ILE ARG GLU ALA ALA ASN GLY ARG LEU LYS GLY ILE
SEQRES 22 B 335 LEU GLY TYR THR ASP GLU LYS LEU VAL SER HIS ASP PHE
SEQRES 23 B 335 ASN HIS ASP SER HIS SER SER VAL PHE HIS THR ASP GLN
SEQRES 24 B 335 THR LYS VAL MET ASP GLY THR MET VAL ARG ILE LEU SER
SEQRES 25 B 335 TRP TYR ASP ASN GLU TRP GLY PHE SER SER ARG MET SER
SEQRES 26 B 335 ASP THR ALA VAL ALA LEU GLY LYS LEU ILE
SEQRES 1 C 335 MET ALA VAL ARG VAL ALA ILE ASN GLY PHE GLY ARG ILE
SEQRES 2 C 335 GLY ARG ASN ILE LEU ARG ALA ILE VAL GLU SER GLY ARG
SEQRES 3 C 335 THR ASP ILE GLN VAL VAL ALA ILE ASN ASP LEU GLY PRO
SEQRES 4 C 335 VAL GLU THR ASN ALA HIS LEU LEU ARG TYR ASP SER VAL
SEQRES 5 C 335 HIS GLY ARG PHE PRO LYS GLU VAL GLU VAL ALA GLY ASP
SEQRES 6 C 335 THR ILE ASP VAL GLY TYR GLY PRO ILE LYS VAL HIS ALA
SEQRES 7 C 335 VAL ARG ASN PRO ALA GLU LEU PRO TRP LYS GLU GLU ASN
SEQRES 8 C 335 VAL ASP ILE ALA LEU GLU CYS THR GLY ILE PHE THR SER
SEQRES 9 C 335 ARG ASP LYS ALA ALA LEU HIS LEU GLU ALA GLY ALA LYS
SEQRES 10 C 335 ARG VAL ILE VAL SER ALA PRO ALA ASP GLY ALA ASP LEU
SEQRES 11 C 335 THR VAL VAL TYR GLY VAL ASN ASN ASP LYS LEU THR LYS
SEQRES 12 C 335 ASP HIS LEU VAL ILE SER ASN ALA SER CYS THR THR ASN
SEQRES 13 C 335 CYS LEU ALA PRO VAL ALA GLN VAL LEU ASN ASP THR ILE
SEQRES 14 C 335 GLY ILE GLU LYS GLY PHE MET THR THR ILE HIS SER TYR
SEQRES 15 C 335 THR GLY ASP GLN PRO THR LEU ASP THR MET HIS LYS ASP
SEQRES 16 C 335 LEU TYR ARG ALA ARG ALA ALA ALA LEU SER MET ILE PRO
SEQRES 17 C 335 THR SER THR GLY ALA ALA LYS ALA VAL GLY LEU VAL LEU
SEQRES 18 C 335 PRO GLU LEU LYS GLY LYS LEU ASP GLY VAL ALA ILE ARG
SEQRES 19 C 335 VAL PRO THR PRO ASN VAL SER VAL VAL ASP LEU THR PHE
SEQRES 20 C 335 ILE ALA LYS ARG GLU THR THR VAL GLU GLU VAL ASN ASN
SEQRES 21 C 335 ALA ILE ARG GLU ALA ALA ASN GLY ARG LEU LYS GLY ILE
SEQRES 22 C 335 LEU GLY TYR THR ASP GLU LYS LEU VAL SER HIS ASP PHE
SEQRES 23 C 335 ASN HIS ASP SER HIS SER SER VAL PHE HIS THR ASP GLN
SEQRES 24 C 335 THR LYS VAL MET ASP GLY THR MET VAL ARG ILE LEU SER
SEQRES 25 C 335 TRP TYR ASP ASN GLU TRP GLY PHE SER SER ARG MET SER
SEQRES 26 C 335 ASP THR ALA VAL ALA LEU GLY LYS LEU ILE
SEQRES 1 D 335 MET ALA VAL ARG VAL ALA ILE ASN GLY PHE GLY ARG ILE
SEQRES 2 D 335 GLY ARG ASN ILE LEU ARG ALA ILE VAL GLU SER GLY ARG
SEQRES 3 D 335 THR ASP ILE GLN VAL VAL ALA ILE ASN ASP LEU GLY PRO
SEQRES 4 D 335 VAL GLU THR ASN ALA HIS LEU LEU ARG TYR ASP SER VAL
SEQRES 5 D 335 HIS GLY ARG PHE PRO LYS GLU VAL GLU VAL ALA GLY ASP
SEQRES 6 D 335 THR ILE ASP VAL GLY TYR GLY PRO ILE LYS VAL HIS ALA
SEQRES 7 D 335 VAL ARG ASN PRO ALA GLU LEU PRO TRP LYS GLU GLU ASN
SEQRES 8 D 335 VAL ASP ILE ALA LEU GLU CYS THR GLY ILE PHE THR SER
SEQRES 9 D 335 ARG ASP LYS ALA ALA LEU HIS LEU GLU ALA GLY ALA LYS
SEQRES 10 D 335 ARG VAL ILE VAL SER ALA PRO ALA ASP GLY ALA ASP LEU
SEQRES 11 D 335 THR VAL VAL TYR GLY VAL ASN ASN ASP LYS LEU THR LYS
SEQRES 12 D 335 ASP HIS LEU VAL ILE SER ASN ALA SER CYS THR THR ASN
SEQRES 13 D 335 CYS LEU ALA PRO VAL ALA GLN VAL LEU ASN ASP THR ILE
SEQRES 14 D 335 GLY ILE GLU LYS GLY PHE MET THR THR ILE HIS SER TYR
SEQRES 15 D 335 THR GLY ASP GLN PRO THR LEU ASP THR MET HIS LYS ASP
SEQRES 16 D 335 LEU TYR ARG ALA ARG ALA ALA ALA LEU SER MET ILE PRO
SEQRES 17 D 335 THR SER THR GLY ALA ALA LYS ALA VAL GLY LEU VAL LEU
SEQRES 18 D 335 PRO GLU LEU LYS GLY LYS LEU ASP GLY VAL ALA ILE ARG
SEQRES 19 D 335 VAL PRO THR PRO ASN VAL SER VAL VAL ASP LEU THR PHE
SEQRES 20 D 335 ILE ALA LYS ARG GLU THR THR VAL GLU GLU VAL ASN ASN
SEQRES 21 D 335 ALA ILE ARG GLU ALA ALA ASN GLY ARG LEU LYS GLY ILE
SEQRES 22 D 335 LEU GLY TYR THR ASP GLU LYS LEU VAL SER HIS ASP PHE
SEQRES 23 D 335 ASN HIS ASP SER HIS SER SER VAL PHE HIS THR ASP GLN
SEQRES 24 D 335 THR LYS VAL MET ASP GLY THR MET VAL ARG ILE LEU SER
SEQRES 25 D 335 TRP TYR ASP ASN GLU TRP GLY PHE SER SER ARG MET SER
SEQRES 26 D 335 ASP THR ALA VAL ALA LEU GLY LYS LEU ILE
HET NAD A 901 44
HET NAD B 901 44
HET NAD C 901 44
HET NAD D 901 44
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
FORMUL 5 NAD 4(C21 H27 N7 O14 P2)
FORMUL 9 HOH *521(H2 O)
HELIX 1 1 GLY A 11 SER A 24 1 14
HELIX 2 2 PRO A 39 ARG A 48 1 10
HELIX 3 3 SER A 104 ALA A 109 1 6
HELIX 4 4 ALA A 109 ALA A 114 1 6
HELIX 5 5 ASN A 137 LEU A 141 5 5
HELIX 6 6 SER A 152 ILE A 169 1 18
HELIX 7 7 GLY A 212 LEU A 221 1 10
HELIX 8 8 PRO A 222 LYS A 225 5 4
HELIX 9 9 THR A 254 ASN A 267 1 14
HELIX 10 10 VAL A 282 ASN A 287 5 6
HELIX 11 11 ASP A 298 THR A 300 5 3
HELIX 12 12 GLU A 317 LEU A 334 1 18
HELIX 13 13 GLY B 11 GLY B 25 1 15
HELIX 14 14 PRO B 39 TYR B 49 1 11
HELIX 15 15 ASN B 81 LEU B 85 5 5
HELIX 16 16 SER B 104 ALA B 109 1 6
HELIX 17 17 ALA B 109 ALA B 114 1 6
HELIX 18 18 ASN B 137 LEU B 141 5 5
HELIX 19 19 SER B 152 ILE B 169 1 18
HELIX 20 20 ALA B 216 LEU B 221 1 6
HELIX 21 21 PRO B 222 LYS B 225 5 4
HELIX 22 22 THR B 254 ASN B 267 1 14
HELIX 23 23 VAL B 282 ASN B 287 5 6
HELIX 24 24 ASP B 298 THR B 300 5 3
HELIX 25 25 GLU B 317 ILE B 335 1 19
HELIX 26 26 GLY C 11 GLY C 25 1 15
HELIX 27 27 PRO C 39 TYR C 49 1 11
HELIX 28 28 ASN C 81 LEU C 85 5 5
HELIX 29 29 SER C 104 ALA C 109 1 6
HELIX 30 30 ALA C 109 GLY C 115 1 7
HELIX 31 31 ASN C 137 LEU C 141 5 5
HELIX 32 32 SER C 152 GLY C 170 1 19
HELIX 33 33 GLY C 212 GLY C 218 1 7
HELIX 34 34 LEU C 219 VAL C 220 5 2
HELIX 35 35 LEU C 221 LYS C 225 5 5
HELIX 36 36 THR C 254 GLY C 268 1 15
HELIX 37 37 VAL C 282 ASN C 287 5 6
HELIX 38 38 ASP C 298 THR C 300 5 3
HELIX 39 39 GLU C 317 LEU C 334 1 18
HELIX 40 40 GLY D 11 GLY D 25 1 15
HELIX 41 41 PRO D 39 TYR D 49 1 11
HELIX 42 42 ASN D 81 LEU D 85 5 5
HELIX 43 43 PRO D 86 ASN D 91 1 6
HELIX 44 44 SER D 104 ALA D 109 1 6
HELIX 45 45 ALA D 109 GLY D 115 1 7
HELIX 46 46 ASN D 137 LEU D 141 5 5
HELIX 47 47 SER D 152 ILE D 169 1 18
HELIX 48 48 GLY D 212 LEU D 221 1 10
HELIX 49 49 PRO D 222 LYS D 225 5 4
HELIX 50 50 THR D 254 GLY D 268 1 15
HELIX 51 51 VAL D 282 ASN D 287 5 6
HELIX 52 52 ASP D 298 THR D 300 5 3
HELIX 53 53 GLU D 317 LYS D 333 1 17
SHEET 1 A 9 GLU A 61 VAL A 62 0
SHEET 2 A 9 THR A 66 ASP A 68 -1 O ASP A 68 N GLU A 61
SHEET 3 A 9 PRO A 73 HIS A 77 -1 O ILE A 74 N ILE A 67
SHEET 4 A 9 ILE A 29 ASN A 35 1 N ILE A 34 O HIS A 77
SHEET 5 A 9 VAL A 3 ASN A 8 1 N VAL A 5 O GLN A 30
SHEET 6 A 9 ILE A 94 GLU A 97 1 O LEU A 96 N ALA A 6
SHEET 7 A 9 ARG A 118 VAL A 121 1 O ILE A 120 N GLU A 97
SHEET 8 A 9 VAL A 147 SER A 149 1 O ILE A 148 N VAL A 121
SHEET 9 A 9 LEU A 130 THR A 131 1 N LEU A 130 O SER A 149
SHEET 1 B 2 TYR A 49 ASP A 50 0
SHEET 2 B 2 GLY A 54 ARG A 55 -1 O GLY A 54 N ASP A 50
SHEET 1 C 7 ILE A 207 SER A 210 0
SHEET 2 C 7 LEU A 228 VAL A 235 -1 O ARG A 234 N ILE A 207
SHEET 3 C 7 ILE A 171 SER A 181 1 N MET A 176 O ASP A 229
SHEET 4 C 7 SER A 241 ALA A 249 -1 O THR A 246 N PHE A 175
SHEET 5 C 7 MET A 307 TYR A 314 -1 O TYR A 314 N SER A 241
SHEET 6 C 7 SER A 293 HIS A 296 -1 N HIS A 296 O LEU A 311
SHEET 7 C 7 LEU A 274 THR A 277 1 N THR A 277 O PHE A 295
SHEET 1 D 6 ILE A 207 SER A 210 0
SHEET 2 D 6 LEU A 228 VAL A 235 -1 O ARG A 234 N ILE A 207
SHEET 3 D 6 ILE A 171 SER A 181 1 N MET A 176 O ASP A 229
SHEET 4 D 6 SER A 241 ALA A 249 -1 O THR A 246 N PHE A 175
SHEET 5 D 6 MET A 307 TYR A 314 -1 O TYR A 314 N SER A 241
SHEET 6 D 6 LYS A 301 MET A 303 -1 N LYS A 301 O ARG A 309
SHEET 1 E 8 GLU B 61 VAL B 62 0
SHEET 2 E 8 THR B 66 ASP B 68 -1 O ASP B 68 N GLU B 61
SHEET 3 E 8 PRO B 73 HIS B 77 -1 O ILE B 74 N ILE B 67
SHEET 4 E 8 ILE B 29 ASN B 35 1 N ILE B 34 O HIS B 77
SHEET 5 E 8 VAL B 3 ASN B 8 1 N VAL B 5 O VAL B 32
SHEET 6 E 8 ILE B 94 GLU B 97 1 O LEU B 96 N ALA B 6
SHEET 7 E 8 VAL B 119 VAL B 121 1 O ILE B 120 N GLU B 97
SHEET 8 E 8 VAL B 147 SER B 149 1 O ILE B 148 N VAL B 121
SHEET 1 F 7 ILE B 207 THR B 209 0
SHEET 2 F 7 LEU B 228 VAL B 235 -1 O ARG B 234 N ILE B 207
SHEET 3 F 7 ILE B 171 SER B 181 1 N MET B 176 O ASP B 229
SHEET 4 F 7 SER B 241 ALA B 249 -1 O ILE B 248 N LYS B 173
SHEET 5 F 7 MET B 307 TYR B 314 -1 O SER B 312 N VAL B 243
SHEET 6 F 7 SER B 293 HIS B 296 -1 N VAL B 294 O TRP B 313
SHEET 7 F 7 LEU B 274 THR B 277 1 N GLY B 275 O SER B 293
SHEET 1 G 6 ILE B 207 THR B 209 0
SHEET 2 G 6 LEU B 228 VAL B 235 -1 O ARG B 234 N ILE B 207
SHEET 3 G 6 ILE B 171 SER B 181 1 N MET B 176 O ASP B 229
SHEET 4 G 6 SER B 241 ALA B 249 -1 O ILE B 248 N LYS B 173
SHEET 5 G 6 MET B 307 TYR B 314 -1 O SER B 312 N VAL B 243
SHEET 6 G 6 LYS B 301 MET B 303 -1 N MET B 303 O MET B 307
SHEET 1 H 9 GLU C 61 ALA C 63 0
SHEET 2 H 9 THR C 66 ASP C 68 -1 O ASP C 68 N GLU C 61
SHEET 3 H 9 PRO C 73 HIS C 77 -1 O ILE C 74 N ILE C 67
SHEET 4 H 9 ILE C 29 ASN C 35 1 N ILE C 34 O HIS C 77
SHEET 5 H 9 VAL C 3 ASN C 8 1 N ILE C 7 O ALA C 33
SHEET 6 H 9 ILE C 94 GLU C 97 1 O LEU C 96 N ALA C 6
SHEET 7 H 9 ARG C 118 VAL C 121 1 O ARG C 118 N ALA C 95
SHEET 8 H 9 VAL C 147 SER C 149 1 O ILE C 148 N VAL C 121
SHEET 9 H 9 LEU C 130 THR C 131 1 N LEU C 130 O SER C 149
SHEET 1 I 7 ILE C 207 THR C 209 0
SHEET 2 I 7 LEU C 228 VAL C 235 -1 O ALA C 232 N THR C 209
SHEET 3 I 7 ILE C 171 SER C 181 1 N MET C 176 O ASP C 229
SHEET 4 I 7 SER C 241 ALA C 249 -1 O THR C 246 N PHE C 175
SHEET 5 I 7 MET C 307 TYR C 314 -1 O VAL C 308 N PHE C 247
SHEET 6 I 7 SER C 293 HIS C 296 -1 N HIS C 296 O LEU C 311
SHEET 7 I 7 LEU C 274 THR C 277 1 N GLY C 275 O SER C 293
SHEET 1 J 6 ILE C 207 THR C 209 0
SHEET 2 J 6 LEU C 228 VAL C 235 -1 O ALA C 232 N THR C 209
SHEET 3 J 6 ILE C 171 SER C 181 1 N MET C 176 O ASP C 229
SHEET 4 J 6 SER C 241 ALA C 249 -1 O THR C 246 N PHE C 175
SHEET 5 J 6 MET C 307 TYR C 314 -1 O VAL C 308 N PHE C 247
SHEET 6 J 6 LYS C 301 MET C 303 -1 N MET C 303 O MET C 307
SHEET 1 K 8 GLU D 61 ALA D 63 0
SHEET 2 K 8 THR D 66 ASP D 68 -1 O ASP D 68 N GLU D 61
SHEET 3 K 8 PRO D 73 HIS D 77 -1 O ILE D 74 N ILE D 67
SHEET 4 K 8 ILE D 29 ASN D 35 1 N ILE D 34 O HIS D 77
SHEET 5 K 8 VAL D 3 ASN D 8 1 N VAL D 5 O GLN D 30
SHEET 6 K 8 ILE D 94 GLU D 97 1 O LEU D 96 N ALA D 6
SHEET 7 K 8 ARG D 118 VAL D 121 1 O ILE D 120 N ALA D 95
SHEET 8 K 8 VAL D 147 SER D 149 1 O ILE D 148 N VAL D 121
SHEET 1 L 7 ILE D 207 THR D 209 0
SHEET 2 L 7 LEU D 228 VAL D 235 -1 O ARG D 234 N ILE D 207
SHEET 3 L 7 ILE D 171 SER D 181 1 N MET D 176 O ASP D 229
SHEET 4 L 7 SER D 241 ALA D 249 -1 O THR D 246 N PHE D 175
SHEET 5 L 7 MET D 307 TYR D 314 -1 O TYR D 314 N SER D 241
SHEET 6 L 7 SER D 293 HIS D 296 -1 N VAL D 294 O TRP D 313
SHEET 7 L 7 LEU D 274 THR D 277 1 N GLY D 275 O SER D 293
SHEET 1 M 6 ILE D 207 THR D 209 0
SHEET 2 M 6 LEU D 228 VAL D 235 -1 O ARG D 234 N ILE D 207
SHEET 3 M 6 ILE D 171 SER D 181 1 N MET D 176 O ASP D 229
SHEET 4 M 6 SER D 241 ALA D 249 -1 O THR D 246 N PHE D 175
SHEET 5 M 6 MET D 307 TYR D 314 -1 O TYR D 314 N SER D 241
SHEET 6 M 6 LYS D 301 MET D 303 -1 N MET D 303 O MET D 307
SITE 1 AC1 12 GLY A 9 PHE A 10 GLY A 11 ARG A 12
SITE 2 AC1 12 ILE A 13 ASP A 36 SER A 122 ALA A 123
SITE 3 AC1 12 CYS A 153 ASN A 316 GLU A 317 PHE A 320
SITE 1 AC2 14 GLY B 9 GLY B 11 ARG B 12 ILE B 13
SITE 2 AC2 14 ASN B 35 ASP B 36 ARG B 80 CYS B 98
SITE 3 AC2 14 THR B 99 GLY B 100 SER B 122 ALA B 123
SITE 4 AC2 14 CYS B 153 ASN B 316
SITE 1 AC3 14 GLY D 9 GLY D 11 ARG D 12 ILE D 13
SITE 2 AC3 14 ASN D 35 ASP D 36 LEU D 37 ARG D 80
SITE 3 AC3 14 CYS D 98 THR D 99 GLY D 100 SER D 122
SITE 4 AC3 14 ALA D 123 ASN D 316
SITE 1 AC4 15 GLY C 9 GLY C 11 ARG C 12 ILE C 13
SITE 2 AC4 15 ASN C 35 ASP C 36 LEU C 37 ARG C 80
SITE 3 AC4 15 CYS C 98 THR C 99 GLY C 100 SER C 122
SITE 4 AC4 15 ALA C 123 CYS C 153 ASN C 316
CRYST1 71.975 106.333 90.776 90.00 107.89 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 0.013894 0.000000 0.004485 0.00000
SCALE2 0.000000 0.009404 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011576 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
