HEADER OXIDOREDUCTASE 21-JUL-18 6ABI
TITLE THE APO-STRUCTURE OF D-LACTATE DEHYDROGENASE FROM FUSOBACTERIUM
TITLE 2 NUCLEATUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: D-LACTATE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.1.1.28;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FUSOBACTERIUM NUCLEATUM SUBSP. NUCLEATUM
SOURCE 3 (STRAIN ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131);
SOURCE 4 ORGANISM_TAXID: 190304;
SOURCE 5 STRAIN: ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131;
SOURCE 6 ATCC: 25586;
SOURCE 7 GENE: FN0511;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_VARIANT: ROSETTA2 (DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PCOLDI
KEYWDS ROSSMANN FOLD, DEHYDROGENASE, NADH BINDING, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.FURUKAWA,A.MIYANAGA,M.NAKAJIMA,H.TAGUCHI
REVDAT 4 22-NOV-23 6ABI 1 REMARK
REVDAT 3 27-APR-22 6ABI 1 REMARK
REVDAT 2 26-SEP-18 6ABI 1 JRNL
REVDAT 1 19-SEP-18 6ABI 0
SPRSDE 19-SEP-18 6ABI 3WWY
JRNL AUTH N.FURUKAWA,A.MIYANAGA,M.NAKAJIMA,H.TAGUCHI
JRNL TITL STRUCTURAL BASIS OF SEQUENTIAL ALLOSTERIC TRANSITIONS IN
JRNL TITL 2 TETRAMERIC D-LACTATE DEHYDROGENASES FROM THREE GRAM-NEGATIVE
JRNL TITL 3 BACTERIA
JRNL REF BIOCHEMISTRY V. 57 5388 2018
JRNL REFN ISSN 1520-4995
JRNL PMID 30149697
JRNL DOI 10.1021/ACS.BIOCHEM.8B00557
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 89290
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4714
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6502
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 379
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5281
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 302
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.01000
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): 0.116
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.080
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.142
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5433 ; 0.024 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 5319 ; 0.007 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7314 ; 2.102 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12228 ; 1.375 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 661 ; 6.395 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 250 ;37.940 ;25.080
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1004 ;15.198 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;26.624 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 846 ; 0.138 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6024 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1190 ; 0.006 ; 0.020
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): 2653 ; 2.399 ; 2.220
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2652 ; 2.397 ; 2.219
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3311 ; 3.350 ; 3.309
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3312 ; 3.350 ; 3.311
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2780 ; 4.122 ; 2.777
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2780 ; 4.122 ; 2.777
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4004 ; 6.235 ; 3.951
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6400 ; 7.663 ;18.969
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6401 ; 7.662 ;18.973
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 2 334 B 2 334 19857 0.15 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 334
REMARK 3 ORIGIN FOR THE GROUP (A): 10.9932 34.6142 14.5496
REMARK 3 T TENSOR
REMARK 3 T11: 0.0155 T22: 0.0698
REMARK 3 T33: 0.0852 T12: -0.0141
REMARK 3 T13: 0.0088 T23: 0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 0.2863 L22: 0.0310
REMARK 3 L33: 0.4779 L12: -0.0677
REMARK 3 L13: -0.1287 L23: -0.0473
REMARK 3 S TENSOR
REMARK 3 S11: 0.0081 S12: -0.0403 S13: -0.0456
REMARK 3 S21: 0.0033 S22: 0.0155 S23: 0.0170
REMARK 3 S31: -0.0467 S32: -0.0110 S33: -0.0236
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 334
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6078 49.2455 -13.1564
REMARK 3 T TENSOR
REMARK 3 T11: 0.0880 T22: 0.0069
REMARK 3 T33: 0.0682 T12: -0.0004
REMARK 3 T13: 0.0003 T23: 0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 0.0109 L22: 0.2379
REMARK 3 L33: 0.3448 L12: -0.0355
REMARK 3 L13: -0.0177 L23: -0.0473
REMARK 3 S TENSOR
REMARK 3 S11: 0.0232 S12: -0.0004 S13: -0.0001
REMARK 3 S21: -0.0159 S22: -0.0031 S23: -0.0245
REMARK 3 S31: -0.0557 S32: -0.0155 S33: -0.0202
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 6ABI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1300008464.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NUMERICAL LINK TYPE SI(111)
REMARK 200 DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94385
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 37.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.50
REMARK 200 R MERGE (I) : 0.17100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 13.70
REMARK 200 R MERGE FOR SHELL (I) : 0.83100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
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: 1J49
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 74.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES-NA (PH 6.0) AND 1.26 M
REMARK 280 AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 117.20000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 58.14500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 58.14500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 175.80000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 58.14500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 58.14500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 58.60000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 58.14500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 58.14500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 175.80000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 58.14500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 58.14500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 58.60000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 117.20000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 25470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -323.0 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 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -22
REMARK 465 ASN A -21
REMARK 465 HIS A -20
REMARK 465 LYS A -19
REMARK 465 VAL A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 ILE A -11
REMARK 465 GLU A -10
REMARK 465 GLY A -9
REMARK 465 ARG A -8
REMARK 465 HIS A -7
REMARK 465 MET A -6
REMARK 465 GLU A -5
REMARK 465 LEU A -4
REMARK 465 GLY A -3
REMARK 465 THR A -2
REMARK 465 LEU A -1
REMARK 465 GLU A 0
REMARK 465 MET A 1
REMARK 465 GLN A 335
REMARK 465 MET B -22
REMARK 465 ASN B -21
REMARK 465 HIS B -20
REMARK 465 LYS B -19
REMARK 465 VAL B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 ILE B -11
REMARK 465 GLU B -10
REMARK 465 GLY B -9
REMARK 465 ARG B -8
REMARK 465 HIS B -7
REMARK 465 MET B -6
REMARK 465 GLU B -5
REMARK 465 LEU B -4
REMARK 465 GLY B -3
REMARK 465 THR B -2
REMARK 465 LEU B -1
REMARK 465 GLU B 0
REMARK 465 MET B 1
REMARK 465 PHE B 82
REMARK 465 ASN B 83
REMARK 465 GLN B 335
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 27 32.83 70.15
REMARK 500 ILE A 59 78.49 -103.15
REMARK 500 PHE A 82 20.43 -154.60
REMARK 500 TYR A 102 -95.08 -142.78
REMARK 500 SER A 103 66.42 32.32
REMARK 500 TYR A 145 125.05 -39.50
REMARK 500 GLU A 146 -1.15 68.69
REMARK 500 TYR A 269 -46.39 -135.71
REMARK 500 PHE A 271 -6.62 64.41
REMARK 500 TYR B 14 -5.61 70.26
REMARK 500 ASP B 25 19.84 52.38
REMARK 500 ILE B 59 71.30 -100.70
REMARK 500 ALA B 101 42.98 -90.89
REMARK 500 TYR B 145 122.44 -38.72
REMARK 500 GLU B 146 -2.51 70.90
REMARK 500 ASN B 207 41.25 -141.40
REMARK 500 TYR B 269 -41.78 -134.93
REMARK 500 PHE B 271 -7.05 69.51
REMARK 500 PHE B 302 67.54 -69.03
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 SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 411
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WWY RELATED DB: PDB
DBREF 6ABI A 1 335 UNP Q8RG11 Q8RG11_FUSNN 1 335
DBREF 6ABI B 1 335 UNP Q8RG11 Q8RG11_FUSNN 1 335
SEQADV 6ABI MET A -22 UNP Q8RG11 INITIATING METHIONINE
SEQADV 6ABI ASN A -21 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS A -20 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI LYS A -19 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI VAL A -18 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS A -17 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS A -16 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS A -15 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS A -14 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS A -13 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS A -12 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI ILE A -11 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI GLU A -10 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI GLY A -9 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI ARG A -8 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS A -7 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI MET A -6 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI GLU A -5 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI LEU A -4 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI GLY A -3 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI THR A -2 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI LEU A -1 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI GLU A 0 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI MET B -22 UNP Q8RG11 INITIATING METHIONINE
SEQADV 6ABI ASN B -21 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS B -20 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI LYS B -19 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI VAL B -18 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS B -17 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS B -16 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS B -15 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS B -14 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS B -13 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS B -12 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI ILE B -11 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI GLU B -10 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI GLY B -9 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI ARG B -8 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI HIS B -7 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI MET B -6 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI GLU B -5 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI LEU B -4 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI GLY B -3 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI THR B -2 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI LEU B -1 UNP Q8RG11 EXPRESSION TAG
SEQADV 6ABI GLU B 0 UNP Q8RG11 EXPRESSION TAG
SEQRES 1 A 358 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 A 358 GLY ARG HIS MET GLU LEU GLY THR LEU GLU MET GLN LYS
SEQRES 3 A 358 THR LYS ILE ILE PHE PHE ASP ILE LYS ASP TYR ASP LYS
SEQRES 4 A 358 GLU PHE PHE LYS LYS TYR GLY ALA ASP TYR ASN PHE GLU
SEQRES 5 A 358 MET THR PHE LEU LYS VAL ARG LEU THR GLU GLU THR ALA
SEQRES 6 A 358 ASN LEU THR LYS GLY TYR ASP VAL VAL CYS GLY PHE ALA
SEQRES 7 A 358 ASN ASP ASN ILE ASN LYS GLU THR ILE ASP ILE MET ALA
SEQRES 8 A 358 GLU ASN GLY ILE LYS LEU LEU ALA MET ARG CYS ALA GLY
SEQRES 9 A 358 PHE ASN ASN VAL SER LEU LYS ASP VAL ASN GLU ARG PHE
SEQRES 10 A 358 LYS VAL VAL ARG VAL PRO ALA TYR SER PRO HIS ALA ILE
SEQRES 11 A 358 ALA GLU TYR THR VAL GLY LEU ILE LEU ALA VAL ASN ARG
SEQRES 12 A 358 LYS ILE ASN LYS ALA TYR VAL ARG THR ARG GLU GLY ASN
SEQRES 13 A 358 PHE SER ILE ASN GLY LEU MET GLY ILE ASP LEU TYR GLU
SEQRES 14 A 358 LYS THR ALA GLY ILE ILE GLY THR GLY LYS ILE GLY GLN
SEQRES 15 A 358 ILE LEU ILE LYS ILE LEU ARG GLY PHE ASP MET LYS VAL
SEQRES 16 A 358 ILE ALA TYR ASP LEU PHE PRO ASN GLN LYS VAL ALA ASP
SEQRES 17 A 358 GLU LEU GLY PHE GLU TYR VAL SER LEU ASP GLU LEU TYR
SEQRES 18 A 358 ALA ASN SER ASP ILE ILE SER LEU ASN CYS PRO LEU THR
SEQRES 19 A 358 LYS ASP THR LYS TYR MET ILE ASN ARG ARG SER MET LEU
SEQRES 20 A 358 LYS MET LYS ASP GLY VAL ILE LEU VAL ASN THR GLY ARG
SEQRES 21 A 358 GLY MET LEU ILE ASP SER ALA ASP LEU VAL GLU ALA LEU
SEQRES 22 A 358 LYS ASP LYS LYS ILE GLY ALA VAL ALA LEU ASP VAL TYR
SEQRES 23 A 358 GLU GLU GLU GLU ASN TYR PHE PHE GLU ASP LYS SER THR
SEQRES 24 A 358 GLN VAL ILE GLU ASP ASP ILE LEU GLY ARG LEU LEU SER
SEQRES 25 A 358 PHE TYR ASN VAL LEU ILE THR SER HIS GLN ALA TYR PHE
SEQRES 26 A 358 THR LYS GLU ALA VAL GLY ALA ILE THR VAL THR THR LEU
SEQRES 27 A 358 ASN ASN ILE LYS ASP PHE VAL GLU GLY ARG PRO LEU VAL
SEQRES 28 A 358 ASN GLU VAL PRO GLN ASN GLN
SEQRES 1 B 358 MET ASN HIS LYS VAL HIS HIS HIS HIS HIS HIS ILE GLU
SEQRES 2 B 358 GLY ARG HIS MET GLU LEU GLY THR LEU GLU MET GLN LYS
SEQRES 3 B 358 THR LYS ILE ILE PHE PHE ASP ILE LYS ASP TYR ASP LYS
SEQRES 4 B 358 GLU PHE PHE LYS LYS TYR GLY ALA ASP TYR ASN PHE GLU
SEQRES 5 B 358 MET THR PHE LEU LYS VAL ARG LEU THR GLU GLU THR ALA
SEQRES 6 B 358 ASN LEU THR LYS GLY TYR ASP VAL VAL CYS GLY PHE ALA
SEQRES 7 B 358 ASN ASP ASN ILE ASN LYS GLU THR ILE ASP ILE MET ALA
SEQRES 8 B 358 GLU ASN GLY ILE LYS LEU LEU ALA MET ARG CYS ALA GLY
SEQRES 9 B 358 PHE ASN ASN VAL SER LEU LYS ASP VAL ASN GLU ARG PHE
SEQRES 10 B 358 LYS VAL VAL ARG VAL PRO ALA TYR SER PRO HIS ALA ILE
SEQRES 11 B 358 ALA GLU TYR THR VAL GLY LEU ILE LEU ALA VAL ASN ARG
SEQRES 12 B 358 LYS ILE ASN LYS ALA TYR VAL ARG THR ARG GLU GLY ASN
SEQRES 13 B 358 PHE SER ILE ASN GLY LEU MET GLY ILE ASP LEU TYR GLU
SEQRES 14 B 358 LYS THR ALA GLY ILE ILE GLY THR GLY LYS ILE GLY GLN
SEQRES 15 B 358 ILE LEU ILE LYS ILE LEU ARG GLY PHE ASP MET LYS VAL
SEQRES 16 B 358 ILE ALA TYR ASP LEU PHE PRO ASN GLN LYS VAL ALA ASP
SEQRES 17 B 358 GLU LEU GLY PHE GLU TYR VAL SER LEU ASP GLU LEU TYR
SEQRES 18 B 358 ALA ASN SER ASP ILE ILE SER LEU ASN CYS PRO LEU THR
SEQRES 19 B 358 LYS ASP THR LYS TYR MET ILE ASN ARG ARG SER MET LEU
SEQRES 20 B 358 LYS MET LYS ASP GLY VAL ILE LEU VAL ASN THR GLY ARG
SEQRES 21 B 358 GLY MET LEU ILE ASP SER ALA ASP LEU VAL GLU ALA LEU
SEQRES 22 B 358 LYS ASP LYS LYS ILE GLY ALA VAL ALA LEU ASP VAL TYR
SEQRES 23 B 358 GLU GLU GLU GLU ASN TYR PHE PHE GLU ASP LYS SER THR
SEQRES 24 B 358 GLN VAL ILE GLU ASP ASP ILE LEU GLY ARG LEU LEU SER
SEQRES 25 B 358 PHE TYR ASN VAL LEU ILE THR SER HIS GLN ALA TYR PHE
SEQRES 26 B 358 THR LYS GLU ALA VAL GLY ALA ILE THR VAL THR THR LEU
SEQRES 27 B 358 ASN ASN ILE LYS ASP PHE VAL GLU GLY ARG PRO LEU VAL
SEQRES 28 B 358 ASN GLU VAL PRO GLN ASN GLN
HET SO4 A 401 5
HET SO4 A 402 5
HET SO4 A 403 5
HET SO4 A 404 5
HET GOL A 405 6
HET SO4 B 401 5
HET SO4 B 402 5
HET SO4 B 403 5
HET SO4 B 404 5
HET GOL B 405 6
HET GOL B 406 6
HET GOL B 407 6
HET GOL B 408 6
HET GOL B 409 6
HET GOL B 410 6
HET GOL B 411 6
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 SO4 8(O4 S 2-)
FORMUL 7 GOL 8(C3 H8 O3)
FORMUL 19 HOH *302(H2 O)
HELIX 1 AA1 LYS A 12 ALA A 24 1 13
HELIX 2 AA2 THR A 41 LYS A 46 5 6
HELIX 3 AA3 ASN A 60 ASN A 70 1 11
HELIX 4 AA4 SER A 86 ASN A 91 1 6
HELIX 5 AA5 SER A 103 LYS A 121 1 19
HELIX 6 AA6 LYS A 121 GLU A 131 1 11
HELIX 7 AA7 GLY A 155 PHE A 168 1 14
HELIX 8 AA8 ASN A 180 GLY A 188 1 9
HELIX 9 AA9 SER A 193 SER A 201 1 9
HELIX 10 AB1 ASN A 219 LYS A 225 1 7
HELIX 11 AB2 ARG A 237 ILE A 241 5 5
HELIX 12 AB3 ASP A 242 ASP A 252 1 11
HELIX 13 AB4 GLU A 265 TYR A 269 5 5
HELIX 14 AB5 ASP A 281 LEU A 288 1 8
HELIX 15 AB6 THR A 303 GLU A 323 1 21
HELIX 16 AB7 TYR B 14 GLY B 23 1 10
HELIX 17 AB8 THR B 41 LYS B 46 5 6
HELIX 18 AB9 ASN B 60 ASN B 70 1 11
HELIX 19 AC1 SER B 86 ASN B 91 1 6
HELIX 20 AC2 SER B 103 ARG B 120 1 18
HELIX 21 AC3 LYS B 121 GLU B 131 1 11
HELIX 22 AC4 GLY B 155 PHE B 168 1 14
HELIX 23 AC5 ASN B 180 GLY B 188 1 9
HELIX 24 AC6 SER B 193 SER B 201 1 9
HELIX 25 AC7 ASN B 219 LYS B 225 1 7
HELIX 26 AC8 ARG B 237 ILE B 241 5 5
HELIX 27 AC9 ASP B 242 ASP B 252 1 11
HELIX 28 AD1 GLU B 265 TYR B 269 5 5
HELIX 29 AD2 ASP B 281 LEU B 288 1 8
HELIX 30 AD3 THR B 303 GLU B 323 1 21
SHEET 1 AA1 5 PHE A 28 PHE A 32 0
SHEET 2 AA1 5 THR A 4 PHE A 8 1 N ILE A 6 O GLU A 29
SHEET 3 AA1 5 VAL A 50 GLY A 53 1 O CYS A 52 N ILE A 7
SHEET 4 AA1 5 LEU A 74 MET A 77 1 O ALA A 76 N VAL A 51
SHEET 5 AA1 5 LYS A 95 VAL A 97 1 O VAL A 97 N MET A 77
SHEET 1 AA2 7 GLU A 190 TYR A 191 0
SHEET 2 AA2 7 LYS A 171 TYR A 175 1 N ALA A 174 O GLU A 190
SHEET 3 AA2 7 THR A 148 ILE A 152 1 N ALA A 149 O LYS A 171
SHEET 4 AA2 7 ILE A 203 LEU A 206 1 O ILE A 203 N GLY A 150
SHEET 5 AA2 7 VAL A 230 ASN A 234 1 O ILE A 231 N ILE A 204
SHEET 6 AA2 7 ILE A 255 LEU A 260 1 O ALA A 257 N LEU A 232
SHEET 7 AA2 7 VAL A 293 ILE A 295 1 O LEU A 294 N LEU A 260
SHEET 1 AA3 5 PHE B 28 PHE B 32 0
SHEET 2 AA3 5 THR B 4 PHE B 8 1 N ILE B 6 O GLU B 29
SHEET 3 AA3 5 VAL B 50 PHE B 54 1 O CYS B 52 N ILE B 7
SHEET 4 AA3 5 LEU B 74 ARG B 78 1 O ALA B 76 N VAL B 51
SHEET 5 AA3 5 LYS B 95 VAL B 99 1 O VAL B 97 N LEU B 75
SHEET 1 AA4 7 GLU B 190 TYR B 191 0
SHEET 2 AA4 7 LYS B 171 TYR B 175 1 N ALA B 174 O GLU B 190
SHEET 3 AA4 7 THR B 148 ILE B 152 1 N ALA B 149 O ILE B 173
SHEET 4 AA4 7 ILE B 203 LEU B 206 1 O ILE B 203 N GLY B 150
SHEET 5 AA4 7 VAL B 230 ASN B 234 1 O ILE B 231 N ILE B 204
SHEET 6 AA4 7 ILE B 255 LEU B 260 1 O ALA B 259 N ASN B 234
SHEET 7 AA4 7 VAL B 293 ILE B 295 1 O LEU B 294 N LEU B 260
SITE 1 AC1 6 VAL A 35 ARG A 36 HOH A 503 HOH A 545
SITE 2 AC1 6 LYS B 34 VAL B 35
SITE 1 AC2 5 PRO A 209 LEU A 210 ARG A 237 HOH A 507
SITE 2 AC2 5 LYS B 95
SITE 1 AC3 3 THR A 313 ASN A 316 HOH A 561
SITE 1 AC4 3 HIS A 105 LYS A 156 TYR B 145
SITE 1 AC5 5 ASN A 119 LYS A 121 GLY A 229 GLY A 256
SITE 2 AC5 5 HOH A 532
SITE 1 AC6 5 TYR A 145 HIS B 105 LYS B 156 GOL B 409
SITE 2 AC6 5 HOH B 511
SITE 1 AC7 7 CYS B 79 ALA B 80 ARG B 98 PRO B 100
SITE 2 AC7 7 ALA B 101 ARG B 237 GOL B 408
SITE 1 AC8 5 LYS A 95 PRO B 209 LEU B 210 ARG B 237
SITE 2 AC8 5 GOL B 410
SITE 1 AC9 3 THR B 313 ASN B 316 HOH B 521
SITE 1 AD1 8 ASP A 143 PRO B 104 HIS B 105 ALA B 106
SITE 2 AD1 8 GLU B 305 ALA B 306 HOH B 501 HOH B 511
SITE 1 AD2 9 PHE A 321 GLY B 155 ASP B 176 LEU B 177
SITE 2 AD2 9 PHE B 178 GOL B 410 HOH B 502 HOH B 508
SITE 3 AD2 9 HOH B 557
SITE 1 AD3 5 ASN B 119 LYS B 121 GLY B 229 GLY B 256
SITE 2 AD3 5 HOH B 541
SITE 1 AD4 6 ILE B 107 THR B 235 GLY B 236 ARG B 237
SITE 2 AD4 6 HIS B 298 SO4 B 402
SITE 1 AD5 5 ARG A 325 TYR B 102 LYS B 156 SO4 B 401
SITE 2 AD5 5 HOH B 511
SITE 1 AD6 8 ASP A 320 PHE A 321 GLY A 324 ARG A 325
SITE 2 AD6 8 LEU A 327 PRO B 209 SO4 B 403 GOL B 406
SITE 1 AD7 6 VAL B 99 PRO B 100 TYR B 102 ALA B 309
SITE 2 AD7 6 ILE B 310 THR B 313
CRYST1 116.290 116.290 234.400 90.00 90.00 90.00 P 43 21 2 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 0.008599 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008599 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004266 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
