HEADER OXIDOREDUCTASE 15-JAN-10 3AD8
TITLE HETEROTETRAMERIC SARCOSINE OXIDASE FROM CORYNEBACTERIUM SP. U-96 IN
TITLE 2 COMPLEX WITH PYRROLE 2-CARBOXYLATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SARCOSINE OXIDASE ALPHA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: SARCOSINE OXIDASE BETA SUBUNIT;
COMPND 7 CHAIN: B;
COMPND 8 EC: 1.5.3.1;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: SARCOSINE OXIDASE GAMMA SUBUNIT;
COMPND 12 CHAIN: C;
COMPND 13 FRAGMENT: UNP RESIDUES 11-205;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 4;
COMPND 16 MOLECULE: SARCOSINE OXIDASE DELTA SUBUNIT;
COMPND 17 CHAIN: D;
COMPND 18 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM SP. U-96;
SOURCE 3 ORGANISM_TAXID: 31944;
SOURCE 4 GENE: SOXA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET31B;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM SP. U-96;
SOURCE 12 ORGANISM_TAXID: 31944;
SOURCE 13 GENE: SOXB;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET31B;
SOURCE 19 MOL_ID: 3;
SOURCE 20 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM SP. U-96;
SOURCE 21 ORGANISM_TAXID: 31944;
SOURCE 22 GENE: SOXG;
SOURCE 23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 24 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 25 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 26 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 27 EXPRESSION_SYSTEM_PLASMID: PET31B;
SOURCE 28 MOL_ID: 4;
SOURCE 29 ORGANISM_SCIENTIFIC: CORYNEBACTERIUM SP. U-96;
SOURCE 30 ORGANISM_TAXID: 31944;
SOURCE 31 GENE: SOXD;
SOURCE 32 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 33 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 34 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 35 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 36 EXPRESSION_SYSTEM_PLASMID: PET31B
KEYWDS SARCOSINE OXIDASE, LIGAND COMPLEX, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.SUZUKI,T.MORIGUCHI,K.IDA
REVDAT 3 01-NOV-23 3AD8 1 REMARK LINK
REVDAT 2 04-SEP-13 3AD8 1 JRNL VERSN
REVDAT 1 25-AUG-10 3AD8 0
JRNL AUTH T.MORIGUCHI,K.IDA,T.HIKIMA,G.UENO,M.YAMAMOTO,H.SUZUKI
JRNL TITL CHANNELING AND CONFORMATIONAL CHANGES IN THE
JRNL TITL 2 HETEROTETRAMERIC SARCOSINE OXIDASE FROM CORYNEBACTERIUM SP.
JRNL TITL 3 U-96.
JRNL REF J.BIOCHEM. V. 148 491 2010
JRNL REFN ISSN 0021-924X
JRNL PMID 20675294
JRNL DOI 10.1093/JB/MVQ083
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 109866
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) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5799
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8041
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1730
REMARK 3 BIN FREE R VALUE SET COUNT : 413
REMARK 3 BIN FREE R VALUE : 0.2360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12519
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 197
REMARK 3 SOLVENT ATOMS : 1020
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.78
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.180
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.163
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.101
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.847
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12981 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17695 ; 1.850 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1649 ; 6.956 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 571 ;36.786 ;23.783
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1988 ;15.301 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 93 ;17.455 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1985 ; 0.145 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9939 ; 0.010 ; 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): 8182 ; 1.005 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13067 ; 1.789 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4799 ; 3.220 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4628 ; 4.824 ; 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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3AD8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000029108.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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) : 1.00817
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 115711
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 61.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : 0.08000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.23300
REMARK 200 R SYM FOR SHELL (I) : 0.23300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.100
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: 1X31
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.84
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 1.9M AMMONIUM SULFATE,
REMARK 280 10MM CUSO4, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 131.21267
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 65.60633
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 98.40950
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 32.80317
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 164.01583
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 131.21267
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 65.60633
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 32.80317
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 98.40950
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 164.01583
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: 16380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1161 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 964
REMARK 465 LEU C 201
REMARK 465 GLU C 202
REMARK 465 HIS C 203
REMARK 465 HIS C 204
REMARK 465 HIS C 205
REMARK 465 HIS C 206
REMARK 465 HIS C 207
REMARK 465 HIS C 208
REMARK 465 ASP D 92
REMARK 465 SER D 93
REMARK 465 THR D 94
REMARK 465 GLU D 95
REMARK 465 GLY D 96
REMARK 465 GLY D 97
REMARK 465 THR D 98
REMARK 465 ARG D 99
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 NE2 HIS B 172 C8M FMN B 406 1.71
REMARK 500 OD1 ASP A 830 CE1 HIS A 909 1.88
REMARK 500 O ARG A 868 O LYS A 926 1.95
REMARK 500 NH2 ARG A 736 O ASP A 963 1.99
REMARK 500 CB ALA A 696 O3 SO4 A 2509 2.14
REMARK 500 OE2 GLU B 118 O HOH B 802 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE2 HIS A 477 NE2 HIS A 477 11555 1.27
REMARK 500 O HOH A 1080 O HOH A 1080 9555 1.63
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 HIS A 477 CA HIS A 477 CB 0.177
REMARK 500 HIS A 477 CB HIS A 477 CG 0.167
REMARK 500 HIS A 477 CG HIS A 477 CD2 0.065
REMARK 500 HIS A 477 CA HIS A 477 C 0.178
REMARK 500 PHE D 53 CE1 PHE D 53 CZ 0.121
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 15 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 15 NE - CZ - NH2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 LEU A 214 CA - CB - CG ANGL. DEV. = -15.3 DEGREES
REMARK 500 LEU A 214 CB - CG - CD1 ANGL. DEV. = 10.4 DEGREES
REMARK 500 PRO A 226 C - N - CA ANGL. DEV. = -9.0 DEGREES
REMARK 500 HIS A 477 CB - CA - C ANGL. DEV. = 16.4 DEGREES
REMARK 500 ARG A 770 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 819 CG - CD - NE ANGL. DEV. = -13.5 DEGREES
REMARK 500 ARG A 819 CD - NE - CZ ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG A 819 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG A 819 NE - CZ - NH2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG A 918 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 918 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 117 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG B 181 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 387 NE - CZ - NH1 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG B 387 NE - CZ - NH2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG C 28 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG C 28 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG C 165 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG C 176 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG C 176 NE - CZ - NH2 ANGL. DEV. = -4.4 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 CYS A 51 -156.71 -126.52
REMARK 500 SER A 227 -113.46 -59.32
REMARK 500 ALA A 247 53.20 -144.56
REMARK 500 ALA A 249 -160.41 68.49
REMARK 500 ALA A 406 -129.25 -83.98
REMARK 500 LEU A 466 103.49 -164.25
REMARK 500 SER A 513 8.87 81.77
REMARK 500 SER A 622 -93.12 -145.26
REMARK 500 ASP B 2 -137.68 -114.55
REMARK 500 LEU B 3 -17.12 -150.61
REMARK 500 ASN B 14 69.58 -114.64
REMARK 500 ASP B 202 -62.02 -90.45
REMARK 500 GLU B 204 32.61 -94.86
REMARK 500 ALA B 226 -112.50 40.86
REMARK 500 ALA B 284 -136.34 -153.41
REMARK 500 LEU C 7 -26.69 87.94
REMARK 500 GLU C 93 123.15 -34.37
REMARK 500 SER C 136 -6.57 -149.90
REMARK 500 THR C 154 -161.83 -167.58
REMARK 500 GLN C 169 51.49 -144.09
REMARK 500 HIS D 24 30.29 71.03
REMARK 500 ASN D 48 42.99 -141.41
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 SER A 227 GLY A 228 -135.77
REMARK 500 VAL C 199 ALA C 200 -148.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 100 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 6 SG
REMARK 620 2 CYS D 9 SG 118.4
REMARK 620 3 HIS D 59 ND1 109.6 100.7
REMARK 620 4 CYS D 63 SG 102.1 111.9 114.7
REMARK 620 N 1 2 3
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 965
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYC B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2511
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2508
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 2503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1X31 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH DIMETHYLGLYCINE
REMARK 900 RELATED ID: 1VRQ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH FOLINIC ACID
REMARK 900 RELATED ID: 3AD7 RELATED DB: PDB
REMARK 900 RELATED ID: 3AD9 RELATED DB: PDB
REMARK 900 RELATED ID: 3ADA RELATED DB: PDB
DBREF 3AD8 A 1 964 UNP Q50LF0 Q50LF0_9CORY 2 965
DBREF 3AD8 B 1 404 UNP Q50LF2 Q50LF2_9CORY 2 405
DBREF 3AD8 C 6 200 UNP Q50LE9 Q50LE9_9CORY 11 205
DBREF 3AD8 D 1 99 UNP Q50LF1 Q50LF1_9CORY 1 99
SEQRES 1 A 964 SER LYS PRO GLN ARG LEU SER ALA ALA GLN THR ALA GLY
SEQRES 2 A 964 ALA ARG ILE ASN ARG ASP GLU ALA LEU THR LEU THR VAL
SEQRES 3 A 964 ASP GLY GLN GLN LEU SER ALA PHE ARG GLY ASP THR VAL
SEQRES 4 A 964 ALA SER ALA MET LEU ALA ASN GLY LEU ARG SER CYS GLY
SEQRES 5 A 964 ASN SER MET TYR LEU ASP ARG PRO ARG GLY ILE PHE SER
SEQRES 6 A 964 ALA GLY VAL GLU GLU PRO ASN ALA LEU ILE THR VAL GLY
SEQRES 7 A 964 ALA ARG HIS GLN ALA ASP ILE ASN GLU SER MET LEU PRO
SEQRES 8 A 964 ALA THR THR VAL SER VAL THR ASP GLY LEU ASN ALA THR
SEQRES 9 A 964 LEU LEU SER GLY LEU GLY VAL LEU ASP PRO SER GLU ASP
SEQRES 10 A 964 PRO ALA TYR TYR ASP HIS VAL HIS VAL HIS THR ASP VAL
SEQRES 11 A 964 LEU VAL VAL GLY ALA GLY PRO ALA GLY LEU ALA ALA ALA
SEQRES 12 A 964 ARG GLU ALA SER ARG SER GLY ALA ARG VAL MET LEU LEU
SEQRES 13 A 964 ASP GLU ARG PRO GLU ALA GLY GLY THR LEU ARG GLU ALA
SEQRES 14 A 964 SER GLY GLU GLN ILE ASP GLY ILE ASP ALA ALA GLN TRP
SEQRES 15 A 964 ILE ASP ALA VAL THR GLU GLU LEU ALA ALA ALA GLU GLU
SEQRES 16 A 964 THR THR HIS LEU GLN ARG THR THR VAL PHE GLY SER TYR
SEQRES 17 A 964 ASP ALA ASN TYR ILE LEU ALA ALA GLN ARG ARG THR VAL
SEQRES 18 A 964 HIS LEU ASP GLY PRO SER GLY GLN GLY VAL SER ARG GLU
SEQRES 19 A 964 ARG ILE TRP HIS ILE ARG ALA LYS GLN VAL VAL LEU ALA
SEQRES 20 A 964 THR ALA ALA HIS GLU ARG PRO ILE VAL PHE GLU ASN ASN
SEQRES 21 A 964 ASP ARG PRO GLY ILE MET LEU ALA GLY SER VAL ARG SER
SEQRES 22 A 964 TYR LEU ASN ARG PHE GLY VAL ARG ALA GLY SER LYS ILE
SEQRES 23 A 964 ALA VAL ALA THR THR ASN ASP SER VAL TYR PRO LEU VAL
SEQRES 24 A 964 SER GLU LEU ALA ALA SER GLY GLY VAL VAL ALA VAL ILE
SEQRES 25 A 964 ASP ALA ARG GLN ASN ILE SER ALA ALA ALA ALA GLN ALA
SEQRES 26 A 964 VAL THR ASP GLY VAL THR VAL LEU THR GLY SER VAL VAL
SEQRES 27 A 964 ALA ASN THR GLU ALA ASP ALA SER GLY GLU LEU SER ALA
SEQRES 28 A 964 VAL LEU VAL ALA THR LEU ASP GLU GLN ARG ASN LEU GLY
SEQRES 29 A 964 GLU ALA GLN ARG PHE GLU ALA ASP VAL LEU ALA VAL SER
SEQRES 30 A 964 GLY GLY PHE ASN PRO VAL VAL HIS LEU HIS SER GLN ARG
SEQRES 31 A 964 GLN GLY LYS LEU ASN TRP ASP THR SER ILE HIS ALA PHE
SEQRES 32 A 964 VAL PRO ALA ASP ALA VAL ALA ASN GLN HIS LEU ALA GLY
SEQRES 33 A 964 ALA LEU THR GLY LEU LEU ASP THR ALA SER ALA LEU SER
SEQRES 34 A 964 THR GLY ALA ALA THR GLY ALA ALA ALA ALA SER ALA ALA
SEQRES 35 A 964 GLY PHE GLU LYS ILE ALA GLU VAL PRO GLN ALA LEU ALA
SEQRES 36 A 964 VAL PRO ALA GLY GLU THR ARG PRO VAL TRP LEU VAL PRO
SEQRES 37 A 964 SER LEU SER GLY ASP ASP ALA VAL HIS TYR LYS PHE HIS
SEQRES 38 A 964 PHE VAL ASP LEU GLN ARG ASP GLN THR VAL ALA ASP VAL
SEQRES 39 A 964 LEU ARG ALA THR GLY ALA GLY MET GLN SER VAL GLU HIS
SEQRES 40 A 964 ILE LYS ARG TYR THR SER ILE SER THR ALA ASN ASP GLN
SEQRES 41 A 964 GLY LYS THR SER GLY VAL ALA ALA ILE GLY VAL ILE ALA
SEQRES 42 A 964 ALA VAL LEU GLY ILE GLU ASN PRO ALA GLN ILE GLY THR
SEQRES 43 A 964 THR THR PHE ARG ALA PRO TYR THR PRO VAL SER PHE ALA
SEQRES 44 A 964 ALA LEU ALA GLY ARG THR ARG GLY GLU LEU LEU ASP PRO
SEQRES 45 A 964 ALA ARG LEU THR ALA MET HIS PRO TRP HIS LEU ALA HIS
SEQRES 46 A 964 GLY ALA LYS PHE GLU ASP VAL GLY GLN TRP LYS ARG PRO
SEQRES 47 A 964 TRP TYR TYR PRO GLN ASP GLY GLU SER MET ASP GLU ALA
SEQRES 48 A 964 VAL TYR ARG GLU CYS LYS ALA VAL ARG ASP SER VAL GLY
SEQRES 49 A 964 MET LEU ASP ALA SER THR LEU GLY LYS ILE GLU ILE ARG
SEQRES 50 A 964 GLY LYS ASP ALA ALA GLU PHE LEU ASN ARG MET TYR THR
SEQRES 51 A 964 ASN GLY TYR THR LYS LEU LYS VAL GLY MET GLY ARG TYR
SEQRES 52 A 964 GLY VAL MET CYS LYS ALA ASP GLY MET ILE PHE ASP ASP
SEQRES 53 A 964 GLY VAL THR LEU ARG LEU ALA GLU ASP ARG PHE LEU MET
SEQRES 54 A 964 HIS THR THR THR GLY GLY ALA ALA ASP VAL LEU ASP TRP
SEQRES 55 A 964 LEU GLU GLU TRP LEU GLN THR GLU TRP PRO GLU LEU ASP
SEQRES 56 A 964 VAL THR CYS THR SER VAL THR GLU GLN LEU ALA THR VAL
SEQRES 57 A 964 ALA VAL VAL GLY PRO ARG SER ARG ASP VAL ILE ALA LYS
SEQRES 58 A 964 LEU ALA SER SER LEU ASP VAL SER ASN ASP ALA PHE LYS
SEQRES 59 A 964 PHE MET ALA PHE GLN ASP VAL THR LEU ASP SER GLY ILE
SEQRES 60 A 964 GLU ALA ARG ILE SER ARG ILE SER PHE SER GLY GLU LEU
SEQRES 61 A 964 ALA PHE GLU ILE ALA ILE PRO ALA TRP HIS GLY LEU GLN
SEQRES 62 A 964 VAL TRP GLU ASP VAL TYR ALA ALA GLY GLN GLU PHE ASN
SEQRES 63 A 964 ILE THR PRO TYR GLY THR GLU THR MET HIS VAL LEU ARG
SEQRES 64 A 964 ALA GLU LYS GLY PHE ILE ILE VAL GLY GLN ASP THR ASP
SEQRES 65 A 964 GLY THR VAL THR PRO GLN ASP ALA GLY MET GLU TRP VAL
SEQRES 66 A 964 VAL SER LYS LEU LYS ASP PHE VAL GLY LYS ARG SER PHE
SEQRES 67 A 964 SER ARG GLU ASP ASN VAL ARG GLU ASP ARG LYS HIS LEU
SEQRES 68 A 964 VAL SER VAL LEU PRO VAL ASP SER SER LEU ARG LEU ALA
SEQRES 69 A 964 GLU GLY ALA ALA LEU VAL ALA ALA ASP ALA VAL ALA SER
SEQRES 70 A 964 GLU GLY VAL THR PRO MET GLU GLY TRP VAL THR HIS ALA
SEQRES 71 A 964 TYR ASN SER PRO ALA LEU GLY ARG THR PHE GLY LEU ALA
SEQRES 72 A 964 LEU ILE LYS ASN GLY ARG ASN ARG ILE GLY GLU VAL LEU
SEQRES 73 A 964 LYS THR PRO VAL ASP GLY GLN LEU VAL ASP VAL GLN VAL
SEQRES 74 A 964 SER ASP LEU VAL LEU PHE ASP PRO GLU GLY SER ARG ARG
SEQRES 75 A 964 ASP GLY
SEQRES 1 B 404 ALA ASP LEU LEU PRO GLU HIS PRO GLU PHE LEU TRP ASN
SEQRES 2 B 404 ASN PRO GLU PRO LYS LYS SER TYR ASP VAL VAL ILE VAL
SEQRES 3 B 404 GLY GLY GLY GLY HIS GLY LEU ALA THR ALA TYR TYR LEU
SEQRES 4 B 404 ALA LYS ASN HIS GLY ILE THR ASN VAL ALA VAL LEU GLU
SEQRES 5 B 404 LYS GLY TRP LEU ALA GLY GLY ASN MET ALA ARG ASN THR
SEQRES 6 B 404 THR ILE ILE ARG SER ASN TYR LEU TRP ASP GLU SER ALA
SEQRES 7 B 404 GLY ILE TYR GLU LYS SER LEU LYS LEU TRP GLU GLU LEU
SEQRES 8 B 404 PRO GLU GLU LEU GLU TYR ASP PHE LEU PHE SER GLN ARG
SEQRES 9 B 404 GLY VAL LEU ASN LEU ALA HIS THR LEU GLY ASP VAL ARG
SEQRES 10 B 404 GLU SER ILE ARG ARG VAL GLU ALA ASN LYS PHE ASN GLY
SEQRES 11 B 404 VAL ASP ALA GLU TRP LEU THR PRO GLU GLN VAL LYS GLU
SEQRES 12 B 404 VAL CYS PRO ILE ILE ASN THR GLY ASP ASN ILE ARG TYR
SEQRES 13 B 404 PRO VAL MET GLY ALA THR TYR GLN PRO ARG ALA GLY ILE
SEQRES 14 B 404 ALA LYS HIS ASP HIS VAL ALA TRP ALA PHE ALA ARG LYS
SEQRES 15 B 404 ALA ASN GLU MET GLY VAL ASP ILE ILE GLN ASN CYS GLU
SEQRES 16 B 404 VAL THR GLY PHE LEU LYS ASP GLY GLU LYS VAL THR GLY
SEQRES 17 B 404 VAL LYS THR THR ARG GLY THR ILE LEU ALA GLY LYS VAL
SEQRES 18 B 404 ALA LEU ALA GLY ALA GLY HIS SER SER VAL LEU ALA GLU
SEQRES 19 B 404 LEU ALA GLY PHE GLU LEU PRO ILE GLN SER HIS PRO LEU
SEQRES 20 B 404 GLN ALA LEU VAL SER GLU LEU PHE GLU PRO VAL HIS PRO
SEQRES 21 B 404 THR VAL VAL MET SER ASN HIS ILE HIS VAL TYR VAL SER
SEQRES 22 B 404 GLN ALA HIS LYS GLY GLU LEU VAL MET GLY ALA GLY ILE
SEQRES 23 B 404 ASP SER TYR ASN GLY TYR GLY GLN ARG GLY ALA PHE HIS
SEQRES 24 B 404 VAL ILE GLU GLU GLN MET ALA ALA ALA VAL GLU LEU PHE
SEQRES 25 B 404 PRO ILE PHE ALA ARG ALA HIS VAL LEU ARG THR TRP GLY
SEQRES 26 B 404 GLY ILE VAL ASP THR THR MET ASP ALA SER PRO ILE ILE
SEQRES 27 B 404 SER LYS THR PRO ILE GLN ASN LEU TYR VAL ASN CYS GLY
SEQRES 28 B 404 TRP GLY THR GLY GLY PHE LYS GLY THR PRO GLY ALA GLY
SEQRES 29 B 404 TYR THR LEU ALA HIS THR ILE ALA HIS ASP GLU PRO HIS
SEQRES 30 B 404 LYS LEU ASN ALA PRO PHE ALA LEU GLU ARG PHE GLU THR
SEQRES 31 B 404 GLY HIS LEU ILE ASP GLU HIS GLY ALA ALA ALA VAL ALA
SEQRES 32 B 404 HIS
SEQRES 1 C 203 GLN LEU ARG ARG SER PRO ALA ALA HIS LEU ALA ALA ALA
SEQRES 2 C 203 MET GLU ALA ALA GLU VAL ALA GLY GLU ARG ALA VAL THR
SEQRES 3 C 203 LEU ARG GLU VAL ALA PHE THR THR GLN LEU GLY LEU ARG
SEQRES 4 C 203 ALA VAL PRO GLY SER THR GLY HIS ALA ALA LEU ALA ALA
SEQRES 5 C 203 ALA THR GLY VAL GLY LEU PRO ALA ALA VAL GLY GLU VAL
SEQRES 6 C 203 ALA GLY ASP VAL SER GLY THR ALA VAL LEU TRP LEU GLY
SEQRES 7 C 203 PRO ASP GLU PHE LEU LEU ALA ALA GLU GLU ASN PRO ALA
SEQRES 8 C 203 LEU LEU ASP THR LEU GLN GLY ALA LEU GLY GLN GLU PRO
SEQRES 9 C 203 GLY GLN VAL LEU ASP LEU SER ALA ASN ARG SER VAL LEU
SEQRES 10 C 203 GLN LEU GLU GLY PRO ALA ALA ALA LEU VAL LEU ARG LYS
SEQRES 11 C 203 SER CYS PRO ALA ASP LEU HIS PRO ARG GLU PHE GLY VAL
SEQRES 12 C 203 ASN ARG ALA ILE THR THR SER LEU ALA ASN ILE PRO VAL
SEQRES 13 C 203 LEU LEU TRP ARG THR GLY GLU GLN SER TRP ARG ILE LEU
SEQRES 14 C 203 PRO ARG ALA SER PHE THR GLU HIS THR VAL HIS TRP LEU
SEQRES 15 C 203 ILE ASP ALA MET SER GLU PHE SER ALA ALA GLU VAL ALA
SEQRES 16 C 203 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 99 MET MET LEU ILE GLU CYS PRO ASN CYS GLY PRO ARG ASN
SEQRES 2 D 99 GLU ASN GLU PHE LYS TYR GLY GLY GLU ALA HIS VAL ALA
SEQRES 3 D 99 TYR PRO GLU ASP PRO ASN ALA LEU SER ASP LYS GLU TRP
SEQRES 4 D 99 SER ARG TYR LEU PHE TYR ARG GLY ASN LYS LYS GLY ILE
SEQRES 5 D 99 PHE ALA GLU ARG TRP VAL HIS SER GLY GLY CYS ARG LYS
SEQRES 6 D 99 TRP PHE ASN ALA LEU ARG ASP THR VAL SER TYR GLU PHE
SEQRES 7 D 99 LYS ALA VAL TYR ARG ALA GLY GLU ALA ARG PRO GLN LEU
SEQRES 8 D 99 ASP SER THR GLU GLY GLY THR ARG
HET NAD A 965 44
HET SO4 A2500 5
HET SO4 A2501 5
HET SO4 A2502 5
HET SO4 A2504 5
HET SO4 A2506 5
HET SO4 A2507 5
HET SO4 A2509 5
HET FAD B 405 53
HET FMN B 406 31
HET PYC B 801 8
HET SO4 B2505 5
HET SO4 B2510 5
HET SO4 B2511 5
HET SO4 C2508 5
HET ZN D 100 1
HET SO4 D2503 5
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM SO4 SULFATE ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM PYC PYRROLE-2-CARBOXYLATE
HETNAM ZN ZINC ION
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 5 NAD C21 H27 N7 O14 P2
FORMUL 6 SO4 12(O4 S 2-)
FORMUL 13 FAD C27 H33 N9 O15 P2
FORMUL 14 FMN C17 H21 N4 O9 P
FORMUL 15 PYC C5 H4 N O2 1-
FORMUL 20 ZN ZN 2+
FORMUL 22 HOH *1020(H2 O)
HELIX 1 1 ALA A 8 ALA A 12 5 5
HELIX 2 2 THR A 38 ASN A 46 1 9
HELIX 3 3 GLY A 136 SER A 149 1 14
HELIX 4 4 GLY A 163 ALA A 169 5 7
HELIX 5 5 ALA A 179 ALA A 193 1 15
HELIX 6 6 ALA A 268 GLY A 279 1 12
HELIX 7 7 ASN A 292 SER A 294 5 3
HELIX 8 8 VAL A 295 ALA A 303 1 9
HELIX 9 9 ALA A 304 GLY A 306 5 3
HELIX 10 10 SER A 319 ASP A 328 1 10
HELIX 11 11 VAL A 384 ARG A 390 1 7
HELIX 12 12 GLY A 416 GLY A 420 5 5
HELIX 13 13 ASP A 423 ALA A 442 1 20
HELIX 14 14 ASP A 474 LYS A 479 5 6
HELIX 15 15 VAL A 491 ALA A 500 1 10
HELIX 16 16 SER A 504 SER A 513 1 10
HELIX 17 17 SER A 524 GLY A 537 1 14
HELIX 18 18 ASN A 540 GLY A 545 1 6
HELIX 19 19 PHE A 558 GLY A 563 1 6
HELIX 20 20 ARG A 566 ASP A 571 5 6
HELIX 21 21 MET A 578 HIS A 585 1 8
HELIX 22 22 SER A 607 SER A 622 1 16
HELIX 23 23 ASP A 640 TYR A 649 1 10
HELIX 24 24 GLY A 695 GLU A 710 1 16
HELIX 25 25 ARG A 734 ALA A 743 1 10
HELIX 26 26 HIS A 790 GLN A 803 1 14
HELIX 27 27 GLU A 804 ASN A 806 5 3
HELIX 28 28 GLY A 811 LYS A 822 1 12
HELIX 29 29 MET A 842 VAL A 846 5 5
HELIX 30 30 GLY A 854 ARG A 865 5 12
HELIX 31 31 ASN A 927 ARG A 931 5 5
HELIX 32 32 GLY B 29 GLY B 44 1 16
HELIX 33 33 GLY B 59 ARG B 63 5 5
HELIX 34 34 TRP B 74 GLU B 96 1 23
HELIX 35 35 THR B 112 ASN B 129 1 18
HELIX 36 36 THR B 137 CYS B 145 1 9
HELIX 37 37 LYS B 171 MET B 186 1 16
HELIX 38 38 GLY B 225 GLY B 227 5 3
HELIX 39 39 HIS B 228 GLY B 237 1 10
HELIX 40 40 PHE B 298 PHE B 312 1 15
HELIX 41 41 PRO B 313 ARG B 317 5 5
HELIX 42 42 GLY B 359 ASP B 374 1 16
HELIX 43 43 ASN B 380 LEU B 385 5 6
HELIX 44 44 GLU B 386 GLY B 391 1 6
HELIX 45 45 GLU B 396 ALA B 401 1 6
HELIX 46 46 ALA C 12 HIS C 14 5 3
HELIX 47 47 LEU C 15 ALA C 22 1 8
HELIX 48 48 SER C 49 THR C 59 1 11
HELIX 49 49 PRO C 95 GLY C 106 1 12
HELIX 50 50 ALA C 128 ARG C 134 1 7
HELIX 51 51 ARG C 176 SER C 178 5 3
HELIX 52 52 PHE C 179 ALA C 196 1 18
HELIX 53 53 ASN D 15 PHE D 17 5 3
HELIX 54 54 ASP D 30 LEU D 34 5 5
HELIX 55 55 SER D 35 TYR D 45 1 11
SHEET 1 A 2 GLN A 4 ARG A 5 0
SHEET 2 A 2 VAL A 280 ARG A 281 -1 O ARG A 281 N GLN A 4
SHEET 1 B 5 GLN A 29 ARG A 35 0
SHEET 2 B 5 ASN A 17 VAL A 26 -1 N LEU A 24 O LEU A 31
SHEET 3 B 5 LEU A 101 LEU A 105 1 O ALA A 103 N THR A 25
SHEET 4 B 5 LEU A 74 VAL A 77 -1 N THR A 76 O THR A 104
SHEET 5 B 5 GLU A 87 PRO A 91 -1 O GLU A 87 N VAL A 77
SHEET 1 C 6 THR A 196 LEU A 199 0
SHEET 2 C 6 VAL A 153 LEU A 156 1 N VAL A 153 O THR A 197
SHEET 3 C 6 TYR A 121 VAL A 133 1 N VAL A 132 O MET A 154
SHEET 4 C 6 GLU A 234 LEU A 246 1 O VAL A 245 N VAL A 133
SHEET 5 C 6 TYR A 212 ARG A 218 -1 N ILE A 213 O ILE A 239
SHEET 6 C 6 THR A 202 TYR A 208 -1 N PHE A 205 O LEU A 214
SHEET 1 D 5 THR A 196 LEU A 199 0
SHEET 2 D 5 VAL A 153 LEU A 156 1 N VAL A 153 O THR A 197
SHEET 3 D 5 TYR A 121 VAL A 133 1 N VAL A 132 O MET A 154
SHEET 4 D 5 GLU A 234 LEU A 246 1 O VAL A 245 N VAL A 133
SHEET 5 D 5 GLN A 412 LEU A 414 1 O HIS A 413 N LEU A 246
SHEET 1 E 2 GLN A 173 ILE A 174 0
SHEET 2 E 2 ILE A 177 ASP A 178 -1 O ILE A 177 N ILE A 174
SHEET 1 F 2 ALA A 250 GLU A 252 0
SHEET 2 F 2 PHE A 380 PRO A 382 -1 O ASN A 381 N HIS A 251
SHEET 1 G 5 ILE A 265 LEU A 267 0
SHEET 2 G 5 VAL A 373 SER A 377 1 O VAL A 376 N MET A 266
SHEET 3 G 5 ILE A 286 THR A 290 1 N ALA A 287 O ALA A 375
SHEET 4 G 5 VAL A 311 ASP A 313 1 O ILE A 312 N VAL A 288
SHEET 5 G 5 VAL A 332 LEU A 333 1 O LEU A 333 N VAL A 311
SHEET 1 H 3 SER A 336 ALA A 343 0
SHEET 2 H 3 LEU A 349 THR A 356 -1 O LEU A 353 N ALA A 339
SHEET 3 H 3 GLN A 367 GLU A 370 -1 O GLN A 367 N VAL A 354
SHEET 1 I 2 LEU A 394 ASP A 397 0
SHEET 2 I 2 ALA A 402 PRO A 405 -1 O ALA A 402 N ASP A 397
SHEET 1 J 2 PHE A 482 ASP A 484 0
SHEET 2 J 2 GLN A 489 THR A 490 -1 O GLN A 489 N VAL A 483
SHEET 1 K 9 VAL A 556 SER A 557 0
SHEET 2 K 9 HIS B 319 THR B 330 -1 O VAL B 320 N VAL A 556
SHEET 3 K 9 GLN B 243 LEU B 254 -1 N HIS B 245 O VAL B 328
SHEET 4 K 9 GLU B 279 ILE B 286 -1 O MET B 282 N LEU B 250
SHEET 5 K 9 VAL B 270 GLN B 274 -1 N SER B 273 O VAL B 281
SHEET 6 K 9 VAL B 262 SER B 265 -1 N VAL B 263 O VAL B 272
SHEET 7 K 9 VAL B 106 ALA B 110 1 N LEU B 107 O VAL B 262
SHEET 8 K 9 GLY B 160 GLN B 164 -1 O GLY B 160 N ALA B 110
SHEET 9 K 9 GLU B 134 LEU B 136 -1 N LEU B 136 O ALA B 161
SHEET 1 L 2 LYS A 588 VAL A 592 0
SHEET 2 L 2 TRP A 595 TYR A 600 -1 O TRP A 599 N LYS A 588
SHEET 1 M 6 PHE A 758 THR A 762 0
SHEET 2 M 6 GLU A 768 SER A 772 -1 O ALA A 769 N VAL A 761
SHEET 3 M 6 ALA A 781 PRO A 787 -1 O GLU A 783 N SER A 772
SHEET 4 M 6 LEU A 725 VAL A 731 -1 N VAL A 730 O PHE A 782
SHEET 5 M 6 GLY A 624 ASP A 627 -1 N GLY A 624 O VAL A 731
SHEET 6 M 6 THR A 808 PRO A 809 1 O THR A 808 N MET A 625
SHEET 1 N 5 GLY A 661 CYS A 667 0
SHEET 2 N 5 ILE A 673 ALA A 683 -1 O PHE A 674 N MET A 666
SHEET 3 N 5 ARG A 686 THR A 691 -1 O LEU A 688 N LEU A 680
SHEET 4 N 5 GLY A 632 ARG A 637 -1 N ILE A 634 O MET A 689
SHEET 5 N 5 THR A 717 SER A 720 -1 O THR A 719 N GLU A 635
SHEET 1 O 7 HIS A 870 PRO A 876 0
SHEET 2 O 7 ARG A 918 ILE A 925 -1 O ILE A 925 N HIS A 870
SHEET 3 O 7 GLY A 905 SER A 913 -1 N TRP A 906 O LEU A 924
SHEET 4 O 7 ALA A 888 ALA A 891 -1 N LEU A 889 O GLY A 905
SHEET 5 O 7 VAL A 935 VAL A 940 -1 O LYS A 937 N VAL A 890
SHEET 6 O 7 GLN A 943 SER A 950 -1 O VAL A 947 N LEU A 936
SHEET 7 O 7 HIS A 870 PRO A 876 -1 N LEU A 875 O GLN A 948
SHEET 1 P 6 ASP B 189 ILE B 191 0
SHEET 2 P 6 VAL B 48 LEU B 51 1 N VAL B 50 O ILE B 191
SHEET 3 P 6 SER B 20 VAL B 26 1 N ILE B 25 O ALA B 49
SHEET 4 P 6 ILE B 216 LEU B 223 1 O ALA B 222 N VAL B 26
SHEET 5 P 6 VAL B 206 THR B 211 -1 N THR B 207 O ALA B 218
SHEET 6 P 6 VAL B 196 LYS B 201 -1 N LEU B 200 O THR B 207
SHEET 1 Q 6 ASP B 189 ILE B 191 0
SHEET 2 Q 6 VAL B 48 LEU B 51 1 N VAL B 50 O ILE B 191
SHEET 3 Q 6 SER B 20 VAL B 26 1 N ILE B 25 O ALA B 49
SHEET 4 Q 6 ILE B 216 LEU B 223 1 O ALA B 222 N VAL B 26
SHEET 5 Q 6 LEU B 346 CYS B 350 1 O ASN B 349 N LEU B 223
SHEET 6 Q 6 ILE B 337 LYS B 340 -1 N SER B 339 O VAL B 348
SHEET 1 R 2 ILE B 67 ILE B 68 0
SHEET 2 R 2 GLY B 168 ILE B 169 -1 O GLY B 168 N ILE B 68
SHEET 1 S 5 THR C 31 GLU C 34 0
SHEET 2 S 5 LEU C 122 GLU C 125 -1 O GLN C 123 N ARG C 33
SHEET 3 S 5 SER C 170 LEU C 174 -1 O ILE C 173 N LEU C 122
SHEET 4 S 5 ILE C 159 GLY C 167 -1 N TRP C 164 O ARG C 172
SHEET 5 S 5 ARG C 150 LEU C 156 -1 N ARG C 150 O ARG C 165
SHEET 1 T 5 VAL C 70 GLY C 72 0
SHEET 2 T 5 THR C 77 GLY C 83 -1 O VAL C 79 N ALA C 71
SHEET 3 T 5 GLU C 86 ALA C 91 -1 O LEU C 88 N LEU C 80
SHEET 4 T 5 THR C 39 ARG C 44 -1 N THR C 39 O ALA C 91
SHEET 5 T 5 GLN C 111 ASP C 114 -1 O GLN C 111 N ARG C 44
SHEET 1 U 2 LEU D 3 CYS D 6 0
SHEET 2 U 2 GLY D 10 ASN D 13 -1 O ARG D 12 N ILE D 4
SHEET 1 V 4 LYS D 18 GLU D 22 0
SHEET 2 V 4 ILE D 52 VAL D 58 -1 O ARG D 56 N GLY D 20
SHEET 3 V 4 TRP D 66 ASP D 72 -1 O ARG D 71 N PHE D 53
SHEET 4 V 4 PHE D 78 ARG D 83 -1 O LYS D 79 N LEU D 70
LINK SG CYS D 6 ZN ZN D 100 1555 1555 2.31
LINK SG CYS D 9 ZN ZN D 100 1555 1555 2.29
LINK ND1 HIS D 59 ZN ZN D 100 1555 1555 2.16
LINK SG CYS D 63 ZN ZN D 100 1555 1555 2.31
CISPEP 1 ALA A 551 PRO A 552 0 3.53
SITE 1 AC1 31 GLY A 134 GLY A 136 PRO A 137 ALA A 138
SITE 2 AC1 31 ASP A 157 GLU A 158 ARG A 159 GLY A 164
SITE 3 AC1 31 THR A 165 THR A 202 THR A 203 VAL A 204
SITE 4 AC1 31 ALA A 247 THR A 248 ALA A 249 SER A 294
SITE 5 AC1 31 PHE A 380 LEU A 386 GLY A 416 ALA A 417
SITE 6 AC1 31 LEU A 422 ASP A 423 THR A 424 TYR A 553
SITE 7 AC1 31 HOH A 972 HOH A 978 HOH A1010 HOH A1022
SITE 8 AC1 31 HOH A1133 HOH A1148 HOH A1312
SITE 1 AC2 5 ARG A 597 LEU A 631 THR A 692 THR A 693
SITE 2 AC2 5 HOH A1596
SITE 1 AC3 5 ASN A 651 GLY A 652 SER A 847 LEU A 849
SITE 2 AC3 5 HOH A1529
SITE 1 AC4 2 SER A 7 ALA A 8
SITE 1 AC5 6 GLN A 217 ARG A 219 HOH A1154 HOH A1214
SITE 2 AC5 6 HOH A1378 VAL C 199
SITE 1 AC6 3 ARG A 686 HOH A1199 GLN C 102
SITE 1 AC7 2 ARG A 929 ASN A 930
SITE 1 AC8 6 ARG A 574 ALA A 696 ALA A 697 THR A 722
SITE 2 AC8 6 HOH A1574 ARG C 176
SITE 1 AC9 40 VAL B 26 GLY B 27 GLY B 29 GLY B 30
SITE 2 AC9 40 HIS B 31 LEU B 51 GLU B 52 LYS B 53
SITE 3 AC9 40 GLY B 59 ASN B 60 MET B 61 ARG B 63
SITE 4 AC9 40 ASN B 64 THR B 65 THR B 66 ILE B 67
SITE 5 AC9 40 CYS B 194 GLU B 195 VAL B 196 ALA B 224
SITE 6 AC9 40 GLY B 225 ALA B 226 HIS B 228 LEU B 232
SITE 7 AC9 40 LEU B 247 GLY B 326 GLY B 353 THR B 354
SITE 8 AC9 40 GLY B 355 GLY B 356 PHE B 357 LYS B 358
SITE 9 AC9 40 HOH B 412 HOH B 420 HOH B 475 HOH B 605
SITE 10 AC9 40 HOH B 654 PYC B 801 HOH B 862 HOH B 906
SITE 1 BC1 22 LYS A 509 ARG A 510 THR A 516 GLN A 520
SITE 2 BC1 22 THR A 548 ARG A 550 HOH A1030 ALA B 62
SITE 3 BC1 22 ARG B 63 ASN B 64 THR B 66 HIS B 172
SITE 4 BC1 22 VAL B 251 LYS B 277 GLU B 279 ARG B 322
SITE 5 BC1 22 TRP B 324 HOH B 437 HOH B 450 HOH B 495
SITE 6 BC1 22 HOH B 534 HOH B 544
SITE 1 BC2 12 THR B 65 ILE B 67 ARG B 69 TYR B 72
SITE 2 BC2 12 MET B 264 TYR B 271 THR B 354 GLY B 355
SITE 3 BC2 12 LYS B 358 VAL B 402 FAD B 405 HOH B 423
SITE 1 BC3 3 ASN B 13 ASN B 14 HOH B 458
SITE 1 BC4 5 PRO B 8 GLU B 9 PHE B 10 ARG B 181
SITE 2 BC4 5 HOH B 599
SITE 1 BC5 5 LYS B 171 HIS B 174 LYS B 277 HOH B 426
SITE 2 BC5 5 HOH B 848
SITE 1 BC6 5 GLN A 30 ALA C 25 GLY C 26 GLU C 27
SITE 2 BC6 5 ARG C 28
SITE 1 BC7 4 CYS D 6 CYS D 9 HIS D 59 CYS D 63
SITE 1 BC8 1 ARG D 83
CRYST1 198.796 198.796 196.819 90.00 90.00 120.00 P 65 2 2 12
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 0.005030 0.002904 0.000000 0.00000
SCALE2 0.000000 0.005808 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005081 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
