HEADER LYASE 12-JUN-17 5O86
TITLE MUTANT OF CLAAS II CPD PHOTOLYASE FROM METHANOSARCINA MAZEI - W388F
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEOXYRIBODIPYRIMIDINE PHOTOLYASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 4.1.99.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOSARCINA MAZEI GO1;
SOURCE 3 ORGANISM_TAXID: 192952;
SOURCE 4 GENE: MM_0852;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PHOTOREDUCTION, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.IGNATZ,L.-O.ESSEN
REVDAT 5 16-OCT-19 5O86 1 REMARK
REVDAT 4 24-JAN-18 5O86 1 JRNL
REVDAT 3 22-NOV-17 5O86 1 JRNL
REVDAT 2 08-NOV-17 5O86 1 JRNL
REVDAT 1 13-SEP-17 5O86 0
JRNL AUTH E.IGNATZ,Y.GEISSELBRECHT,S.KIONTKE,L.O.ESSEN
JRNL TITL NICOTINAMIDE ADENINE DINUCLEOTIDES ARREST PHOTOREDUCTION OF
JRNL TITL 2 CLASS II DNA PHOTOLYASES IN FADH ̇ STATE.
JRNL REF PHOTOCHEM. PHOTOBIOL. V. 94 81 2018
JRNL REFN ISSN 1751-1097
JRNL PMID 28858395
JRNL DOI 10.1111/PHP.12834
REMARK 2
REMARK 2 RESOLUTION. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 68732
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.480
REMARK 3 FREE R VALUE TEST SET COUNT : 1020
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.3205 - 3.2269 1.00 10227 140 0.1695 0.2063
REMARK 3 2 3.2269 - 2.5613 1.00 9740 150 0.1873 0.2347
REMARK 3 3 2.5613 - 2.2375 1.00 9619 147 0.2026 0.2388
REMARK 3 4 2.2375 - 2.0329 1.00 9625 132 0.2174 0.2615
REMARK 3 5 2.0329 - 1.8872 1.00 9490 161 0.2395 0.2629
REMARK 3 6 1.8872 - 1.7760 1.00 9507 142 0.2645 0.2720
REMARK 3 7 1.7760 - 1.6870 1.00 9504 148 0.2984 0.3453
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 3847
REMARK 3 ANGLE : 1.090 5224
REMARK 3 CHIRALITY : 0.056 536
REMARK 3 PLANARITY : 0.008 659
REMARK 3 DIHEDRAL : 14.833 2253
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2187 25.1060 105.1786
REMARK 3 T TENSOR
REMARK 3 T11: 0.1073 T22: 0.1596
REMARK 3 T33: -0.0222 T12: 0.0316
REMARK 3 T13: -0.0042 T23: -0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 1.0412 L22: 0.6500
REMARK 3 L33: 1.6067 L12: 0.0932
REMARK 3 L13: 0.0859 L23: -0.0268
REMARK 3 S TENSOR
REMARK 3 S11: -0.0185 S12: 0.1214 S13: -0.0013
REMARK 3 S21: -0.0636 S22: 0.0013 S23: 0.0356
REMARK 3 S31: -0.0881 S32: -0.0223 S33: 0.0099
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5O86 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1200005049.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979003
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68915
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.687
REMARK 200 RESOLUTION RANGE LOW (A) : 81.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.20000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 M LITHIUM SULFATE, 7.5% (W/V) PEG
REMARK 280 6000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.15K
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 121.92500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.86000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.86000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 182.88750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.86000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.86000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 60.96250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.86000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.86000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 182.88750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.86000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.86000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 60.96250
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 121.92500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -143.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ILE A 2
REMARK 465 GLU A 189
REMARK 465 LEU A 190
REMARK 465 SER A 191
REMARK 465 ALA A 192
REMARK 465 GLY A 193
REMARK 465 ALA A 194
REMARK 465 GLY A 195
REMARK 465 MET A 196
REMARK 465 VAL A 197
REMARK 465 ALA A 463
REMARK 465 LEU A 464
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 ARG A 94 NE CZ NH1 NH2
REMARK 470 LYS A 106 CD CE NZ
REMARK 470 LEU A 218 CG CD1 CD2
REMARK 470 LYS A 219 CG CD CE NZ
REMARK 470 ASN A 220 CG OD1 ND2
REMARK 470 LYS A 221 CG CD CE NZ
REMARK 470 GLU A 348 CD OE1 OE2
REMARK 470 LYS A 394 CE NZ
REMARK 470 LYS A 455 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 OE2 GLU A 351 HH TYR A 406 1.54
REMARK 500 H GLY A 293 O4 SO4 A 507 1.57
REMARK 500 O SER A 290 O HOH A 601 1.78
REMARK 500 O3 GOL A 511 O HOH A 602 1.88
REMARK 500 O1 GOL A 511 O HOH A 603 1.94
REMARK 500 O1 SO4 A 508 O HOH A 604 2.05
REMARK 500 O HOH A 833 O HOH A 902 2.14
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 O HOH A 701 O HOH A 914 7556 1.73
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 121 NE - CZ - NH2 ANGL. DEV. = -3.2 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 SER A 26 -62.61 -140.21
REMARK 500 ALA A 64 -144.76 -121.87
REMARK 500 ASN A 220 2.05 -67.07
REMARK 500 LEU A 303 -67.20 -98.94
REMARK 500 VAL A 436 -66.64 69.04
REMARK 500 TYR A 461 57.47 -113.35
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 FAD A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 512
DBREF 5O86 A 1 464 UNP Q8PYK9 Q8PYK9_METMA 1 464
SEQADV 5O86 MET A -19 UNP Q8PYK9 INITIATING METHIONINE
SEQADV 5O86 GLY A -18 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 SER A -17 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 SER A -16 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 HIS A -15 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 HIS A -14 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 HIS A -13 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 HIS A -12 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 HIS A -11 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 HIS A -10 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 SER A -9 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 SER A -8 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 GLY A -7 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 LEU A -6 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 VAL A -5 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 PRO A -4 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 ARG A -3 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 GLY A -2 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 SER A -1 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 HIS A 0 UNP Q8PYK9 EXPRESSION TAG
SEQADV 5O86 THR A 377 UNP Q8PYK9 MET 377 ENGINEERED MUTATION
SEQADV 5O86 PHE A 388 UNP Q8PYK9 TRP 388 ENGINEERED MUTATION
SEQRES 1 A 484 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 484 LEU VAL PRO ARG GLY SER HIS MET ILE MET ASN PRO LYS
SEQRES 3 A 484 ARG ILE ARG ALA LEU LYS SER GLY LYS GLN GLY ASP GLY
SEQRES 4 A 484 PRO VAL VAL TYR TRP MET SER ARG ASP GLN ARG ALA GLU
SEQRES 5 A 484 ASP ASN TRP ALA LEU LEU PHE SER ARG ALA ILE ALA LYS
SEQRES 6 A 484 GLU ALA ASN VAL PRO VAL VAL VAL VAL PHE CYS LEU THR
SEQRES 7 A 484 ASP GLU PHE LEU GLU ALA GLY ILE ARG GLN TYR GLU PHE
SEQRES 8 A 484 MET LEU LYS GLY LEU GLN GLU LEU GLU VAL SER LEU SER
SEQRES 9 A 484 ARG LYS LYS ILE PRO SER PHE PHE LEU ARG GLY ASP PRO
SEQRES 10 A 484 GLY GLU LYS ILE SER ARG PHE VAL LYS ASP TYR ASN ALA
SEQRES 11 A 484 GLY THR LEU VAL THR ASP PHE SER PRO LEU ARG ILE LYS
SEQRES 12 A 484 ASN GLN TRP ILE GLU LYS VAL ILE SER GLY ILE SER ILE
SEQRES 13 A 484 PRO PHE PHE GLU VAL ASP ALA HIS ASN VAL VAL PRO CYS
SEQRES 14 A 484 TRP GLU ALA SER GLN LYS HIS GLU TYR ALA ALA HIS THR
SEQRES 15 A 484 PHE ARG PRO LYS LEU TYR ALA LEU LEU PRO GLU PHE LEU
SEQRES 16 A 484 GLU GLU PHE PRO GLU LEU GLU PRO ASN SER VAL THR PRO
SEQRES 17 A 484 GLU LEU SER ALA GLY ALA GLY MET VAL GLU THR LEU SER
SEQRES 18 A 484 ASP VAL LEU GLU THR GLY VAL LYS ALA LEU LEU PRO GLU
SEQRES 19 A 484 ARG ALA LEU LEU LYS ASN LYS ASP PRO LEU PHE GLU PRO
SEQRES 20 A 484 TRP HIS PHE GLU PRO GLY GLU LYS ALA ALA LYS LYS VAL
SEQRES 21 A 484 MET GLU SER PHE ILE ALA ASP ARG LEU ASP SER TYR GLY
SEQRES 22 A 484 ALA LEU ARG ASN ASP PRO THR LYS ASN MET LEU SER ASN
SEQRES 23 A 484 LEU SER PRO TYR LEU HIS PHE GLY GLN ILE SER SER GLN
SEQRES 24 A 484 ARG VAL VAL LEU GLU VAL GLU LYS ALA GLU SER ASN PRO
SEQRES 25 A 484 GLY SER LYS LYS ALA PHE LEU ASP GLU ILE LEU ILE TRP
SEQRES 26 A 484 LYS GLU ILE SER ASP ASN PHE CYS TYR TYR ASN PRO GLY
SEQRES 27 A 484 TYR ASP GLY PHE GLU SER PHE PRO SER TRP ALA LYS GLU
SEQRES 28 A 484 SER LEU ASN ALA HIS ARG ASN ASP VAL ARG SER HIS ILE
SEQRES 29 A 484 TYR THR LEU GLU GLU PHE GLU ALA GLY LYS THR HIS ASP
SEQRES 30 A 484 PRO LEU TRP ASN ALA SER GLN MET GLU LEU LEU SER THR
SEQRES 31 A 484 GLY LYS MET HIS GLY TYR THR ARG MET TYR TRP ALA LYS
SEQRES 32 A 484 LYS ILE LEU GLU PHE SER GLU SER PRO GLU LYS ALA LEU
SEQRES 33 A 484 GLU ILE ALA ILE CYS LEU ASN ASP ARG TYR GLU LEU ASP
SEQRES 34 A 484 GLY ARG ASP PRO ASN GLY TYR ALA GLY ILE ALA TRP SER
SEQRES 35 A 484 ILE GLY GLY VAL HIS ASP ARG ALA TRP GLY GLU ARG GLU
SEQRES 36 A 484 VAL THR GLY LYS ILE ARG TYR MET SER TYR GLU GLY CYS
SEQRES 37 A 484 LYS ARG LYS PHE ASP VAL LYS LEU TYR ILE GLU LYS TYR
SEQRES 38 A 484 SER ALA LEU
HET FAD A 501 83
HET SO4 A 502 5
HET SO4 A 503 5
HET SO4 A 504 5
HET SO4 A 505 5
HET SO4 A 506 5
HET SO4 A 507 5
HET SO4 A 508 5
HET SO4 A 509 5
HET SO4 A 510 5
HET GOL A 511 14
HET GOL A 512 14
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 FAD C27 H33 N9 O15 P2
FORMUL 3 SO4 9(O4 S 2-)
FORMUL 12 GOL 2(C3 H8 O3)
FORMUL 14 HOH *314(H2 O)
HELIX 1 AA1 ASN A 4 LYS A 6 5 3
HELIX 2 AA2 ASN A 34 ASN A 48 1 15
HELIX 3 AA3 THR A 58 ALA A 64 5 7
HELIX 4 AA4 GLY A 65 LYS A 86 1 22
HELIX 5 AA5 ASP A 96 TYR A 108 1 13
HELIX 6 AA6 LEU A 120 ILE A 134 1 15
HELIX 7 AA7 PRO A 148 SER A 153 1 6
HELIX 8 AA8 ALA A 159 LEU A 175 1 17
HELIX 9 AA9 THR A 199 LEU A 212 1 14
HELIX 10 AB1 PRO A 213 ARG A 215 5 3
HELIX 11 AB2 GLY A 233 ARG A 248 1 16
HELIX 12 AB3 ARG A 248 ARG A 256 1 9
HELIX 13 AB4 LEU A 267 PHE A 273 1 7
HELIX 14 AB5 SER A 277 ALA A 288 1 12
HELIX 15 AB6 GLY A 293 LEU A 303 1 11
HELIX 16 AB7 LEU A 303 ASN A 316 1 14
HELIX 17 AB8 GLY A 321 PHE A 325 5 5
HELIX 18 AB9 PRO A 326 HIS A 336 1 11
HELIX 19 AC1 THR A 346 ALA A 352 1 7
HELIX 20 AC2 ASP A 357 GLY A 371 1 15
HELIX 21 AC3 HIS A 374 PHE A 388 1 15
HELIX 22 AC4 SER A 391 GLU A 407 1 17
HELIX 23 AC5 ASP A 412 GLY A 425 1 14
HELIX 24 AC6 SER A 444 ARG A 450 1 7
HELIX 25 AC7 ASP A 453 TYR A 461 1 9
SHEET 1 AA1 6 ILE A 8 LYS A 12 0
SHEET 2 AA1 6 PHE A 138 VAL A 141 -1 O PHE A 138 N LEU A 11
SHEET 3 AA1 6 THR A 112 ASP A 116 1 N LEU A 113 O PHE A 139
SHEET 4 AA1 6 VAL A 21 TRP A 24 1 N TRP A 24 O VAL A 114
SHEET 5 AA1 6 VAL A 51 LEU A 57 1 O VAL A 52 N TYR A 23
SHEET 6 AA1 6 SER A 90 ARG A 94 1 O LEU A 93 N PHE A 55
SITE 1 AC1 30 TYR A 252 LEU A 264 SER A 265 ASN A 266
SITE 2 AC1 30 LEU A 267 SER A 268 LEU A 271 PHE A 298
SITE 3 AC1 30 GLU A 301 ILE A 302 TRP A 305 LYS A 306
SITE 4 AC1 30 SER A 309 LYS A 372 GLY A 375 ARG A 378
SITE 5 AC1 30 MET A 379 ALA A 382 ASN A 403 ASP A 409
SITE 6 AC1 30 GLY A 410 ASN A 414 GLY A 415 SER A 422
SITE 7 AC1 30 GOL A 512 HOH A 614 HOH A 722 HOH A 732
SITE 8 AC1 30 HOH A 746 HOH A 807
SITE 1 AC2 9 ILE A 66 ARG A 67 ARG A 215 ALA A 216
SITE 2 AC2 9 PHE A 225 ARG A 405 HOH A 704 HOH A 789
SITE 3 AC2 9 HOH A 795
SITE 1 AC3 6 ALA A 159 ALA A 160 HIS A 161 ARG A 164
SITE 2 AC3 6 HOH A 708 HOH A 835
SITE 1 AC4 9 LYS A 129 HIS A 156 TYR A 158 PRO A 326
SITE 2 AC4 9 HOH A 617 HOH A 620 HOH A 638 HOH A 763
SITE 3 AC4 9 HOH A 794
SITE 1 AC5 6 GLN A 77 GLU A 80 THR A 199 LEU A 200
SITE 2 AC5 6 SER A 201 HOH A 626
SITE 1 AC6 5 LYS A 449 PHE A 452 ASP A 453 VAL A 454
SITE 2 AC6 5 LYS A 455
SITE 1 AC7 6 PRO A 292 GLY A 293 SER A 294 LYS A 295
SITE 2 AC7 6 LYS A 296 HOH A 852
SITE 1 AC8 8 ASP A 96 GLY A 98 GLU A 99 SER A 327
SITE 2 AC8 8 LYS A 330 HOH A 604 HOH A 617 HOH A 763
SITE 1 AC9 4 SER A 153 GLN A 154 LYS A 166 HOH A 661
SITE 1 AD1 5 SER A 26 SER A 118 TRP A 126 HOH A 731
SITE 2 AD1 5 HOH A 780
SITE 1 AD2 6 ARG A 121 ILE A 122 TYR A 319 HOH A 602
SITE 2 AD2 6 HOH A 603 HOH A 649
SITE 1 AD3 7 TRP A 305 MET A 379 GLY A 418 TRP A 421
SITE 2 AD3 7 FAD A 501 HOH A 614 HOH A 625
CRYST1 69.720 69.720 243.850 90.00 90.00 90.00 P 43 21 2 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 0.014343 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014343 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004101 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
