HEADER OXIDOREDUCTASE 11-JAN-10 3LCM
TITLE CRYSTAL STRUCTURE OF SMU.1420 FROM STREPTOCOCCUS MUTANS UA159
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE OXIDOREDUCTASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: SMU.1420;
COMPND 5 EC: 1.6.99.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS MUTANS;
SOURCE 3 ORGANISM_TAXID: 210007;
SOURCE 4 STRAIN: UA159;
SOURCE 5 GENE: SMU.1420;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-21B
KEYWDS NADPH:QUINONE OXIDOREDUCTASE, MDAB, SMU.1420, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.X.WANG,X.-D.SU
REVDAT 4 01-NOV-23 3LCM 1 REMARK SEQADV
REVDAT 3 04-OCT-17 3LCM 1 REMARK
REVDAT 2 16-APR-14 3LCM 1 JRNL VERSN
REVDAT 1 12-JAN-11 3LCM 0
JRNL AUTH Z.X.WANG,L.LI,Y.H.DONG,X.-D.SU
JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF MDAB FROM
JRNL TITL 2 CARIOGENIC STREPTOCOCCUS MUTANS REVEALS AN NADPH-SPECIFIC
JRNL TITL 3 QUINONE OXIDOREDUCTASE
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 912 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 24699637
JRNL DOI 10.1107/S1399004713033749
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 73733
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.810
REMARK 3 FREE R VALUE TEST SET COUNT : 2072
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 29.0224 - 4.8768 0.98 3815 106 0.1534 0.1575
REMARK 3 2 4.8768 - 3.8738 0.98 3808 106 0.1006 0.1257
REMARK 3 3 3.8738 - 3.3850 0.98 3792 106 0.1176 0.1485
REMARK 3 4 3.3850 - 3.0759 0.98 3809 107 0.1395 0.1619
REMARK 3 5 3.0759 - 2.8556 0.98 3793 105 0.1556 0.1944
REMARK 3 6 2.8556 - 2.6874 0.98 3762 105 0.1696 0.2202
REMARK 3 7 2.6874 - 2.5529 0.98 3760 104 0.1713 0.2092
REMARK 3 8 2.5529 - 2.4418 0.98 3728 105 0.1745 0.2038
REMARK 3 9 2.4418 - 2.3478 0.98 3658 102 0.1762 0.1927
REMARK 3 10 2.3478 - 2.2668 0.98 3591 100 0.1807 0.1910
REMARK 3 11 2.2668 - 2.1960 0.98 3506 98 0.1862 0.2195
REMARK 3 12 2.1960 - 2.1332 0.98 3526 98 0.1911 0.2105
REMARK 3 13 2.1332 - 2.0771 0.98 3460 97 0.1922 0.2756
REMARK 3 14 2.0771 - 2.0264 0.98 3423 95 0.1987 0.2185
REMARK 3 15 2.0264 - 1.9804 0.98 3491 97 0.2089 0.2190
REMARK 3 16 1.9804 - 1.9382 0.98 3366 94 0.2139 0.2486
REMARK 3 17 1.9382 - 1.8995 0.98 3497 97 0.2273 0.2595
REMARK 3 18 1.8995 - 1.8636 0.98 3435 96 0.2350 0.2538
REMARK 3 19 1.8636 - 1.8304 0.98 3461 97 0.2507 0.2706
REMARK 3 20 1.8304 - 1.7993 0.98 3052 85 0.2674 0.3269
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 : 0.39
REMARK 3 B_SOL : 44.14
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.69700
REMARK 3 B22 (A**2) : -1.33400
REMARK 3 B33 (A**2) : 3.03100
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -5.60100
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: 0.4250
REMARK 3 OPERATOR: H,-K,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 6503
REMARK 3 ANGLE : 1.034 8919
REMARK 3 CHIRALITY : 0.063 981
REMARK 3 PLANARITY : 0.005 1085
REMARK 3 DIHEDRAL : 18.566 2394
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 3LCM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000057111.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BSRF
REMARK 200 BEAMLINE : 1W2B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9796
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR555 FLAT PANEL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73792
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.799
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.30500
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1ZX1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M KCL, 0.05M HEPES PH7.5, 35% V/V
REMARK 280 PENTAERYTHRITOL PROPOXYLATE(5/4 PO/OH), VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 39.55900
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 LEU B 189
REMARK 465 GLU B 190
REMARK 465 HIS B 191
REMARK 465 HIS B 192
REMARK 465 HIS B 193
REMARK 465 HIS B 194
REMARK 465 HIS B 195
REMARK 465 HIS B 196
REMARK 465 LEU D 189
REMARK 465 GLU D 190
REMARK 465 HIS D 191
REMARK 465 HIS D 192
REMARK 465 HIS D 193
REMARK 465 HIS D 194
REMARK 465 HIS D 195
REMARK 465 HIS D 196
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 21 CE NZ
REMARK 470 LYS A 54 CG CD CE NZ
REMARK 470 ARG A 56 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 60 CE NZ
REMARK 470 LYS A 109 CG CD CE NZ
REMARK 470 LYS A 110 CG CD CE NZ
REMARK 470 GLU A 114 CG CD OE1 OE2
REMARK 470 LYS A 147 CD CE NZ
REMARK 470 LYS A 151 CG CD CE NZ
REMARK 470 GLU A 167 CG CD OE1 OE2
REMARK 470 LYS A 168 CG CD CE NZ
REMARK 470 ASP A 171 CG OD1 OD2
REMARK 470 GLN A 175 CG CD OE1 NE2
REMARK 470 LYS A 176 CE NZ
REMARK 470 GLU A 190 CG CD OE1 OE2
REMARK 470 LYS B 21 CG CD CE NZ
REMARK 470 LYS B 29 CG CD CE NZ
REMARK 470 GLU B 30 CG CD OE1 OE2
REMARK 470 LYS B 54 CG CD CE NZ
REMARK 470 ARG B 56 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 60 CG CD CE NZ
REMARK 470 GLU B 65 CG CD OE1 OE2
REMARK 470 LYS B 66 CE NZ
REMARK 470 LYS B 109 CG CD CE NZ
REMARK 470 LYS B 110 CG CD CE NZ
REMARK 470 VAL B 111 CG1 CG2
REMARK 470 GLU B 114 CG CD OE1 OE2
REMARK 470 PHE B 137 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 147 CG CD CE NZ
REMARK 470 GLU B 173 CG CD OE1 OE2
REMARK 470 LYS B 180 CD CE NZ
REMARK 470 LYS C 21 CD CE NZ
REMARK 470 LYS C 54 CG CD CE NZ
REMARK 470 ARG C 56 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 60 CG CD CE NZ
REMARK 470 LYS C 109 CG CD CE NZ
REMARK 470 LYS C 110 CG CD CE NZ
REMARK 470 VAL C 111 CG1 CG2
REMARK 470 GLU C 114 CG CD OE1 OE2
REMARK 470 GLN C 118 CG CD OE1 NE2
REMARK 470 LYS C 143 CE NZ
REMARK 470 LYS C 151 CG CD CE NZ
REMARK 470 LYS C 159 CG CD CE NZ
REMARK 470 LYS C 176 CG CD CE NZ
REMARK 470 LYS C 180 CD CE NZ
REMARK 470 GLN C 183 CG CD OE1 NE2
REMARK 470 LYS D 21 CD CE NZ
REMARK 470 LYS D 29 CG CD CE NZ
REMARK 470 GLU D 30 CG CD OE1 OE2
REMARK 470 HIS D 42 CG ND1 CD2 CE1 NE2
REMARK 470 GLU D 51 CG CD OE1 OE2
REMARK 470 ARG D 56 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 60 CG CD CE NZ
REMARK 470 ASP D 103 CG OD1 OD2
REMARK 470 LYS D 109 CG CD CE NZ
REMARK 470 LYS D 110 CG CD CE NZ
REMARK 470 VAL D 111 CG1 CG2
REMARK 470 LEU D 113 CG CD1 CD2
REMARK 470 LYS D 147 CG CD CE NZ
REMARK 470 LYS D 151 CG CD CE NZ
REMARK 470 GLU D 167 CG CD OE1 OE2
REMARK 470 LYS D 168 CG CD CE NZ
REMARK 470 LYS D 176 CG CD CE NZ
REMARK 470 HIS D 179 CG ND1 CD2 CE1 NE2
REMARK 470 LYS D 180 CG CD CE NZ
REMARK 470 GLN D 183 CG CD OE1 NE2
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 50 -171.44 -170.78
REMARK 500 PHE A 104 -65.61 -129.43
REMARK 500 ASP A 140 -112.94 66.07
REMARK 500 ILE A 149 -69.33 -124.08
REMARK 500 SER A 156 141.07 -172.05
REMARK 500 ASN B 50 -162.30 179.88
REMARK 500 PRO B 89 150.65 -49.79
REMARK 500 PHE B 104 -62.98 -122.98
REMARK 500 LEU B 117 33.03 -98.48
REMARK 500 ASP B 140 -111.56 68.25
REMARK 500 ILE B 149 -64.07 -125.57
REMARK 500 ALA B 154 9.23 81.54
REMARK 500 PHE C 49 146.01 -174.58
REMARK 500 ASN C 50 -159.52 -152.68
REMARK 500 SER C 86 -0.15 76.16
REMARK 500 PHE C 104 -60.04 -120.58
REMARK 500 LYS C 109 -158.45 -94.53
REMARK 500 ASP C 140 -108.74 75.09
REMARK 500 ILE C 149 -62.15 -134.06
REMARK 500 ASN D 50 -159.55 -160.24
REMARK 500 THR D 52 -75.01 -80.26
REMARK 500 PHE D 104 -74.14 -133.34
REMARK 500 ASP D 140 -117.95 64.57
REMARK 500 ILE D 149 -73.21 -126.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 NAP A 198
REMARK 610 NAP B 198
REMARK 610 NAP C 198
REMARK 610 NAP C 199
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 197
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 198
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 197
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 198
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 197
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C 198
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C 199
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D 197
DBREF 3LCM A 1 188 UNP Q8DTD1 Q8DTD1_STRMU 1 188
DBREF 3LCM B 1 188 UNP Q8DTD1 Q8DTD1_STRMU 1 188
DBREF 3LCM C 1 188 UNP Q8DTD1 Q8DTD1_STRMU 1 188
DBREF 3LCM D 1 188 UNP Q8DTD1 Q8DTD1_STRMU 1 188
SEQADV 3LCM LEU A 189 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM GLU A 190 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS A 191 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS A 192 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS A 193 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS A 194 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS A 195 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS A 196 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM LEU B 189 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM GLU B 190 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS B 191 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS B 192 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS B 193 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS B 194 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS B 195 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS B 196 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM LEU C 189 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM GLU C 190 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS C 191 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS C 192 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS C 193 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS C 194 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS C 195 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS C 196 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM LEU D 189 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM GLU D 190 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS D 191 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS D 192 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS D 193 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS D 194 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS D 195 UNP Q8DTD1 EXPRESSION TAG
SEQADV 3LCM HIS D 196 UNP Q8DTD1 EXPRESSION TAG
SEQRES 1 A 196 MET LYS ILE LEU ILE VAL TYR THR HIS PRO ASN PRO THR
SEQRES 2 A 196 SER PHE ASN ALA GLU ILE LEU LYS GLN VAL GLN THR ASN
SEQRES 3 A 196 LEU SER LYS GLU HIS THR VAL SER THR LEU ASP LEU TYR
SEQRES 4 A 196 ALA GLU HIS PHE ASP PRO VAL LEU GLN PHE ASN GLU THR
SEQRES 5 A 196 HIS LYS ARG ARG ASP LEU ALA LYS VAL ALA GLU MET GLU
SEQRES 6 A 196 LYS TYR ARG ASP LEU VAL THR TRP ALA ASP HIS LEU ILE
SEQRES 7 A 196 PHE ILE PHE PRO ILE TRP TRP SER GLY MET PRO ALA ILE
SEQRES 8 A 196 LEU LYS GLY PHE ILE ASP ARG VAL PHE VAL ALA ASP PHE
SEQRES 9 A 196 ALA TYR SER TYR LYS LYS VAL GLY LEU GLU GLY HIS LEU
SEQRES 10 A 196 GLN GLY LYS SER ALA TRP ILE ILE THR THR HIS ASN THR
SEQRES 11 A 196 PRO SER PHE ALA MET PRO PHE VAL GLN ASP TYR GLY LYS
SEQRES 12 A 196 VAL LEU LYS LYS GLN ILE LEU LYS PRO CYS ALA ILE SER
SEQRES 13 A 196 PRO VAL LYS LEU THR GLU LEU THR SER ILE GLU LYS ILE
SEQRES 14 A 196 SER ASP ASP GLU ARG GLN LYS LEU LEU HIS LYS VAL ALA
SEQRES 15 A 196 GLN ILE THR ARG ASN ILE LEU GLU HIS HIS HIS HIS HIS
SEQRES 16 A 196 HIS
SEQRES 1 B 196 MET LYS ILE LEU ILE VAL TYR THR HIS PRO ASN PRO THR
SEQRES 2 B 196 SER PHE ASN ALA GLU ILE LEU LYS GLN VAL GLN THR ASN
SEQRES 3 B 196 LEU SER LYS GLU HIS THR VAL SER THR LEU ASP LEU TYR
SEQRES 4 B 196 ALA GLU HIS PHE ASP PRO VAL LEU GLN PHE ASN GLU THR
SEQRES 5 B 196 HIS LYS ARG ARG ASP LEU ALA LYS VAL ALA GLU MET GLU
SEQRES 6 B 196 LYS TYR ARG ASP LEU VAL THR TRP ALA ASP HIS LEU ILE
SEQRES 7 B 196 PHE ILE PHE PRO ILE TRP TRP SER GLY MET PRO ALA ILE
SEQRES 8 B 196 LEU LYS GLY PHE ILE ASP ARG VAL PHE VAL ALA ASP PHE
SEQRES 9 B 196 ALA TYR SER TYR LYS LYS VAL GLY LEU GLU GLY HIS LEU
SEQRES 10 B 196 GLN GLY LYS SER ALA TRP ILE ILE THR THR HIS ASN THR
SEQRES 11 B 196 PRO SER PHE ALA MET PRO PHE VAL GLN ASP TYR GLY LYS
SEQRES 12 B 196 VAL LEU LYS LYS GLN ILE LEU LYS PRO CYS ALA ILE SER
SEQRES 13 B 196 PRO VAL LYS LEU THR GLU LEU THR SER ILE GLU LYS ILE
SEQRES 14 B 196 SER ASP ASP GLU ARG GLN LYS LEU LEU HIS LYS VAL ALA
SEQRES 15 B 196 GLN ILE THR ARG ASN ILE LEU GLU HIS HIS HIS HIS HIS
SEQRES 16 B 196 HIS
SEQRES 1 C 196 MET LYS ILE LEU ILE VAL TYR THR HIS PRO ASN PRO THR
SEQRES 2 C 196 SER PHE ASN ALA GLU ILE LEU LYS GLN VAL GLN THR ASN
SEQRES 3 C 196 LEU SER LYS GLU HIS THR VAL SER THR LEU ASP LEU TYR
SEQRES 4 C 196 ALA GLU HIS PHE ASP PRO VAL LEU GLN PHE ASN GLU THR
SEQRES 5 C 196 HIS LYS ARG ARG ASP LEU ALA LYS VAL ALA GLU MET GLU
SEQRES 6 C 196 LYS TYR ARG ASP LEU VAL THR TRP ALA ASP HIS LEU ILE
SEQRES 7 C 196 PHE ILE PHE PRO ILE TRP TRP SER GLY MET PRO ALA ILE
SEQRES 8 C 196 LEU LYS GLY PHE ILE ASP ARG VAL PHE VAL ALA ASP PHE
SEQRES 9 C 196 ALA TYR SER TYR LYS LYS VAL GLY LEU GLU GLY HIS LEU
SEQRES 10 C 196 GLN GLY LYS SER ALA TRP ILE ILE THR THR HIS ASN THR
SEQRES 11 C 196 PRO SER PHE ALA MET PRO PHE VAL GLN ASP TYR GLY LYS
SEQRES 12 C 196 VAL LEU LYS LYS GLN ILE LEU LYS PRO CYS ALA ILE SER
SEQRES 13 C 196 PRO VAL LYS LEU THR GLU LEU THR SER ILE GLU LYS ILE
SEQRES 14 C 196 SER ASP ASP GLU ARG GLN LYS LEU LEU HIS LYS VAL ALA
SEQRES 15 C 196 GLN ILE THR ARG ASN ILE LEU GLU HIS HIS HIS HIS HIS
SEQRES 16 C 196 HIS
SEQRES 1 D 196 MET LYS ILE LEU ILE VAL TYR THR HIS PRO ASN PRO THR
SEQRES 2 D 196 SER PHE ASN ALA GLU ILE LEU LYS GLN VAL GLN THR ASN
SEQRES 3 D 196 LEU SER LYS GLU HIS THR VAL SER THR LEU ASP LEU TYR
SEQRES 4 D 196 ALA GLU HIS PHE ASP PRO VAL LEU GLN PHE ASN GLU THR
SEQRES 5 D 196 HIS LYS ARG ARG ASP LEU ALA LYS VAL ALA GLU MET GLU
SEQRES 6 D 196 LYS TYR ARG ASP LEU VAL THR TRP ALA ASP HIS LEU ILE
SEQRES 7 D 196 PHE ILE PHE PRO ILE TRP TRP SER GLY MET PRO ALA ILE
SEQRES 8 D 196 LEU LYS GLY PHE ILE ASP ARG VAL PHE VAL ALA ASP PHE
SEQRES 9 D 196 ALA TYR SER TYR LYS LYS VAL GLY LEU GLU GLY HIS LEU
SEQRES 10 D 196 GLN GLY LYS SER ALA TRP ILE ILE THR THR HIS ASN THR
SEQRES 11 D 196 PRO SER PHE ALA MET PRO PHE VAL GLN ASP TYR GLY LYS
SEQRES 12 D 196 VAL LEU LYS LYS GLN ILE LEU LYS PRO CYS ALA ILE SER
SEQRES 13 D 196 PRO VAL LYS LEU THR GLU LEU THR SER ILE GLU LYS ILE
SEQRES 14 D 196 SER ASP ASP GLU ARG GLN LYS LEU LEU HIS LYS VAL ALA
SEQRES 15 D 196 GLN ILE THR ARG ASN ILE LEU GLU HIS HIS HIS HIS HIS
SEQRES 16 D 196 HIS
HET FAD A 197 53
HET NAP A 198 9
HET FAD B 197 53
HET NAP B 198 9
HET FAD C 197 53
HET NAP C 198 26
HET NAP C 199 9
HET FAD D 197 53
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 5 FAD 4(C27 H33 N9 O15 P2)
FORMUL 6 NAP 4(C21 H28 N7 O17 P3)
FORMUL 13 HOH *367(H2 O)
HELIX 1 1 SER A 14 LEU A 27 1 14
HELIX 2 2 LYS A 54 GLU A 63 5 10
HELIX 3 3 MET A 64 ALA A 74 1 11
HELIX 4 4 PRO A 89 PHE A 100 1 12
HELIX 5 5 PRO A 131 MET A 135 5 5
HELIX 6 6 GLY A 142 ILE A 149 1 8
HELIX 7 7 LEU A 150 ALA A 154 5 5
HELIX 8 8 SER A 170 ASN A 187 1 18
HELIX 9 9 SER B 14 LEU B 27 1 14
HELIX 10 10 LYS B 54 GLU B 63 5 10
HELIX 11 11 MET B 64 ALA B 74 1 11
HELIX 12 12 PRO B 89 PHE B 100 1 12
HELIX 13 13 PRO B 131 VAL B 138 5 8
HELIX 14 14 GLY B 142 ILE B 149 1 8
HELIX 15 15 SER B 170 ASN B 187 1 18
HELIX 16 16 SER C 14 LEU C 27 1 14
HELIX 17 17 LEU C 38 HIS C 42 1 5
HELIX 18 18 LYS C 54 GLU C 63 5 10
HELIX 19 19 MET C 64 ALA C 74 1 11
HELIX 20 20 PRO C 89 PHE C 100 1 12
HELIX 21 21 PRO C 131 VAL C 138 5 8
HELIX 22 22 GLY C 142 GLN C 148 1 7
HELIX 23 23 LEU C 150 ALA C 154 5 5
HELIX 24 24 SER C 170 ARG C 186 1 17
HELIX 25 25 SER D 14 LEU D 27 1 14
HELIX 26 26 LYS D 54 GLU D 63 5 10
HELIX 27 27 MET D 64 ALA D 74 1 11
HELIX 28 28 PRO D 89 PHE D 100 1 12
HELIX 29 29 ALA D 134 VAL D 138 5 5
HELIX 30 30 GLY D 142 ILE D 149 1 8
HELIX 31 31 SER D 170 ASN D 187 1 18
SHEET 1 A 5 THR A 32 ASP A 37 0
SHEET 2 A 5 LYS A 2 TYR A 7 1 N ILE A 5 O LEU A 36
SHEET 3 A 5 HIS A 76 PRO A 82 1 O ILE A 78 N VAL A 6
SHEET 4 A 5 SER A 121 THR A 127 1 O ILE A 125 N PHE A 79
SHEET 5 A 5 VAL A 158 LEU A 163 1 O THR A 161 N ILE A 124
SHEET 1 B 2 TYR A 106 TYR A 108 0
SHEET 2 B 2 LEU A 113 GLY A 115 -1 O GLU A 114 N SER A 107
SHEET 1 C 5 THR B 32 ASP B 37 0
SHEET 2 C 5 LYS B 2 TYR B 7 1 N ILE B 5 O LEU B 36
SHEET 3 C 5 HIS B 76 PRO B 82 1 O ILE B 78 N LEU B 4
SHEET 4 C 5 SER B 121 THR B 127 1 O ILE B 125 N PHE B 79
SHEET 5 C 5 VAL B 158 LEU B 163 1 O LYS B 159 N ILE B 124
SHEET 1 D 2 TYR B 106 TYR B 108 0
SHEET 2 D 2 LEU B 113 GLY B 115 -1 O GLU B 114 N SER B 107
SHEET 1 E 5 THR C 32 ASP C 37 0
SHEET 2 E 5 LYS C 2 TYR C 7 1 N ILE C 5 O LEU C 36
SHEET 3 E 5 HIS C 76 PRO C 82 1 O HIS C 76 N LEU C 4
SHEET 4 E 5 SER C 121 THR C 127 1 O ILE C 125 N PHE C 79
SHEET 5 E 5 VAL C 158 LEU C 163 1 O THR C 161 N ILE C 124
SHEET 1 F 2 TYR C 106 TYR C 108 0
SHEET 2 F 2 LEU C 113 GLY C 115 -1 O GLU C 114 N SER C 107
SHEET 1 G 5 THR D 32 ASP D 37 0
SHEET 2 G 5 LYS D 2 TYR D 7 1 N ILE D 5 O LEU D 36
SHEET 3 G 5 HIS D 76 PRO D 82 1 O ILE D 78 N LEU D 4
SHEET 4 G 5 SER D 121 THR D 127 1 O ILE D 125 N PHE D 79
SHEET 5 G 5 VAL D 158 LEU D 163 1 O THR D 161 N ILE D 124
SHEET 1 H 2 TYR D 106 LYS D 109 0
SHEET 2 H 2 GLY D 112 GLY D 115 -1 O GLU D 114 N SER D 107
CISPEP 1 SER A 156 PRO A 157 0 1.70
CISPEP 2 SER B 156 PRO B 157 0 1.71
CISPEP 3 SER C 156 PRO C 157 0 -1.18
CISPEP 4 SER D 156 PRO D 157 0 0.23
SITE 1 AC1 22 HIS A 9 SER A 14 PHE A 15 ASN A 16
SITE 2 AC1 22 PRO A 82 ILE A 83 TRP A 84 TRP A 85
SITE 3 AC1 22 SER A 86 THR A 127 HIS A 128 ASN A 129
SITE 4 AC1 22 THR A 130 TYR A 141 ARG A 174 HOH A 222
SITE 5 AC1 22 HOH A 228 HOH A 340 LEU B 47 ARG B 55
SITE 6 AC1 22 NAP B 198 HOH B 236
SITE 1 AC2 6 ARG A 55 TYR A 106 TYR A 108 HOH A 225
SITE 2 AC2 6 TRP B 85 FAD B 197
SITE 1 AC3 29 LEU A 47 ARG A 55 NAP A 198 HOH A 219
SITE 2 AC3 29 HIS B 9 SER B 14 PHE B 15 ASN B 16
SITE 3 AC3 29 PRO B 82 ILE B 83 TRP B 84 TRP B 85
SITE 4 AC3 29 SER B 86 THR B 127 HIS B 128 ASN B 129
SITE 5 AC3 29 THR B 130 TYR B 141 GLU B 167 ARG B 174
SITE 6 AC3 29 GLN B 175 HOH B 213 HOH B 224 HOH B 226
SITE 7 AC3 29 HOH B 239 HOH B 259 HOH B 274 HOH B 282
SITE 8 AC3 29 HOH B 355
SITE 1 AC4 6 TRP A 85 ASN A 129 FAD A 197 ARG B 55
SITE 2 AC4 6 TYR B 106 TYR B 108
SITE 1 AC5 23 HIS C 9 SER C 14 PHE C 15 ASN C 16
SITE 2 AC5 23 ILE C 83 TRP C 84 TRP C 85 SER C 86
SITE 3 AC5 23 THR C 127 HIS C 128 ASN C 129 THR C 130
SITE 4 AC5 23 TYR C 141 GLU C 167 ARG C 174 GLN C 175
SITE 5 AC5 23 NAP C 198 HOH C 229 HOH C 236 HOH C 237
SITE 6 AC5 23 HOH C 307 ARG D 55 HOH D 201
SITE 1 AC6 10 TRP C 85 THR C 130 ALA C 134 TYR C 141
SITE 2 AC6 10 FAD C 197 ARG D 55 TYR D 106 TYR D 108
SITE 3 AC6 10 GLN D 148 PRO D 152
SITE 1 AC7 3 TYR C 106 TYR C 108 FAD D 197
SITE 1 AC8 26 LEU C 47 ARG C 55 NAP C 199 HIS D 9
SITE 2 AC8 26 SER D 14 PHE D 15 ASN D 16 GLU D 18
SITE 3 AC8 26 PRO D 82 ILE D 83 TRP D 84 TRP D 85
SITE 4 AC8 26 SER D 86 THR D 127 HIS D 128 ASN D 129
SITE 5 AC8 26 THR D 130 TYR D 141 ASP D 171 ARG D 174
SITE 6 AC8 26 GLN D 175 HOH D 202 HOH D 216 HOH D 230
SITE 7 AC8 26 HOH D 236 HOH D 247
CRYST1 50.601 79.118 106.281 90.00 90.01 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019762 0.000000 0.000003 0.00000
SCALE2 0.000000 0.012639 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009409 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
