HEADER OXIDOREDUCTASE 13-MAY-13 4BN8
TITLE NITROREDUCTASE CIND FROM LACTOCOCCUS LACTIS IN COMPLEX WITH 4-
TITLE 2 NITROPHENOL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER INDUCED NITROREDUCTASE D;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: FLAVIN MONONUCLEOTIDE COFACTOR - IN COMPLEX WITH 2 4-
COMPND 6 NITROPHENOL
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOCOCCUS LACTIS;
SOURCE 3 ORGANISM_TAXID: 272623;
SOURCE 4 STRAIN: IL1403;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 668369;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5[ALPHA]
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.E.OBERHOLZER,S.WALTERSPERGER,R.BAUMGARTNER
REVDAT 2 20-DEC-23 4BN8 1 REMARK
REVDAT 1 28-MAY-14 4BN8 0
JRNL AUTH A.E.OBERHOLZER,S.WALTERSPERGER,R.BAUMGARTNER
JRNL TITL NITROREDUCTASE CIND FROM LACTOCOCCUS LACTIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.40
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 17078
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 855
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 60.4327 - 3.4434 0.99 2979 157 0.1501 0.1789
REMARK 3 2 3.4434 - 2.7331 1.00 2880 152 0.1467 0.1797
REMARK 3 3 2.7331 - 2.3876 1.00 2869 151 0.1517 0.1733
REMARK 3 4 2.3876 - 2.1693 1.00 2830 149 0.1706 0.2116
REMARK 3 5 2.1693 - 2.0138 0.94 2683 142 0.2125 0.2454
REMARK 3 6 2.0138 - 1.8951 0.70 1982 104 0.2829 0.3229
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) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.400
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.80
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 : 0.004 1570
REMARK 3 ANGLE : 0.804 2138
REMARK 3 CHIRALITY : 0.052 230
REMARK 3 PLANARITY : 0.003 276
REMARK 3 DIHEDRAL : 14.748 575
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 2 THROUGH 22 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.3000 -29.7028 13.9601
REMARK 3 T TENSOR
REMARK 3 T11: 0.1837 T22: 0.1691
REMARK 3 T33: 0.1722 T12: 0.0489
REMARK 3 T13: -0.0368 T23: 0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 4.7913 L22: 1.6587
REMARK 3 L33: 2.6449 L12: -0.1099
REMARK 3 L13: -1.6400 L23: 1.9027
REMARK 3 S TENSOR
REMARK 3 S11: 0.0594 S12: -0.2572 S13: -0.1759
REMARK 3 S21: 0.0125 S22: -0.0466 S23: 0.0043
REMARK 3 S31: 0.0130 S32: 0.2982 S33: 0.0319
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 23 THROUGH 35 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.9787 -29.0490 2.3439
REMARK 3 T TENSOR
REMARK 3 T11: 0.2337 T22: 0.2287
REMARK 3 T33: 0.2190 T12: 0.0090
REMARK 3 T13: 0.0198 T23: -0.0707
REMARK 3 L TENSOR
REMARK 3 L11: 3.4801 L22: 4.8389
REMARK 3 L33: 4.4700 L12: -1.7829
REMARK 3 L13: -2.1900 L23: -0.1260
REMARK 3 S TENSOR
REMARK 3 S11: -0.3094 S12: 0.6854 S13: -0.9404
REMARK 3 S21: -0.4984 S22: -0.1446 S23: 0.2868
REMARK 3 S31: 0.5250 S32: 0.0856 S33: 0.1986
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 36 THROUGH 96 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6579 -14.6293 3.0984
REMARK 3 T TENSOR
REMARK 3 T11: 0.2369 T22: 0.2142
REMARK 3 T33: 0.2642 T12: -0.0514
REMARK 3 T13: -0.0078 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 0.9932 L22: 2.4008
REMARK 3 L33: 1.8778 L12: -0.9907
REMARK 3 L13: 0.3349 L23: -0.6510
REMARK 3 S TENSOR
REMARK 3 S11: -0.0263 S12: 0.3177 S13: 0.3801
REMARK 3 S21: -0.1816 S22: -0.1076 S23: -0.4804
REMARK 3 S31: -0.1745 S32: 0.3474 S33: -0.0574
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 97 THROUGH 115 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.5051 -8.8044 5.6288
REMARK 3 T TENSOR
REMARK 3 T11: 0.2694 T22: 0.1576
REMARK 3 T33: 0.2548 T12: 0.0416
REMARK 3 T13: -0.0401 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 3.8690 L22: 1.2597
REMARK 3 L33: 3.0872 L12: -0.2893
REMARK 3 L13: -1.1300 L23: 0.2607
REMARK 3 S TENSOR
REMARK 3 S11: -0.1456 S12: 0.3950 S13: 0.4501
REMARK 3 S21: 0.0824 S22: 0.0172 S23: 0.1150
REMARK 3 S31: -0.3958 S32: -0.5158 S33: 0.0999
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESID 116 THROUGH 144 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.7860 -16.0145 13.7388
REMARK 3 T TENSOR
REMARK 3 T11: 0.1829 T22: 0.1304
REMARK 3 T33: 0.1814 T12: 0.0054
REMARK 3 T13: -0.0198 T23: -0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 4.6100 L22: 6.3030
REMARK 3 L33: 2.8033 L12: -3.5442
REMARK 3 L13: -0.3864 L23: 0.0333
REMARK 3 S TENSOR
REMARK 3 S11: -0.0575 S12: -0.3169 S13: 0.1580
REMARK 3 S21: -0.0930 S22: 0.1651 S23: 0.2676
REMARK 3 S31: -0.4426 S32: -0.1746 S33: -0.0735
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESID 145 THROUGH 180 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.3690 -12.2066 3.5162
REMARK 3 T TENSOR
REMARK 3 T11: 0.2416 T22: 0.2367
REMARK 3 T33: 0.2733 T12: -0.0337
REMARK 3 T13: 0.0107 T23: 0.0325
REMARK 3 L TENSOR
REMARK 3 L11: 2.1043 L22: 3.6051
REMARK 3 L33: 2.5222 L12: -1.3286
REMARK 3 L13: 0.0803 L23: -0.9335
REMARK 3 S TENSOR
REMARK 3 S11: 0.0840 S12: 0.2366 S13: 0.3626
REMARK 3 S21: -0.2172 S22: -0.1396 S23: -0.2404
REMARK 3 S31: -0.3328 S32: 0.1429 S33: 0.0739
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND (RESID 181 THROUGH 202 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.3834 -23.3328 28.8986
REMARK 3 T TENSOR
REMARK 3 T11: 0.2073 T22: 0.1972
REMARK 3 T33: 0.2046 T12: 0.0097
REMARK 3 T13: -0.0312 T23: 0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 1.9746 L22: 1.0421
REMARK 3 L33: 5.5390 L12: -0.6170
REMARK 3 L13: -1.7735 L23: 1.2305
REMARK 3 S TENSOR
REMARK 3 S11: -0.0911 S12: -0.4860 S13: -0.0058
REMARK 3 S21: 0.1969 S22: 0.1446 S23: -0.1126
REMARK 3 S31: 0.1402 S32: 0.4846 S33: -0.0289
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 4BN8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-MAY-13.
REMARK 100 THE DEPOSITION ID IS D_1290056863.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17092
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.100
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 69.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.00000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.120
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2WQF
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 34.28600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 34.28600
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 26.94400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 60.40200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.94400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 60.40200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 34.28600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.94400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 60.40200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 34.28600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.94400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 60.40200
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.1 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -53.88800
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 34.28600
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 A2003 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2122 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2126 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2127 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2148 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 GLN A 75
REMARK 465 GLY A 76
REMARK 465 VAL A 77
REMARK 465 PRO A 78
REMARK 465 GLU A 79
REMARK 465 SER A 80
REMARK 465 ALA A 81
REMARK 465 TRP A 82
REMARK 465 ASP A 83
REMARK 465 ASN A 84
REMARK 465 THR A 85
REMARK 465 ARG A 86
REMARK 465 ALA A 87
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 88 CG CD CE NZ
REMARK 470 LYS A 202 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 2109 O HOH A 2182 1.94
REMARK 500 O HOH A 2071 O HOH A 2072 1.96
REMARK 500 OE1 GLU A 8 O HOH A 2007 2.02
REMARK 500 O LYS A 88 O HOH A 2129 2.04
REMARK 500 O HOH A 2139 O HOH A 2142 2.09
REMARK 500 NH1 ARG A 18 O HOH A 2046 2.18
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 2134 O HOH A 2213 3455 2.05
REMARK 500 O HOH A 2018 O HOH A 2074 3455 2.15
REMARK 500 O HOH A 2019 O HOH A 2099 6445 2.17
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 FMN A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NPO A 505
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BN6 RELATED DB: PDB
REMARK 900 NITROREDUCTASE CIND FROM LACTOCOCCUS LACTIS IN COMPLEX WITH
REMARK 900 CHLORAMPHENICOL
REMARK 900 RELATED ID: 4BN7 RELATED DB: PDB
REMARK 900 NITROREDUCTASE CIND FROM LACTOCOCCUS LACTIS IN COMPLEX WITH 2,6-
REMARK 900 DICHLOROPHENOLINDOPHENOL
REMARK 900 RELATED ID: 4BN9 RELATED DB: PDB
REMARK 900 NITROREDUCTASE CIND FROM LACTOCOCCUS LACTIS IN COMPLEX WITH
REMARK 900 NICOTINIC ACID
REMARK 900 RELATED ID: 4BNB RELATED DB: PDB
REMARK 900 NITROREDUCTASE CIND FROM LACTOCOCCUS LACTIS IN COMPLEX WITH 4-
REMARK 900 NITROQUINOLINE 1-OXIDE
DBREF 4BN8 A 2 202 UNP Q9CED0 Q9CED0_LACLA 2 202
SEQRES 1 A 201 SER PHE ILE LYS SER LEU GLU ASN ARG ARG THR ILE TYR
SEQRES 2 A 201 ALA LEU GLY ARG ASN VAL GLN ASP GLU GLU LYS VAL ILE
SEQRES 3 A 201 GLU THR ILE LYS GLU ALA VAL ARG PHE SER PRO THR ALA
SEQRES 4 A 201 PHE ASN SER GLN THR GLY ARG LEU LEU ILE LEU THR GLY
SEQRES 5 A 201 ASP ALA GLN ASP LYS LEU TRP ASP GLU ILE VAL ALA PRO
SEQRES 6 A 201 GLU LEU LYS ALA ALA MET GLU ALA GLN GLY VAL PRO GLU
SEQRES 7 A 201 SER ALA TRP ASP ASN THR ARG ALA LYS LEU ASP GLY PHE
SEQRES 8 A 201 LYS ALA ALA PHE GLY THR ILE LEU PHE PHE GLU ASP GLN
SEQRES 9 A 201 ALA VAL VAL LYS ASN LEU GLN GLU GLN PHE ALA LEU TYR
SEQRES 10 A 201 ALA ASP ASN PHE PRO VAL TRP SER GLU GLN GLY SER GLY
SEQRES 11 A 201 ILE ILE SER VAL ASN VAL TRP THR ALA LEU ALA GLU LEU
SEQRES 12 A 201 GLY LEU GLY ALA ASN LEU GLN HIS TYR ASN PRO LEU ILE
SEQRES 13 A 201 ASP GLU ALA VAL ALA LYS GLU TRP ASN LEU PRO GLU SER
SEQRES 14 A 201 TRP LYS LEU ARG GLY GLN LEU VAL PHE GLY SER ILE GLU
SEQRES 15 A 201 ALA PRO ALA GLY GLU LYS THR PHE MET ASP ASP ALA ASP
SEQRES 16 A 201 ARG PHE ILE VAL ALA LYS
HET FMN A 504 50
HET NPO A 505 15
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM NPO P-NITROPHENOL
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 2 FMN C17 H21 N4 O9 P
FORMUL 3 NPO C6 H5 N O3
FORMUL 4 HOH *219(H2 O)
HELIX 1 1 SER A 2 ARG A 10 1 9
HELIX 2 2 ASP A 22 PHE A 36 1 15
HELIX 3 3 THR A 39 SER A 43 5 5
HELIX 4 4 GLY A 53 ILE A 63 1 11
HELIX 5 5 ILE A 63 ALA A 74 1 12
HELIX 6 6 LEU A 89 ALA A 94 1 6
HELIX 7 7 GLN A 105 PHE A 115 1 11
HELIX 8 8 ALA A 116 ALA A 119 5 4
HELIX 9 9 ASP A 120 LEU A 144 1 25
HELIX 10 10 ILE A 157 TRP A 165 1 9
HELIX 11 11 ASP A 193 ARG A 197 5 5
SHEET 1 AA 2 LEU A 16 GLY A 17 0
SHEET 2 AA 2 TRP A 171 ILE A 182 -1 O SER A 181 N GLY A 17
SHEET 1 AB 4 GLY A 46 THR A 52 0
SHEET 2 AB 4 GLY A 97 ASP A 104 -1 O THR A 98 N LEU A 51
SHEET 3 AB 4 TRP A 171 ILE A 182 -1 O LYS A 172 N GLU A 103
SHEET 4 AB 4 LEU A 146 GLN A 151 1 O GLY A 147 N GLY A 180
SHEET 1 AC 4 GLY A 46 THR A 52 0
SHEET 2 AC 4 GLY A 97 ASP A 104 -1 O THR A 98 N LEU A 51
SHEET 3 AC 4 TRP A 171 ILE A 182 -1 O LYS A 172 N GLU A 103
SHEET 4 AC 4 LEU A 16 GLY A 17 -1 O GLY A 17 N SER A 181
SHEET 1 AD 2 LEU A 146 GLN A 151 0
SHEET 2 AD 2 TRP A 171 ILE A 182 1 O GLN A 176 N GLN A 151
CISPEP 1 ASN A 154 PRO A 155 0 3.54
SITE 1 AC1 18 ARG A 10 ARG A 11 THR A 12 TYR A 14
SITE 2 AC1 18 PRO A 38 THR A 39 ALA A 40 PHE A 41
SITE 3 AC1 18 ASN A 42 GLN A 128 LEU A 150 GLN A 151
SITE 4 AC1 18 HIS A 152 LYS A 189 NPO A 505 HOH A2034
SITE 5 AC1 18 HOH A2042 HOH A2219
SITE 1 AC2 3 PHE A 41 TYR A 118 FMN A 504
CRYST1 53.888 120.804 68.572 90.00 90.00 90.00 C 2 2 21 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 0.018557 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008278 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014583 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
