HEADER FLAVOPROTEIN 10-MAR-16 5IQ4
TITLE CRYSTAL STRUCTURE OF RNTMM MUTANT Y207S SOAKING
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLAVIN-CONTAINING MONOOXYGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ROSEOVARIUS NUBINHIBENS (STRAIN ATCC BAA-591 /
SOURCE 3 DSM 15170 / ISM);
SOURCE 4 ORGANISM_TAXID: 89187;
SOURCE 5 STRAIN: ATCC BAA-591 / DSM 15170 / ISM;
SOURCE 6 GENE: ISM_08155;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FLAVIN-CONTAINING MONOOXYGENASE, FLAVOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.Z.ZHANG,C.Y.LI
REVDAT 3 08-NOV-23 5IQ4 1 REMARK
REVDAT 2 22-MAR-17 5IQ4 1 JRNL
REVDAT 1 18-JAN-17 5IQ4 0
JRNL AUTH C.Y.LI,X.L.CHEN,D.ZHANG,P.WANG,Q.SHENG,M.PENG,B.B.XIE,
JRNL AUTH 2 Q.L.QIN,P.Y.LI,X.Y.ZHANG,H.N.SU,X.Y.SONG,M.SHI,B.C.ZHOU,
JRNL AUTH 3 L.Y.XUN,Y.CHEN,Y.Z.ZHANG
JRNL TITL STRUCTURAL MECHANISM FOR BACTERIAL OXIDATION OF OCEANIC
JRNL TITL 2 TRIMETHYLAMINE INTO TRIMETHYLAMINE N-OXIDE
JRNL REF MOL. MICROBIOL. V. 103 992 2017
JRNL REFN ESSN 1365-2958
JRNL PMID 27997715
JRNL DOI 10.1111/MMI.13605
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.6.4_486
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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 85.8
REMARK 3 NUMBER OF REFLECTIONS : 127197
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 6375
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 35.7272 - 4.6530 0.96 4688 242 0.1524 0.1814
REMARK 3 2 4.6530 - 3.6944 0.61 2670 124 0.1255 0.1402
REMARK 3 3 3.6944 - 3.2278 0.76 2360 130 0.1592 0.1929
REMARK 3 4 3.2278 - 2.9328 1.00 4675 269 0.1608 0.1932
REMARK 3 5 2.9328 - 2.7227 1.00 4705 275 0.1623 0.2042
REMARK 3 6 2.7227 - 2.5622 1.00 4710 232 0.1562 0.1956
REMARK 3 7 2.5622 - 2.4339 1.00 4660 265 0.1596 0.2045
REMARK 3 8 2.4339 - 2.3280 1.00 4669 264 0.1546 0.2129
REMARK 3 9 2.3280 - 2.2384 0.71 1447 71 0.1594 0.1985
REMARK 3 10 2.2384 - 2.1611 0.74 2380 124 0.1546 0.1998
REMARK 3 11 2.1611 - 2.0936 0.99 4657 233 0.1597 0.2199
REMARK 3 12 2.0936 - 2.0337 0.99 4623 274 0.1651 0.2091
REMARK 3 13 2.0337 - 1.9802 0.99 4605 243 0.1574 0.2133
REMARK 3 14 1.9802 - 1.9319 0.69 3227 163 0.1723 0.2231
REMARK 3 15 1.9319 - 1.8880 0.48 1249 71 0.3276 0.4369
REMARK 3 16 1.8880 - 1.8478 0.79 3447 161 0.1236 0.2136
REMARK 3 17 1.8478 - 1.8108 0.97 4487 262 0.1240 0.1864
REMARK 3 18 1.8108 - 1.7767 0.98 4587 244 0.1302 0.2016
REMARK 3 19 1.7767 - 1.7449 0.98 4534 230 0.1300 0.1970
REMARK 3 20 1.7449 - 1.7154 0.97 4548 243 0.1358 0.2153
REMARK 3 21 1.7154 - 1.6877 0.97 4518 266 0.1436 0.2077
REMARK 3 22 1.6877 - 1.6617 0.96 4467 203 0.1412 0.2029
REMARK 3 23 1.6617 - 1.6373 0.96 4554 230 0.1401 0.2053
REMARK 3 24 1.6373 - 1.6142 0.95 4387 232 0.1517 0.2388
REMARK 3 25 1.6142 - 1.5924 0.95 4454 222 0.1569 0.2143
REMARK 3 26 1.5924 - 1.5717 0.95 4489 213 0.1746 0.2588
REMARK 3 27 1.5717 - 1.5521 0.94 4355 231 0.1773 0.2654
REMARK 3 28 1.5521 - 1.5334 0.93 4345 219 0.1889 0.2594
REMARK 3 29 1.5334 - 1.5156 0.92 4317 224 0.1992 0.2581
REMARK 3 30 1.5156 - 1.4985 0.86 4008 215 0.2195 0.2890
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 36.91
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.210
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) : 0.51700
REMARK 3 B22 (A**2) : 0.76620
REMARK 3 B33 (A**2) : -1.28330
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.95320
REMARK 3 B23 (A**2) : 0.00000
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 : 0.005 7611
REMARK 3 ANGLE : 1.081 10375
REMARK 3 CHIRALITY : 0.074 1047
REMARK 3 PLANARITY : 0.004 1320
REMARK 3 DIHEDRAL : 20.021 2889
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 5IQ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219251.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-SEP-15
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 : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 130501
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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 (%) : 88.2
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.53
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: 5IPY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, 0.1 M BIS-TRIS
REMARK 280 PROPANE (PH 6.5) AND 20% (W/V) PEG 3350. THE Y207S SOAKING
REMARK 280 CRYSTALS WERE OBTAINED USING CRYSTALS OF Y207S SOAKED WITH 15 MM
REMARK 280 TMA FOR 15 MIN., VAPOR DIFFUSION, HANGING 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 30.68200
REMARK 290 SMTRY3 2 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: 8970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 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 1
REMARK 465 ASN A 447
REMARK 465 HIS A 448
REMARK 465 HIS A 449
REMARK 465 HIS A 450
REMARK 465 HIS A 451
REMARK 465 HIS A 452
REMARK 465 HIS A 453
REMARK 465 MET B 1
REMARK 465 ASN B 447
REMARK 465 HIS B 448
REMARK 465 HIS B 449
REMARK 465 HIS B 450
REMARK 465 HIS B 451
REMARK 465 HIS B 452
REMARK 465 HIS B 453
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 GLU A 153 CG CD OE1 OE2
REMARK 470 ASP A 154 CG OD1 OD2
REMARK 470 GLU B 153 CG CD OE1 OE2
REMARK 470 ASP B 154 CG OD1 OD2
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 OD1 ASP B 317 O3D NAP B 501 1.81
REMARK 500 OD1 ASP A 317 O3D NAP A 501 2.11
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 TYR A 84 87.79 -165.17
REMARK 500 HIS A 164 23.53 -145.60
REMARK 500 ALA A 205 32.44 -147.05
REMARK 500 SER A 206 -157.09 -125.90
REMARK 500 SER A 230 -108.93 -127.12
REMARK 500 PRO A 245 -169.83 -76.15
REMARK 500 CYS A 271 55.84 -99.62
REMARK 500 LYS A 300 19.58 57.13
REMARK 500 TRP A 319 -60.41 -92.31
REMARK 500 THR A 321 -85.83 -129.99
REMARK 500 ASP A 414 57.11 -93.30
REMARK 500 SER A 440 150.72 -48.83
REMARK 500 TYR B 84 90.18 -166.83
REMARK 500 HIS B 89 -78.36 -83.02
REMARK 500 LYS B 92 -169.80 -70.22
REMARK 500 ALA B 95 174.37 -58.26
REMARK 500 HIS B 164 23.80 -145.38
REMARK 500 ARG B 190 -50.15 -128.84
REMARK 500 ALA B 205 29.34 -149.57
REMARK 500 SER B 206 -157.16 -122.56
REMARK 500 SER B 230 -111.53 -123.39
REMARK 500 PRO B 245 -168.86 -75.98
REMARK 500 CYS B 271 57.24 -97.71
REMARK 500 ASN B 307 92.09 -160.15
REMARK 500 TRP B 319 -60.84 -90.15
REMARK 500 THR B 321 -88.77 -126.21
REMARK 500 ASP B 414 50.98 -94.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1113 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH B1061 DISTANCE = 5.84 ANGSTROMS
REMARK 525 HOH B1062 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH B1063 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH B1064 DISTANCE = 8.20 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAP B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5IPY RELATED DB: PDB
REMARK 900 RELATED ID: 5IQ1 RELATED DB: PDB
DBREF 5IQ4 A 1 447 UNP A3SLM3 A3SLM3_ROSNI 1 447
DBREF 5IQ4 B 1 447 UNP A3SLM3 A3SLM3_ROSNI 1 447
SEQADV 5IQ4 SER A 207 UNP A3SLM3 TYR 207 ENGINEERED MUTATION
SEQADV 5IQ4 HIS A 448 UNP A3SLM3 EXPRESSION TAG
SEQADV 5IQ4 HIS A 449 UNP A3SLM3 EXPRESSION TAG
SEQADV 5IQ4 HIS A 450 UNP A3SLM3 EXPRESSION TAG
SEQADV 5IQ4 HIS A 451 UNP A3SLM3 EXPRESSION TAG
SEQADV 5IQ4 HIS A 452 UNP A3SLM3 EXPRESSION TAG
SEQADV 5IQ4 HIS A 453 UNP A3SLM3 EXPRESSION TAG
SEQADV 5IQ4 SER B 207 UNP A3SLM3 TYR 207 ENGINEERED MUTATION
SEQADV 5IQ4 HIS B 448 UNP A3SLM3 EXPRESSION TAG
SEQADV 5IQ4 HIS B 449 UNP A3SLM3 EXPRESSION TAG
SEQADV 5IQ4 HIS B 450 UNP A3SLM3 EXPRESSION TAG
SEQADV 5IQ4 HIS B 451 UNP A3SLM3 EXPRESSION TAG
SEQADV 5IQ4 HIS B 452 UNP A3SLM3 EXPRESSION TAG
SEQADV 5IQ4 HIS B 453 UNP A3SLM3 EXPRESSION TAG
SEQRES 1 A 453 MET THR LYS ARG VAL ALA VAL ILE GLY ALA GLY PRO SER
SEQRES 2 A 453 GLY LEU ALA GLN LEU ARG ALA PHE GLN SER ALA ALA ASP
SEQRES 3 A 453 GLN GLY ALA GLU ILE PRO GLU ILE VAL CYS PHE GLU LYS
SEQRES 4 A 453 GLN ALA ASN TRP GLY GLY LEU TRP ASN TYR THR TRP ARG
SEQRES 5 A 453 THR GLY LEU ASP GLU ASN GLY GLU PRO VAL HIS CYS SER
SEQRES 6 A 453 MET TYR ARG TYR LEU TRP SER ASN GLY PRO LYS GLU GLY
SEQRES 7 A 453 LEU GLU PHE ALA ASP TYR SER PHE GLU GLU HIS PHE GLY
SEQRES 8 A 453 LYS GLN ILE ALA SER TYR PRO PRO ARG ALA VAL LEU PHE
SEQRES 9 A 453 ASP TYR ILE GLU GLY ARG VAL HIS LYS ALA ASP VAL ARG
SEQRES 10 A 453 LYS TRP ILE ARG PHE ASN SER PRO VAL ARG TRP VAL SER
SEQRES 11 A 453 TYR ASP ALA GLU THR ALA LYS PHE THR VAL THR ALA HIS
SEQRES 12 A 453 ASN HIS GLU THR ASP SER THR TYR SER GLU ASP PHE ASP
SEQRES 13 A 453 HIS VAL ILE CYS ALA SER GLY HIS PHE SER THR PRO ASN
SEQRES 14 A 453 VAL PRO PHE TYR GLU GLY PHE ASP THR PHE ASN GLY ARG
SEQRES 15 A 453 ILE VAL HIS ALA HIS ASP PHE ARG ASP ALA ARG GLU PHE
SEQRES 16 A 453 GLU GLY LYS ASP VAL LEU VAL MET GLY ALA SER SER SER
SEQRES 17 A 453 ALA GLU ASP ILE GLY SER GLN CYS TRP LYS TYR GLY ALA
SEQRES 18 A 453 LYS SER ILE THR SER CYS TYR ARG SER ALA PRO MET GLY
SEQRES 19 A 453 TYR ALA TRP PRO ASP ASN TRP GLU GLU LYS PRO ALA LEU
SEQRES 20 A 453 GLU LYS LEU THR GLY LYS THR ALA HIS PHE ALA ASP GLY
SEQRES 21 A 453 SER THR ARG ASP VAL ASP ALA ILE ILE LEU CYS THR GLY
SEQRES 22 A 453 TYR LYS HIS PHE PHE SER PHE LEU PRO ASP ASP LEU ARG
SEQRES 23 A 453 LEU LYS THR ALA ASN ARG LEU ALA THR ALA ASP LEU TYR
SEQRES 24 A 453 LYS GLY VAL ALA TYR VAL HIS ASN PRO ALA MET PHE TYR
SEQRES 25 A 453 LEU GLY MET GLN ASP GLN TRP PHE THR PHE ASN MET PHE
SEQRES 26 A 453 ASP ALA GLN ALA TRP TRP VAL ARG ASP ALA ILE LEU GLY
SEQRES 27 A 453 ARG ILE THR LEU PRO LYS ASP LYS ALA ALA MET LEU ALA
SEQRES 28 A 453 ASP VAL ALA GLU ARG GLU THR ARG GLU GLU ALA SER ASP
SEQRES 29 A 453 ASP VAL LYS TYR ALA ILE ARG TYR GLN ALA ASP TYR VAL
SEQRES 30 A 453 LYS GLU LEU VAL ALA GLU THR ASP TYR PRO SER PHE ASP
SEQRES 31 A 453 ILE ASP GLY ALA CYS ASP ALA PHE PHE GLU TRP LYS LYS
SEQRES 32 A 453 HIS LYS ALA LYS ASP ILE MET ALA PHE ARG ASP ASN SER
SEQRES 33 A 453 TYR LYS SER VAL ILE THR GLY THR MET ALA PRO VAL HIS
SEQRES 34 A 453 HIS THR PRO TRP LYS GLU ALA LEU ASP ASP SER MET GLU
SEQRES 35 A 453 ALA TYR LEU GLN ASN HIS HIS HIS HIS HIS HIS
SEQRES 1 B 453 MET THR LYS ARG VAL ALA VAL ILE GLY ALA GLY PRO SER
SEQRES 2 B 453 GLY LEU ALA GLN LEU ARG ALA PHE GLN SER ALA ALA ASP
SEQRES 3 B 453 GLN GLY ALA GLU ILE PRO GLU ILE VAL CYS PHE GLU LYS
SEQRES 4 B 453 GLN ALA ASN TRP GLY GLY LEU TRP ASN TYR THR TRP ARG
SEQRES 5 B 453 THR GLY LEU ASP GLU ASN GLY GLU PRO VAL HIS CYS SER
SEQRES 6 B 453 MET TYR ARG TYR LEU TRP SER ASN GLY PRO LYS GLU GLY
SEQRES 7 B 453 LEU GLU PHE ALA ASP TYR SER PHE GLU GLU HIS PHE GLY
SEQRES 8 B 453 LYS GLN ILE ALA SER TYR PRO PRO ARG ALA VAL LEU PHE
SEQRES 9 B 453 ASP TYR ILE GLU GLY ARG VAL HIS LYS ALA ASP VAL ARG
SEQRES 10 B 453 LYS TRP ILE ARG PHE ASN SER PRO VAL ARG TRP VAL SER
SEQRES 11 B 453 TYR ASP ALA GLU THR ALA LYS PHE THR VAL THR ALA HIS
SEQRES 12 B 453 ASN HIS GLU THR ASP SER THR TYR SER GLU ASP PHE ASP
SEQRES 13 B 453 HIS VAL ILE CYS ALA SER GLY HIS PHE SER THR PRO ASN
SEQRES 14 B 453 VAL PRO PHE TYR GLU GLY PHE ASP THR PHE ASN GLY ARG
SEQRES 15 B 453 ILE VAL HIS ALA HIS ASP PHE ARG ASP ALA ARG GLU PHE
SEQRES 16 B 453 GLU GLY LYS ASP VAL LEU VAL MET GLY ALA SER SER SER
SEQRES 17 B 453 ALA GLU ASP ILE GLY SER GLN CYS TRP LYS TYR GLY ALA
SEQRES 18 B 453 LYS SER ILE THR SER CYS TYR ARG SER ALA PRO MET GLY
SEQRES 19 B 453 TYR ALA TRP PRO ASP ASN TRP GLU GLU LYS PRO ALA LEU
SEQRES 20 B 453 GLU LYS LEU THR GLY LYS THR ALA HIS PHE ALA ASP GLY
SEQRES 21 B 453 SER THR ARG ASP VAL ASP ALA ILE ILE LEU CYS THR GLY
SEQRES 22 B 453 TYR LYS HIS PHE PHE SER PHE LEU PRO ASP ASP LEU ARG
SEQRES 23 B 453 LEU LYS THR ALA ASN ARG LEU ALA THR ALA ASP LEU TYR
SEQRES 24 B 453 LYS GLY VAL ALA TYR VAL HIS ASN PRO ALA MET PHE TYR
SEQRES 25 B 453 LEU GLY MET GLN ASP GLN TRP PHE THR PHE ASN MET PHE
SEQRES 26 B 453 ASP ALA GLN ALA TRP TRP VAL ARG ASP ALA ILE LEU GLY
SEQRES 27 B 453 ARG ILE THR LEU PRO LYS ASP LYS ALA ALA MET LEU ALA
SEQRES 28 B 453 ASP VAL ALA GLU ARG GLU THR ARG GLU GLU ALA SER ASP
SEQRES 29 B 453 ASP VAL LYS TYR ALA ILE ARG TYR GLN ALA ASP TYR VAL
SEQRES 30 B 453 LYS GLU LEU VAL ALA GLU THR ASP TYR PRO SER PHE ASP
SEQRES 31 B 453 ILE ASP GLY ALA CYS ASP ALA PHE PHE GLU TRP LYS LYS
SEQRES 32 B 453 HIS LYS ALA LYS ASP ILE MET ALA PHE ARG ASP ASN SER
SEQRES 33 B 453 TYR LYS SER VAL ILE THR GLY THR MET ALA PRO VAL HIS
SEQRES 34 B 453 HIS THR PRO TRP LYS GLU ALA LEU ASP ASP SER MET GLU
SEQRES 35 B 453 ALA TYR LEU GLN ASN HIS HIS HIS HIS HIS HIS
HET NAP A 501 48
HET FAD A 502 53
HET NAP B 501 48
HET FAD B 502 53
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 NAP 2(C21 H28 N7 O17 P3)
FORMUL 4 FAD 2(C27 H33 N9 O15 P2)
FORMUL 7 HOH *977(H2 O)
HELIX 1 AA1 GLY A 11 GLY A 28 1 18
HELIX 2 AA2 GLY A 44 ASN A 48 5 5
HELIX 3 AA3 PRO A 75 LEU A 79 5 5
HELIX 4 AA4 SER A 85 GLY A 91 1 7
HELIX 5 AA5 PRO A 99 ASP A 115 1 17
HELIX 6 AA6 VAL A 116 LYS A 118 5 3
HELIX 7 AA7 HIS A 187 PHE A 189 5 3
HELIX 8 AA8 ASP A 191 GLU A 196 5 6
HELIX 9 AA9 SER A 206 TYR A 219 1 14
HELIX 10 AB1 LYS A 300 VAL A 302 5 3
HELIX 11 AB2 THR A 321 LEU A 337 1 17
HELIX 12 AB3 ASP A 345 ALA A 362 1 18
HELIX 13 AB4 ASP A 365 GLU A 383 1 19
HELIX 14 AB5 ASP A 390 ASP A 408 1 19
HELIX 15 AB6 PRO A 432 ALA A 436 5 5
HELIX 16 AB7 SER A 440 GLN A 446 1 7
HELIX 17 AB8 GLY B 11 GLN B 27 1 17
HELIX 18 AB9 GLY B 44 ASN B 48 5 5
HELIX 19 AC1 PRO B 75 LEU B 79 5 5
HELIX 20 AC2 SER B 85 GLY B 91 1 7
HELIX 21 AC3 PRO B 99 ASP B 115 1 17
HELIX 22 AC4 VAL B 116 LYS B 118 5 3
HELIX 23 AC5 HIS B 187 PHE B 189 5 3
HELIX 24 AC6 ASP B 191 GLU B 196 5 6
HELIX 25 AC7 SER B 206 TYR B 219 1 14
HELIX 26 AC8 LYS B 300 VAL B 302 5 3
HELIX 27 AC9 THR B 321 LEU B 337 1 17
HELIX 28 AD1 ASP B 345 ALA B 362 1 18
HELIX 29 AD2 ASP B 365 GLU B 383 1 19
HELIX 30 AD3 ASP B 390 ASP B 408 1 19
HELIX 31 AD4 PRO B 432 ALA B 436 5 5
HELIX 32 AD5 SER B 440 GLN B 446 1 7
SHEET 1 AA1 5 ILE A 120 ARG A 121 0
SHEET 2 AA1 5 GLU A 33 PHE A 37 1 N CYS A 36 O ARG A 121
SHEET 3 AA1 5 ARG A 4 ILE A 8 1 N VAL A 5 O GLU A 33
SHEET 4 AA1 5 HIS A 157 CYS A 160 1 O ILE A 159 N ALA A 6
SHEET 5 AA1 5 MET A 310 TYR A 312 1 O PHE A 311 N CYS A 160
SHEET 1 AA2 3 VAL A 126 ASP A 132 0
SHEET 2 AA2 3 LYS A 137 ASN A 144 -1 O THR A 141 N ARG A 127
SHEET 3 AA2 3 SER A 149 PHE A 155 -1 O PHE A 155 N PHE A 138
SHEET 1 AA3 5 ARG A 182 HIS A 185 0
SHEET 2 AA3 5 ALA A 267 LEU A 270 1 O ILE A 268 N ARG A 182
SHEET 3 AA3 5 ASP A 199 MET A 203 1 N LEU A 201 O ILE A 269
SHEET 4 AA3 5 SER A 223 CYS A 227 1 O THR A 225 N VAL A 202
SHEET 5 AA3 5 TRP A 241 LYS A 244 1 O LYS A 244 N SER A 226
SHEET 1 AA4 3 LEU A 247 THR A 251 0
SHEET 2 AA4 3 THR A 254 PHE A 257 -1 O HIS A 256 N GLU A 248
SHEET 3 AA4 3 THR A 262 ASP A 264 -1 O ARG A 263 N ALA A 255
SHEET 1 AA5 2 LEU A 298 TYR A 299 0
SHEET 2 AA5 2 ALA A 303 TYR A 304 -1 O ALA A 303 N TYR A 299
SHEET 1 AA6 5 ILE B 120 ARG B 121 0
SHEET 2 AA6 5 GLU B 33 PHE B 37 1 N CYS B 36 O ARG B 121
SHEET 3 AA6 5 ARG B 4 ILE B 8 1 N VAL B 7 O VAL B 35
SHEET 4 AA6 5 HIS B 157 CYS B 160 1 O ILE B 159 N ALA B 6
SHEET 5 AA6 5 MET B 310 TYR B 312 1 O PHE B 311 N CYS B 160
SHEET 1 AA7 3 VAL B 126 ASP B 132 0
SHEET 2 AA7 3 LYS B 137 ASN B 144 -1 O THR B 141 N TRP B 128
SHEET 3 AA7 3 SER B 149 PHE B 155 -1 O PHE B 155 N PHE B 138
SHEET 1 AA8 5 ARG B 182 HIS B 185 0
SHEET 2 AA8 5 ALA B 267 LEU B 270 1 O ILE B 268 N ARG B 182
SHEET 3 AA8 5 ASP B 199 MET B 203 1 N LEU B 201 O ILE B 269
SHEET 4 AA8 5 SER B 223 CYS B 227 1 O THR B 225 N VAL B 202
SHEET 5 AA8 5 TRP B 241 LYS B 244 1 O LYS B 244 N SER B 226
SHEET 1 AA9 3 LEU B 247 THR B 251 0
SHEET 2 AA9 3 THR B 254 PHE B 257 -1 O HIS B 256 N GLU B 248
SHEET 3 AA9 3 THR B 262 ASP B 264 -1 O ARG B 263 N ALA B 255
SHEET 1 AB1 2 LEU B 298 TYR B 299 0
SHEET 2 AB1 2 ALA B 303 TYR B 304 -1 O ALA B 303 N TYR B 299
SITE 1 AC1 34 ASN A 73 PHE A 165 ASN A 169 PRO A 171
SITE 2 AC1 34 TYR A 173 MET A 203 GLY A 204 ALA A 205
SITE 3 AC1 34 SER A 206 SER A 207 SER A 208 ARG A 229
SITE 4 AC1 34 SER A 230 CYS A 271 THR A 272 GLY A 273
SITE 5 AC1 34 ASN A 291 ASP A 317 GLN A 318 FAD A 502
SITE 6 AC1 34 HOH A 601 HOH A 617 HOH A 640 HOH A 647
SITE 7 AC1 34 HOH A 677 HOH A 714 HOH A 739 HOH A 790
SITE 8 AC1 34 HOH A 802 HOH A 857 HOH A 895 HOH A 897
SITE 9 AC1 34 HOH A 913 HOH A 926
SITE 1 AC2 35 GLY A 9 GLY A 11 PRO A 12 SER A 13
SITE 2 AC2 35 PHE A 37 GLU A 38 LYS A 39 GLN A 40
SITE 3 AC2 35 GLY A 45 LEU A 46 TRP A 47 HIS A 63
SITE 4 AC2 35 SER A 65 MET A 66 SER A 72 ASN A 73
SITE 5 AC2 35 LEU A 79 PRO A 125 VAL A 126 ALA A 161
SITE 6 AC2 35 SER A 162 GLY A 163 PHE A 165 PHE A 280
SITE 7 AC2 35 GLN A 318 THR A 321 PHE A 322 NAP A 501
SITE 8 AC2 35 HOH A 634 HOH A 684 HOH A 701 HOH A 778
SITE 9 AC2 35 HOH A 812 HOH A 822 HOH A 923
SITE 1 AC3 30 ASN B 73 PHE B 165 ASN B 169 PRO B 171
SITE 2 AC3 30 TYR B 173 MET B 203 ALA B 205 SER B 206
SITE 3 AC3 30 SER B 207 SER B 208 ARG B 229 SER B 230
SITE 4 AC3 30 CYS B 271 THR B 272 GLY B 273 ASP B 317
SITE 5 AC3 30 GLN B 318 FAD B 502 HOH B 651 HOH B 669
SITE 6 AC3 30 HOH B 671 HOH B 748 HOH B 758 HOH B 761
SITE 7 AC3 30 HOH B 767 HOH B 839 HOH B 843 HOH B 850
SITE 8 AC3 30 HOH B 885 HOH B 896
SITE 1 AC4 36 GLY B 9 GLY B 11 PRO B 12 SER B 13
SITE 2 AC4 36 PHE B 37 GLU B 38 LYS B 39 GLN B 40
SITE 3 AC4 36 GLY B 45 LEU B 46 TRP B 47 HIS B 63
SITE 4 AC4 36 SER B 65 MET B 66 SER B 72 ASN B 73
SITE 5 AC4 36 LEU B 79 PRO B 125 VAL B 126 ALA B 161
SITE 6 AC4 36 SER B 162 GLY B 163 PHE B 165 PHE B 280
SITE 7 AC4 36 GLN B 318 THR B 321 PHE B 325 NAP B 501
SITE 8 AC4 36 HOH B 614 HOH B 625 HOH B 668 HOH B 721
SITE 9 AC4 36 HOH B 788 HOH B 789 HOH B 849 HOH B 876
CRYST1 72.969 61.364 104.706 90.00 94.04 90.00 P 1 21 1 4
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 0.013704 0.000000 0.000969 0.00000
SCALE2 0.000000 0.016296 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009574 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
