HEADER OXIDOREDUCTASE 19-APR-16 5JFC
TITLE NADH-DEPENDENT FERREDOXIN:NADP OXIDOREDUCTASE (NFNI) FROM PYROCOCCUS
TITLE 2 FURIOSUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NADH-DEPENDENT FERREDOXIN:NADP OXIDOREDUCTASE SUBUNIT
COMPND 3 ALPHA;
COMPND 4 CHAIN: L;
COMPND 5 SYNONYM: SUDH,FERREDOXIN:NADP OXIDOREDUCTASE,FNOR;
COMPND 6 EC: 1.6.1.4;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NADH-DEPENDENT FERREDOXIN:NADP OXIDOREDUCTASE SUBUNIT BETA;
COMPND 9 CHAIN: S;
COMPND 10 SYNONYM: SUDH,FERREDOXIN:NADP OXIDOREDUCTASE,FNOR;
COMPND 11 EC: 1.6.1.4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 2261;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 6 ORGANISM_TAXID: 2261
KEYWDS NFNI, OXIDOREDUCTASE, PYROCOCCUS FURIOSUS, NADP(H) BOUND NFNI
EXPDTA X-RAY DIFFRACTION
AUTHOR O.A.ZADVORNYY,G.J.SCHUT,D.M.NGUYEN,J.H.ARTZ,M.TOKMINA-LUKASZEWSKA,
AUTHOR 2 G.LIPSCOMB,P.W.KING,M.W.ADAMS,J.W.PETERS
REVDAT 6 06-MAR-24 5JFC 1 LINK
REVDAT 5 04-DEC-19 5JFC 1 REMARK
REVDAT 4 27-SEP-17 5JFC 1 REMARK
REVDAT 3 31-MAY-17 5JFC 1 JRNL
REVDAT 2 26-APR-17 5JFC 1 JRNL
REVDAT 1 12-APR-17 5JFC 0
JRNL AUTH C.E.LUBNER,D.P.JENNINGS,D.W.MULDER,G.J.SCHUT,O.A.ZADVORNYY,
JRNL AUTH 2 J.P.HOBEN,M.TOKMINA-LUKASZEWSKA,L.BERRY,D.M.NGUYEN,
JRNL AUTH 3 G.L.LIPSCOMB,B.BOTHNER,A.K.JONES,A.F.MILLER,P.W.KING,
JRNL AUTH 4 M.W.W.ADAMS,J.W.PETERS
JRNL TITL MECHANISTIC INSIGHTS INTO ENERGY CONSERVATION BY
JRNL TITL 2 FLAVIN-BASED ELECTRON BIFURCATION.
JRNL REF NAT. CHEM. BIOL. V. 13 655 2017
JRNL REFN ESSN 1552-4469
JRNL PMID 28394885
JRNL DOI 10.1038/NCHEMBIO.2348
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2313: ???)
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 197382
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.159
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 9712
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 47.6131 - 4.9633 1.00 6525 334 0.1530 0.1746
REMARK 3 2 4.9633 - 3.9401 1.00 6308 369 0.1264 0.1334
REMARK 3 3 3.9401 - 3.4422 1.00 6316 349 0.1339 0.1591
REMARK 3 4 3.4422 - 3.1276 1.00 6355 267 0.1470 0.1464
REMARK 3 5 3.1276 - 2.9034 1.00 6260 316 0.1578 0.1708
REMARK 3 6 2.9034 - 2.7323 1.00 6312 325 0.1572 0.1672
REMARK 3 7 2.7323 - 2.5954 1.00 6226 355 0.1546 0.1583
REMARK 3 8 2.5954 - 2.4825 1.00 6365 274 0.1478 0.1668
REMARK 3 9 2.4825 - 2.3869 1.00 6241 339 0.1471 0.1465
REMARK 3 10 2.3869 - 2.3045 1.00 6193 351 0.1454 0.1561
REMARK 3 11 2.3045 - 2.2325 1.00 6239 380 0.1440 0.1648
REMARK 3 12 2.2325 - 2.1687 1.00 6171 378 0.1455 0.1510
REMARK 3 13 2.1687 - 2.1116 1.00 6285 330 0.1393 0.1467
REMARK 3 14 2.1116 - 2.0601 1.00 6229 333 0.1453 0.1618
REMARK 3 15 2.0601 - 2.0132 1.00 6206 313 0.1428 0.1567
REMARK 3 16 2.0132 - 1.9704 1.00 6211 355 0.1437 0.1524
REMARK 3 17 1.9704 - 1.9310 1.00 6240 351 0.1417 0.1605
REMARK 3 18 1.9310 - 1.8945 1.00 6257 307 0.1453 0.1621
REMARK 3 19 1.8945 - 1.8607 1.00 6258 308 0.1487 0.1643
REMARK 3 20 1.8607 - 1.8291 1.00 6234 293 0.1484 0.1763
REMARK 3 21 1.8291 - 1.7996 1.00 6259 314 0.1493 0.1583
REMARK 3 22 1.7996 - 1.7719 1.00 6258 332 0.1509 0.1518
REMARK 3 23 1.7719 - 1.7459 1.00 6190 318 0.1520 0.1700
REMARK 3 24 1.7459 - 1.7213 1.00 6251 315 0.1535 0.1726
REMARK 3 25 1.7213 - 1.6980 1.00 6270 283 0.1584 0.1661
REMARK 3 26 1.6980 - 1.6760 1.00 6214 315 0.1533 0.1772
REMARK 3 27 1.6760 - 1.6550 1.00 6262 295 0.1555 0.1719
REMARK 3 28 1.6550 - 1.6351 1.00 6314 264 0.1639 0.1827
REMARK 3 29 1.6351 - 1.6161 1.00 6160 332 0.1730 0.1892
REMARK 3 30 1.6161 - 1.5979 0.97 6061 317 0.1798 0.1914
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) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.24
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 6103
REMARK 3 ANGLE : 1.496 8271
REMARK 3 CHIRALITY : 0.068 918
REMARK 3 PLANARITY : 0.007 1043
REMARK 3 DIHEDRAL : 15.228 3691
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): -60.5701 65.1181 9.7865
REMARK 3 T TENSOR
REMARK 3 T11: 0.0690 T22: 0.1121
REMARK 3 T33: 0.0710 T12: -0.0193
REMARK 3 T13: -0.0180 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 0.3929 L22: 0.8518
REMARK 3 L33: 0.4103 L12: 0.3665
REMARK 3 L13: -0.1506 L23: -0.2131
REMARK 3 S TENSOR
REMARK 3 S11: 0.0104 S12: -0.0255 S13: -0.0504
REMARK 3 S21: -0.0254 S22: -0.0300 S23: -0.0285
REMARK 3 S31: 0.0241 S32: 0.0715 S33: 0.0090
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 5JFC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220322.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8-8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.88
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 197382
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.589
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.300
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.5 M AMMONIUM FORMATE, 0.1 M HEPES PH
REMARK 280 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.86133
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 26.93067
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 26.93067
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 53.86133
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: 7820 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, S
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -220.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, S
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -26.93067
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 L 1
REMARK 465 GLY L 375
REMARK 465 GLU L 376
REMARK 465 PRO L 377
REMARK 465 ASP L 378
REMARK 465 GLU L 379
REMARK 465 SER L 380
REMARK 465 GLY L 381
REMARK 465 ARG L 382
REMARK 465 GLU L 473
REMARK 465 LYS L 474
REMARK 465 MET S 1
REMARK 465 VAL S 2
REMARK 465 VAL S 3
REMARK 465 MET S 4
REMARK 465 VAL S 5
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 L 914 O HOH L 931 1.75
REMARK 500 OE2 GLU L 184 O2B FAD L 503 1.80
REMARK 500 O HOH S 853 O HOH S 907 1.84
REMARK 500 O HOH L 1185 O HOH L 1186 1.92
REMARK 500 O HOH L 658 O HOH L 954 1.94
REMARK 500 O HOH S 770 O HOH S 805 1.94
REMARK 500 O HOH S 756 O HOH S 858 1.96
REMARK 500 O HOH L 853 O HOH L 1065 1.98
REMARK 500 O HOH S 622 O HOH S 912 2.01
REMARK 500 O HOH S 865 O HOH S 942 2.03
REMARK 500 O HOH L 772 O HOH L 1028 2.03
REMARK 500 O HOH S 710 O HOH S 885 2.04
REMARK 500 O HOH L 1067 O HOH L 1086 2.04
REMARK 500 O HOH L 629 O HOH L 1115 2.05
REMARK 500 O HOH L 1123 O HOH S 881 2.06
REMARK 500 O HOH L 1056 O HOH L 1122 2.06
REMARK 500 O HOH S 888 O HOH S 1034 2.06
REMARK 500 O HOH S 830 O HOH S 933 2.06
REMARK 500 O HOH L 1102 O HOH L 1119 2.06
REMARK 500 O HOH S 927 O HOH S 980 2.07
REMARK 500 O HOH L 1016 O HOH L 1165 2.07
REMARK 500 O HOH S 623 O HOH S 970 2.07
REMARK 500 O HOH S 627 O HOH S 897 2.09
REMARK 500 O HOH S 860 O HOH S 983 2.10
REMARK 500 O HOH S 963 O HOH S 971 2.10
REMARK 500 O HOH S 913 O HOH S 932 2.10
REMARK 500 O HOH S 648 O HOH S 755 2.11
REMARK 500 O HOH S 865 O HOH S 967 2.11
REMARK 500 O HOH L 998 O HOH L 1012 2.12
REMARK 500 O HOH L 1030 O HOH L 1101 2.13
REMARK 500 O HOH L 1022 O HOH L 1113 2.13
REMARK 500 O HOH L 836 O HOH L 1077 2.14
REMARK 500 O HOH L 850 O HOH S 817 2.14
REMARK 500 O HOH S 877 O HOH S 998 2.15
REMARK 500 O HOH S 888 O HOH S 1013 2.16
REMARK 500 O HOH S 919 O HOH S 926 2.16
REMARK 500 O HOH L 688 O HOH L 720 2.17
REMARK 500 O HOH L 970 O HOH L 1162 2.17
REMARK 500 O HOH L 1088 O HOH L 1168 2.18
REMARK 500 O HOH S 604 O HOH S 901 2.18
REMARK 500 O HOH L 673 O HOH L 950 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH L 650 O HOH L 1188 2564 1.86
REMARK 500 O HOH S 639 O HOH S 884 6554 2.05
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 GLN L 106 -119.46 -134.41
REMARK 500 LYS L 229 -62.96 -124.76
REMARK 500 ARG L 325 -155.46 -109.82
REMARK 500 ALA L 450 -122.03 -138.44
REMARK 500 SER S 27 81.33 -161.81
REMARK 500 VAL S 222 -76.22 -122.24
REMARK 500 CYS S 228 -24.26 -142.63
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 L1184 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH L1185 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH L1186 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH L1187 DISTANCE = 7.04 ANGSTROMS
REMARK 525 HOH L1188 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH S1039 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH S1040 DISTANCE = 6.35 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 502 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 42 SG
REMARK 620 2 SF4 L 502 S1 133.7
REMARK 620 3 SF4 L 502 S2 128.2 90.0
REMARK 620 4 SF4 L 502 S4 111.9 90.0 90.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 502 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 45 SG
REMARK 620 2 SF4 L 502 S2 132.2
REMARK 620 3 SF4 L 502 S3 128.3 90.0
REMARK 620 4 SF4 L 502 S4 113.8 90.0 90.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 502 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 52 SG
REMARK 620 2 SF4 L 502 S1 125.5
REMARK 620 3 SF4 L 502 S3 120.3 90.0
REMARK 620 4 SF4 L 502 S4 129.6 90.0 90.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 501 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 56 SG
REMARK 620 2 SF4 L 501 S1 121.8
REMARK 620 3 SF4 L 501 S2 122.0 90.0
REMARK 620 4 SF4 L 501 S3 131.6 90.0 90.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 101 SG
REMARK 620 2 SF4 L 501 S1 130.3
REMARK 620 3 SF4 L 501 S3 125.0 90.0
REMARK 620 4 SF4 L 501 S4 120.3 90.0 90.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 501 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 107 SG
REMARK 620 2 SF4 L 501 S1 117.8
REMARK 620 3 SF4 L 501 S2 125.9 90.0
REMARK 620 4 SF4 L 501 S4 131.5 90.0 90.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 502 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 111 SG
REMARK 620 2 SF4 L 502 S1 122.2
REMARK 620 3 SF4 L 502 S2 129.5 90.0
REMARK 620 4 SF4 L 502 S3 123.9 90.0 90.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU L 126 OE1
REMARK 620 2 SF4 L 501 S2 135.0
REMARK 620 3 SF4 L 501 S3 126.7 90.0
REMARK 620 4 SF4 L 501 S4 112.2 90.0 90.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG S 502 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU S 49 OE1
REMARK 620 2 FAD S 500 O1A 163.6
REMARK 620 3 FAD S 500 O1P 94.9 83.0
REMARK 620 4 HOH S 607 O 87.2 76.7 92.3
REMARK 620 5 HOH S 626 O 90.9 91.9 174.0 89.7
REMARK 620 6 HOH S 762 O 90.0 106.0 86.6 176.9 91.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES S 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP S 223 OD1
REMARK 620 2 FES S 501 S1 114.3
REMARK 620 3 FES S 501 S2 132.0 90.0
REMARK 620 4 CYS S 228 SG 97.7 112.2 110.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES S 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 231 SG
REMARK 620 2 FES S 501 S1 109.8
REMARK 620 3 FES S 501 S2 107.1 90.0
REMARK 620 4 CYS S 243 SG 109.2 129.9 107.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 L 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 L 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD L 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD S 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FES S 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG S 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5JCA RELATED DB: PDB
REMARK 900 5JCA CONTAINS THE SAME PROTEIN WITH NADP(H) BOUND
DBREF 5JFC L 1 474 UNP Q8U195 SUDHA_PYRFU 1 474
DBREF 5JFC S 7 284 UNP Q8U194 SUDHB_PYRFU 1 278
SEQADV 5JFC MET S 1 UNP Q8U194 EXPRESSION TAG
SEQADV 5JFC VAL S 2 UNP Q8U194 EXPRESSION TAG
SEQADV 5JFC VAL S 3 UNP Q8U194 EXPRESSION TAG
SEQADV 5JFC MET S 4 UNP Q8U194 EXPRESSION TAG
SEQADV 5JFC VAL S 5 UNP Q8U194 EXPRESSION TAG
SEQADV 5JFC MET S 6 UNP Q8U194 EXPRESSION TAG
SEQRES 1 L 474 MET PRO ARG LEU ILE LYS ASP ARG VAL PRO THR PRO GLU
SEQRES 2 L 474 ARG SER VAL GLY GLU ARG VAL ARG ASP PHE GLY GLU VAL
SEQRES 3 L 474 ASN LEU GLY TYR SER TRP GLU LEU ALA LEU ARG GLU ALA
SEQRES 4 L 474 GLU ARG CYS LEU GLN CYS PRO VAL GLU TYR ALA PRO CYS
SEQRES 5 L 474 ILE LYS GLY CYS PRO VAL HIS ILE ASN ILE PRO GLY PHE
SEQRES 6 L 474 ILE LYS ALA LEU ARG GLU ASN ARG ASP ASN PRO SER LYS
SEQRES 7 L 474 ALA VAL ARG GLU ALA LEU ARG ILE ILE TRP ARG ASP ASN
SEQRES 8 L 474 THR LEU PRO ALA ILE THR GLY ARG VAL CYS PRO GLN GLU
SEQRES 9 L 474 GLU GLN CYS GLU GLY ALA CYS VAL VAL GLY LYS VAL GLY
SEQRES 10 L 474 ASP PRO ILE ASN ILE GLY LYS LEU GLU ARG PHE VAL ALA
SEQRES 11 L 474 ASP TYR ALA ARG GLU HIS GLY ILE ASP ASP GLU LEU LEU
SEQRES 12 L 474 LEU GLU GLU ILE LYS GLY ILE LYS ARG ASN GLY LYS LYS
SEQRES 13 L 474 VAL ALA ILE ILE GLY ALA GLY PRO ALA GLY LEU THR CYS
SEQRES 14 L 474 ALA ALA ASP LEU ALA LYS MET GLY TYR GLU VAL THR ILE
SEQRES 15 L 474 TYR GLU ALA LEU HIS GLN PRO GLY GLY VAL LEU ILE TYR
SEQRES 16 L 474 GLY ILE PRO GLU PHE ARG LEU PRO LYS GLU ILE VAL LYS
SEQRES 17 L 474 LYS GLU LEU GLU ASN LEU ARG ARG LEU GLY VAL LYS ILE
SEQRES 18 L 474 GLU THR ASN VAL LEU VAL GLY LYS THR ILE THR PHE GLU
SEQRES 19 L 474 GLU LEU ARG GLU GLU TYR ASP ALA ILE PHE ILE GLY THR
SEQRES 20 L 474 GLY ALA GLY THR PRO ARG ILE TYR PRO TRP PRO GLY VAL
SEQRES 21 L 474 ASN LEU ASN GLY ILE TYR SER ALA ASN GLU PHE LEU THR
SEQRES 22 L 474 ARG ILE ASN LEU MET LYS ALA TYR LYS PHE PRO GLU TYR
SEQRES 23 L 474 ASP THR PRO ILE LYS VAL GLY LYS ARG VAL ALA VAL ILE
SEQRES 24 L 474 GLY GLY GLY ASN THR ALA MET ASP ALA ALA ARG SER ALA
SEQRES 25 L 474 LEU ARG LEU GLY ALA GLU VAL TRP ILE LEU TYR ARG ARG
SEQRES 26 L 474 THR ARG LYS GLU MET THR ALA ARG GLU GLU GLU ILE LYS
SEQRES 27 L 474 HIS ALA GLU GLU GLU GLY VAL LYS PHE MET PHE LEU VAL
SEQRES 28 L 474 THR PRO LYS ARG PHE ILE GLY ASP GLU ASN GLY ASN LEU
SEQRES 29 L 474 LYS ALA ILE GLU LEU GLU LYS MET LYS LEU GLY GLU PRO
SEQRES 30 L 474 ASP GLU SER GLY ARG ARG ARG PRO ILE PRO THR GLY GLU
SEQRES 31 L 474 THR PHE ILE MET GLU PHE ASP THR ALA ILE ILE ALA ILE
SEQRES 32 L 474 GLY GLN THR PRO ASN LYS THR PHE LEU GLU THR VAL PRO
SEQRES 33 L 474 GLY LEU LYS VAL ASP GLU TRP GLY ARG ILE VAL VAL ASP
SEQRES 34 L 474 GLU ASN LEU MET THR SER ILE PRO GLY VAL PHE ALA GLY
SEQRES 35 L 474 GLY ASP ALA ILE ARG GLY GLU ALA THR VAL ILE LEU ALA
SEQRES 36 L 474 MET GLY ASP GLY ARG LYS ALA ALA LYS ALA ILE HIS GLN
SEQRES 37 L 474 TYR LEU SER LYS GLU LYS
SEQRES 1 S 284 MET VAL VAL MET VAL MET MET PHE LYS ILE LEU ARG LYS
SEQRES 2 S 284 GLU ARG LEU ALA PRO GLY ILE ASN LEU PHE GLU ILE GLU
SEQRES 3 S 284 SER PRO ARG ILE ALA LYS HIS ALA LYS PRO GLY GLN PHE
SEQRES 4 S 284 VAL MET ILE ARG LEU HIS GLU LYS GLY GLU ARG ILE PRO
SEQRES 5 S 284 LEU THR ILE ALA ASP VAL ASP ILE SER LYS GLY SER ILE
SEQRES 6 S 284 THR ILE VAL ALA GLN GLU VAL GLY LYS THR THR ARG GLU
SEQRES 7 S 284 LEU GLY THR TYR GLU ALA GLY ASP TYR ILE LEU ASP VAL
SEQRES 8 S 284 LEU GLY PRO LEU GLY LYS PRO SER HIS ILE ASP TYR PHE
SEQRES 9 S 284 GLY THR VAL VAL MET ILE GLY GLY GLY VAL GLY VAL ALA
SEQRES 10 S 284 GLU ILE TYR PRO VAL ALA LYS ALA MET LYS GLU LYS GLY
SEQRES 11 S 284 ASN TYR VAL ILE SER ILE LEU GLY PHE ARG THR LYS ASP
SEQRES 12 S 284 LEU VAL PHE TRP GLU ASP LYS LEU ARG SER VAL SER ASP
SEQRES 13 S 284 GLU VAL ILE VAL THR THR ASN ASP GLY SER TYR GLY MET
SEQRES 14 S 284 LYS GLY PHE THR THR HIS ALA LEU GLN LYS LEU ILE GLU
SEQRES 15 S 284 GLU GLY ARG LYS ILE ASP LEU VAL HIS ALA VAL GLY PRO
SEQRES 16 S 284 ALA ILE MET MET LYS ALA VAL ALA GLU LEU THR LYS PRO
SEQRES 17 S 284 TYR GLY ILE LYS THR VAL ALA SER LEU ASN PRO ILE MET
SEQRES 18 S 284 VAL ASP GLY THR GLY MET CYS GLY ALA CYS ARG VAL THR
SEQRES 19 S 284 VAL GLY GLY GLU VAL LYS PHE ALA CYS VAL ASP GLY PRO
SEQRES 20 S 284 GLU PHE ASP ALA HIS LEU VAL ASP TRP ASP GLN LEU MET
SEQRES 21 S 284 ASN ARG LEU ALA TYR TYR ARG ASP LEU GLU LYS ILE SER
SEQRES 22 S 284 LEU GLU LYS TRP GLU ARG GLU ARG ARG MET VAL
HET SF4 L 501 8
HET SF4 L 502 8
HET FAD L 503 53
HET FAD S 500 84
HET FES S 501 4
HET MG S 502 1
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM MG MAGNESIUM ION
FORMUL 3 SF4 2(FE4 S4)
FORMUL 5 FAD 2(C27 H33 N9 O15 P2)
FORMUL 7 FES FE2 S2
FORMUL 8 MG MG 2+
FORMUL 9 HOH *1028(H2 O)
HELIX 1 AA1 SER L 15 VAL L 20 1 6
HELIX 2 AA2 SER L 31 GLU L 40 1 10
HELIX 3 AA3 ALA L 50 CYS L 56 1 7
HELIX 4 AA4 ASN L 61 GLU L 71 1 11
HELIX 5 AA5 ASN L 75 ARG L 89 1 15
HELIX 6 AA6 LEU L 93 CYS L 101 1 9
HELIX 7 AA7 PRO L 102 GLU L 105 5 4
HELIX 8 AA8 GLN L 106 CYS L 111 1 6
HELIX 9 AA9 VAL L 112 VAL L 116 5 5
HELIX 10 AB1 ASN L 121 HIS L 136 1 16
HELIX 11 AB2 GLY L 137 GLY L 149 1 13
HELIX 12 AB3 GLY L 163 MET L 176 1 14
HELIX 13 AB4 GLY L 191 GLY L 196 1 6
HELIX 14 AB5 PRO L 203 GLY L 218 1 16
HELIX 15 AB6 THR L 232 TYR L 240 1 9
HELIX 16 AB7 ALA L 268 LEU L 277 1 10
HELIX 17 AB8 LYS L 279 PHE L 283 5 5
HELIX 18 AB9 GLY L 302 LEU L 315 1 14
HELIX 19 AC1 THR L 326 MET L 330 5 5
HELIX 20 AC2 ARG L 333 GLY L 344 1 12
HELIX 21 AC3 ASN L 408 VAL L 415 1 8
HELIX 22 AC4 GLY L 443 GLY L 448 1 6
HELIX 23 AC5 THR L 451 LYS L 472 1 22
HELIX 24 AC6 SER S 27 ALA S 34 1 8
HELIX 25 AC7 ILE S 60 LYS S 62 5 3
HELIX 26 AC8 GLY S 73 THR S 81 1 9
HELIX 27 AC9 VAL S 114 LYS S 129 1 16
HELIX 28 AD1 THR S 141 VAL S 145 5 5
HELIX 29 AD2 TRP S 147 SER S 153 1 7
HELIX 30 AD3 PHE S 172 GLU S 183 1 12
HELIX 31 AD4 PRO S 195 LYS S 207 1 13
HELIX 32 AD5 PRO S 208 GLY S 210 5 3
HELIX 33 AD6 ALA S 242 GLY S 246 1 5
HELIX 34 AD7 HIS S 252 VAL S 254 5 3
HELIX 35 AD8 ASP S 255 ALA S 264 1 10
HELIX 36 AD9 TYR S 266 GLU S 280 1 15
SHEET 1 AA1 5 LYS L 220 GLU L 222 0
SHEET 2 AA1 5 GLU L 179 TYR L 183 1 N ILE L 182 O GLU L 222
SHEET 3 AA1 5 LYS L 156 ILE L 160 1 N ILE L 159 O TYR L 183
SHEET 4 AA1 5 ALA L 242 ILE L 245 1 O PHE L 244 N ILE L 160
SHEET 5 AA1 5 VAL L 439 ALA L 441 1 O PHE L 440 N ILE L 243
SHEET 1 AA2 2 THR L 251 PRO L 252 0
SHEET 2 AA2 2 GLN L 405 THR L 406 -1 O THR L 406 N THR L 251
SHEET 1 AA3 5 ILE L 265 SER L 267 0
SHEET 2 AA3 5 THR L 398 ILE L 401 1 O ALA L 399 N TYR L 266
SHEET 3 AA3 5 ARG L 295 ILE L 299 1 N ILE L 299 O ILE L 400
SHEET 4 AA3 5 GLU L 318 LEU L 322 1 O TRP L 320 N VAL L 298
SHEET 5 AA3 5 LYS L 346 MET L 348 1 O LYS L 346 N ILE L 321
SHEET 1 AA4 3 VAL L 351 GLY L 358 0
SHEET 2 AA4 3 LEU L 364 LYS L 373 -1 O LYS L 365 N ILE L 357
SHEET 3 AA4 3 ILE L 386 GLU L 395 -1 O PHE L 392 N LEU L 369
SHEET 1 AA5 5 ASP S 57 ASP S 59 0
SHEET 2 AA5 5 SER S 64 GLN S 70 -1 O SER S 64 N ASP S 59
SHEET 3 AA5 5 ILE S 20 GLU S 26 -1 N ILE S 25 O ILE S 65
SHEET 4 AA5 5 PHE S 8 ALA S 17 -1 N GLU S 14 O LEU S 22
SHEET 5 AA5 5 TYR S 87 ILE S 88 -1 O ILE S 88 N PHE S 8
SHEET 1 AA6 3 ILE S 51 THR S 54 0
SHEET 2 AA6 3 PHE S 39 ARG S 43 -1 N VAL S 40 O LEU S 53
SHEET 3 AA6 3 ASP S 90 LEU S 95 -1 O LEU S 95 N PHE S 39
SHEET 1 AA7 7 MET S 169 LYS S 170 0
SHEET 2 AA7 7 GLU S 157 THR S 162 1 N VAL S 160 O MET S 169
SHEET 3 AA7 7 TYR S 132 PHE S 139 1 N LEU S 137 O THR S 161
SHEET 4 AA7 7 THR S 106 GLY S 112 1 N MET S 109 O ILE S 136
SHEET 5 AA7 7 LEU S 189 VAL S 193 1 O HIS S 191 N ILE S 110
SHEET 6 AA7 7 THR S 213 SER S 216 1 O VAL S 214 N VAL S 190
SHEET 7 AA7 7 GLU S 248 ASP S 250 -1 O PHE S 249 N ALA S 215
SHEET 1 AA8 2 ARG S 232 VAL S 235 0
SHEET 2 AA8 2 GLU S 238 PHE S 241 -1 O GLU S 238 N VAL S 235
LINK SG CYS L 42 FE3 SF4 L 502 1555 1555 2.20
LINK SG CYS L 45 FE1 SF4 L 502 1555 1555 2.27
LINK SG CYS L 52 FE2 SF4 L 502 1555 1555 2.07
LINK SG CYS L 56 FE4 SF4 L 501 1555 1555 2.17
LINK SG CYS L 101 FE2 SF4 L 501 1555 1555 2.16
LINK SG CYS L 107 FE3 SF4 L 501 1555 1555 2.14
LINK SG CYS L 111 FE4 SF4 L 502 1555 1555 2.22
LINK OE1 GLU L 126 FE1 SF4 L 501 1555 1555 1.88
LINK OE1 GLU S 49 MG MG S 502 1555 1555 2.04
LINK OD1 ASP S 223 FE2 FES S 501 1555 1555 1.90
LINK SG CYS S 228 FE2 FES S 501 1555 1555 2.34
LINK SG CYS S 231 FE1 FES S 501 1555 1555 2.34
LINK SG CYS S 243 FE1 FES S 501 1555 1555 2.15
LINK O1A FAD S 500 MG MG S 502 1555 1555 1.81
LINK O1P FAD S 500 MG MG S 502 1555 1555 2.08
LINK MG MG S 502 O HOH S 607 1555 1555 2.13
LINK MG MG S 502 O HOH S 626 1555 1555 2.10
LINK MG MG S 502 O HOH S 762 1555 1555 2.08
CISPEP 1 PHE L 283 PRO L 284 0 4.30
CISPEP 2 GLY S 93 PRO S 94 0 -5.89
CISPEP 3 GLY S 246 PRO S 247 0 12.91
SITE 1 AC1 6 CYS L 56 THR L 97 CYS L 101 GLN L 106
SITE 2 AC1 6 CYS L 107 GLU L 126
SITE 1 AC2 5 CYS L 42 LEU L 43 CYS L 45 CYS L 52
SITE 2 AC2 5 CYS L 111
SITE 1 AC3 36 VAL L 100 GLY L 161 ALA L 162 GLY L 163
SITE 2 AC3 36 PRO L 164 ALA L 165 GLU L 184 ALA L 185
SITE 3 AC3 36 LEU L 186 GLY L 191 VAL L 192 ILE L 197
SITE 4 AC3 36 ARG L 201 VAL L 225 VAL L 227 GLY L 246
SITE 5 AC3 36 THR L 247 GLY L 248 ASN L 303 THR L 304
SITE 6 AC3 36 ASP L 307 ARG L 333 GLN L 405 PHE L 411
SITE 7 AC3 36 GLY L 443 ASP L 444 ALA L 450 THR L 451
SITE 8 AC3 36 VAL L 452 ALA L 455 HOH L 609 HOH L 616
SITE 9 AC3 36 HOH L 704 HOH L 706 HOH L 816 HOH L 934
SITE 1 AC4 35 GLU S 49 ILE S 51 PRO S 52 LEU S 53
SITE 2 AC4 35 THR S 54 VAL S 68 ALA S 69 GLN S 70
SITE 3 AC4 35 VAL S 72 GLY S 73 THR S 75 THR S 76
SITE 4 AC4 35 VAL S 114 GLU S 118 ASN S 218 PRO S 219
SITE 5 AC4 35 ILE S 220 MET S 221 LEU S 263 GLU S 270
SITE 6 AC4 35 MG S 502 HOH S 607 HOH S 626 HOH S 653
SITE 7 AC4 35 HOH S 665 HOH S 666 HOH S 667 HOH S 672
SITE 8 AC4 35 HOH S 686 HOH S 711 HOH S 722 HOH S 743
SITE 9 AC4 35 HOH S 762 HOH S 791 HOH S 863
SITE 1 AC5 9 VAL S 222 ASP S 223 GLY S 224 GLY S 226
SITE 2 AC5 9 MET S 227 CYS S 228 GLY S 229 CYS S 231
SITE 3 AC5 9 CYS S 243
SITE 1 AC6 5 GLU S 49 FAD S 500 HOH S 607 HOH S 626
SITE 2 AC6 5 HOH S 762
CRYST1 179.927 179.927 80.792 90.00 90.00 120.00 P 32 2 1 6
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 0.005558 0.003209 0.000000 0.00000
SCALE2 0.000000 0.006418 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012377 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
