HEADER ELECTRON TRANSPORT 10-SEP-18 6HL4
TITLE WILD-TYPE NUOEF FROM AQUIFEX AEOLICUS - REDUCED FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NADH-QUINONE OXIDOREDUCTASE SUBUNIT E;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: NADH DEHYDROGENASE I SUBUNIT E,NDH-1 SUBUNIT E;
COMPND 5 EC: 1.6.5.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NADH-QUINONE OXIDOREDUCTASE SUBUNIT F;
COMPND 9 CHAIN: B, D;
COMPND 10 SYNONYM: NADH DEHYDROGENASE I SUBUNIT F,NDH-1 SUBUNIT F;
COMPND 11 EC: 1.6.5.11;
COMPND 12 ENGINEERED: YES;
COMPND 13 OTHER_DETAILS: SEQUENCE CONTAINS C-TERMINAL 6XHIS-EXPRESSIONTAG
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS VF5;
SOURCE 3 ORGANISM_TAXID: 224324;
SOURCE 4 GENE: NUOE, AQ_574;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS VF5;
SOURCE 9 ORGANISM_TAXID: 224324;
SOURCE 10 GENE: NUOF, AQ_573;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COMPLEX I, NUOEF, ELECTRON TRANSFER, AQUIFEX AEOLICUS, ELECTRON
KEYWDS 2 TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GERHARDT,T.FRIEDRICH,O.EINSLE,E.GNANDT,M.SCHULTE,D.FIEGEN
REVDAT 1 26-JUN-19 6HL4 0
JRNL AUTH M.SCHULTE,K.FRICK,E.GNANDT,S.JURKOVIC,S.BURSCHEL,R.LABATZKE,
JRNL AUTH 2 K.AIERSTOCK,D.FIEGEN,D.WOHLWEND,S.GERHARDT,O.EINSLE,
JRNL AUTH 3 T.FRIEDRICH
JRNL TITL A MECHANISM TO PREVENT PRODUCTION OF REACTIVE OXYGEN SPECIES
JRNL TITL 2 BY ESCHERICHIA COLI RESPIRATORY COMPLEX I.
JRNL REF NAT COMMUN V. 10 2551 2019
JRNL REFN ESSN 2041-1723
JRNL PMID 31186428
JRNL DOI 10.1038/S41467-019-10429-0
REMARK 2
REMARK 2 RESOLUTION. 2.06 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.7
REMARK 3 NUMBER OF REFLECTIONS : 65618
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 3277
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 50
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.09
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 46.50
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1313
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2212
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1242
REMARK 3 BIN R VALUE (WORKING SET) : 0.2209
REMARK 3 BIN FREE R VALUE : 0.2269
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.41
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9053
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 87
REMARK 3 SOLVENT ATOMS : 127
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.22
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.41460
REMARK 3 B22 (A**2) : -5.66650
REMARK 3 B33 (A**2) : 4.25190
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.340
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.243
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.187
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.251
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.192
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 9371 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 12704 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3234 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 1610 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 9371 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1181 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 11364 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.98
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.59
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9469 10.9784 -10.5622
REMARK 3 T TENSOR
REMARK 3 T11: -0.0111 T22: -0.0714
REMARK 3 T33: -0.0606 T12: 0.0258
REMARK 3 T13: -0.0256 T23: -0.0751
REMARK 3 L TENSOR
REMARK 3 L11: 0.6326 L22: 0.0000
REMARK 3 L33: 2.3373 L12: 0.2335
REMARK 3 L13: 0.4610 L23: -0.0010
REMARK 3 S TENSOR
REMARK 3 S11: -0.0301 S12: -0.2337 S13: 0.4715
REMARK 3 S21: -0.0254 S22: -0.0029 S23: 0.0566
REMARK 3 S31: -0.5308 S32: 0.0131 S33: 0.0331
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1908 -12.2853 -16.3992
REMARK 3 T TENSOR
REMARK 3 T11: -0.0588 T22: -0.0288
REMARK 3 T33: -0.1059 T12: 0.0072
REMARK 3 T13: -0.0496 T23: -0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 1.5866 L22: 0.1379
REMARK 3 L33: 1.2411 L12: -0.1597
REMARK 3 L13: 0.5323 L23: -0.1062
REMARK 3 S TENSOR
REMARK 3 S11: 0.0928 S12: -0.1170 S13: -0.1229
REMARK 3 S21: 0.0022 S22: -0.0014 S23: 0.1078
REMARK 3 S31: 0.0713 S32: 0.1319 S33: -0.0914
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6711 -11.5367 -59.1934
REMARK 3 T TENSOR
REMARK 3 T11: 0.0048 T22: -0.1102
REMARK 3 T33: -0.1045 T12: -0.0208
REMARK 3 T13: -0.0035 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 3.3805 L22: 1.1765
REMARK 3 L33: 1.0585 L12: -0.4655
REMARK 3 L13: 0.1575 L23: 0.0821
REMARK 3 S TENSOR
REMARK 3 S11: -0.0193 S12: 0.3169 S13: -0.3249
REMARK 3 S21: -0.0206 S22: -0.0011 S23: 0.0751
REMARK 3 S31: 0.2762 S32: 0.0486 S33: 0.0204
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3965 11.5473 -52.5491
REMARK 3 T TENSOR
REMARK 3 T11: -0.0599 T22: -0.0644
REMARK 3 T33: -0.0796 T12: -0.0030
REMARK 3 T13: -0.0119 T23: 0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 1.1956 L22: 0.3778
REMARK 3 L33: 1.2372 L12: 0.0226
REMARK 3 L13: -0.1921 L23: -0.0387
REMARK 3 S TENSOR
REMARK 3 S11: 0.0454 S12: 0.0234 S13: 0.1621
REMARK 3 S21: -0.0211 S22: 0.0112 S23: -0.0089
REMARK 3 S31: -0.0250 S32: 0.0488 S33: -0.0566
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6HL4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1200011871.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9 - 7.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54179
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65727
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060
REMARK 200 RESOLUTION RANGE LOW (A) : 188.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.7
REMARK 200 DATA REDUNDANCY : 4.900
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.31200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: IN-HOUSE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS/HCL 0.1M SODIUM CITRATE, PH
REMARK 280 6.9, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 29.87050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 94.09050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.05850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 94.09050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.87050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.05850
REMARK 290 SMTRY3 4 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: 5750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.0 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: 5660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 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 MET A 1
REMARK 465 PHE A 2
REMARK 465 LYS A 3
REMARK 465 THR A 4
REMARK 465 GLU A 5
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 LYS B 419
REMARK 465 LYS B 420
REMARK 465 SER B 421
REMARK 465 ALA B 422
REMARK 465 SER B 423
REMARK 465 LEU B 424
REMARK 465 PRO B 425
REMARK 465 LEU B 426
REMARK 465 ALA B 427
REMARK 465 GLY B 428
REMARK 465 HIS B 429
REMARK 465 HIS B 430
REMARK 465 HIS B 431
REMARK 465 HIS B 432
REMARK 465 HIS B 433
REMARK 465 HIS B 434
REMARK 465 MET C 1
REMARK 465 PHE C 2
REMARK 465 LYS C 3
REMARK 465 THR C 4
REMARK 465 GLU C 5
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 ARG D 418
REMARK 465 LYS D 419
REMARK 465 LYS D 420
REMARK 465 SER D 421
REMARK 465 ALA D 422
REMARK 465 SER D 423
REMARK 465 LEU D 424
REMARK 465 PRO D 425
REMARK 465 LEU D 426
REMARK 465 ALA D 427
REMARK 465 GLY D 428
REMARK 465 HIS D 429
REMARK 465 HIS D 430
REMARK 465 HIS D 431
REMARK 465 HIS D 432
REMARK 465 HIS D 433
REMARK 465 HIS D 434
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 GLU A 76 -69.40 -94.43
REMARK 500 CYS A 127 121.78 -35.04
REMARK 500 ALA A 130 31.26 -150.56
REMARK 500 ASN A 140 -118.69 59.01
REMARK 500 MET B 18 -84.43 -114.18
REMARK 500 GLU B 95 91.34 7.42
REMARK 500 PHE B 101 15.04 -143.49
REMARK 500 TYR B 138 64.15 -115.63
REMARK 500 ASN B 161 61.13 38.32
REMARK 500 ALA B 177 37.02 -143.24
REMARK 500 LYS B 257 31.45 -80.09
REMARK 500 MET B 309 32.60 -91.09
REMARK 500 GLU C 76 -69.21 -94.58
REMARK 500 CYS C 127 123.40 -33.29
REMARK 500 ALA C 130 32.12 -151.48
REMARK 500 ASN C 140 -119.40 61.57
REMARK 500 MET D 18 -84.27 -114.38
REMARK 500 ALA D 23 0.78 -69.44
REMARK 500 GLU D 95 83.85 8.52
REMARK 500 PHE D 101 19.47 -143.50
REMARK 500 TYR D 138 64.10 -115.33
REMARK 500 ASN D 161 61.48 37.56
REMARK 500 ALA D 177 38.75 -144.61
REMARK 500 TYR D 246 56.25 -107.37
REMARK 500 LYS D 257 31.95 -80.20
REMARK 500 MET D 309 31.99 -91.06
REMARK 500
REMARK 500 REMARK: NULL
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 FES A 200 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 86 SG
REMARK 620 2 FES A 200 S1 111.4
REMARK 620 3 FES A 200 S2 112.5 103.8
REMARK 620 4 CYS A 91 SG 102.9 103.8 122.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 200 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 127 SG
REMARK 620 2 FES A 200 S1 122.3
REMARK 620 3 FES A 200 S2 114.2 103.7
REMARK 620 4 CYS A 131 SG 88.2 118.0 110.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 347 SG
REMARK 620 2 SF4 B 501 S2 101.7
REMARK 620 3 SF4 B 501 S3 118.2 103.9
REMARK 620 4 SF4 B 501 S4 122.5 104.4 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 501 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 350 SG
REMARK 620 2 SF4 B 501 S1 116.1
REMARK 620 3 SF4 B 501 S2 117.7 104.8
REMARK 620 4 SF4 B 501 S3 108.3 104.7 103.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 353 SG
REMARK 620 2 SF4 B 501 S1 104.3
REMARK 620 3 SF4 B 501 S3 108.6 104.7
REMARK 620 4 SF4 B 501 S4 128.5 104.2 104.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 501 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 393 SG
REMARK 620 2 SF4 B 501 S1 116.4
REMARK 620 3 SF4 B 501 S2 120.0 104.7
REMARK 620 4 SF4 B 501 S4 105.3 104.3 104.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C 200 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 86 SG
REMARK 620 2 FES C 200 S1 122.1
REMARK 620 3 FES C 200 S2 99.6 104.4
REMARK 620 4 CYS C 91 SG 106.1 104.7 121.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C 200 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 127 SG
REMARK 620 2 FES C 200 S1 106.2
REMARK 620 3 FES C 200 S2 107.4 104.3
REMARK 620 4 CYS C 131 SG 87.2 118.3 129.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 500 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 347 SG
REMARK 620 2 SF4 D 500 S2 107.1
REMARK 620 3 SF4 D 500 S3 110.2 104.1
REMARK 620 4 SF4 D 500 S4 124.5 104.7 104.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 500 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 350 SG
REMARK 620 2 SF4 D 500 S1 113.3
REMARK 620 3 SF4 D 500 S2 119.7 104.6
REMARK 620 4 SF4 D 500 S3 109.2 104.8 104.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 500 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 353 SG
REMARK 620 2 SF4 D 500 S1 99.7
REMARK 620 3 SF4 D 500 S3 114.8 105.3
REMARK 620 4 SF4 D 500 S4 126.5 104.4 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 500 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 393 SG
REMARK 620 2 SF4 D 500 S1 125.7
REMARK 620 3 SF4 D 500 S2 112.9 104.2
REMARK 620 4 SF4 D 500 S4 103.8 104.0 104.0
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 FES A 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FES C 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN D 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6HL2 RELATED DB: PDB
REMARK 900 6HL2 CONTAINS THE SAME PROTEIN IN THE OXIDIZED STATE
REMARK 900 RELATED ID: 6HL3 RELATED DB: PDB
REMARK 900 6HL3 CONTAINS THE SAME PROTEIN IN THE OXIDIZED STATE WITH BOUND NAD+
DBREF 6HL4 A 1 160 UNP O66842 NUOE_AQUAE 1 160
DBREF 6HL4 B 1 426 UNP O66841 NUOF_AQUAE 1 426
DBREF 6HL4 C 1 160 UNP O66842 NUOE_AQUAE 1 160
DBREF 6HL4 D 1 426 UNP O66841 NUOF_AQUAE 1 426
SEQADV 6HL4 ALA B 427 UNP O66841 EXPRESSION TAG
SEQADV 6HL4 GLY B 428 UNP O66841 EXPRESSION TAG
SEQADV 6HL4 HIS B 429 UNP O66841 EXPRESSION TAG
SEQADV 6HL4 HIS B 430 UNP O66841 EXPRESSION TAG
SEQADV 6HL4 HIS B 431 UNP O66841 EXPRESSION TAG
SEQADV 6HL4 HIS B 432 UNP O66841 EXPRESSION TAG
SEQADV 6HL4 HIS B 433 UNP O66841 EXPRESSION TAG
SEQADV 6HL4 HIS B 434 UNP O66841 EXPRESSION TAG
SEQADV 6HL4 ALA D 427 UNP O66841 EXPRESSION TAG
SEQADV 6HL4 GLY D 428 UNP O66841 EXPRESSION TAG
SEQADV 6HL4 HIS D 429 UNP O66841 EXPRESSION TAG
SEQADV 6HL4 HIS D 430 UNP O66841 EXPRESSION TAG
SEQADV 6HL4 HIS D 431 UNP O66841 EXPRESSION TAG
SEQADV 6HL4 HIS D 432 UNP O66841 EXPRESSION TAG
SEQADV 6HL4 HIS D 433 UNP O66841 EXPRESSION TAG
SEQADV 6HL4 HIS D 434 UNP O66841 EXPRESSION TAG
SEQRES 1 A 160 MET PHE LYS THR GLU PHE GLU PHE PRO GLU GLU LEU LYS
SEQRES 2 A 160 THR LYS LEU GLN GLU HIS ILE ASN TYR PHE PRO LYS LYS
SEQRES 3 A 160 ARG GLN ALA ILE LEU LEU CYS LEU HIS GLU ILE GLN ASN
SEQRES 4 A 160 TYR TYR GLY TYR ILE PRO PRO GLU SER LEU LYS PRO LEU
SEQRES 5 A 160 ALA ASP MET LEU GLU LEU PRO LEU ASN HIS VAL GLU GLY
SEQRES 6 A 160 VAL VAL ALA PHE TYR ASP MET PHE ASP ARG GLU ASP LYS
SEQRES 7 A 160 ALA LYS TYR ARG ILE ARG VAL CYS VAL SER ILE VAL CYS
SEQRES 8 A 160 HIS LEU MET GLY THR ASN LYS LEU LEU LYS ALA LEU GLU
SEQRES 9 A 160 ASN ILE LEU GLY ILE LYS PRO GLY GLU VAL THR PRO ASP
SEQRES 10 A 160 GLY LYS PHE LYS ILE VAL PRO VAL GLN CYS LEU GLY ALA
SEQRES 11 A 160 CYS SER GLU ALA PRO VAL PHE MET VAL ASN ASP ASP GLU
SEQRES 12 A 160 TYR LYS PHE GLU SER GLU VAL GLN LEU ASN GLU ILE LEU
SEQRES 13 A 160 SER ARG TYR THR
SEQRES 1 B 434 MET ARG SER TYR PRO ALA ILE PRO ARG ILE TYR ALA GLU
SEQRES 2 B 434 THR THR LEU ASN MET LEU LEU LYS ARG ALA LYS LYS PRO
SEQRES 3 B 434 ARG VAL HIS SER ILE ASP GLU TYR LEU LYS ASP GLY GLY
SEQRES 4 B 434 TYR GLN ALA LEU GLU LYS ALA LEU ASN MET SER PRO GLU
SEQRES 5 B 434 GLU ILE ILE ASP TRP VAL ASP LYS SER THR LEU ARG GLY
SEQRES 6 B 434 ARG GLY GLY ALA GLY PHE PRO THR GLY LYS LYS TRP LYS
SEQRES 7 B 434 PHE ALA VAL GLN ASN PRO GLY PRO ARG TYR PHE ILE CYS
SEQRES 8 B 434 ASN ALA ASP GLU SER GLU PRO GLY THR PHE LYS ASP ARG
SEQRES 9 B 434 ILE ILE ILE GLU ARG ASP PRO HIS LEU LEU ILE GLU GLY
SEQRES 10 B 434 ILE ILE ILE SER SER TYR ALA ILE GLY ALA ASN GLU ALA
SEQRES 11 B 434 TYR ILE TYR ILE ARG GLY GLU TYR PRO ALA GLY TYR TYR
SEQRES 12 B 434 ILE LEU ARG ASP ALA ILE GLU GLU ALA LYS LYS LYS GLY
SEQRES 13 B 434 PHE LEU GLY LYS ASN ILE LEU GLY SER GLY PHE ASP LEU
SEQRES 14 B 434 GLU ILE TYR VAL ALA ARG GLY ALA GLY ALA TYR ILE CYS
SEQRES 15 B 434 GLY GLU GLU THR ALA LEU ILE GLU SER LEU GLU GLY LYS
SEQRES 16 B 434 ARG GLY HIS PRO ARG LEU LYS PRO PRO TYR PRO VAL GLN
SEQRES 17 B 434 LYS GLY LEU TRP GLY LYS PRO THR VAL VAL ASN ASN VAL
SEQRES 18 B 434 GLU THR ILE ALA ASN VAL PRO PHE ILE ILE SER MET GLY
SEQRES 19 B 434 TRP GLU GLU TYR ARG TYR ILE GLY PRO SER ASP TYR ALA
SEQRES 20 B 434 GLY PRO LYS LEU PHE PRO VAL SER GLY LYS VAL LYS LYS
SEQRES 21 B 434 PRO GLY VAL TYR GLU LEU PRO MET ASN THR THR LEU ARG
SEQRES 22 B 434 GLU VAL ILE PHE LYS TYR ALA GLY GLY THR LEU GLY ASN
SEQRES 23 B 434 LYS LYS VAL LYS ALA VAL PHE SER GLY ALA LEU ASP CYS
SEQRES 24 B 434 PHE SER SER GLU GLU LEU ASP ILE PRO MET ASP TYR SER
SEQRES 25 B 434 PRO LEU GLY PHE GLY GLY THR GLY THR VAL ILE VAL LEU
SEQRES 26 B 434 THR GLU GLU ASP ASP ILE VAL GLU ALA ALA LEU LYS ILE
SEQRES 27 B 434 ALA GLU PHE TYR GLU HIS GLU THR CYS GLY GLN CYS THR
SEQRES 28 B 434 PRO CYS ARG VAL GLY CYS TYR GLU GLN ALA ASN LEU LEU
SEQRES 29 B 434 GLU LYS ILE TYR LYS GLY GLU ALA THR GLU GLN ASP TRP
SEQRES 30 B 434 GLU GLY PHE ASP PHE VAL ASN ARG ASN ILE GLN PRO THR
SEQRES 31 B 434 SER ILE CYS GLY LEU GLY ALA VAL ALA GLY ARG LEU ILE
SEQRES 32 B 434 ARG GLN THR LEU GLU LYS PHE PRO GLU GLU TRP GLU LYS
SEQRES 33 B 434 TYR ARG LYS LYS SER ALA SER LEU PRO LEU ALA GLY HIS
SEQRES 34 B 434 HIS HIS HIS HIS HIS
SEQRES 1 C 160 MET PHE LYS THR GLU PHE GLU PHE PRO GLU GLU LEU LYS
SEQRES 2 C 160 THR LYS LEU GLN GLU HIS ILE ASN TYR PHE PRO LYS LYS
SEQRES 3 C 160 ARG GLN ALA ILE LEU LEU CYS LEU HIS GLU ILE GLN ASN
SEQRES 4 C 160 TYR TYR GLY TYR ILE PRO PRO GLU SER LEU LYS PRO LEU
SEQRES 5 C 160 ALA ASP MET LEU GLU LEU PRO LEU ASN HIS VAL GLU GLY
SEQRES 6 C 160 VAL VAL ALA PHE TYR ASP MET PHE ASP ARG GLU ASP LYS
SEQRES 7 C 160 ALA LYS TYR ARG ILE ARG VAL CYS VAL SER ILE VAL CYS
SEQRES 8 C 160 HIS LEU MET GLY THR ASN LYS LEU LEU LYS ALA LEU GLU
SEQRES 9 C 160 ASN ILE LEU GLY ILE LYS PRO GLY GLU VAL THR PRO ASP
SEQRES 10 C 160 GLY LYS PHE LYS ILE VAL PRO VAL GLN CYS LEU GLY ALA
SEQRES 11 C 160 CYS SER GLU ALA PRO VAL PHE MET VAL ASN ASP ASP GLU
SEQRES 12 C 160 TYR LYS PHE GLU SER GLU VAL GLN LEU ASN GLU ILE LEU
SEQRES 13 C 160 SER ARG TYR THR
SEQRES 1 D 434 MET ARG SER TYR PRO ALA ILE PRO ARG ILE TYR ALA GLU
SEQRES 2 D 434 THR THR LEU ASN MET LEU LEU LYS ARG ALA LYS LYS PRO
SEQRES 3 D 434 ARG VAL HIS SER ILE ASP GLU TYR LEU LYS ASP GLY GLY
SEQRES 4 D 434 TYR GLN ALA LEU GLU LYS ALA LEU ASN MET SER PRO GLU
SEQRES 5 D 434 GLU ILE ILE ASP TRP VAL ASP LYS SER THR LEU ARG GLY
SEQRES 6 D 434 ARG GLY GLY ALA GLY PHE PRO THR GLY LYS LYS TRP LYS
SEQRES 7 D 434 PHE ALA VAL GLN ASN PRO GLY PRO ARG TYR PHE ILE CYS
SEQRES 8 D 434 ASN ALA ASP GLU SER GLU PRO GLY THR PHE LYS ASP ARG
SEQRES 9 D 434 ILE ILE ILE GLU ARG ASP PRO HIS LEU LEU ILE GLU GLY
SEQRES 10 D 434 ILE ILE ILE SER SER TYR ALA ILE GLY ALA ASN GLU ALA
SEQRES 11 D 434 TYR ILE TYR ILE ARG GLY GLU TYR PRO ALA GLY TYR TYR
SEQRES 12 D 434 ILE LEU ARG ASP ALA ILE GLU GLU ALA LYS LYS LYS GLY
SEQRES 13 D 434 PHE LEU GLY LYS ASN ILE LEU GLY SER GLY PHE ASP LEU
SEQRES 14 D 434 GLU ILE TYR VAL ALA ARG GLY ALA GLY ALA TYR ILE CYS
SEQRES 15 D 434 GLY GLU GLU THR ALA LEU ILE GLU SER LEU GLU GLY LYS
SEQRES 16 D 434 ARG GLY HIS PRO ARG LEU LYS PRO PRO TYR PRO VAL GLN
SEQRES 17 D 434 LYS GLY LEU TRP GLY LYS PRO THR VAL VAL ASN ASN VAL
SEQRES 18 D 434 GLU THR ILE ALA ASN VAL PRO PHE ILE ILE SER MET GLY
SEQRES 19 D 434 TRP GLU GLU TYR ARG TYR ILE GLY PRO SER ASP TYR ALA
SEQRES 20 D 434 GLY PRO LYS LEU PHE PRO VAL SER GLY LYS VAL LYS LYS
SEQRES 21 D 434 PRO GLY VAL TYR GLU LEU PRO MET ASN THR THR LEU ARG
SEQRES 22 D 434 GLU VAL ILE PHE LYS TYR ALA GLY GLY THR LEU GLY ASN
SEQRES 23 D 434 LYS LYS VAL LYS ALA VAL PHE SER GLY ALA LEU ASP CYS
SEQRES 24 D 434 PHE SER SER GLU GLU LEU ASP ILE PRO MET ASP TYR SER
SEQRES 25 D 434 PRO LEU GLY PHE GLY GLY THR GLY THR VAL ILE VAL LEU
SEQRES 26 D 434 THR GLU GLU ASP ASP ILE VAL GLU ALA ALA LEU LYS ILE
SEQRES 27 D 434 ALA GLU PHE TYR GLU HIS GLU THR CYS GLY GLN CYS THR
SEQRES 28 D 434 PRO CYS ARG VAL GLY CYS TYR GLU GLN ALA ASN LEU LEU
SEQRES 29 D 434 GLU LYS ILE TYR LYS GLY GLU ALA THR GLU GLN ASP TRP
SEQRES 30 D 434 GLU GLY PHE ASP PHE VAL ASN ARG ASN ILE GLN PRO THR
SEQRES 31 D 434 SER ILE CYS GLY LEU GLY ALA VAL ALA GLY ARG LEU ILE
SEQRES 32 D 434 ARG GLN THR LEU GLU LYS PHE PRO GLU GLU TRP GLU LYS
SEQRES 33 D 434 TYR ARG LYS LYS SER ALA SER LEU PRO LEU ALA GLY HIS
SEQRES 34 D 434 HIS HIS HIS HIS HIS
HET FES A 200 4
HET SF4 B 501 8
HET FMN B 502 31
HET CL B 503 1
HET FES C 200 4
HET SF4 D 500 8
HET FMN D 501 31
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM CL CHLORIDE ION
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
FORMUL 5 FES 2(FE2 S2)
FORMUL 6 SF4 2(FE4 S4)
FORMUL 7 FMN 2(C17 H21 N4 O9 P)
FORMUL 8 CL CL 1-
FORMUL 12 HOH *127(H2 O)
HELIX 1 AA1 PRO A 9 PHE A 23 1 15
HELIX 2 AA2 LYS A 25 GLN A 28 5 4
HELIX 3 AA3 ALA A 29 GLY A 42 1 14
HELIX 4 AA4 PRO A 45 GLU A 47 5 3
HELIX 5 AA5 SER A 48 GLU A 57 1 10
HELIX 6 AA6 PRO A 59 TYR A 70 1 12
HELIX 7 AA7 SER A 88 GLY A 95 1 8
HELIX 8 AA8 GLY A 95 GLY A 108 1 14
HELIX 9 AA9 ALA A 130 ALA A 134 5 5
HELIX 10 AB1 SER A 148 SER A 157 1 10
HELIX 11 AB2 SER B 30 ASP B 37 1 8
HELIX 12 AB3 TYR B 40 ASN B 48 1 9
HELIX 13 AB4 SER B 50 THR B 62 1 13
HELIX 14 AB5 PRO B 72 GLN B 82 1 11
HELIX 15 AB6 PHE B 101 ASP B 110 1 10
HELIX 16 AB7 ASP B 110 GLY B 126 1 17
HELIX 17 AB8 TYR B 138 LYS B 155 1 18
HELIX 18 AB9 ASN B 161 SER B 165 5 5
HELIX 19 AC1 ALA B 179 GLY B 183 5 5
HELIX 20 AC2 GLU B 184 GLU B 193 1 10
HELIX 21 AC3 GLY B 210 LYS B 214 5 5
HELIX 22 AC4 VAL B 221 ASN B 226 1 6
HELIX 23 AC5 ASN B 226 GLY B 234 1 9
HELIX 24 AC6 GLY B 234 ILE B 241 1 8
HELIX 25 AC7 THR B 271 LYS B 278 1 8
HELIX 26 AC8 THR B 283 LYS B 287 5 5
HELIX 27 AC9 GLU B 303 LEU B 305 5 3
HELIX 28 AD1 ASP B 330 THR B 346 1 17
HELIX 29 AD2 CYS B 350 LYS B 369 1 20
HELIX 30 AD3 THR B 373 ASN B 386 1 14
HELIX 31 AD4 CYS B 393 ALA B 399 1 7
HELIX 32 AD5 GLY B 400 PHE B 410 1 11
HELIX 33 AD6 PHE B 410 ARG B 418 1 9
HELIX 34 AD7 PRO C 9 PHE C 23 1 15
HELIX 35 AD8 LYS C 25 GLN C 28 5 4
HELIX 36 AD9 ALA C 29 GLY C 42 1 14
HELIX 37 AE1 PRO C 45 GLU C 47 5 3
HELIX 38 AE2 SER C 48 GLU C 57 1 10
HELIX 39 AE3 PRO C 59 TYR C 70 1 12
HELIX 40 AE4 SER C 88 GLY C 95 1 8
HELIX 41 AE5 GLY C 95 GLY C 108 1 14
HELIX 42 AE6 ALA C 130 ALA C 134 5 5
HELIX 43 AE7 SER C 148 SER C 157 1 10
HELIX 44 AE8 SER D 30 ASP D 37 1 8
HELIX 45 AE9 TYR D 40 ASN D 48 1 9
HELIX 46 AF1 SER D 50 THR D 62 1 13
HELIX 47 AF2 PRO D 72 GLN D 82 1 11
HELIX 48 AF3 PHE D 101 ASP D 110 1 10
HELIX 49 AF4 ASP D 110 GLY D 126 1 17
HELIX 50 AF5 TYR D 138 LYS D 155 1 18
HELIX 51 AF6 ASN D 161 SER D 165 5 5
HELIX 52 AF7 ALA D 179 GLY D 183 5 5
HELIX 53 AF8 GLU D 184 GLU D 193 1 10
HELIX 54 AF9 GLY D 210 LYS D 214 5 5
HELIX 55 AG1 VAL D 221 ASN D 226 1 6
HELIX 56 AG2 ASN D 226 GLY D 234 1 9
HELIX 57 AG3 GLY D 234 TYR D 240 1 7
HELIX 58 AG4 THR D 271 LYS D 278 1 8
HELIX 59 AG5 THR D 283 LYS D 287 5 5
HELIX 60 AG6 GLU D 303 LEU D 305 5 3
HELIX 61 AG7 ASP D 330 THR D 346 1 17
HELIX 62 AG8 CYS D 350 LYS D 369 1 20
HELIX 63 AG9 THR D 373 ASN D 386 1 14
HELIX 64 AH1 CYS D 393 ALA D 399 1 7
HELIX 65 AH2 GLY D 400 PHE D 410 1 11
HELIX 66 AH3 PHE D 410 LYS D 416 1 7
SHEET 1 AA1 4 PHE A 120 VAL A 125 0
SHEET 2 AA1 4 TYR A 81 CYS A 86 1 N ILE A 83 O VAL A 123
SHEET 3 AA1 4 VAL A 136 VAL A 139 -1 O MET A 138 N ARG A 84
SHEET 4 AA1 4 ASP A 142 LYS A 145 -1 O TYR A 144 N PHE A 137
SHEET 1 AA2 6 ALA B 12 THR B 14 0
SHEET 2 AA2 6 GLY B 262 PRO B 267 1 O VAL B 263 N GLU B 13
SHEET 3 AA2 6 PRO B 249 GLY B 256 -1 N VAL B 254 O GLY B 262
SHEET 4 AA2 6 VAL B 322 THR B 326 1 O VAL B 322 N SER B 255
SHEET 5 AA2 6 VAL B 289 SER B 294 -1 N ALA B 291 O LEU B 325
SHEET 6 AA2 6 ASP B 298 SER B 301 -1 O PHE B 300 N VAL B 292
SHEET 1 AA3 4 GLU B 170 ARG B 175 0
SHEET 2 AA3 4 GLU B 129 ILE B 134 1 N ALA B 130 O GLU B 170
SHEET 3 AA3 4 TYR B 88 ALA B 93 1 N CYS B 91 O TYR B 131
SHEET 4 AA3 4 THR B 216 ASN B 220 1 O VAL B 217 N ILE B 90
SHEET 1 AA4 4 PHE C 120 VAL C 125 0
SHEET 2 AA4 4 TYR C 81 CYS C 86 1 N ILE C 83 O VAL C 123
SHEET 3 AA4 4 VAL C 136 VAL C 139 -1 O MET C 138 N ARG C 84
SHEET 4 AA4 4 ASP C 142 LYS C 145 -1 O TYR C 144 N PHE C 137
SHEET 1 AA5 6 ALA D 12 THR D 14 0
SHEET 2 AA5 6 GLY D 262 PRO D 267 1 O GLU D 265 N GLU D 13
SHEET 3 AA5 6 PRO D 249 GLY D 256 -1 N VAL D 254 O GLY D 262
SHEET 4 AA5 6 VAL D 322 THR D 326 1 O VAL D 324 N SER D 255
SHEET 5 AA5 6 VAL D 289 SER D 294 -1 N ALA D 291 O LEU D 325
SHEET 6 AA5 6 ASP D 298 SER D 301 -1 O PHE D 300 N VAL D 292
SHEET 1 AA6 4 GLU D 170 ARG D 175 0
SHEET 2 AA6 4 GLU D 129 ILE D 134 1 N ALA D 130 O GLU D 170
SHEET 3 AA6 4 TYR D 88 ALA D 93 1 N CYS D 91 O TYR D 131
SHEET 4 AA6 4 THR D 216 ASN D 220 1 O VAL D 217 N ILE D 90
LINK SG CYS A 86 FE1 FES A 200 1555 1555 2.27
LINK SG CYS A 91 FE1 FES A 200 1555 1555 2.31
LINK SG CYS A 127 FE2 FES A 200 1555 1555 2.42
LINK SG CYS A 131 FE2 FES A 200 1555 1555 2.29
LINK SG CYS B 347 FE1 SF4 B 501 1555 1555 2.22
LINK SG CYS B 350 FE4 SF4 B 501 1555 1555 2.21
LINK SG CYS B 353 FE2 SF4 B 501 1555 1555 2.33
LINK SG CYS B 393 FE3 SF4 B 501 1555 1555 2.26
LINK SG CYS C 86 FE1 FES C 200 1555 1555 2.27
LINK SG CYS C 91 FE1 FES C 200 1555 1555 2.43
LINK SG CYS C 127 FE2 FES C 200 1555 1555 2.65
LINK SG CYS C 131 FE2 FES C 200 1555 1555 2.17
LINK SG CYS D 347 FE1 SF4 D 500 1555 1555 2.24
LINK SG CYS D 350 FE4 SF4 D 500 1555 1555 2.21
LINK SG CYS D 353 FE2 SF4 D 500 1555 1555 2.30
LINK SG CYS D 393 FE3 SF4 D 500 1555 1555 2.23
CISPEP 1 ALA A 134 PRO A 135 0 -0.17
CISPEP 2 GLY B 85 PRO B 86 0 -0.27
CISPEP 3 LYS B 202 PRO B 203 0 -1.23
CISPEP 4 PRO B 203 PRO B 204 0 3.71
CISPEP 5 GLY B 242 PRO B 243 0 -4.54
CISPEP 6 ALA C 134 PRO C 135 0 0.08
CISPEP 7 GLY D 85 PRO D 86 0 0.04
CISPEP 8 LYS D 202 PRO D 203 0 -1.43
CISPEP 9 PRO D 203 PRO D 204 0 3.88
SITE 1 AC1 8 CYS A 86 SER A 88 VAL A 90 CYS A 91
SITE 2 AC1 8 CYS A 127 LEU A 128 ALA A 130 CYS A 131
SITE 1 AC2 12 ILE B 181 PRO B 199 THR B 346 CYS B 347
SITE 2 AC2 12 GLY B 348 GLN B 349 CYS B 350 CYS B 353
SITE 3 AC2 12 SER B 391 CYS B 393 LEU B 395 GLY B 396
SITE 1 AC3 20 GLY B 65 ARG B 66 GLY B 67 LYS B 76
SITE 2 AC3 20 ASN B 92 ASP B 94 GLU B 95 TYR B 180
SITE 3 AC3 20 GLY B 183 GLU B 184 GLU B 185 VAL B 218
SITE 4 AC3 20 ASN B 219 ASN B 220 THR B 223 GLY B 394
SITE 5 AC3 20 HOH B 616 HOH B 620 HOH B 630 HOH B 638
SITE 1 AC4 2 THR B 14 LYS D 154
SITE 1 AC5 9 CYS C 86 SER C 88 VAL C 90 CYS C 91
SITE 2 AC5 9 CYS C 127 LEU C 128 GLY C 129 ALA C 130
SITE 3 AC5 9 CYS C 131
SITE 1 AC6 13 ILE D 181 PRO D 199 THR D 346 CYS D 347
SITE 2 AC6 13 GLY D 348 GLN D 349 CYS D 350 CYS D 353
SITE 3 AC6 13 SER D 391 ILE D 392 CYS D 393 LEU D 395
SITE 4 AC6 13 GLY D 396
SITE 1 AC7 21 GLY D 65 ARG D 66 GLY D 67 LYS D 76
SITE 2 AC7 21 ASN D 92 ASP D 94 GLU D 95 TYR D 180
SITE 3 AC7 21 GLY D 183 GLU D 184 GLU D 185 VAL D 218
SITE 4 AC7 21 ASN D 219 ASN D 220 THR D 223 GLY D 394
SITE 5 AC7 21 HOH D 603 HOH D 607 HOH D 618 HOH D 622
SITE 6 AC7 21 HOH D 630
CRYST1 59.741 108.117 188.181 90.00 90.00 90.00 P 21 21 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 0.016739 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009249 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005314 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
