HEADER OXIDOREDUCTASE 16-MAR-15 4YRY
TITLE INSIGHTS INTO FLAVIN-BASED ELECTRON BIFURCATION VIA THE NADH-DEPENDENT
TITLE 2 REDUCED FERREDOXIN-NADP OXIDOREDUCTASE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER
COMPND 3 SUBUNIT HOMOLOG;
COMPND 4 CHAIN: A, C;
COMPND 5 SYNONYM: DIHYDROOROTATE OXIDASE B,ELECTRON TRANSFER SUBUNIT HOMOLOG;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DIHYDROPYRIMIDINE DEHYDROGENASE SUBUNIT A;
COMPND 9 CHAIN: B, D;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 GENE: TM_1639;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-51B(+);
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 11 ORGANISM_TAXID: 2336;
SOURCE 12 GENE: THEMA_06045;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 16 EXPRESSION_SYSTEM_VARIANT: C41
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR U.ERMLER,R.K.THAUER,J.K.DEMMER,H.HUANG,S.WANG,U.DEMMER
REVDAT 5 10-JAN-24 4YRY 1 REMARK
REVDAT 4 21-NOV-18 4YRY 1 REMARK
REVDAT 3 16-SEP-15 4YRY 1 JRNL
REVDAT 2 15-JUL-15 4YRY 1 JRNL
REVDAT 1 08-JUL-15 4YRY 0
JRNL AUTH J.K.DEMMER,H.HUANG,S.WANG,U.DEMMER,R.K.THAUER,U.ERMLER
JRNL TITL INSIGHTS INTO FLAVIN-BASED ELECTRON BIFURCATION VIA THE
JRNL TITL 2 NADH-DEPENDENT REDUCED FERREDOXIN:NADP OXIDOREDUCTASE
JRNL TITL 3 STRUCTURE.
JRNL REF J.BIOL.CHEM. V. 290 21985 2015
JRNL REFN ESSN 1083-351X
JRNL PMID 26139605
JRNL DOI 10.1074/JBC.M115.656520
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.96
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 76728
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 3787
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 19.3200 - 6.4409 0.94 3673 175 0.1621 0.1792
REMARK 3 2 6.4409 - 5.1441 0.94 3653 199 0.1796 0.2185
REMARK 3 3 5.1441 - 4.5033 0.94 3640 179 0.1535 0.1868
REMARK 3 4 4.5033 - 4.0958 0.94 3641 192 0.1502 0.2340
REMARK 3 5 4.0958 - 3.8046 0.94 3655 190 0.1709 0.2154
REMARK 3 6 3.8046 - 3.5818 0.95 3638 180 0.1930 0.2547
REMARK 3 7 3.5818 - 3.4034 0.94 3657 177 0.1957 0.2355
REMARK 3 8 3.4034 - 3.2560 0.95 3627 184 0.2040 0.2644
REMARK 3 9 3.2560 - 3.1312 0.94 3624 224 0.2189 0.2770
REMARK 3 10 3.1312 - 3.0236 0.95 3666 186 0.2265 0.3072
REMARK 3 11 3.0236 - 2.9294 0.95 3696 182 0.2291 0.2989
REMARK 3 12 2.9294 - 2.8459 0.94 3639 217 0.2387 0.2707
REMARK 3 13 2.8459 - 2.7712 0.95 3671 182 0.2542 0.3105
REMARK 3 14 2.7712 - 2.7038 0.95 3649 185 0.2564 0.2690
REMARK 3 15 2.7038 - 2.6425 0.95 3649 195 0.2702 0.3025
REMARK 3 16 2.6425 - 2.5864 0.95 3701 186 0.2832 0.2969
REMARK 3 17 2.5864 - 2.5347 0.95 3632 164 0.2799 0.3405
REMARK 3 18 2.5347 - 2.4870 0.95 3667 176 0.2808 0.3724
REMARK 3 19 2.4870 - 2.4427 0.92 3573 206 0.2919 0.3504
REMARK 3 20 2.4427 - 2.4014 0.92 3523 168 0.3083 0.4125
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) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.440
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) : 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 : 0.005 12068
REMARK 3 ANGLE : 0.909 16347
REMARK 3 CHIRALITY : 0.034 1793
REMARK 3 PLANARITY : 0.003 2057
REMARK 3 DIHEDRAL : 15.313 4474
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN 'A' AND (RESID 1 THROUGH 276 )) OR (CHAIN 'C'
REMARK 3 AND (RESID 1 THROUGH 276 ))
REMARK 3 ORIGIN FOR THE GROUP (A): -19.6626 39.8765 39.9793
REMARK 3 T TENSOR
REMARK 3 T11: 0.5929 T22: 0.4646
REMARK 3 T33: 0.3335 T12: 0.0006
REMARK 3 T13: -0.2956 T23: -0.0738
REMARK 3 L TENSOR
REMARK 3 L11: 0.4781 L22: 1.3906
REMARK 3 L33: 0.6515 L12: 0.4604
REMARK 3 L13: 0.1381 L23: 0.9560
REMARK 3 S TENSOR
REMARK 3 S11: 0.0002 S12: 0.0387 S13: 0.1792
REMARK 3 S21: -0.0146 S22: -0.0342 S23: 0.1190
REMARK 3 S31: -0.0618 S32: 0.0358 S33: 0.0977
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN 'B' AND (RESID 1 THROUGH 468 )) OR (CHAIN 'D'
REMARK 3 AND (RESID 1 THROUGH 468 ))
REMARK 3 ORIGIN FOR THE GROUP (A): -20.1995 39.4168 39.7848
REMARK 3 T TENSOR
REMARK 3 T11: 0.3828 T22: 0.3585
REMARK 3 T33: 0.2653 T12: 0.0653
REMARK 3 T13: -0.1076 T23: 0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 0.3015 L22: 0.4699
REMARK 3 L33: 1.1321 L12: 0.4545
REMARK 3 L13: 0.4837 L23: 0.7464
REMARK 3 S TENSOR
REMARK 3 S11: -0.0372 S12: -0.0067 S13: 0.0160
REMARK 3 S21: -0.0074 S22: -0.0785 S23: 0.0346
REMARK 3 S31: -0.0364 S32: -0.0103 S33: 0.0767
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 4YRY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207697.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76947
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.89600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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: 4YLF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.225M NH4H2PO4, 5 % (V,V) ETHANOL, 20
REMARK 280 % GLYCEROL. SOAKED FOR 40 MIN IN 5 MM NADH, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
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 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 153.71500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 230.57250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 76.85750
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: 8580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -95.0 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: 8450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 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 ALA C 174
REMARK 465 MET C 175
REMARK 465 ASP C 176
REMARK 465 LYS C 177
REMARK 465 LEU C 178
REMARK 465 PHE C 179
REMARK 465 LEU C 201
REMARK 465 LYS C 202
REMARK 465 ALA C 203
REMARK 465 ARG C 204
REMARK 465 GLU C 205
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 ASN B 19 NH1 ARG B 300 2.17
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 OD2 ASP B 365 OG SER D 367 3554 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO B 134 C - N - CA ANGL. DEV. = 16.2 DEGREES
REMARK 500 PRO B 134 C - N - CD ANGL. DEV. = -14.9 DEGREES
REMARK 500 PRO B 372 C - N - CA ANGL. DEV. = 10.0 DEGREES
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 ASN A 102 75.10 -100.96
REMARK 500 THR A 140 -155.03 -146.71
REMARK 500 LYS A 141 -98.17 -90.97
REMARK 500 ASP A 155 -176.59 -170.88
REMARK 500 THR A 160 79.80 -116.93
REMARK 500 ASP A 162 34.24 -94.04
REMARK 500 SER A 164 -127.72 -135.65
REMARK 500 PHE A 179 -83.98 48.97
REMARK 500 GLU A 181 -77.07 -87.24
REMARK 500 ARG A 182 -171.65 59.83
REMARK 500 LEU A 201 4.96 -68.62
REMARK 500 ALA A 203 -36.28 -19.91
REMARK 500 GLU A 205 -143.12 49.83
REMARK 500 VAL A 219 -70.63 -117.69
REMARK 500 CYS A 225 -47.57 -131.09
REMARK 500 SER A 233 -108.87 54.38
REMARK 500 LYS B 2 -91.34 -89.40
REMARK 500 HIS B 45 74.03 31.92
REMARK 500 GLN B 95 -101.62 -122.33
REMARK 500 ASN B 127 -60.88 -130.17
REMARK 500 GLU B 130 -105.29 -107.64
REMARK 500 VAL B 132 -73.63 -100.01
REMARK 500 LYS B 133 -168.76 62.75
REMARK 500 LYS B 215 -67.01 -120.97
REMARK 500 PRO B 270 32.91 -95.49
REMARK 500 ASN B 350 144.14 173.69
REMARK 500 LYS B 362 -75.50 -136.10
REMARK 500 ALA B 364 -95.86 -66.19
REMARK 500 SER B 367 108.29 -167.52
REMARK 500 PRO B 370 59.68 -96.67
REMARK 500 ALA B 390 75.71 -119.45
REMARK 500 ASN B 409 -151.83 -92.50
REMARK 500 ALA B 439 -143.04 -158.64
REMARK 500 LEU C 6 -119.42 38.74
REMARK 500 GLU C 17 -72.84 -60.17
REMARK 500 ASP C 56 162.39 179.99
REMARK 500 ASN C 102 73.13 -101.40
REMARK 500 THR C 117 -31.61 -160.61
REMARK 500 LYS C 141 -99.20 53.38
REMARK 500 SER C 164 -70.54 -138.04
REMARK 500 MET C 167 179.75 55.68
REMARK 500 LYS C 168 -83.73 -121.85
REMARK 500 GLU C 181 30.12 -86.29
REMARK 500 PHE C 184 91.71 44.84
REMARK 500 CYS C 199 -113.67 35.72
REMARK 500 VAL C 219 -70.36 -119.41
REMARK 500 SER C 233 -109.64 54.46
REMARK 500 LYS D 2 -102.59 50.99
REMARK 500 HIS D 45 74.06 32.92
REMARK 500 GLN D 95 -100.29 -123.67
REMARK 500
REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS.
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 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 220 OD1
REMARK 620 2 FES A 501 S1 93.4
REMARK 620 3 FES A 501 S2 108.7 95.5
REMARK 620 4 CYS A 225 SG 96.6 139.7 117.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 228 SG
REMARK 620 2 FES A 501 S1 112.1
REMARK 620 3 FES A 501 S2 119.9 98.8
REMARK 620 4 CYS A 240 SG 94.8 120.8 111.9
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 39 SG
REMARK 620 2 SF4 B 501 S1 116.3
REMARK 620 3 SF4 B 501 S2 134.4 86.2
REMARK 620 4 SF4 B 501 S3 128.9 91.3 86.2
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 42 SG
REMARK 620 2 SF4 B 501 S1 123.1
REMARK 620 3 SF4 B 501 S2 125.3 86.7
REMARK 620 4 SF4 B 501 S4 136.9 85.5 83.5
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 47 SG
REMARK 620 2 SF4 B 501 S1 118.6
REMARK 620 3 SF4 B 501 S3 134.0 91.4
REMARK 620 4 SF4 B 501 S4 121.6 85.8 92.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 502 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 51 SG
REMARK 620 2 SF4 B 502 S1 130.6
REMARK 620 3 SF4 B 502 S2 119.4 85.6
REMARK 620 4 SF4 B 502 S3 129.2 90.8 87.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 502 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 90 SG
REMARK 620 2 SF4 B 502 S1 131.4
REMARK 620 3 SF4 B 502 S3 126.1 90.6
REMARK 620 4 SF4 B 502 S4 119.2 85.3 91.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 502 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 96 SG
REMARK 620 2 SF4 B 502 S1 121.0
REMARK 620 3 SF4 B 502 S2 129.7 86.0
REMARK 620 4 SF4 B 502 S4 135.1 85.3 83.7
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 100 SG
REMARK 620 2 SF4 B 501 S2 127.0
REMARK 620 3 SF4 B 501 S3 132.8 86.1
REMARK 620 4 SF4 B 501 S4 120.1 84.0 92.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 502 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 117 OE1
REMARK 620 2 SF4 B 502 S2 140.7
REMARK 620 3 SF4 B 502 S3 127.6 86.5
REMARK 620 4 SF4 B 502 S4 110.1 84.0 91.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 220 OD1
REMARK 620 2 FES C 501 S1 95.5
REMARK 620 3 FES C 501 S2 171.4 92.4
REMARK 620 4 ASP C 220 OD2 64.1 121.6 108.6
REMARK 620 5 CYS C 225 SG 77.0 107.2 104.0 118.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 228 SG
REMARK 620 2 FES C 501 S1 113.0
REMARK 620 3 FES C 501 S2 120.3 98.0
REMARK 620 4 CYS C 240 SG 99.1 121.2 106.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 501 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 39 SG
REMARK 620 2 SF4 D 501 S1 129.4
REMARK 620 3 SF4 D 501 S2 128.5 85.5
REMARK 620 4 SF4 D 501 S3 122.4 91.5 86.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 42 SG
REMARK 620 2 SF4 D 501 S2 125.9
REMARK 620 3 SF4 D 501 S3 114.9 86.1
REMARK 620 4 SF4 D 501 S4 139.1 83.8 92.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 47 SG
REMARK 620 2 SF4 D 501 S1 110.6
REMARK 620 3 SF4 D 501 S3 137.1 91.6
REMARK 620 4 SF4 D 501 S4 124.6 86.1 92.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 502 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 51 SG
REMARK 620 2 SF4 D 502 S1 125.6
REMARK 620 3 SF4 D 502 S2 126.1 85.7
REMARK 620 4 SF4 D 502 S3 128.9 91.0 86.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 502 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 90 SG
REMARK 620 2 SF4 D 502 S2 127.2
REMARK 620 3 SF4 D 502 S3 124.4 85.8
REMARK 620 4 SF4 D 502 S4 130.0 83.5 92.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 502 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 96 SG
REMARK 620 2 SF4 D 502 S1 131.9
REMARK 620 3 SF4 D 502 S2 119.5 86.1
REMARK 620 4 SF4 D 502 S4 134.2 85.1 83.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 501 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 100 SG
REMARK 620 2 SF4 D 501 S1 129.2
REMARK 620 3 SF4 D 501 S2 136.4 85.9
REMARK 620 4 SF4 D 501 S4 119.2 85.8 83.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D 502 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 117 OE1
REMARK 620 2 SF4 D 502 S1 136.7
REMARK 620 3 SF4 D 502 S3 105.8 90.8
REMARK 620 4 SF4 D 502 S4 132.6 85.1 91.7
REMARK 620 5 GLU D 117 OE2 61.6 111.1 157.6 85.7
REMARK 620 N 1 2 3 4
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 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 NAD A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FES C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD D 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NAD D 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 D 505
DBREF 4YRY A 1 276 UNP Q9X1X4 PYRKH_THEMA 1 276
DBREF 4YRY B 1 468 UNP V9X7T9 V9X7T9_THEMA 3 470
DBREF 4YRY C 1 276 UNP Q9X1X4 PYRKH_THEMA 1 276
DBREF 4YRY D 1 468 UNP V9X7T9 V9X7T9_THEMA 3 470
SEQRES 1 A 276 MET GLY GLY THR ALA LEU ASN GLU ILE VAL LYS LYS VAL
SEQRES 2 A 276 LYS ILE ALA GLU ASP VAL PHE ASP PHE TRP ILE HIS SER
SEQRES 3 A 276 PRO SER VAL SER LYS GLU ALA ARG PRO GLY GLN PHE VAL
SEQRES 4 A 276 VAL ILE ARG LEU HIS GLU LYS GLY GLU ARG ILE PRO LEU
SEQRES 5 A 276 THR VAL ALA ASP THR LYS PRO GLU GLU GLY LEU PHE ARG
SEQRES 6 A 276 MET VAL VAL LYS VAL VAL GLY LYS THR THR HIS GLU LEU
SEQRES 7 A 276 SER LEU LYS LYS GLU GLY ASP THR ILE LEU ASP VAL VAL
SEQRES 8 A 276 GLY PRO LEU GLY ASN PRO SER GLU ILE GLU ASN TYR GLY
SEQRES 9 A 276 ASN VAL LEU LEU VAL GLY GLY GLY VAL GLY ILE ALA THR
SEQRES 10 A 276 LEU TYR PRO ILE ALA LYS ALA LEU LYS GLU ALA GLY ASN
SEQRES 11 A 276 ASN ILE THR THR VAL LEU GLY ALA ARG THR LYS ASP TYR
SEQRES 12 A 276 LEU ILE MET VAL ASP GLU PHE LYS GLU ILE SER ASP VAL
SEQRES 13 A 276 LEU LEU VAL THR ASP ASP GLY SER ALA GLY MET LYS GLY
SEQRES 14 A 276 VAL VAL THR ASP ALA MET ASP LYS LEU PHE ARG GLU ARG
SEQRES 15 A 276 LYS PHE ASP ILE CYS TRP ALA VAL GLY PRO THR ILE MET
SEQRES 16 A 276 MET LYS PHE CYS THR LEU LYS ALA ARG GLU PHE GLY VAL
SEQRES 17 A 276 PRO ILE TRP VAL SER LEU ASN PRO ILE MET VAL ASP GLY
SEQRES 18 A 276 THR GLY MET CYS GLY ALA CYS ARG VAL THR VAL SER GLY
SEQRES 19 A 276 GLN ILE LYS PHE ALA CYS VAL ASP GLY PRO GLU PHE ARG
SEQRES 20 A 276 GLY GLU GLU VAL ASP TRP ASP GLU LEU LEU LYS ARG LEU
SEQRES 21 A 276 ALA GLN TYR ARG GLU GLN GLU LYS ILE SER TYR GLU ARG
SEQRES 22 A 276 PHE LEU LYS
SEQRES 1 B 468 MET LYS ASN ARG LYS THR PRO MET LYS GLU GLN SER PRO
SEQRES 2 B 468 GLU SER ARG ARG ARG ASN PHE GLU GLU VAL ALA LEU GLY
SEQRES 3 B 468 TYR THR LEU GLU GLU ALA LEU GLU GLU ALA GLN ARG CYS
SEQRES 4 B 468 LEU GLN CYS PRO THR HIS PRO CYS VAL SER GLY CYS PRO
SEQRES 5 B 468 VAL GLU ILE ASP ILE PRO GLY PHE ILE ARG LYS LEU ARG
SEQRES 6 B 468 ASP GLY LYS LEU GLU GLU SER TYR ARG ILE LEU LYS SER
SEQRES 7 B 468 TYR ASN ASN LEU PRO ALA VAL CYS GLY ARG VAL CYS PRO
SEQRES 8 B 468 GLN GLU VAL GLN CYS GLU SER ARG CYS VAL VAL GLY LYS
SEQRES 9 B 468 MET LYS ASP SER GLU PRO VAL ALA ILE GLY ARG LEU GLU
SEQRES 10 B 468 ARG PHE VAL ALA ASP TRP ALA ALA GLU ASN LEU GLU GLU
SEQRES 11 B 468 ASP VAL LYS PRO LEU ALA GLY SER LYS LYS GLU LYS VAL
SEQRES 12 B 468 ALA VAL VAL GLY SER GLY PRO ALA GLY LEU THR ALA ALA
SEQRES 13 B 468 ALA ASP LEU ALA LYS MET GLY TYR HIS VAL ASP ILE PHE
SEQRES 14 B 468 GLU ALA PHE HIS LYS PRO GLY GLY VAL LEU VAL TYR GLY
SEQRES 15 B 468 ILE PRO GLU PHE ARG LEU PRO LYS ARG ILE VAL GLU ARG
SEQRES 16 B 468 GLU VAL SER TYR ILE ARG LYS LEU GLY VAL ASN PHE HIS
SEQRES 17 B 468 LEU ASN THR VAL VAL GLY LYS THR VAL LYS VAL LYS GLU
SEQRES 18 B 468 LEU LEU SER GLU TYR ASP ALA VAL PHE ILE GLY THR GLY
SEQRES 19 B 468 ALA GLY THR PRO LYS PHE MET GLY ILE PRO GLY THR ASN
SEQRES 20 B 468 LEU ASN GLY VAL TYR SER ALA ASN GLU PHE LEU THR ARG
SEQRES 21 B 468 VAL ASN LEU MET LYS ALA TYR LEU PHE PRO GLU TYR ASP
SEQRES 22 B 468 THR PRO ILE ARG VAL GLY LYS LYS VAL ALA VAL ILE GLY
SEQRES 23 B 468 ALA GLY ASN THR ALA MET ASP ALA ALA ARG SER ALA LEU
SEQRES 24 B 468 ARG LEU GLY ALA GLU LYS VAL TYR ILE VAL TYR ARG ARG
SEQRES 25 B 468 THR GLU ARG GLU MET PRO ALA ARG ARG GLU GLU TYR HIS
SEQRES 26 B 468 HIS ALA LEU GLU GLU GLY ILE GLU PHE LEU TRP LEU THR
SEQRES 27 B 468 LEU PRO ILE ARG TYR ILE GLY ASP ALA ASN GLY ASN VAL
SEQRES 28 B 468 GLU ALA MET GLU CYS VAL ARG MET GLU LEU LYS GLU ALA
SEQRES 29 B 468 ASP GLY SER GLY ARG PRO ARG PRO VAL PRO ILE GLU GLY
SEQRES 30 B 468 SER ASN PHE VAL LEU GLU VAL ASP MET VAL ILE GLU ALA
SEQRES 31 B 468 ILE GLY GLN GLY PRO ASN ARG VAL LEU LEU SER GLU PHE
SEQRES 32 B 468 PRO GLY LEU GLU LEU ASN GLU ARG GLY TYR ILE LYS ALA
SEQRES 33 B 468 ASP GLU ASP THR GLY ALA THR SER VAL LYS GLY VAL PHE
SEQRES 34 B 468 ALA GLY GLY ASP ILE VAL THR GLY ALA ALA THR VAL ILE
SEQRES 35 B 468 LYS ALA MET GLY ALA GLY LYS LYS ALA ALA GLN PHE ILE
SEQRES 36 B 468 HIS SER TYR LEU THR GLY GLU TRP ASN PRO TRP GLN LYS
SEQRES 1 C 276 MET GLY GLY THR ALA LEU ASN GLU ILE VAL LYS LYS VAL
SEQRES 2 C 276 LYS ILE ALA GLU ASP VAL PHE ASP PHE TRP ILE HIS SER
SEQRES 3 C 276 PRO SER VAL SER LYS GLU ALA ARG PRO GLY GLN PHE VAL
SEQRES 4 C 276 VAL ILE ARG LEU HIS GLU LYS GLY GLU ARG ILE PRO LEU
SEQRES 5 C 276 THR VAL ALA ASP THR LYS PRO GLU GLU GLY LEU PHE ARG
SEQRES 6 C 276 MET VAL VAL LYS VAL VAL GLY LYS THR THR HIS GLU LEU
SEQRES 7 C 276 SER LEU LYS LYS GLU GLY ASP THR ILE LEU ASP VAL VAL
SEQRES 8 C 276 GLY PRO LEU GLY ASN PRO SER GLU ILE GLU ASN TYR GLY
SEQRES 9 C 276 ASN VAL LEU LEU VAL GLY GLY GLY VAL GLY ILE ALA THR
SEQRES 10 C 276 LEU TYR PRO ILE ALA LYS ALA LEU LYS GLU ALA GLY ASN
SEQRES 11 C 276 ASN ILE THR THR VAL LEU GLY ALA ARG THR LYS ASP TYR
SEQRES 12 C 276 LEU ILE MET VAL ASP GLU PHE LYS GLU ILE SER ASP VAL
SEQRES 13 C 276 LEU LEU VAL THR ASP ASP GLY SER ALA GLY MET LYS GLY
SEQRES 14 C 276 VAL VAL THR ASP ALA MET ASP LYS LEU PHE ARG GLU ARG
SEQRES 15 C 276 LYS PHE ASP ILE CYS TRP ALA VAL GLY PRO THR ILE MET
SEQRES 16 C 276 MET LYS PHE CYS THR LEU LYS ALA ARG GLU PHE GLY VAL
SEQRES 17 C 276 PRO ILE TRP VAL SER LEU ASN PRO ILE MET VAL ASP GLY
SEQRES 18 C 276 THR GLY MET CYS GLY ALA CYS ARG VAL THR VAL SER GLY
SEQRES 19 C 276 GLN ILE LYS PHE ALA CYS VAL ASP GLY PRO GLU PHE ARG
SEQRES 20 C 276 GLY GLU GLU VAL ASP TRP ASP GLU LEU LEU LYS ARG LEU
SEQRES 21 C 276 ALA GLN TYR ARG GLU GLN GLU LYS ILE SER TYR GLU ARG
SEQRES 22 C 276 PHE LEU LYS
SEQRES 1 D 468 MET LYS ASN ARG LYS THR PRO MET LYS GLU GLN SER PRO
SEQRES 2 D 468 GLU SER ARG ARG ARG ASN PHE GLU GLU VAL ALA LEU GLY
SEQRES 3 D 468 TYR THR LEU GLU GLU ALA LEU GLU GLU ALA GLN ARG CYS
SEQRES 4 D 468 LEU GLN CYS PRO THR HIS PRO CYS VAL SER GLY CYS PRO
SEQRES 5 D 468 VAL GLU ILE ASP ILE PRO GLY PHE ILE ARG LYS LEU ARG
SEQRES 6 D 468 ASP GLY LYS LEU GLU GLU SER TYR ARG ILE LEU LYS SER
SEQRES 7 D 468 TYR ASN ASN LEU PRO ALA VAL CYS GLY ARG VAL CYS PRO
SEQRES 8 D 468 GLN GLU VAL GLN CYS GLU SER ARG CYS VAL VAL GLY LYS
SEQRES 9 D 468 MET LYS ASP SER GLU PRO VAL ALA ILE GLY ARG LEU GLU
SEQRES 10 D 468 ARG PHE VAL ALA ASP TRP ALA ALA GLU ASN LEU GLU GLU
SEQRES 11 D 468 ASP VAL LYS PRO LEU ALA GLY SER LYS LYS GLU LYS VAL
SEQRES 12 D 468 ALA VAL VAL GLY SER GLY PRO ALA GLY LEU THR ALA ALA
SEQRES 13 D 468 ALA ASP LEU ALA LYS MET GLY TYR HIS VAL ASP ILE PHE
SEQRES 14 D 468 GLU ALA PHE HIS LYS PRO GLY GLY VAL LEU VAL TYR GLY
SEQRES 15 D 468 ILE PRO GLU PHE ARG LEU PRO LYS ARG ILE VAL GLU ARG
SEQRES 16 D 468 GLU VAL SER TYR ILE ARG LYS LEU GLY VAL ASN PHE HIS
SEQRES 17 D 468 LEU ASN THR VAL VAL GLY LYS THR VAL LYS VAL LYS GLU
SEQRES 18 D 468 LEU LEU SER GLU TYR ASP ALA VAL PHE ILE GLY THR GLY
SEQRES 19 D 468 ALA GLY THR PRO LYS PHE MET GLY ILE PRO GLY THR ASN
SEQRES 20 D 468 LEU ASN GLY VAL TYR SER ALA ASN GLU PHE LEU THR ARG
SEQRES 21 D 468 VAL ASN LEU MET LYS ALA TYR LEU PHE PRO GLU TYR ASP
SEQRES 22 D 468 THR PRO ILE ARG VAL GLY LYS LYS VAL ALA VAL ILE GLY
SEQRES 23 D 468 ALA GLY ASN THR ALA MET ASP ALA ALA ARG SER ALA LEU
SEQRES 24 D 468 ARG LEU GLY ALA GLU LYS VAL TYR ILE VAL TYR ARG ARG
SEQRES 25 D 468 THR GLU ARG GLU MET PRO ALA ARG ARG GLU GLU TYR HIS
SEQRES 26 D 468 HIS ALA LEU GLU GLU GLY ILE GLU PHE LEU TRP LEU THR
SEQRES 27 D 468 LEU PRO ILE ARG TYR ILE GLY ASP ALA ASN GLY ASN VAL
SEQRES 28 D 468 GLU ALA MET GLU CYS VAL ARG MET GLU LEU LYS GLU ALA
SEQRES 29 D 468 ASP GLY SER GLY ARG PRO ARG PRO VAL PRO ILE GLU GLY
SEQRES 30 D 468 SER ASN PHE VAL LEU GLU VAL ASP MET VAL ILE GLU ALA
SEQRES 31 D 468 ILE GLY GLN GLY PRO ASN ARG VAL LEU LEU SER GLU PHE
SEQRES 32 D 468 PRO GLY LEU GLU LEU ASN GLU ARG GLY TYR ILE LYS ALA
SEQRES 33 D 468 ASP GLU ASP THR GLY ALA THR SER VAL LYS GLY VAL PHE
SEQRES 34 D 468 ALA GLY GLY ASP ILE VAL THR GLY ALA ALA THR VAL ILE
SEQRES 35 D 468 LYS ALA MET GLY ALA GLY LYS LYS ALA ALA GLN PHE ILE
SEQRES 36 D 468 HIS SER TYR LEU THR GLY GLU TRP ASN PRO TRP GLN LYS
HET FES A 501 4
HET FAD A 502 53
HET NAD A 503 44
HET SF4 B 501 8
HET SF4 B 502 8
HET FAD B 503 53
HET FES C 501 4
HET FAD C 502 53
HET SF4 D 501 8
HET SF4 D 502 8
HET FAD D 503 53
HET NAD D 504 44
HET PO4 D 505 5
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM PO4 PHOSPHATE ION
FORMUL 5 FES 2(FE2 S2)
FORMUL 6 FAD 4(C27 H33 N9 O15 P2)
FORMUL 7 NAD 2(C21 H27 N7 O14 P2)
FORMUL 8 SF4 4(FE4 S4)
FORMUL 17 PO4 O4 P 3-
FORMUL 18 HOH *132(H2 O)
HELIX 1 AA1 SER A 26 GLU A 32 1 7
HELIX 2 AA2 GLY A 72 LYS A 81 1 10
HELIX 3 AA3 VAL A 113 ALA A 128 1 16
HELIX 4 AA4 VAL A 147 ASP A 155 1 9
HELIX 5 AA5 VAL A 171 LYS A 177 1 7
HELIX 6 AA6 PRO A 192 LEU A 201 1 10
HELIX 7 AA7 LYS A 202 GLU A 205 5 4
HELIX 8 AA8 ASP A 252 ALA A 261 1 10
HELIX 9 AA9 GLN A 266 LEU A 275 1 10
HELIX 10 AB1 SER B 12 ARG B 17 1 6
HELIX 11 AB2 THR B 28 GLN B 37 1 10
HELIX 12 AB3 HIS B 45 GLY B 50 1 6
HELIX 13 AB4 ASP B 56 ASP B 66 1 11
HELIX 14 AB5 LYS B 68 ASN B 80 1 13
HELIX 15 AB6 LEU B 82 CYS B 90 1 9
HELIX 16 AB7 PRO B 91 GLN B 95 5 5
HELIX 17 AB8 CYS B 100 LYS B 104 5 5
HELIX 18 AB9 ALA B 112 ASN B 127 1 16
HELIX 19 AC1 GLY B 149 MET B 162 1 14
HELIX 20 AC2 GLY B 176 VAL B 180 5 5
HELIX 21 AC3 PRO B 189 LEU B 203 1 15
HELIX 22 AC4 LYS B 218 TYR B 226 1 9
HELIX 23 AC5 ALA B 254 ASN B 262 1 9
HELIX 24 AC6 LYS B 265 PHE B 269 5 5
HELIX 25 AC7 GLY B 288 ARG B 300 1 13
HELIX 26 AC8 ARG B 320 GLU B 330 1 11
HELIX 27 AC9 ASN B 396 GLU B 402 1 7
HELIX 28 AD1 GLY B 432 GLY B 437 1 6
HELIX 29 AD2 THR B 440 THR B 460 1 21
HELIX 30 AD3 SER C 26 ALA C 33 1 8
HELIX 31 AD4 GLY C 72 LEU C 80 1 9
HELIX 32 AD5 THR C 117 ALA C 128 1 12
HELIX 33 AD6 VAL C 147 ASP C 155 1 9
HELIX 34 AD7 PRO C 192 LYS C 197 1 6
HELIX 35 AD8 GLU C 249 VAL C 251 5 3
HELIX 36 AD9 ASP C 252 ALA C 261 1 10
HELIX 37 AE1 ARG C 264 ARG C 273 1 10
HELIX 38 AE2 PHE C 274 LYS C 276 5 3
HELIX 39 AE3 SER D 12 ARG D 17 1 6
HELIX 40 AE4 THR D 28 ARG D 38 1 11
HELIX 41 AE5 HIS D 45 GLY D 50 1 6
HELIX 42 AE6 ASP D 56 ASP D 66 1 11
HELIX 43 AE7 LYS D 68 ASN D 80 1 13
HELIX 44 AE8 LEU D 82 CYS D 90 1 9
HELIX 45 AE9 CYS D 100 LYS D 104 5 5
HELIX 46 AF1 ALA D 112 ASN D 127 1 16
HELIX 47 AF2 GLY D 149 MET D 162 1 14
HELIX 48 AF3 GLY D 177 GLY D 182 1 6
HELIX 49 AF4 PRO D 189 LEU D 203 1 15
HELIX 50 AF5 LYS D 218 TYR D 226 1 9
HELIX 51 AF6 ALA D 254 ASN D 262 1 9
HELIX 52 AF7 GLY D 288 ARG D 300 1 13
HELIX 53 AF8 ARG D 320 GLY D 331 1 12
HELIX 54 AF9 ASN D 396 GLU D 402 1 7
HELIX 55 AG1 GLY D 432 GLY D 437 1 6
HELIX 56 AG2 THR D 440 GLY D 461 1 22
SHEET 1 AA1 4 GLU A 8 LYS A 14 0
SHEET 2 AA1 4 VAL A 19 HIS A 25 -1 O HIS A 25 N GLU A 8
SHEET 3 AA1 4 LEU A 63 LYS A 69 -1 O MET A 66 N PHE A 22
SHEET 4 AA1 4 ASP A 56 LYS A 58 -1 N LYS A 58 O LEU A 63
SHEET 1 AA2 3 ILE A 50 THR A 53 0
SHEET 2 AA2 3 PHE A 38 ARG A 42 -1 N VAL A 39 O LEU A 52
SHEET 3 AA2 3 ASP A 89 LEU A 94 -1 O LEU A 94 N PHE A 38
SHEET 1 AA3 6 VAL A 156 VAL A 159 0
SHEET 2 AA3 6 ASN A 131 GLY A 137 1 N THR A 134 O LEU A 158
SHEET 3 AA3 6 ASN A 105 GLY A 111 1 N LEU A 108 O VAL A 135
SHEET 4 AA3 6 CYS A 187 VAL A 190 1 O TRP A 188 N VAL A 109
SHEET 5 AA3 6 ILE A 210 SER A 213 1 O TRP A 211 N CYS A 187
SHEET 6 AA3 6 GLU A 245 ARG A 247 -1 O PHE A 246 N VAL A 212
SHEET 1 AA4 2 ARG A 229 VAL A 232 0
SHEET 2 AA4 2 GLN A 235 PHE A 238 -1 O LYS A 237 N VAL A 230
SHEET 1 AA5 5 ASN B 206 HIS B 208 0
SHEET 2 AA5 5 HIS B 165 PHE B 169 1 N ILE B 168 O HIS B 208
SHEET 3 AA5 5 LYS B 142 VAL B 146 1 N VAL B 143 O HIS B 165
SHEET 4 AA5 5 ALA B 228 ILE B 231 1 O PHE B 230 N ALA B 144
SHEET 5 AA5 5 VAL B 428 ALA B 430 1 O PHE B 429 N VAL B 229
SHEET 1 AA6 5 VAL B 251 SER B 253 0
SHEET 2 AA6 5 MET B 386 GLU B 389 1 O GLU B 389 N TYR B 252
SHEET 3 AA6 5 LYS B 281 ILE B 285 1 N ALA B 283 O ILE B 388
SHEET 4 AA6 5 LYS B 305 VAL B 309 1 O TYR B 307 N VAL B 282
SHEET 5 AA6 5 GLU B 333 LEU B 335 1 O GLU B 333 N ILE B 308
SHEET 1 AA7 3 THR B 338 GLY B 345 0
SHEET 2 AA7 3 VAL B 351 LEU B 361 -1 O GLU B 355 N ILE B 341
SHEET 3 AA7 3 PRO B 372 GLU B 383 -1 O PHE B 380 N CYS B 356
SHEET 1 AA8 4 ILE C 9 LYS C 11 0
SHEET 2 AA8 4 VAL C 19 HIS C 25 -1 O TRP C 23 N LYS C 11
SHEET 3 AA8 4 LEU C 63 LYS C 69 -1 O MET C 66 N PHE C 22
SHEET 4 AA8 4 ASP C 56 LYS C 58 -1 N ASP C 56 O ARG C 65
SHEET 1 AA9 3 ILE C 50 THR C 53 0
SHEET 2 AA9 3 PHE C 38 ARG C 42 -1 N VAL C 39 O LEU C 52
SHEET 3 AA9 3 ASP C 89 LEU C 94 -1 O LEU C 94 N PHE C 38
SHEET 1 AB1 6 VAL C 156 VAL C 159 0
SHEET 2 AB1 6 ASN C 131 LEU C 136 1 N THR C 134 O LEU C 158
SHEET 3 AB1 6 ASN C 105 GLY C 110 1 N LEU C 108 O VAL C 135
SHEET 4 AB1 6 ILE C 186 VAL C 190 1 O TRP C 188 N LEU C 107
SHEET 5 AB1 6 ILE C 210 SER C 213 1 O TRP C 211 N ALA C 189
SHEET 6 AB1 6 GLU C 245 ARG C 247 -1 O PHE C 246 N VAL C 212
SHEET 1 AB2 2 ARG C 229 VAL C 232 0
SHEET 2 AB2 2 GLN C 235 PHE C 238 -1 O LYS C 237 N VAL C 230
SHEET 1 AB3 5 ASN D 206 HIS D 208 0
SHEET 2 AB3 5 HIS D 165 PHE D 169 1 N VAL D 166 O ASN D 206
SHEET 3 AB3 5 LYS D 142 VAL D 146 1 N VAL D 145 O PHE D 169
SHEET 4 AB3 5 ALA D 228 ILE D 231 1 O PHE D 230 N VAL D 146
SHEET 5 AB3 5 VAL D 428 ALA D 430 1 O PHE D 429 N VAL D 229
SHEET 1 AB4 5 VAL D 251 SER D 253 0
SHEET 2 AB4 5 MET D 386 GLU D 389 1 O VAL D 387 N TYR D 252
SHEET 3 AB4 5 LYS D 281 ILE D 285 1 N ALA D 283 O MET D 386
SHEET 4 AB4 5 LYS D 305 VAL D 309 1 O TYR D 307 N VAL D 284
SHEET 5 AB4 5 GLU D 333 LEU D 335 1 O GLU D 333 N VAL D 306
SHEET 1 AB5 3 THR D 338 GLY D 345 0
SHEET 2 AB5 3 VAL D 351 LYS D 362 -1 O GLU D 355 N ILE D 341
SHEET 3 AB5 3 ARG D 369 PRO D 374 -1 O VAL D 373 N GLU D 360
SHEET 1 AB6 3 THR D 338 GLY D 345 0
SHEET 2 AB6 3 VAL D 351 LYS D 362 -1 O GLU D 355 N ILE D 341
SHEET 3 AB6 3 PHE D 380 GLU D 383 -1 O PHE D 380 N CYS D 356
LINK OD1 ASP A 220 FE2 FES A 501 1555 1555 2.13
LINK SG CYS A 225 FE2 FES A 501 1555 1555 2.26
LINK SG CYS A 228 FE1 FES A 501 1555 1555 2.29
LINK SG CYS A 240 FE1 FES A 501 1555 1555 2.29
LINK SG CYS B 39 FE4 SF4 B 501 1555 1555 2.29
LINK SG CYS B 42 FE3 SF4 B 501 1555 1555 2.30
LINK SG CYS B 47 FE2 SF4 B 501 1555 1555 2.27
LINK SG CYS B 51 FE4 SF4 B 502 1555 1555 2.25
LINK SG CYS B 90 FE2 SF4 B 502 1555 1555 2.31
LINK SG CYS B 96 FE3 SF4 B 502 1555 1555 2.28
LINK SG CYS B 100 FE1 SF4 B 501 1555 1555 2.28
LINK OE1 GLU B 117 FE1 SF4 B 502 1555 1555 1.87
LINK OD1 ASP C 220 FE2 FES C 501 1555 1555 1.90
LINK OD2 ASP C 220 FE2 FES C 501 1555 1555 2.20
LINK SG CYS C 225 FE2 FES C 501 1555 1555 2.32
LINK SG CYS C 228 FE1 FES C 501 1555 1555 2.30
LINK SG CYS C 240 FE1 FES C 501 1555 1555 2.28
LINK SG CYS D 39 FE4 SF4 D 501 1555 1555 2.29
LINK SG CYS D 42 FE1 SF4 D 501 1555 1555 2.31
LINK SG CYS D 47 FE2 SF4 D 501 1555 1555 2.30
LINK SG CYS D 51 FE4 SF4 D 502 1555 1555 2.28
LINK SG CYS D 90 FE1 SF4 D 502 1555 1555 2.30
LINK SG CYS D 96 FE3 SF4 D 502 1555 1555 2.30
LINK SG CYS D 100 FE3 SF4 D 501 1555 1555 2.28
LINK OE1 GLU D 117 FE2 SF4 D 502 1555 1555 2.27
LINK OE2 GLU D 117 FE2 SF4 D 502 1555 1555 1.97
CISPEP 1 GLY A 92 PRO A 93 0 -0.46
CISPEP 2 GLY A 243 PRO A 244 0 1.51
CISPEP 3 LYS B 133 PRO B 134 0 11.76
CISPEP 4 PRO B 175 GLY B 176 0 -1.62
CISPEP 5 THR B 237 PRO B 238 0 -6.96
CISPEP 6 PHE B 269 PRO B 270 0 0.84
CISPEP 7 GLY C 92 PRO C 93 0 0.06
CISPEP 8 GLY C 243 PRO C 244 0 1.26
CISPEP 9 THR D 237 PRO D 238 0 -7.20
CISPEP 10 PHE D 269 PRO D 270 0 2.85
SITE 1 AC1 11 MET A 218 VAL A 219 ASP A 220 GLY A 221
SITE 2 AC1 11 GLY A 223 MET A 224 CYS A 225 GLY A 226
SITE 3 AC1 11 ALA A 227 CYS A 228 CYS A 240
SITE 1 AC2 21 PHE A 38 GLU A 48 PRO A 51 LEU A 52
SITE 2 AC2 21 THR A 53 VAL A 67 VAL A 68 LYS A 69
SITE 3 AC2 21 VAL A 71 GLY A 72 LYS A 73 THR A 74
SITE 4 AC2 21 THR A 75 ASN A 215 PRO A 216 MET A 218
SITE 5 AC2 21 LEU A 260 GLN A 266 ILE A 269 NAD A 503
SITE 6 AC2 21 HOH A 604
SITE 1 AC3 22 LYS A 69 GLY A 111 GLY A 112 VAL A 113
SITE 2 AC3 22 GLY A 114 THR A 117 GLY A 137 ALA A 138
SITE 3 AC3 22 ARG A 139 VAL A 170 VAL A 171 VAL A 190
SITE 4 AC3 22 GLY A 191 PRO A 192 ILE A 194 MET A 195
SITE 5 AC3 22 MET A 196 PHE A 198 SER A 213 ASN A 215
SITE 6 AC3 22 FAD A 502 HOH A 601
SITE 1 AC4 7 CYS B 39 LEU B 40 CYS B 42 CYS B 47
SITE 2 AC4 7 CYS B 100 VAL B 101 VAL B 102
SITE 1 AC5 5 CYS B 51 CYS B 90 GLN B 95 CYS B 96
SITE 2 AC5 5 GLU B 117
SITE 1 AC6 33 VAL B 89 PRO B 91 GLY B 147 SER B 148
SITE 2 AC6 33 GLY B 149 PRO B 150 ALA B 151 GLU B 170
SITE 3 AC6 33 ALA B 171 PHE B 172 GLY B 177 VAL B 178
SITE 4 AC6 33 TYR B 181 ILE B 183 ARG B 187 THR B 211
SITE 5 AC6 33 VAL B 213 GLY B 232 THR B 233 GLY B 234
SITE 6 AC6 33 ASN B 289 THR B 290 GLN B 393 LEU B 399
SITE 7 AC6 33 GLY B 432 ASP B 433 ALA B 439 THR B 440
SITE 8 AC6 33 VAL B 441 ALA B 444 HOH B 608 HOH B 609
SITE 9 AC6 33 HOH B 621
SITE 1 AC7 9 VAL C 219 ASP C 220 GLY C 221 GLY C 223
SITE 2 AC7 9 MET C 224 CYS C 225 GLY C 226 CYS C 228
SITE 3 AC7 9 CYS C 240
SITE 1 AC8 23 GLU C 48 ILE C 50 PRO C 51 LEU C 52
SITE 2 AC8 23 THR C 53 VAL C 67 VAL C 68 LYS C 69
SITE 3 AC8 23 VAL C 71 GLY C 72 LYS C 73 THR C 74
SITE 4 AC8 23 THR C 75 ILE C 115 ASN C 215 PRO C 216
SITE 5 AC8 23 ILE C 217 MET C 218 LEU C 260 GLN C 266
SITE 6 AC8 23 GLU C 267 SER C 270 HOH C 611
SITE 1 AC9 6 CYS D 39 LEU D 40 CYS D 42 CYS D 47
SITE 2 AC9 6 CYS D 100 VAL D 101
SITE 1 AD1 5 CYS D 51 CYS D 90 GLN D 95 CYS D 96
SITE 2 AD1 5 GLU D 117
SITE 1 AD2 31 VAL D 89 GLY D 147 SER D 148 GLY D 149
SITE 2 AD2 31 PRO D 150 ALA D 151 PHE D 169 GLU D 170
SITE 3 AD2 31 ALA D 171 VAL D 178 GLY D 182 ILE D 183
SITE 4 AD2 31 ARG D 187 THR D 211 VAL D 212 VAL D 213
SITE 5 AD2 31 GLY D 232 THR D 233 GLY D 234 LEU D 258
SITE 6 AD2 31 ASN D 289 THR D 290 ASP D 293 GLY D 432
SITE 7 AD2 31 ASP D 433 ALA D 439 THR D 440 VAL D 441
SITE 8 AD2 31 NAD D 504 HOH D 612 HOH D 618
SITE 1 AD3 13 LYS D 239 GLY D 288 ASN D 289 THR D 290
SITE 2 AD3 13 TYR D 310 ARG D 311 ARG D 371 PRO D 372
SITE 3 AD3 13 ILE D 391 GLY D 392 ALA D 438 ALA D 439
SITE 4 AD3 13 FAD D 503
SITE 1 AD4 4 ARG D 62 LYS D 63 ASP D 66 LYS D 68
CRYST1 81.400 81.400 307.430 90.00 90.00 90.00 P 43 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 0.012285 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012285 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003253 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
