HEADER OXIDOREDUCTASE 10-FEB-10 3AET
TITLE STRUCTURE OF THE LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE
TITLE 2 CATALYZING A KEY REDUCTION FOR GREENING IN THE DARK
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT N;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: LI-POR SUBUNIT N, DPOR SUBUNIT N, DARK-OPERATIVE
COMPND 5 PROTOCHLOROPHYLLIDE OXIDOREDUCTASE N-PROTEIN;
COMPND 6 EC: 1.18.-.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B;
COMPND 10 CHAIN: B, D;
COMPND 11 SYNONYM: LI-POR SUBUNIT B, DPOR SUBUNIT B, DARK-OPERATIVE
COMPND 12 PROTOCHLOROPHYLLIDE OXIDOREDUCTASE B-PROTEIN;
COMPND 13 EC: 1.18.-.-;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER CAPSULATUS;
SOURCE 3 ORGANISM_TAXID: 1061;
SOURCE 4 GENE: BCHN;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PASK-IBA5PLUS;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: RHODOBACTER CAPSULATUS;
SOURCE 12 ORGANISM_TAXID: 1061;
SOURCE 13 GENE: BCHB, BCHK;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PASK-IBA5PLUS
KEYWDS IRON/SULFUR CLUSTER, BACTERIOCHLOROPHYLL BIOSYNTHESIS, CHLOROPHYLL
KEYWDS 2 BIOSYNTHESIS, OXIDOREDUCTASE, PHOTOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR N.MURAKI,J.NOMATA,T.SHIBA,Y.FUJITA,G.KURISU
REVDAT 5 01-NOV-23 3AET 1 REMARK
REVDAT 4 10-NOV-21 3AET 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 3AET 1 VERSN
REVDAT 2 19-MAY-10 3AET 1 JRNL
REVDAT 1 21-APR-10 3AET 0
JRNL AUTH N.MURAKI,J.NOMATA,K.EBATA,T.MIZOGUCHI,T.SHIBA,H.TAMIAKI,
JRNL AUTH 2 G.KURISU,Y.FUJITA
JRNL TITL X-RAY CRYSTAL STRUCTURE OF THE LIGHT-INDEPENDENT
JRNL TITL 2 PROTOCHLOROPHYLLIDE REDUCTASE
JRNL REF NATURE V. 465 110 2010
JRNL REFN ISSN 0028-0836
JRNL PMID 20400946
JRNL DOI 10.1038/NATURE08950
REMARK 2
REMARK 2 RESOLUTION. 2.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 3 NUMBER OF REFLECTIONS : 40688
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2171
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.91
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1732
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 51.06
REMARK 3 BIN R VALUE (WORKING SET) : 0.3790
REMARK 3 BIN FREE R VALUE SET COUNT : 92
REMARK 3 BIN FREE R VALUE : 0.4770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12760
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 6
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 69.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.64
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.88000
REMARK 3 B22 (A**2) : -2.41000
REMARK 3 B33 (A**2) : -2.14000
REMARK 3 B12 (A**2) : 1.00000
REMARK 3 B13 (A**2) : -0.63000
REMARK 3 B23 (A**2) : -0.87000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.474
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.371
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 42.917
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.930
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.873
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13052 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17759 ; 1.484 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1665 ; 6.947 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 538 ;37.486 ;23.086
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2146 ;21.760 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 108 ;21.934 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2060 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9826 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 6629 ; 0.240 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8950 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 454 ; 0.146 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 37 ; 0.256 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.180 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 8501 ; 0.419 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13373 ; 0.765 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5003 ; 1.072 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4362 ; 1.844 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 7 A 80 3
REMARK 3 1 C 7 C 80 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 296 ; 0.06 ; 0.05
REMARK 3 LOOSE POSITIONAL 1 A (A): 275 ; 0.57 ; 5.00
REMARK 3 TIGHT THERMAL 1 A (A**2): 296 ; 0.10 ; 0.50
REMARK 3 LOOSE THERMAL 1 A (A**2): 275 ; 0.80 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 420 3
REMARK 3 1 D 1 D 420 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 1680 ; 0.04 ; 0.05
REMARK 3 LOOSE POSITIONAL 2 B (A): 1538 ; 0.51 ; 5.00
REMARK 3 TIGHT THERMAL 2 B (A**2): 1680 ; 0.11 ; 0.50
REMARK 3 LOOSE THERMAL 2 B (A**2): 1538 ; 0.87 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 90 A 421 4
REMARK 3 1 C 90 C 420 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 2531 ; 0.36 ; 0.50
REMARK 3 MEDIUM THERMAL 3 A (A**2): 2531 ; 0.28 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 7 A 421
REMARK 3 ORIGIN FOR THE GROUP (A): -12.6769 -19.5008 -28.7768
REMARK 3 T TENSOR
REMARK 3 T11: 0.1822 T22: -0.0915
REMARK 3 T33: -0.1780 T12: 0.0403
REMARK 3 T13: 0.0309 T23: -0.0759
REMARK 3 L TENSOR
REMARK 3 L11: 1.1637 L22: 0.7730
REMARK 3 L33: 1.3269 L12: 0.1441
REMARK 3 L13: 0.5463 L23: -0.0355
REMARK 3 S TENSOR
REMARK 3 S11: 0.0686 S12: 0.1083 S13: -0.0400
REMARK 3 S21: -0.3405 S22: -0.0581 S23: 0.0199
REMARK 3 S31: 0.2736 S32: 0.0095 S33: -0.0105
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 420
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1162 -19.7841 -1.0198
REMARK 3 T TENSOR
REMARK 3 T11: -0.0622 T22: -0.0947
REMARK 3 T33: 0.0104 T12: 0.1270
REMARK 3 T13: 0.0544 T23: 0.0900
REMARK 3 L TENSOR
REMARK 3 L11: 0.6670 L22: 1.2240
REMARK 3 L33: 1.7164 L12: 0.0487
REMARK 3 L13: 0.0282 L23: 0.3518
REMARK 3 S TENSOR
REMARK 3 S11: 0.0017 S12: 0.0911 S13: -0.0723
REMARK 3 S21: 0.0534 S22: -0.1754 S23: -0.2766
REMARK 3 S31: 0.4146 S32: 0.2086 S33: 0.1737
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 7 C 420
REMARK 3 ORIGIN FOR THE GROUP (A): -12.9574 19.4563 28.7532
REMARK 3 T TENSOR
REMARK 3 T11: 0.1693 T22: -0.1493
REMARK 3 T33: -0.1847 T12: -0.0381
REMARK 3 T13: -0.0561 T23: -0.0599
REMARK 3 L TENSOR
REMARK 3 L11: 0.9321 L22: 0.7448
REMARK 3 L33: 1.3300 L12: -0.0842
REMARK 3 L13: -0.5335 L23: -0.2121
REMARK 3 S TENSOR
REMARK 3 S11: 0.0105 S12: -0.0693 S13: 0.0170
REMARK 3 S21: 0.3492 S22: -0.0733 S23: 0.0596
REMARK 3 S31: -0.2133 S32: -0.0517 S33: 0.0629
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 420
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7368 20.0087 0.9257
REMARK 3 T TENSOR
REMARK 3 T11: -0.1157 T22: -0.1192
REMARK 3 T33: 0.0485 T12: -0.1372
REMARK 3 T13: -0.0375 T23: 0.1266
REMARK 3 L TENSOR
REMARK 3 L11: 0.4340 L22: 1.3293
REMARK 3 L33: 1.5914 L12: -0.1357
REMARK 3 L13: 0.0824 L23: 0.2365
REMARK 3 S TENSOR
REMARK 3 S11: -0.0411 S12: 0.0711 S13: 0.0981
REMARK 3 S21: -0.0647 S22: -0.1860 S23: -0.3081
REMARK 3 S31: -0.2866 S32: 0.1915 S33: 0.2271
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3AET COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000029163.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42863
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2ZMP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2M SODIUM CLORIDE, 0.1M
REMARK 280 MOPS-NAOH(PH7.0), PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 58080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 -11
REMARK 465 ALA A -10
REMARK 465 SER A -9
REMARK 465 TRP A -8
REMARK 465 SER A -7
REMARK 465 HIS A -6
REMARK 465 PRO A -5
REMARK 465 GLN A -4
REMARK 465 PHE A -3
REMARK 465 GLU A -2
REMARK 465 LYS A -1
REMARK 465 GLY A 0
REMARK 465 ALA A 1
REMARK 465 SER A 2
REMARK 465 LEU A 3
REMARK 465 ASP A 4
REMARK 465 SER A 5
REMARK 465 PRO A 6
REMARK 465 GLY A 422
REMARK 465 ALA A 423
REMARK 465 ALA A 424
REMARK 465 ASP B 421
REMARK 465 PHE B 422
REMARK 465 GLU B 423
REMARK 465 PHE B 424
REMARK 465 HIS B 425
REMARK 465 ASP B 426
REMARK 465 ALA B 427
REMARK 465 ALA B 428
REMARK 465 GLY B 429
REMARK 465 ALA B 430
REMARK 465 SER B 431
REMARK 465 HIS B 432
REMARK 465 HIS B 433
REMARK 465 GLY B 434
REMARK 465 GLY B 435
REMARK 465 LYS B 436
REMARK 465 ALA B 437
REMARK 465 VAL B 438
REMARK 465 ALA B 439
REMARK 465 ARG B 440
REMARK 465 GLU B 441
REMARK 465 GLU B 442
REMARK 465 SER B 443
REMARK 465 PRO B 444
REMARK 465 VAL B 445
REMARK 465 ALA B 446
REMARK 465 PRO B 447
REMARK 465 ALA B 448
REMARK 465 ASP B 449
REMARK 465 LEU B 450
REMARK 465 ALA B 451
REMARK 465 PRO B 452
REMARK 465 ALA B 453
REMARK 465 ALA B 454
REMARK 465 THR B 455
REMARK 465 SER B 456
REMARK 465 ASP B 457
REMARK 465 THR B 458
REMARK 465 PRO B 459
REMARK 465 ALA B 460
REMARK 465 ALA B 461
REMARK 465 PRO B 462
REMARK 465 SER B 463
REMARK 465 PRO B 464
REMARK 465 VAL B 465
REMARK 465 VAL B 466
REMARK 465 VAL B 467
REMARK 465 THR B 468
REMARK 465 GLN B 469
REMARK 465 ALA B 470
REMARK 465 SER B 471
REMARK 465 GLY B 472
REMARK 465 GLU B 473
REMARK 465 ILE B 474
REMARK 465 ARG B 475
REMARK 465 TRP B 476
REMARK 465 MET B 477
REMARK 465 PRO B 478
REMARK 465 GLU B 479
REMARK 465 ALA B 480
REMARK 465 GLU B 481
REMARK 465 ARG B 482
REMARK 465 GLU B 483
REMARK 465 LEU B 484
REMARK 465 ARG B 485
REMARK 465 LYS B 486
REMARK 465 ILE B 487
REMARK 465 PRO B 488
REMARK 465 PHE B 489
REMARK 465 PHE B 490
REMARK 465 VAL B 491
REMARK 465 ARG B 492
REMARK 465 GLY B 493
REMARK 465 LYS B 494
REMARK 465 ALA B 495
REMARK 465 LYS B 496
REMARK 465 ARG B 497
REMARK 465 ASN B 498
REMARK 465 THR B 499
REMARK 465 GLU B 500
REMARK 465 LEU B 501
REMARK 465 TYR B 502
REMARK 465 ALA B 503
REMARK 465 ALA B 504
REMARK 465 HIS B 505
REMARK 465 LYS B 506
REMARK 465 GLY B 507
REMARK 465 VAL B 508
REMARK 465 CYS B 509
REMARK 465 ASP B 510
REMARK 465 ILE B 511
REMARK 465 THR B 512
REMARK 465 VAL B 513
REMARK 465 GLU B 514
REMARK 465 THR B 515
REMARK 465 LEU B 516
REMARK 465 TYR B 517
REMARK 465 GLU B 518
REMARK 465 ALA B 519
REMARK 465 LYS B 520
REMARK 465 ALA B 521
REMARK 465 HIS B 522
REMARK 465 TYR B 523
REMARK 465 ALA B 524
REMARK 465 ARG B 525
REMARK 465 MET C -11
REMARK 465 ALA C -10
REMARK 465 SER C -9
REMARK 465 TRP C -8
REMARK 465 SER C -7
REMARK 465 HIS C -6
REMARK 465 PRO C -5
REMARK 465 GLN C -4
REMARK 465 PHE C -3
REMARK 465 GLU C -2
REMARK 465 LYS C -1
REMARK 465 GLY C 0
REMARK 465 ALA C 1
REMARK 465 SER C 2
REMARK 465 LEU C 3
REMARK 465 ASP C 4
REMARK 465 SER C 5
REMARK 465 PRO C 6
REMARK 465 GLY C 421
REMARK 465 GLY C 422
REMARK 465 ALA C 423
REMARK 465 ALA C 424
REMARK 465 ASP D 421
REMARK 465 PHE D 422
REMARK 465 GLU D 423
REMARK 465 PHE D 424
REMARK 465 HIS D 425
REMARK 465 ASP D 426
REMARK 465 ALA D 427
REMARK 465 ALA D 428
REMARK 465 GLY D 429
REMARK 465 ALA D 430
REMARK 465 SER D 431
REMARK 465 HIS D 432
REMARK 465 HIS D 433
REMARK 465 GLY D 434
REMARK 465 GLY D 435
REMARK 465 LYS D 436
REMARK 465 ALA D 437
REMARK 465 VAL D 438
REMARK 465 ALA D 439
REMARK 465 ARG D 440
REMARK 465 GLU D 441
REMARK 465 GLU D 442
REMARK 465 SER D 443
REMARK 465 PRO D 444
REMARK 465 VAL D 445
REMARK 465 ALA D 446
REMARK 465 PRO D 447
REMARK 465 ALA D 448
REMARK 465 ASP D 449
REMARK 465 LEU D 450
REMARK 465 ALA D 451
REMARK 465 PRO D 452
REMARK 465 ALA D 453
REMARK 465 ALA D 454
REMARK 465 THR D 455
REMARK 465 SER D 456
REMARK 465 ASP D 457
REMARK 465 THR D 458
REMARK 465 PRO D 459
REMARK 465 ALA D 460
REMARK 465 ALA D 461
REMARK 465 PRO D 462
REMARK 465 SER D 463
REMARK 465 PRO D 464
REMARK 465 VAL D 465
REMARK 465 VAL D 466
REMARK 465 VAL D 467
REMARK 465 THR D 468
REMARK 465 GLN D 469
REMARK 465 ALA D 470
REMARK 465 SER D 471
REMARK 465 GLY D 472
REMARK 465 GLU D 473
REMARK 465 ILE D 474
REMARK 465 ARG D 475
REMARK 465 TRP D 476
REMARK 465 MET D 477
REMARK 465 PRO D 478
REMARK 465 GLU D 479
REMARK 465 ALA D 480
REMARK 465 GLU D 481
REMARK 465 ARG D 482
REMARK 465 GLU D 483
REMARK 465 LEU D 484
REMARK 465 ARG D 485
REMARK 465 LYS D 486
REMARK 465 ILE D 487
REMARK 465 PRO D 488
REMARK 465 PHE D 489
REMARK 465 PHE D 490
REMARK 465 VAL D 491
REMARK 465 ARG D 492
REMARK 465 GLY D 493
REMARK 465 LYS D 494
REMARK 465 ALA D 495
REMARK 465 LYS D 496
REMARK 465 ARG D 497
REMARK 465 ASN D 498
REMARK 465 THR D 499
REMARK 465 GLU D 500
REMARK 465 LEU D 501
REMARK 465 TYR D 502
REMARK 465 ALA D 503
REMARK 465 ALA D 504
REMARK 465 HIS D 505
REMARK 465 LYS D 506
REMARK 465 GLY D 507
REMARK 465 VAL D 508
REMARK 465 CYS D 509
REMARK 465 ASP D 510
REMARK 465 ILE D 511
REMARK 465 THR D 512
REMARK 465 VAL D 513
REMARK 465 GLU D 514
REMARK 465 THR D 515
REMARK 465 LEU D 516
REMARK 465 TYR D 517
REMARK 465 GLU D 518
REMARK 465 ALA D 519
REMARK 465 LYS D 520
REMARK 465 ALA D 521
REMARK 465 HIS D 522
REMARK 465 TYR D 523
REMARK 465 ALA D 524
REMARK 465 ARG D 525
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 NE2 GLN B 380 ND1 HIS D 404 2.16
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 A 198 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 LEU B 178 CA - CB - CG ANGL. DEV. = 14.6 DEGREES
REMARK 500 TRP C 33 N - CA - C ANGL. DEV. = -19.8 DEGREES
REMARK 500 LEU C 34 CA - CB - CG ANGL. DEV. = 19.4 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 ARG A 16 97.15 -62.57
REMARK 500 ARG A 68 71.21 -104.58
REMARK 500 LYS A 118 43.17 32.36
REMARK 500 PHE A 150 -105.15 44.05
REMARK 500 PRO A 198 121.43 -13.25
REMARK 500 PHE A 225 36.94 -90.03
REMARK 500 ALA A 243 139.50 -170.20
REMARK 500 ASP A 302 -49.48 -143.31
REMARK 500 THR A 322 -94.93 -91.77
REMARK 500 ASN A 344 17.45 -66.59
REMARK 500 GLN A 351 148.70 -174.36
REMARK 500 ASN A 364 71.89 50.74
REMARK 500 PHE A 398 -177.05 65.49
REMARK 500 ASN A 420 37.69 -156.54
REMARK 500 LEU B 5 -78.99 -95.42
REMARK 500 ASP B 40 -67.26 -27.15
REMARK 500 ARG B 48 26.33 86.05
REMARK 500 SER B 63 48.82 -82.46
REMARK 500 HIS B 64 11.59 -140.78
REMARK 500 THR B 67 0.50 -56.24
REMARK 500 ASP B 68 -27.33 -39.34
REMARK 500 ASN B 112 81.91 58.93
REMARK 500 ASN B 187 -80.74 -72.61
REMARK 500 LEU B 264 97.58 -68.86
REMARK 500 GLU B 327 -19.85 -48.59
REMARK 500 GLN B 380 -39.24 -38.60
REMARK 500 PHE B 382 75.66 -115.56
REMARK 500 ALA B 387 66.23 -152.72
REMARK 500 ARG C 16 97.88 -66.89
REMARK 500 TRP C 33 -49.42 -155.80
REMARK 500 ALA C 65 31.19 -99.81
REMARK 500 GLU C 66 55.67 39.75
REMARK 500 LEU C 82 46.45 -94.12
REMARK 500 ALA C 83 -45.55 -142.79
REMARK 500 ARG C 100 92.47 -166.28
REMARK 500 ILE C 103 143.48 -39.35
REMARK 500 ARG C 104 -23.30 -140.10
REMARK 500 LEU C 131 -39.75 -35.94
REMARK 500 PHE C 150 -113.45 39.05
REMARK 500 LEU C 165 151.08 -45.19
REMARK 500 ALA C 170 151.70 -44.93
REMARK 500 VAL C 182 -71.21 -37.01
REMARK 500 PHE C 225 49.64 -98.84
REMARK 500 ALA C 243 148.18 -177.93
REMARK 500 LEU C 289 -38.39 -37.65
REMARK 500 ASP C 302 -60.87 -158.45
REMARK 500 THR C 322 -87.08 -110.86
REMARK 500 ASN C 344 15.58 -68.46
REMARK 500 ASN C 364 70.44 46.72
REMARK 500 VAL C 396 -22.83 -145.41
REMARK 500
REMARK 500 THIS ENTRY HAS 65 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 197 PRO A 198 -146.89
REMARK 500 VAL C 32 TRP C 33 -94.91
REMARK 500 ARG D 419 GLU D 420 37.98
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 SF4 A 425 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 26 SG
REMARK 620 2 SF4 A 425 S2 116.8
REMARK 620 3 SF4 A 425 S3 94.5 107.0
REMARK 620 4 SF4 A 425 S4 127.4 105.9 101.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 425 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 51 SG
REMARK 620 2 SF4 A 425 S1 139.1
REMARK 620 3 SF4 A 425 S2 97.7 107.7
REMARK 620 4 SF4 A 425 S4 101.9 100.3 107.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 425 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 112 SG
REMARK 620 2 SF4 A 425 S1 113.4
REMARK 620 3 SF4 A 425 S2 106.8 107.8
REMARK 620 4 SF4 A 425 S3 118.2 103.9 106.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 425 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 36 SG
REMARK 620 2 SF4 A 425 S1 102.6
REMARK 620 3 SF4 A 425 S3 120.5 105.3
REMARK 620 4 SF4 A 425 S4 121.8 101.1 102.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C 425 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 26 SG
REMARK 620 2 SF4 C 425 S2 113.4
REMARK 620 3 SF4 C 425 S3 102.3 106.3
REMARK 620 4 SF4 C 425 S4 124.1 106.7 102.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C 425 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 51 SG
REMARK 620 2 SF4 C 425 S1 120.6
REMARK 620 3 SF4 C 425 S2 107.9 106.7
REMARK 620 4 SF4 C 425 S4 112.4 100.4 108.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C 425 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 112 SG
REMARK 620 2 SF4 C 425 S1 111.5
REMARK 620 3 SF4 C 425 S2 115.0 106.6
REMARK 620 4 SF4 C 425 S3 112.1 105.4 105.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C 425 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 36 SG
REMARK 620 2 SF4 C 425 S1 109.8
REMARK 620 3 SF4 C 425 S3 115.5 106.2
REMARK 620 4 SF4 C 425 S4 118.9 101.4 103.4
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 A 425
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C 425
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3AEK RELATED DB: PDB
REMARK 900 RELATED ID: 3AEQ RELATED DB: PDB
REMARK 900 RELATED ID: 3AER RELATED DB: PDB
REMARK 900 RELATED ID: 3AES RELATED DB: PDB
REMARK 900 RELATED ID: 3AEU RELATED DB: PDB
DBREF 3AET A 2 424 UNP P26164 BCHN_RHOCA 2 424
DBREF 3AET B 1 525 UNP P26163 BCHB_RHOCA 1 525
DBREF 3AET C 2 424 UNP P26164 BCHN_RHOCA 2 424
DBREF 3AET D 1 525 UNP P26163 BCHB_RHOCA 1 525
SEQADV 3AET MET A -11 UNP P26164 EXPRESSION TAG
SEQADV 3AET ALA A -10 UNP P26164 EXPRESSION TAG
SEQADV 3AET SER A -9 UNP P26164 EXPRESSION TAG
SEQADV 3AET TRP A -8 UNP P26164 EXPRESSION TAG
SEQADV 3AET SER A -7 UNP P26164 EXPRESSION TAG
SEQADV 3AET HIS A -6 UNP P26164 EXPRESSION TAG
SEQADV 3AET PRO A -5 UNP P26164 EXPRESSION TAG
SEQADV 3AET GLN A -4 UNP P26164 EXPRESSION TAG
SEQADV 3AET PHE A -3 UNP P26164 EXPRESSION TAG
SEQADV 3AET GLU A -2 UNP P26164 EXPRESSION TAG
SEQADV 3AET LYS A -1 UNP P26164 EXPRESSION TAG
SEQADV 3AET GLY A 0 UNP P26164 EXPRESSION TAG
SEQADV 3AET ALA A 1 UNP P26164 EXPRESSION TAG
SEQADV 3AET CYS B 36 UNP P26163 ASP 36 ENGINEERED MUTATION
SEQADV 3AET MET C -11 UNP P26164 EXPRESSION TAG
SEQADV 3AET ALA C -10 UNP P26164 EXPRESSION TAG
SEQADV 3AET SER C -9 UNP P26164 EXPRESSION TAG
SEQADV 3AET TRP C -8 UNP P26164 EXPRESSION TAG
SEQADV 3AET SER C -7 UNP P26164 EXPRESSION TAG
SEQADV 3AET HIS C -6 UNP P26164 EXPRESSION TAG
SEQADV 3AET PRO C -5 UNP P26164 EXPRESSION TAG
SEQADV 3AET GLN C -4 UNP P26164 EXPRESSION TAG
SEQADV 3AET PHE C -3 UNP P26164 EXPRESSION TAG
SEQADV 3AET GLU C -2 UNP P26164 EXPRESSION TAG
SEQADV 3AET LYS C -1 UNP P26164 EXPRESSION TAG
SEQADV 3AET GLY C 0 UNP P26164 EXPRESSION TAG
SEQADV 3AET ALA C 1 UNP P26164 EXPRESSION TAG
SEQADV 3AET CYS D 36 UNP P26163 ASP 36 ENGINEERED MUTATION
SEQRES 1 A 436 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 A 436 SER LEU ASP SER PRO THR PHE GLY CYS THR ASP SER PRO
SEQRES 3 A 436 VAL ARG ARG GLU ARG GLY GLN LYS ALA VAL PHE CYS GLY
SEQRES 4 A 436 LEU THR SER ILE VAL TRP LEU HIS ARG LYS MET GLN ASP
SEQRES 5 A 436 ALA PHE PHE LEU VAL VAL GLY SER ARG THR CYS ALA HIS
SEQRES 6 A 436 LEU LEU GLN ALA ALA ALA GLY VAL MET ILE PHE ALA GLU
SEQRES 7 A 436 PRO ARG PHE GLY THR ALA VAL LEU GLU GLU GLN ASP LEU
SEQRES 8 A 436 ALA GLY LEU ALA ASP ALA HIS LYS GLU LEU ASP ARG GLU
SEQRES 9 A 436 VAL ALA LYS LEU LEU GLU ARG ARG PRO ASP ILE ARG GLN
SEQRES 10 A 436 LEU PHE LEU VAL GLY SER CYS PRO SER GLU VAL LEU LYS
SEQRES 11 A 436 LEU ASP LEU ASP ARG ALA ALA GLU ARG LEU SER GLY LEU
SEQRES 12 A 436 HIS ALA PRO HIS VAL ARG VAL TYR SER TYR THR GLY SER
SEQRES 13 A 436 GLY LEU ASP THR THR PHE THR GLN GLY GLU ASP THR CYS
SEQRES 14 A 436 LEU ALA ALA MET VAL PRO THR LEU ASP THR THR GLU ALA
SEQRES 15 A 436 ALA GLU LEU ILE VAL VAL GLY ALA LEU PRO ASP VAL VAL
SEQRES 16 A 436 GLU ASP GLN CYS LEU SER LEU LEU THR GLN LEU GLY VAL
SEQRES 17 A 436 GLY PRO VAL ARG MET LEU PRO ALA ARG ARG SER ASP ILE
SEQRES 18 A 436 GLU PRO ALA VAL GLY PRO ASN THR ARG PHE ILE LEU ALA
SEQRES 19 A 436 GLN PRO PHE LEU GLY GLU THR THR GLY ALA LEU GLU ARG
SEQRES 20 A 436 ARG GLY ALA LYS ARG ILE ALA ALA PRO PHE PRO PHE GLY
SEQRES 21 A 436 GLU GLU GLY THR THR LEU TRP LEU LYS ALA VAL ALA ASP
SEQRES 22 A 436 ALA TYR GLY VAL SER ALA GLU LYS PHE GLU ALA VAL THR
SEQRES 23 A 436 ALA ALA PRO ARG ALA ARG ALA LYS LYS ALA ILE ALA ALA
SEQRES 24 A 436 HIS LEU GLU THR LEU THR GLY LYS SER LEU PHE MET PHE
SEQRES 25 A 436 PRO ASP SER GLN LEU GLU ILE PRO LEU ALA ARG PHE LEU
SEQRES 26 A 436 ALA ARG GLU CYS GLY MET LYS THR THR GLU ILE ALA THR
SEQRES 27 A 436 PRO PHE LEU HIS LYS ALA ILE MET ALA PRO ASP LEU ALA
SEQRES 28 A 436 LEU LEU PRO SER ASN THR ALA LEU THR GLU GLY GLN ASP
SEQRES 29 A 436 LEU GLU ALA GLN LEU ASP ARG HIS GLU ALA ILE ASN PRO
SEQRES 30 A 436 ASP LEU THR VAL CYS GLY LEU GLY LEU ALA ASN PRO LEU
SEQRES 31 A 436 GLU ALA LYS GLY HIS ALA THR LYS TRP ALA ILE GLU LEU
SEQRES 32 A 436 VAL PHE THR PRO VAL HIS PHE TYR GLU GLN ALA GLY ASP
SEQRES 33 A 436 LEU ALA GLY LEU PHE SER ARG PRO LEU ARG ARG ARG ALA
SEQRES 34 A 436 LEU LEU ASN GLY GLY ALA ALA
SEQRES 1 B 525 MET LYS LEU THR LEU TRP THR TYR GLU GLY PRO PRO HIS
SEQRES 2 B 525 VAL GLY ALA MET ARG VAL ALA THR ALA MET LYS ASP LEU
SEQRES 3 B 525 GLN LEU VAL LEU HIS GLY PRO GLN GLY CYS THR TYR ALA
SEQRES 4 B 525 ASP LEU LEU PHE THR MET ILE GLU ARG ARG ASN ALA ARG
SEQRES 5 B 525 PRO PRO VAL SER PHE SER THR PHE GLU ALA SER HIS MET
SEQRES 6 B 525 GLY THR ASP THR ALA ILE LEU LEU LYS ASP ALA LEU ALA
SEQRES 7 B 525 ALA ALA HIS ALA ARG TYR LYS PRO GLN ALA MET ALA VAL
SEQRES 8 B 525 ALA LEU THR CYS THR ALA GLU LEU LEU GLN ASP ASP PRO
SEQRES 9 B 525 ASN GLY ILE SER ARG ALA LEU ASN LEU PRO VAL PRO VAL
SEQRES 10 B 525 VAL PRO LEU GLU LEU PRO SER TYR SER ARG LYS GLU ASN
SEQRES 11 B 525 TYR GLY ALA ASP GLU THR PHE ARG ALA LEU VAL ARG ALA
SEQRES 12 B 525 LEU ALA VAL PRO MET GLU ARG THR PRO GLU VAL THR CYS
SEQRES 13 B 525 ASN LEU LEU GLY ALA THR ALA LEU GLY PHE ARG HIS ARG
SEQRES 14 B 525 ASP ASP VAL ALA GLU VAL THR LYS LEU LEU ALA THR MET
SEQRES 15 B 525 GLY ILE LYS VAL ASN VAL CYS ALA PRO LEU GLY ALA SER
SEQRES 16 B 525 PRO ASP ASP LEU ARG LYS LEU GLY GLN ALA HIS PHE ASN
SEQRES 17 B 525 VAL LEU MET TYR PRO GLU THR GLY GLU SER ALA ALA ARG
SEQRES 18 B 525 HIS LEU GLU ARG ALA CYS LYS GLN PRO PHE THR LYS ILE
SEQRES 19 B 525 VAL PRO ILE GLY VAL GLY ALA THR ARG ASP PHE LEU ALA
SEQRES 20 B 525 GLU VAL SER LYS ILE THR GLY LEU PRO VAL VAL THR ASP
SEQRES 21 B 525 GLU SER THR LEU ARG GLN PRO TRP TRP SER ALA SER VAL
SEQRES 22 B 525 ASP SER THR TYR LEU THR GLY LYS ARG VAL PHE ILE PHE
SEQRES 23 B 525 GLY ASP GLY THR HIS VAL ILE ALA ALA ALA ARG ILE ALA
SEQRES 24 B 525 ALA LYS GLU VAL GLY PHE GLU VAL VAL GLY MET GLY CYS
SEQRES 25 B 525 TYR ASN ARG GLU MET ALA ARG PRO LEU ARG THR ALA ALA
SEQRES 26 B 525 ALA GLU TYR GLY LEU GLU ALA LEU ILE THR ASP ASP TYR
SEQRES 27 B 525 LEU GLU VAL GLU LYS ALA ILE GLU ALA ALA ALA PRO GLU
SEQRES 28 B 525 LEU ILE LEU GLY THR GLN MET GLU ARG ASN ILE ALA LYS
SEQRES 29 B 525 LYS LEU GLY LEU PRO CYS ALA VAL ILE SER ALA PRO VAL
SEQRES 30 B 525 HIS VAL GLN ASP PHE PRO ALA ARG TYR ALA PRO GLN MET
SEQRES 31 B 525 GLY PHE GLU GLY ALA ASN VAL LEU PHE ASP THR TRP VAL
SEQRES 32 B 525 HIS PRO LEU VAL MET GLY LEU GLU GLU HIS LEU LEU THR
SEQRES 33 B 525 MET PHE ARG GLU ASP PHE GLU PHE HIS ASP ALA ALA GLY
SEQRES 34 B 525 ALA SER HIS HIS GLY GLY LYS ALA VAL ALA ARG GLU GLU
SEQRES 35 B 525 SER PRO VAL ALA PRO ALA ASP LEU ALA PRO ALA ALA THR
SEQRES 36 B 525 SER ASP THR PRO ALA ALA PRO SER PRO VAL VAL VAL THR
SEQRES 37 B 525 GLN ALA SER GLY GLU ILE ARG TRP MET PRO GLU ALA GLU
SEQRES 38 B 525 ARG GLU LEU ARG LYS ILE PRO PHE PHE VAL ARG GLY LYS
SEQRES 39 B 525 ALA LYS ARG ASN THR GLU LEU TYR ALA ALA HIS LYS GLY
SEQRES 40 B 525 VAL CYS ASP ILE THR VAL GLU THR LEU TYR GLU ALA LYS
SEQRES 41 B 525 ALA HIS TYR ALA ARG
SEQRES 1 C 436 MET ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA
SEQRES 2 C 436 SER LEU ASP SER PRO THR PHE GLY CYS THR ASP SER PRO
SEQRES 3 C 436 VAL ARG ARG GLU ARG GLY GLN LYS ALA VAL PHE CYS GLY
SEQRES 4 C 436 LEU THR SER ILE VAL TRP LEU HIS ARG LYS MET GLN ASP
SEQRES 5 C 436 ALA PHE PHE LEU VAL VAL GLY SER ARG THR CYS ALA HIS
SEQRES 6 C 436 LEU LEU GLN ALA ALA ALA GLY VAL MET ILE PHE ALA GLU
SEQRES 7 C 436 PRO ARG PHE GLY THR ALA VAL LEU GLU GLU GLN ASP LEU
SEQRES 8 C 436 ALA GLY LEU ALA ASP ALA HIS LYS GLU LEU ASP ARG GLU
SEQRES 9 C 436 VAL ALA LYS LEU LEU GLU ARG ARG PRO ASP ILE ARG GLN
SEQRES 10 C 436 LEU PHE LEU VAL GLY SER CYS PRO SER GLU VAL LEU LYS
SEQRES 11 C 436 LEU ASP LEU ASP ARG ALA ALA GLU ARG LEU SER GLY LEU
SEQRES 12 C 436 HIS ALA PRO HIS VAL ARG VAL TYR SER TYR THR GLY SER
SEQRES 13 C 436 GLY LEU ASP THR THR PHE THR GLN GLY GLU ASP THR CYS
SEQRES 14 C 436 LEU ALA ALA MET VAL PRO THR LEU ASP THR THR GLU ALA
SEQRES 15 C 436 ALA GLU LEU ILE VAL VAL GLY ALA LEU PRO ASP VAL VAL
SEQRES 16 C 436 GLU ASP GLN CYS LEU SER LEU LEU THR GLN LEU GLY VAL
SEQRES 17 C 436 GLY PRO VAL ARG MET LEU PRO ALA ARG ARG SER ASP ILE
SEQRES 18 C 436 GLU PRO ALA VAL GLY PRO ASN THR ARG PHE ILE LEU ALA
SEQRES 19 C 436 GLN PRO PHE LEU GLY GLU THR THR GLY ALA LEU GLU ARG
SEQRES 20 C 436 ARG GLY ALA LYS ARG ILE ALA ALA PRO PHE PRO PHE GLY
SEQRES 21 C 436 GLU GLU GLY THR THR LEU TRP LEU LYS ALA VAL ALA ASP
SEQRES 22 C 436 ALA TYR GLY VAL SER ALA GLU LYS PHE GLU ALA VAL THR
SEQRES 23 C 436 ALA ALA PRO ARG ALA ARG ALA LYS LYS ALA ILE ALA ALA
SEQRES 24 C 436 HIS LEU GLU THR LEU THR GLY LYS SER LEU PHE MET PHE
SEQRES 25 C 436 PRO ASP SER GLN LEU GLU ILE PRO LEU ALA ARG PHE LEU
SEQRES 26 C 436 ALA ARG GLU CYS GLY MET LYS THR THR GLU ILE ALA THR
SEQRES 27 C 436 PRO PHE LEU HIS LYS ALA ILE MET ALA PRO ASP LEU ALA
SEQRES 28 C 436 LEU LEU PRO SER ASN THR ALA LEU THR GLU GLY GLN ASP
SEQRES 29 C 436 LEU GLU ALA GLN LEU ASP ARG HIS GLU ALA ILE ASN PRO
SEQRES 30 C 436 ASP LEU THR VAL CYS GLY LEU GLY LEU ALA ASN PRO LEU
SEQRES 31 C 436 GLU ALA LYS GLY HIS ALA THR LYS TRP ALA ILE GLU LEU
SEQRES 32 C 436 VAL PHE THR PRO VAL HIS PHE TYR GLU GLN ALA GLY ASP
SEQRES 33 C 436 LEU ALA GLY LEU PHE SER ARG PRO LEU ARG ARG ARG ALA
SEQRES 34 C 436 LEU LEU ASN GLY GLY ALA ALA
SEQRES 1 D 525 MET LYS LEU THR LEU TRP THR TYR GLU GLY PRO PRO HIS
SEQRES 2 D 525 VAL GLY ALA MET ARG VAL ALA THR ALA MET LYS ASP LEU
SEQRES 3 D 525 GLN LEU VAL LEU HIS GLY PRO GLN GLY CYS THR TYR ALA
SEQRES 4 D 525 ASP LEU LEU PHE THR MET ILE GLU ARG ARG ASN ALA ARG
SEQRES 5 D 525 PRO PRO VAL SER PHE SER THR PHE GLU ALA SER HIS MET
SEQRES 6 D 525 GLY THR ASP THR ALA ILE LEU LEU LYS ASP ALA LEU ALA
SEQRES 7 D 525 ALA ALA HIS ALA ARG TYR LYS PRO GLN ALA MET ALA VAL
SEQRES 8 D 525 ALA LEU THR CYS THR ALA GLU LEU LEU GLN ASP ASP PRO
SEQRES 9 D 525 ASN GLY ILE SER ARG ALA LEU ASN LEU PRO VAL PRO VAL
SEQRES 10 D 525 VAL PRO LEU GLU LEU PRO SER TYR SER ARG LYS GLU ASN
SEQRES 11 D 525 TYR GLY ALA ASP GLU THR PHE ARG ALA LEU VAL ARG ALA
SEQRES 12 D 525 LEU ALA VAL PRO MET GLU ARG THR PRO GLU VAL THR CYS
SEQRES 13 D 525 ASN LEU LEU GLY ALA THR ALA LEU GLY PHE ARG HIS ARG
SEQRES 14 D 525 ASP ASP VAL ALA GLU VAL THR LYS LEU LEU ALA THR MET
SEQRES 15 D 525 GLY ILE LYS VAL ASN VAL CYS ALA PRO LEU GLY ALA SER
SEQRES 16 D 525 PRO ASP ASP LEU ARG LYS LEU GLY GLN ALA HIS PHE ASN
SEQRES 17 D 525 VAL LEU MET TYR PRO GLU THR GLY GLU SER ALA ALA ARG
SEQRES 18 D 525 HIS LEU GLU ARG ALA CYS LYS GLN PRO PHE THR LYS ILE
SEQRES 19 D 525 VAL PRO ILE GLY VAL GLY ALA THR ARG ASP PHE LEU ALA
SEQRES 20 D 525 GLU VAL SER LYS ILE THR GLY LEU PRO VAL VAL THR ASP
SEQRES 21 D 525 GLU SER THR LEU ARG GLN PRO TRP TRP SER ALA SER VAL
SEQRES 22 D 525 ASP SER THR TYR LEU THR GLY LYS ARG VAL PHE ILE PHE
SEQRES 23 D 525 GLY ASP GLY THR HIS VAL ILE ALA ALA ALA ARG ILE ALA
SEQRES 24 D 525 ALA LYS GLU VAL GLY PHE GLU VAL VAL GLY MET GLY CYS
SEQRES 25 D 525 TYR ASN ARG GLU MET ALA ARG PRO LEU ARG THR ALA ALA
SEQRES 26 D 525 ALA GLU TYR GLY LEU GLU ALA LEU ILE THR ASP ASP TYR
SEQRES 27 D 525 LEU GLU VAL GLU LYS ALA ILE GLU ALA ALA ALA PRO GLU
SEQRES 28 D 525 LEU ILE LEU GLY THR GLN MET GLU ARG ASN ILE ALA LYS
SEQRES 29 D 525 LYS LEU GLY LEU PRO CYS ALA VAL ILE SER ALA PRO VAL
SEQRES 30 D 525 HIS VAL GLN ASP PHE PRO ALA ARG TYR ALA PRO GLN MET
SEQRES 31 D 525 GLY PHE GLU GLY ALA ASN VAL LEU PHE ASP THR TRP VAL
SEQRES 32 D 525 HIS PRO LEU VAL MET GLY LEU GLU GLU HIS LEU LEU THR
SEQRES 33 D 525 MET PHE ARG GLU ASP PHE GLU PHE HIS ASP ALA ALA GLY
SEQRES 34 D 525 ALA SER HIS HIS GLY GLY LYS ALA VAL ALA ARG GLU GLU
SEQRES 35 D 525 SER PRO VAL ALA PRO ALA ASP LEU ALA PRO ALA ALA THR
SEQRES 36 D 525 SER ASP THR PRO ALA ALA PRO SER PRO VAL VAL VAL THR
SEQRES 37 D 525 GLN ALA SER GLY GLU ILE ARG TRP MET PRO GLU ALA GLU
SEQRES 38 D 525 ARG GLU LEU ARG LYS ILE PRO PHE PHE VAL ARG GLY LYS
SEQRES 39 D 525 ALA LYS ARG ASN THR GLU LEU TYR ALA ALA HIS LYS GLY
SEQRES 40 D 525 VAL CYS ASP ILE THR VAL GLU THR LEU TYR GLU ALA LYS
SEQRES 41 D 525 ALA HIS TYR ALA ARG
HET SF4 A 425 8
HET SF4 C 425 8
HETNAM SF4 IRON/SULFUR CLUSTER
FORMUL 5 SF4 2(FE4 S4)
FORMUL 7 HOH *6(H2 O)
HELIX 1 1 CYS A 26 THR A 29 5 4
HELIX 2 2 SER A 30 MET A 38 1 9
HELIX 3 3 SER A 48 GLY A 60 1 13
HELIX 4 4 VAL A 61 ALA A 65 5 5
HELIX 5 5 GLU A 75 LEU A 79 5 5
HELIX 6 6 ALA A 83 ARG A 100 1 18
HELIX 7 7 SER A 111 LEU A 117 1 7
HELIX 8 8 ASP A 120 HIS A 132 1 13
HELIX 9 9 THR A 151 VAL A 162 1 12
HELIX 10 10 PRO A 163 LEU A 165 5 3
HELIX 11 11 PRO A 180 LEU A 194 1 15
HELIX 12 12 ARG A 206 GLU A 210 5 5
HELIX 13 13 LEU A 226 ARG A 235 1 10
HELIX 14 14 PHE A 247 TYR A 263 1 17
HELIX 15 15 SER A 266 ALA A 287 1 22
HELIX 16 16 HIS A 288 THR A 293 1 6
HELIX 17 17 LEU A 305 GLU A 316 1 12
HELIX 18 18 MET A 334 LEU A 341 1 8
HELIX 19 19 ASP A 352 ASN A 364 1 13
HELIX 20 20 GLY A 371 ALA A 380 1 10
HELIX 21 21 ILE A 389 THR A 394 1 6
HELIX 22 22 GLN A 401 LEU A 419 1 19
HELIX 23 23 PRO B 11 MET B 23 1 13
HELIX 24 24 ALA B 39 ILE B 46 1 8
HELIX 25 25 GLU B 61 GLY B 66 5 6
HELIX 26 26 THR B 67 LYS B 85 1 19
HELIX 27 27 THR B 94 LEU B 99 1 6
HELIX 28 28 ASP B 103 ASN B 112 1 10
HELIX 29 29 LYS B 128 ALA B 145 1 18
HELIX 30 30 ARG B 167 THR B 181 1 15
HELIX 31 31 SER B 195 LYS B 201 1 7
HELIX 32 32 TYR B 212 CYS B 227 1 16
HELIX 33 33 GLY B 238 GLY B 254 1 17
HELIX 34 34 ARG B 265 SER B 272 1 8
HELIX 35 35 VAL B 273 THR B 279 5 7
HELIX 36 36 ASP B 288 GLU B 302 1 15
HELIX 37 37 ASN B 314 GLU B 316 5 3
HELIX 38 38 MET B 317 TYR B 328 1 12
HELIX 39 39 ASP B 337 ALA B 349 1 13
HELIX 40 40 THR B 356 GLY B 367 1 12
HELIX 41 41 HIS B 378 PHE B 382 5 5
HELIX 42 42 MET B 390 PHE B 418 1 29
HELIX 43 43 CYS C 26 THR C 29 5 4
HELIX 44 44 SER C 30 MET C 38 1 9
HELIX 45 45 SER C 48 GLY C 60 1 13
HELIX 46 46 VAL C 61 ALA C 65 5 5
HELIX 47 47 GLU C 75 LEU C 79 5 5
HELIX 48 48 ALA C 83 ARG C 99 1 17
HELIX 49 49 SER C 111 LEU C 117 1 7
HELIX 50 50 ASP C 120 ALA C 133 1 14
HELIX 51 51 THR C 151 VAL C 162 1 12
HELIX 52 52 PRO C 163 LEU C 165 5 3
HELIX 53 53 PRO C 180 LEU C 194 1 15
HELIX 54 54 LEU C 226 ARG C 235 1 10
HELIX 55 55 PHE C 247 TYR C 263 1 17
HELIX 56 56 SER C 266 THR C 293 1 28
HELIX 57 57 LEU C 305 GLY C 318 1 14
HELIX 58 58 MET C 334 LEU C 341 1 8
HELIX 59 59 ASP C 352 ASN C 364 1 13
HELIX 60 60 GLY C 371 ALA C 380 1 10
HELIX 61 61 ILE C 389 THR C 394 1 6
HELIX 62 62 GLN C 401 LEU C 419 1 19
HELIX 63 63 PRO D 11 MET D 23 1 13
HELIX 64 64 ALA D 39 ILE D 46 1 8
HELIX 65 65 GLU D 61 GLY D 66 5 6
HELIX 66 66 THR D 67 LYS D 85 1 19
HELIX 67 67 THR D 94 LEU D 99 1 6
HELIX 68 68 ASP D 103 ASN D 112 1 10
HELIX 69 69 LYS D 128 ALA D 145 1 18
HELIX 70 70 ARG D 167 THR D 181 1 15
HELIX 71 71 SER D 195 LYS D 201 1 7
HELIX 72 72 TYR D 212 CYS D 227 1 16
HELIX 73 73 GLY D 238 GLY D 254 1 17
HELIX 74 74 ARG D 265 SER D 272 1 8
HELIX 75 75 VAL D 273 THR D 279 5 7
HELIX 76 76 ASP D 288 GLU D 302 1 15
HELIX 77 77 ASN D 314 GLU D 316 5 3
HELIX 78 78 MET D 317 GLU D 327 1 11
HELIX 79 79 ASP D 337 ALA D 349 1 13
HELIX 80 80 THR D 356 GLY D 367 1 12
HELIX 81 81 HIS D 378 PHE D 382 5 5
HELIX 82 82 MET D 390 PHE D 418 1 29
SHEET 1 A 6 VAL A 15 GLU A 18 0
SHEET 2 A 6 ALA A 346 GLY A 350 1 O GLU A 349 N GLU A 18
SHEET 3 A 6 LYS A 320 THR A 326 1 N THR A 326 O THR A 348
SHEET 4 A 6 SER A 296 MET A 299 1 N MET A 299 O GLU A 323
SHEET 5 A 6 LEU A 367 CYS A 370 1 O VAL A 369 N PHE A 298
SHEET 6 A 6 ALA A 384 TRP A 387 1 O LYS A 386 N THR A 368
SHEET 1 B 5 ARG A 137 THR A 142 0
SHEET 2 B 5 GLN A 105 GLY A 110 1 N GLY A 110 O TYR A 141
SHEET 3 B 5 ALA A 41 GLY A 47 1 N PHE A 42 O PHE A 107
SHEET 4 B 5 PHE A 69 VAL A 73 1 O ALA A 72 N VAL A 45
SHEET 5 B 5 LYS B 2 THR B 4 -1 O LYS B 2 N VAL A 73
SHEET 1 C 4 VAL A 199 LEU A 202 0
SHEET 2 C 4 LEU A 173 VAL A 176 1 N LEU A 173 O ARG A 200
SHEET 3 C 4 ARG A 218 LEU A 221 1 O ILE A 220 N VAL A 176
SHEET 4 C 4 LYS A 239 ILE A 241 1 O ILE A 241 N PHE A 219
SHEET 1 D 4 VAL B 55 PHE B 57 0
SHEET 2 D 4 LEU B 26 HIS B 31 1 N LEU B 30 O SER B 56
SHEET 3 D 4 ALA B 88 LEU B 93 1 O ALA B 92 N HIS B 31
SHEET 4 D 4 VAL B 117 PRO B 119 1 O VAL B 118 N VAL B 91
SHEET 1 E 3 LYS B 185 ALA B 190 0
SHEET 2 E 3 THR B 155 LEU B 159 1 N CYS B 156 O ASN B 187
SHEET 3 E 3 PHE B 207 LEU B 210 1 O VAL B 209 N ASN B 157
SHEET 1 F 5 LEU B 333 ILE B 334 0
SHEET 2 F 5 GLU B 306 CYS B 312 1 N CYS B 312 O LEU B 333
SHEET 3 F 5 ARG B 282 GLY B 287 1 N VAL B 283 O VAL B 308
SHEET 4 F 5 LEU B 352 GLY B 355 1 O LEU B 354 N PHE B 286
SHEET 5 F 5 CYS B 370 VAL B 372 1 O ALA B 371 N ILE B 353
SHEET 1 G 6 VAL C 15 GLU C 18 0
SHEET 2 G 6 ALA C 346 GLY C 350 1 O LEU C 347 N ARG C 16
SHEET 3 G 6 LYS C 320 THR C 326 1 N THR C 326 O THR C 348
SHEET 4 G 6 SER C 296 MET C 299 1 N LEU C 297 O LYS C 320
SHEET 5 G 6 LEU C 367 CYS C 370 1 O VAL C 369 N PHE C 298
SHEET 6 G 6 ALA C 384 TRP C 387 1 O LYS C 386 N THR C 368
SHEET 1 H 5 ARG C 137 THR C 142 0
SHEET 2 H 5 GLN C 105 GLY C 110 1 N LEU C 108 O TYR C 141
SHEET 3 H 5 ALA C 41 GLY C 47 1 N PHE C 42 O PHE C 107
SHEET 4 H 5 PHE C 69 VAL C 73 1 O ALA C 72 N VAL C 45
SHEET 5 H 5 LYS D 2 THR D 4 -1 O LYS D 2 N VAL C 73
SHEET 1 I 4 VAL C 199 LEU C 202 0
SHEET 2 I 4 LEU C 173 VAL C 176 1 N VAL C 175 O ARG C 200
SHEET 3 I 4 ARG C 218 LEU C 221 1 O ILE C 220 N VAL C 176
SHEET 4 I 4 LYS C 239 ARG C 240 1 O LYS C 239 N PHE C 219
SHEET 1 J 4 VAL D 55 PHE D 57 0
SHEET 2 J 4 LEU D 26 HIS D 31 1 N LEU D 30 O SER D 56
SHEET 3 J 4 ALA D 88 LEU D 93 1 O ALA D 90 N VAL D 29
SHEET 4 J 4 VAL D 117 PRO D 119 1 O VAL D 118 N VAL D 91
SHEET 1 K 3 LYS D 185 ALA D 190 0
SHEET 2 K 3 THR D 155 LEU D 159 1 N CYS D 156 O ASN D 187
SHEET 3 K 3 PHE D 207 LEU D 210 1 O VAL D 209 N ASN D 157
SHEET 1 L 5 LEU D 333 ILE D 334 0
SHEET 2 L 5 GLU D 306 CYS D 312 1 N MET D 310 O LEU D 333
SHEET 3 L 5 ARG D 282 GLY D 287 1 N VAL D 283 O VAL D 308
SHEET 4 L 5 LEU D 352 GLY D 355 1 O LEU D 354 N PHE D 286
SHEET 5 L 5 CYS D 370 VAL D 372 1 O ALA D 371 N GLY D 355
LINK SG CYS A 26 FE1 SF4 A 425 1555 1555 2.52
LINK SG CYS A 51 FE3 SF4 A 425 1555 1555 2.59
LINK SG CYS A 112 FE4 SF4 A 425 1555 1555 2.48
LINK FE2 SF4 A 425 SG CYS B 36 1555 1555 2.46
LINK SG CYS C 26 FE1 SF4 C 425 1555 1555 2.44
LINK SG CYS C 51 FE3 SF4 C 425 1555 1555 2.37
LINK SG CYS C 112 FE4 SF4 C 425 1555 1555 2.43
LINK FE2 SF4 C 425 SG CYS D 36 1555 1555 2.54
CISPEP 1 ALA A 133 PRO A 134 0 -17.82
CISPEP 2 LEU A 202 PRO A 203 0 6.19
CISPEP 3 ALA B 190 PRO B 191 0 4.69
CISPEP 4 ALA B 375 PRO B 376 0 1.47
CISPEP 5 ALA C 80 GLY C 81 0 -18.46
CISPEP 6 ALA C 133 PRO C 134 0 -5.62
CISPEP 7 GLY C 197 PRO C 198 0 -13.84
CISPEP 8 LEU C 202 PRO C 203 0 3.32
CISPEP 9 ALA D 190 PRO D 191 0 3.71
CISPEP 10 ALA D 375 PRO D 376 0 4.95
SITE 1 AC1 10 CYS A 26 LEU A 28 CYS A 51 SER A 111
SITE 2 AC1 10 CYS A 112 GLY A 145 PRO B 33 GLY B 35
SITE 3 AC1 10 CYS B 36 THR B 96
SITE 1 AC2 9 CYS C 26 LEU C 28 CYS C 51 CYS C 112
SITE 2 AC2 9 PRO C 113 GLY C 145 GLY D 35 CYS D 36
SITE 3 AC2 9 THR D 96
CRYST1 80.442 81.440 95.864 102.53 110.89 94.44 P 1 2
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 0.012431 0.000965 0.005180 0.00000
SCALE2 0.000000 0.012316 0.003351 0.00000
SCALE3 0.000000 0.000000 0.011571 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
