HEADER ELECTRON TRANSPORT 04-JUL-13 4LJI
TITLE CRYSTAL STRUCTURE AT 1.5 ANGSTROM RESOLUTION OF THE PSBV2 CYTOCHROME
TITLE 2 FROM THE CYANOBACTERIUM THERMOSYNECHOCOCCUS ELONGATUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C-550-LIKE PROTEIN;
COMPND 3 CHAIN: A, B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;
SOURCE 3 ORGANISM_TAXID: 197221;
SOURCE 4 STRAIN: BP-1
KEYWDS CYTOCHROME C, ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SUGA,T.-L.LAI,M.SUGIURA,J.-R.SHEN,A.BOUSSAC
REVDAT 5 08-NOV-23 4LJI 1 REMARK
REVDAT 4 02-OCT-19 4LJI 1 COMPND HET HETNAM HETSYN
REVDAT 4 2 1 FORMUL LINK ATOM
REVDAT 3 16-OCT-13 4LJI 1 JRNL
REVDAT 2 18-SEP-13 4LJI 1 JRNL
REVDAT 1 28-AUG-13 4LJI 0
JRNL AUTH M.SUGA,T.-L.LAI,M.SUGIURA,J.-R.SHEN,A.BOUSSAC
JRNL TITL CRYSTAL STRUCTURE AT 1.5 ANGSTROM RESOLUTION OF THE PSBV2
JRNL TITL 2 CYTOCHROME FROM THE CYANOBACTERIUM THERMOSYNECHOCOCCUS
JRNL TITL 3 ELONGATUS
JRNL REF FEBS LETT. V. 587 3267 2013
JRNL REFN ISSN 0014-5793
JRNL PMID 23994160
JRNL DOI 10.1016/J.FEBSLET.2013.08.023
REMARK 2
REMARK 2 RESOLUTION. 1.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 72652
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 3653
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 45.4059 - 4.4652 0.94 2638 157 0.1866 0.2006
REMARK 3 2 4.4652 - 3.5446 0.93 2587 153 0.1783 0.1914
REMARK 3 3 3.5446 - 3.0967 0.96 2700 128 0.2169 0.2364
REMARK 3 4 3.0967 - 2.8136 0.97 2645 180 0.2166 0.2556
REMARK 3 5 2.8136 - 2.6119 0.97 2706 148 0.2221 0.3230
REMARK 3 6 2.6119 - 2.4580 0.96 2712 148 0.2202 0.2438
REMARK 3 7 2.4580 - 2.3349 0.96 2670 155 0.2236 0.2860
REMARK 3 8 2.3349 - 2.2332 0.96 2721 139 0.2204 0.2504
REMARK 3 9 2.2332 - 2.1473 0.97 2712 129 0.2145 0.2480
REMARK 3 10 2.1473 - 2.0732 0.97 2729 136 0.2252 0.2940
REMARK 3 11 2.0732 - 2.0083 0.98 2714 167 0.2206 0.2698
REMARK 3 12 2.0083 - 1.9509 0.98 2820 131 0.2298 0.2646
REMARK 3 13 1.9509 - 1.8996 0.99 2673 132 0.2348 0.2723
REMARK 3 14 1.8996 - 1.8532 0.99 2840 161 0.2367 0.2635
REMARK 3 15 1.8532 - 1.8111 0.99 2743 128 0.2335 0.3242
REMARK 3 16 1.8111 - 1.7726 0.98 2748 140 0.2370 0.3290
REMARK 3 17 1.7726 - 1.7371 0.94 2612 161 0.2419 0.2886
REMARK 3 18 1.7371 - 1.7043 0.94 2631 119 0.2452 0.2545
REMARK 3 19 1.7043 - 1.6739 0.94 2654 141 0.2453 0.3115
REMARK 3 20 1.6739 - 1.6455 0.94 2655 133 0.2547 0.2824
REMARK 3 21 1.6455 - 1.6190 0.94 2575 149 0.2531 0.3294
REMARK 3 22 1.6190 - 1.5940 0.93 2620 123 0.2521 0.2732
REMARK 3 23 1.5940 - 1.5706 0.92 2663 120 0.2457 0.2741
REMARK 3 24 1.5706 - 1.5485 0.92 2519 127 0.2579 0.2833
REMARK 3 25 1.5485 - 1.5276 0.92 2666 143 0.2646 0.2514
REMARK 3 26 1.5276 - 1.5077 0.74 2046 105 0.2829 0.3397
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.320
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.68
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.67
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 : 0.011 2202
REMARK 3 ANGLE : 1.415 3026
REMARK 3 CHIRALITY : 0.101 338
REMARK 3 PLANARITY : 0.008 384
REMARK 3 DIHEDRAL : 13.455 822
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0045 -0.4565 0.0780
REMARK 3 T TENSOR
REMARK 3 T11: 0.1138 T22: 0.1172
REMARK 3 T33: 0.1234 T12: 0.0101
REMARK 3 T13: -0.0225 T23: 0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 0.6825 L22: 1.1149
REMARK 3 L33: 1.8456 L12: 0.1188
REMARK 3 L13: -0.4319 L23: 0.9227
REMARK 3 S TENSOR
REMARK 3 S11: 0.0324 S12: -0.0286 S13: -0.0073
REMARK 3 S21: -0.0002 S22: 0.0601 S23: -0.0275
REMARK 3 S31: 0.0055 S32: 0.0289 S33: -0.0870
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE ENTRY CONTAINS FRIEDEL PAIRS IN
REMARK 3 F_PLUS/MINUS COLUMNS
REMARK 4
REMARK 4 4LJI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000080707.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72721
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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: NULL
REMARK 200 STARTING MODEL: 3ARC
REMARK 200
REMARK 200 REMARK: THE ENTRY CONTAINS FRIEDEL PAIRS IN F_PLUS/MINUS COLUMNS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5, VAPOR DIFFUSION, SITTING 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 1
REMARK 465 SER A 135
REMARK 465 PHE A 136
REMARK 465 PRO A 137
REMARK 465 ASP A 138
REMARK 465 SER A 139
REMARK 465 ALA A 140
REMARK 465 PRO A 141
REMARK 465 ALA B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 134
REMARK 465 SER B 135
REMARK 465 PHE B 136
REMARK 465 PRO B 137
REMARK 465 ASP B 138
REMARK 465 SER B 139
REMARK 465 ALA B 140
REMARK 465 PRO B 141
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 134 CG CD OE1 OE2
REMARK 470 VAL B 133 CG1 CG2
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 ASP A 16 -86.53 -103.79
REMARK 500 ASN A 59 84.98 -150.54
REMARK 500 VAL A 62 73.84 -119.18
REMARK 500 ARG A 76 49.77 -107.27
REMARK 500 SER A 88 86.01 -152.50
REMARK 500 ASP B 16 -79.46 -110.89
REMARK 500 CYS B 47 -31.81 -132.78
REMARK 500 ASN B 59 80.60 -162.38
REMARK 500 VAL B 62 64.95 -111.86
REMARK 500 ARG B 76 53.59 -106.08
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 HEC A 301 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 51 NE2
REMARK 620 2 HEC A 301 NA 90.1
REMARK 620 3 HEC A 301 NB 86.8 90.2
REMARK 620 4 HEC A 301 NC 85.6 174.9 86.8
REMARK 620 5 HEC A 301 ND 90.1 89.7 176.9 93.1
REMARK 620 6 CYS A 101 SG 174.2 88.4 87.6 95.5 95.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B 301 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 51 NE2
REMARK 620 2 HEC B 301 NA 89.8
REMARK 620 3 HEC B 301 NB 88.8 91.3
REMARK 620 4 HEC B 301 NC 87.3 176.2 86.1
REMARK 620 5 HEC B 301 ND 89.6 89.5 178.1 92.9
REMARK 620 6 CYS B 101 SG 173.7 90.4 85.0 92.2 96.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 301
DBREF 4LJI A 1 141 UNP Q8DJE2 PSBV2_THEEB 35 175
DBREF 4LJI B 1 141 UNP Q8DJE2 PSBV2_THEEB 35 175
SEQRES 1 A 141 ALA ALA GLY VAL ASP ASN TYR VAL ILE GLN TYR LEU LYS
SEQRES 2 A 141 VAL THR ASP THR VAL GLU LEU PRO VAL ASN ASP ARG GLY
SEQRES 3 A 141 GLU THR LYS THR PHE THR ALA VAL ASP LEU THR ARG GLY
SEQRES 4 A 141 LYS ARG LEU PHE GLU GLU ASN CYS LYS ASN CYS HIS VAL
SEQRES 5 A 141 GLY GLY SER THR LEU PRO ASN PRO LEU VAL SER LEU SER
SEQRES 6 A 141 LEU LYS ASP LEU LYS GLY ALA THR PRO PRO ARG ASP THR
SEQRES 7 A 141 ILE ALA SER LEU VAL ALA PHE GLN ARG SER PRO LYS SER
SEQRES 8 A 141 TYR ASP GLY SER GLU GLU SER TYR SER CYS ARG ARG VAL
SEQRES 9 A 141 SER GLU ASP TRP LEU THR THR GLU GLN LEU GLU THR LEU
SEQRES 10 A 141 ALA ALA PHE ILE LEU ARG ALA ALA ALA VAL ALA PRO GLY
SEQRES 11 A 141 TRP GLY VAL GLU SER PHE PRO ASP SER ALA PRO
SEQRES 1 B 141 ALA ALA GLY VAL ASP ASN TYR VAL ILE GLN TYR LEU LYS
SEQRES 2 B 141 VAL THR ASP THR VAL GLU LEU PRO VAL ASN ASP ARG GLY
SEQRES 3 B 141 GLU THR LYS THR PHE THR ALA VAL ASP LEU THR ARG GLY
SEQRES 4 B 141 LYS ARG LEU PHE GLU GLU ASN CYS LYS ASN CYS HIS VAL
SEQRES 5 B 141 GLY GLY SER THR LEU PRO ASN PRO LEU VAL SER LEU SER
SEQRES 6 B 141 LEU LYS ASP LEU LYS GLY ALA THR PRO PRO ARG ASP THR
SEQRES 7 B 141 ILE ALA SER LEU VAL ALA PHE GLN ARG SER PRO LYS SER
SEQRES 8 B 141 TYR ASP GLY SER GLU GLU SER TYR SER CYS ARG ARG VAL
SEQRES 9 B 141 SER GLU ASP TRP LEU THR THR GLU GLN LEU GLU THR LEU
SEQRES 10 B 141 ALA ALA PHE ILE LEU ARG ALA ALA ALA VAL ALA PRO GLY
SEQRES 11 B 141 TRP GLY VAL GLU SER PHE PRO ASP SER ALA PRO
HET HEC A 301 43
HET CL A 302 1
HET HEC B 301 43
HETNAM HEC HEME C
HETNAM CL CHLORIDE ION
FORMUL 3 HEC 2(C34 H34 FE N4 O4)
FORMUL 4 CL CL 1-
FORMUL 6 HOH *121(H2 O)
HELIX 1 1 ASP A 5 TYR A 11 1 7
HELIX 2 2 ALA A 33 CYS A 47 1 15
HELIX 3 3 CYS A 47 VAL A 52 1 6
HELIX 4 4 GLY A 53 SER A 55 5 3
HELIX 5 5 SER A 65 GLY A 71 1 7
HELIX 6 6 THR A 78 SER A 88 1 11
HELIX 7 7 THR A 110 ALA A 128 1 19
HELIX 8 8 ASP B 5 TYR B 11 1 7
HELIX 9 9 ALA B 33 CYS B 47 1 15
HELIX 10 10 CYS B 47 VAL B 52 1 6
HELIX 11 11 GLY B 53 SER B 55 5 3
HELIX 12 12 SER B 65 LYS B 70 1 6
HELIX 13 13 THR B 78 SER B 88 1 11
HELIX 14 14 THR B 110 ALA B 128 1 19
SHEET 1 A 2 THR A 17 PRO A 21 0
SHEET 2 A 2 THR A 28 THR A 32 -1 O PHE A 31 N VAL A 18
SHEET 1 B 2 THR B 17 PRO B 21 0
SHEET 2 B 2 THR B 28 THR B 32 -1 O PHE B 31 N VAL B 18
LINK SG CYS A 47 CAB HEC A 301 1555 1555 1.67
LINK SG CYS A 50 CAC HEC A 301 1555 1555 1.86
LINK SG CYS B 47 CAB HEC B 301 1555 1555 1.66
LINK SG CYS B 50 CAC HEC B 301 1555 1555 1.85
LINK NE2 HIS A 51 FE HEC A 301 1555 1555 2.11
LINK SG CYS A 101 FE HEC A 301 1555 1555 2.22
LINK NE2 HIS B 51 FE HEC B 301 1555 1555 2.15
LINK SG CYS B 101 FE HEC B 301 1555 1555 2.19
CISPEP 1 THR A 73 PRO A 74 0 -10.00
CISPEP 2 THR B 73 PRO B 74 0 -7.36
SITE 1 AC1 22 ASN A 46 CYS A 47 CYS A 50 HIS A 51
SITE 2 AC1 22 THR A 56 VAL A 62 SER A 63 LEU A 64
SITE 3 AC1 22 ASP A 68 ARG A 76 LEU A 82 PHE A 85
SITE 4 AC1 22 GLN A 86 TYR A 92 SER A 98 SER A 100
SITE 5 AC1 22 CYS A 101 ARG A 102 ILE A 121 HOH A 401
SITE 6 AC1 22 HOH A 404 ASN B 49
SITE 1 AC2 2 ASN A 46 ARG A 102
SITE 1 AC3 23 ASN B 46 CYS B 47 CYS B 50 HIS B 51
SITE 2 AC3 23 THR B 56 VAL B 62 SER B 63 LEU B 64
SITE 3 AC3 23 ASP B 68 LEU B 69 ALA B 72 ARG B 76
SITE 4 AC3 23 LEU B 82 PHE B 85 GLN B 86 TYR B 92
SITE 5 AC3 23 SER B 98 SER B 100 CYS B 101 ARG B 102
SITE 6 AC3 23 ILE B 121 HOH B 401 HOH B 402
CRYST1 38.421 38.430 47.779 71.86 82.22 69.38 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 0.026027 -0.009793 -0.000805 0.00000
SCALE2 0.000000 0.027802 -0.008245 0.00000
SCALE3 0.000000 0.000000 0.022034 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
