HEADER ELECTRON TRANSPORT 25-AUG-09 3IS7
TITLE STRUCTURE OF MINERALIZED BFRB FROM PSEUDOMONAS AERUGINOSA TO 2.1A
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BACTERIOFERRITIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U,
COMPND 4 V, W, X;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: BFRB, PA3531;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ARCTIC EXPRESS RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS ELECTRON TRANSPORT; IRON STORAGE, HEME, IRON, IRON STORAGE, METAL-
KEYWDS 2 BINDING, ELECTRON TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR S.LOVELL,S.K.WEERATUNGA,K.P.BATTAILE,M.RIVERA
REVDAT 4 06-SEP-23 3IS7 1 REMARK LINK
REVDAT 3 01-NOV-17 3IS7 1 REMARK
REVDAT 2 23-FEB-10 3IS7 1 JRNL
REVDAT 1 02-FEB-10 3IS7 0
JRNL AUTH S.K.WEERATUNGA,S.LOVELL,H.YAO,K.P.BATTAILE,C.J.FISCHER,
JRNL AUTH 2 C.E.GEE,M.RIVERA
JRNL TITL STRUCTURAL STUDIES OF BACTERIOFERRITIN B FROM PSEUDOMONAS
JRNL TITL 2 AERUGINOSA SUGGEST A GATING MECHANISM FOR IRON UPTAKE VIA
JRNL TITL 3 THE FERROXIDASE CENTER
JRNL REF BIOCHEMISTRY V. 49 1160 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20067302
JRNL DOI 10.1021/BI9015204
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.5.0066
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 307096
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) : 0.196
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 15512
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 21218
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 1145
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 30298
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 522
REMARK 3 SOLVENT ATOMS : 1512
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.54000
REMARK 3 B22 (A**2) : -0.43000
REMARK 3 B33 (A**2) : -0.11000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.184
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.174
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.121
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.552
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 31402 ; 0.021 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 28223 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 42496 ; 1.824 ; 2.013
REMARK 3 BOND ANGLES OTHERS (DEGREES): 65792 ; 0.844 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3675 ; 4.988 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1679 ;38.071 ;25.855
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 5972 ;17.515 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 120 ;25.247 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 4612 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 34505 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 5571 ; 0.000 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 18280 ; 0.931 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7637 ; 0.277 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 29305 ; 1.765 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 13122 ; 3.233 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 13191 ; 5.249 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3IS7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-09.
REMARK 100 THE DEPOSITION ID IS D_1000054799.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
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 210R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, D*TREK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 309226
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 47.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : 0.10900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1620
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.66900
REMARK 200 R SYM FOR SHELL (I) : 0.66900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.007
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLREP
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1BFR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% MPD, 100MM MES, 200MM LI2SO4, PH
REMARK 280 6.0, VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 62.90300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 103.77300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 101.37800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 103.77300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 62.90300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 101.37800
REMARK 290 SMTRY3 4 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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.
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: 24-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 24-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 80000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 131800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -553.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S,
REMARK 350 AND CHAINS: T, U, V, W, X
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LYS A 2
REMARK 465 GLY A 3
REMARK 465 ASP A 157
REMARK 465 ASP A 158
REMARK 465 MET B 1
REMARK 465 LYS B 2
REMARK 465 ASP B 157
REMARK 465 ASP B 158
REMARK 465 MET C 1
REMARK 465 ASP C 157
REMARK 465 ASP C 158
REMARK 465 MET D 1
REMARK 465 LYS D 2
REMARK 465 ASP D 157
REMARK 465 ASP D 158
REMARK 465 MET E 1
REMARK 465 LYS E 2
REMARK 465 ASP E 157
REMARK 465 ASP E 158
REMARK 465 MET F 1
REMARK 465 LYS F 2
REMARK 465 ASP F 157
REMARK 465 ASP F 158
REMARK 465 MET G 1
REMARK 465 LYS G 2
REMARK 465 ASP G 157
REMARK 465 ASP G 158
REMARK 465 MET H 1
REMARK 465 ASP H 157
REMARK 465 ASP H 158
REMARK 465 MET I 1
REMARK 465 LYS I 2
REMARK 465 ASP I 157
REMARK 465 ASP I 158
REMARK 465 MET J 1
REMARK 465 LYS J 2
REMARK 465 ASP J 157
REMARK 465 ASP J 158
REMARK 465 MET K 1
REMARK 465 LYS K 2
REMARK 465 ASP K 157
REMARK 465 ASP K 158
REMARK 465 MET L 1
REMARK 465 LYS L 2
REMARK 465 ASP L 157
REMARK 465 ASP L 158
REMARK 465 MET M 1
REMARK 465 LYS M 2
REMARK 465 ASP M 157
REMARK 465 ASP M 158
REMARK 465 MET N 1
REMARK 465 LYS N 2
REMARK 465 ASP N 157
REMARK 465 ASP N 158
REMARK 465 MET O 1
REMARK 465 LYS O 2
REMARK 465 ASP O 157
REMARK 465 ASP O 158
REMARK 465 MET P 1
REMARK 465 LYS P 2
REMARK 465 ASP P 157
REMARK 465 ASP P 158
REMARK 465 MET Q 1
REMARK 465 LYS Q 2
REMARK 465 ASP Q 157
REMARK 465 ASP Q 158
REMARK 465 MET R 1
REMARK 465 ASP R 157
REMARK 465 ASP R 158
REMARK 465 MET S 1
REMARK 465 LYS S 2
REMARK 465 ASP S 157
REMARK 465 ASP S 158
REMARK 465 MET T 1
REMARK 465 LYS T 2
REMARK 465 ASP T 157
REMARK 465 ASP T 158
REMARK 465 MET U 1
REMARK 465 LYS U 2
REMARK 465 ASP U 157
REMARK 465 ASP U 158
REMARK 465 MET V 1
REMARK 465 LYS V 2
REMARK 465 ASP V 157
REMARK 465 ASP V 158
REMARK 465 MET W 1
REMARK 465 ASP W 157
REMARK 465 ASP W 158
REMARK 465 MET X 1
REMARK 465 LYS X 2
REMARK 465 ASP X 157
REMARK 465 ASP X 158
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 LYS A 5 CG CD CE NZ
REMARK 470 LYS A 6 CD CE NZ
REMARK 470 LYS A 57 CE NZ
REMARK 470 LYS A 76 CD CE NZ
REMARK 470 LYS A 121 CE NZ
REMARK 470 LYS B 5 CE NZ
REMARK 470 LYS B 6 CD CE NZ
REMARK 470 LYS B 121 CE NZ
REMARK 470 LYS C 2 CG CD CE NZ
REMARK 470 LYS C 5 CD CE NZ
REMARK 470 LYS C 6 CE NZ
REMARK 470 LYS C 38 CE NZ
REMARK 470 LYS C 99 CD CE NZ
REMARK 470 LYS C 121 CD CE NZ
REMARK 470 LYS D 6 CE NZ
REMARK 470 LYS D 76 NZ
REMARK 470 LYS E 5 CE NZ
REMARK 470 LYS E 6 CE NZ
REMARK 470 LYS E 57 CE NZ
REMARK 470 LYS E 76 CE NZ
REMARK 470 LYS E 121 CE NZ
REMARK 470 LYS F 5 CD CE NZ
REMARK 470 LYS F 6 CD CE NZ
REMARK 470 LYS F 76 NZ
REMARK 470 LYS F 121 CE NZ
REMARK 470 LYS G 57 CE NZ
REMARK 470 LYS G 76 NZ
REMARK 470 LYS H 2 CE NZ
REMARK 470 LYS H 5 CE NZ
REMARK 470 LYS H 57 CE NZ
REMARK 470 LYS H 121 CE NZ
REMARK 470 LYS I 5 CD CE NZ
REMARK 470 LYS I 76 CE NZ
REMARK 470 LYS I 121 CE NZ
REMARK 470 LYS J 5 CE NZ
REMARK 470 LYS J 6 CD CE NZ
REMARK 470 LYS J 57 CE NZ
REMARK 470 LYS J 121 CD CE NZ
REMARK 470 LYS K 57 CE NZ
REMARK 470 LYS L 5 CD CE NZ
REMARK 470 LYS L 6 CE NZ
REMARK 470 LYS L 121 NZ
REMARK 470 LYS M 5 CD CE NZ
REMARK 470 LYS M 76 NZ
REMARK 470 GLU M 81 CD OE1 OE2
REMARK 470 LYS M 121 CE NZ
REMARK 470 LYS N 5 CE NZ
REMARK 470 LYS N 57 CE NZ
REMARK 470 LYS N 76 CD CE NZ
REMARK 470 LYS N 99 NZ
REMARK 470 LYS N 121 NZ
REMARK 470 LYS O 5 CE NZ
REMARK 470 LYS O 6 CD CE NZ
REMARK 470 LYS O 57 CE NZ
REMARK 470 LYS O 76 CD CE NZ
REMARK 470 LYS P 5 CD CE NZ
REMARK 470 LYS P 57 CE NZ
REMARK 470 LYS P 76 CE NZ
REMARK 470 LYS Q 5 NZ
REMARK 470 LYS Q 6 CE NZ
REMARK 470 LYS Q 57 CE NZ
REMARK 470 LYS Q 76 CE NZ
REMARK 470 LYS Q 121 CE NZ
REMARK 470 LYS R 6 CE NZ
REMARK 470 LYS R 57 CE NZ
REMARK 470 LYS R 121 CE NZ
REMARK 470 LYS S 5 CD CE NZ
REMARK 470 LYS S 6 CE NZ
REMARK 470 LYS S 57 CE NZ
REMARK 470 LYS S 121 CD CE NZ
REMARK 470 LYS T 6 CD CE NZ
REMARK 470 LYS T 38 CE NZ
REMARK 470 LYS T 57 CE NZ
REMARK 470 LYS T 121 CD CE NZ
REMARK 470 LYS U 5 CD CE NZ
REMARK 470 LYS U 121 CE NZ
REMARK 470 LYS V 5 CE NZ
REMARK 470 LYS V 57 CE NZ
REMARK 470 LYS V 76 CE NZ
REMARK 470 LYS V 99 CD CE NZ
REMARK 470 LYS W 57 CE NZ
REMARK 470 LYS W 99 CE NZ
REMARK 470 LYS X 5 CD CE NZ
REMARK 470 LYS X 6 NZ
REMARK 470 LYS X 99 CE NZ
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 CG2 THR J 98 O HOH J 452 1.89
REMARK 500 OD1 ASP G 34 O HOH G 1089 1.93
REMARK 500 OH TYR M 45 O HOH M 1334 1.94
REMARK 500 OE1 GLU A 135 NZ LYS W 2 2.01
REMARK 500 OE1 GLU E 18 OE1 GLU E 51 2.02
REMARK 500 OE1 GLN B 84 O HOH B 733 2.06
REMARK 500 CG2 THR I 98 O HOH I 1235 2.07
REMARK 500 OE1 GLN W 88 O HOH W 1474 2.09
REMARK 500 OE1 GLU A 127 O HOH A 1216 2.13
REMARK 500 CG2 THR K 98 O HOH K 356 2.13
REMARK 500 OE1 GLN U 88 O HOH U 216 2.15
REMARK 500 OD1 ASP K 50 O HOH K 1293 2.16
REMARK 500 NZ LYS N 96 OD2 ASP N 100 2.17
REMARK 500 O HOH B 1047 O HOH B 1465 2.17
REMARK 500 OE2 GLU P 44 OD2 ASP P 90 2.17
REMARK 500 OE2 GLU A 94 O HOH A 1216 2.17
REMARK 500 O2D HEM F 159 O HOH F 1019 2.18
REMARK 500 NE2 GLN K 84 O HOH K 541 2.18
REMARK 500 CG2 THR V 98 O HOH V 391 2.18
REMARK 500 O LYS G 76 O HOH G 1360 2.19
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 LEU A 63 CB - CG - CD1 ANGL. DEV. = 11.0 DEGREES
REMARK 500 ASP A 90 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG A 117 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG B 117 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG B 117 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 LEU C 101 CB - CG - CD1 ANGL. DEV. = 13.4 DEGREES
REMARK 500 LEU D 101 CA - CB - CG ANGL. DEV. = 14.9 DEGREES
REMARK 500 ARG D 117 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG E 117 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG F 30 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG F 117 NE - CZ - NH1 ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG F 117 NE - CZ - NH2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 LEU F 134 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 LEU G 63 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 ARG G 117 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG G 117 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 LEU H 63 CA - CB - CG ANGL. DEV. = 15.5 DEGREES
REMARK 500 LEU H 63 CB - CG - CD1 ANGL. DEV. = 12.7 DEGREES
REMARK 500 ARG H 117 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG H 117 NE - CZ - NH2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ASP J 90 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG J 117 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG K 30 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 LEU K 101 CA - CB - CG ANGL. DEV. = 15.7 DEGREES
REMARK 500 ARG K 117 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG K 117 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP L 56 CB - CG - OD1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP L 56 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ASP M 56 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 LEU M 63 CB - CG - CD1 ANGL. DEV. = 10.3 DEGREES
REMARK 500 ARG M 117 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 LEU O 63 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 LEU O 101 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 ARG P 117 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG Q 117 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG Q 117 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG R 117 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG S 117 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG T 117 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG T 117 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG U 30 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ASP U 90 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG U 117 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG U 117 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG V 117 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG V 117 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG W 117 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG W 117 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP W 132 CB - CG - OD1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP X 56 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 51 ANGLE DEVIATIONS.
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 LEU E 37 73.66 -100.35
REMARK 500 GLU J 66 34.89 73.12
REMARK 500 LEU L 37 71.21 -100.95
REMARK 500 LEU P 37 68.59 -100.20
REMARK 500 LEU Q 37 68.62 -102.09
REMARK 500 LEU S 37 68.72 -105.48
REMARK 500 GLU U 66 37.55 73.79
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 HEM A 159 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 52 SD
REMARK 620 2 HEM A 159 NA 85.7
REMARK 620 3 HEM A 159 NB 92.7 84.3
REMARK 620 4 HEM A 159 NC 93.2 177.7 93.7
REMARK 620 5 HEM A 159 ND 83.8 90.8 174.2 91.2
REMARK 620 6 MET B 52 SD 167.2 85.3 95.4 96.1 87.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 160 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 148 OD1
REMARK 620 2 GLN A 151 OE1 74.1
REMARK 620 3 ASN L 148 OD1 77.0 73.9
REMARK 620 4 GLN L 151 OE1 144.7 78.3 74.6
REMARK 620 5 GLN M 151 OE1 142.3 123.7 137.0 72.2
REMARK 620 6 GLN X 151 OE1 72.1 77.3 142.3 122.3 79.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 159 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 148 OD1
REMARK 620 2 GLN B 151 OE1 78.6
REMARK 620 3 ASN D 148 OD1 71.4 144.1
REMARK 620 4 GLN D 151 OE1 73.4 76.4 76.5
REMARK 620 5 ASN F 148 OD1 115.1 137.6 74.8 144.9
REMARK 620 6 GLN F 151 OE1 137.8 121.1 73.7 75.9 76.9
REMARK 620 7 GLN H 151 OE1 145.7 75.0 139.9 119.9 73.5 75.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 159 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET C 52 SD
REMARK 620 2 HEM C 159 NA 85.7
REMARK 620 3 HEM C 159 NB 92.3 83.9
REMARK 620 4 HEM C 159 NC 91.1 174.5 91.7
REMARK 620 5 HEM C 159 ND 85.1 98.0 176.6 86.2
REMARK 620 6 MET D 52 SD 169.4 87.6 95.1 96.2 87.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 160 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN C 151 OE1
REMARK 620 2 ASN K 148 OD1 147.4
REMARK 620 3 GLN K 151 OE1 77.6 77.8
REMARK 620 4 GLN S 151 OE1 122.1 72.5 78.0
REMARK 620 5 GLN U 151 OE1 75.8 136.2 122.9 75.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM F 159 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET E 52 SD
REMARK 620 2 HEM F 159 NA 86.8
REMARK 620 3 HEM F 159 NB 91.8 85.9
REMARK 620 4 HEM F 159 NC 94.4 177.5 91.9
REMARK 620 5 HEM F 159 ND 85.1 94.4 176.9 87.9
REMARK 620 6 MET F 52 SD 165.8 82.7 97.1 96.4 86.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K E 159 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN E 148 OD1
REMARK 620 2 GLN E 151 OE1 74.4
REMARK 620 3 GLN J 151 OE1 142.8 77.6
REMARK 620 4 GLN Q 151 OE1 133.8 123.6 82.4
REMARK 620 5 GLN V 151 OE1 71.6 76.6 124.5 72.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM H 159 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET G 52 SD
REMARK 620 2 HEM H 159 NA 87.8
REMARK 620 3 HEM H 159 NB 97.3 85.2
REMARK 620 4 HEM H 159 NC 94.2 176.4 91.5
REMARK 620 5 HEM H 159 ND 85.3 91.3 175.6 91.8
REMARK 620 6 MET H 52 SD 169.0 84.6 89.9 93.9 87.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K G 159 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN G 151 OE1
REMARK 620 2 GLN I 151 OE1 75.2
REMARK 620 3 GLN O 151 OE1 123.2 77.6
REMARK 620 4 GLN W 151 OE1 77.4 123.0 77.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM J 159 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET I 52 SD
REMARK 620 2 HEM J 159 NA 85.3
REMARK 620 3 HEM J 159 NB 93.7 81.4
REMARK 620 4 HEM J 159 NC 90.4 174.5 95.5
REMARK 620 5 HEM J 159 ND 82.6 98.3 176.3 84.5
REMARK 620 6 MET J 52 SD 168.9 86.6 92.5 98.1 91.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM K 159 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET K 52 SD
REMARK 620 2 HEM K 159 NA 85.0
REMARK 620 3 HEM K 159 NB 92.0 87.1
REMARK 620 4 HEM K 159 NC 88.2 172.6 90.3
REMARK 620 5 HEM K 159 ND 80.7 94.6 172.3 87.1
REMARK 620 6 MET L 52 SD 168.4 86.4 95.3 100.7 92.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM N 159 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET M 52 SD
REMARK 620 2 HEM N 159 NA 87.1
REMARK 620 3 HEM N 159 NB 96.0 85.6
REMARK 620 4 HEM N 159 NC 94.0 175.1 89.5
REMARK 620 5 HEM N 159 ND 87.5 95.5 176.4 89.3
REMARK 620 6 MET N 52 SD 167.8 85.9 93.5 93.7 83.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K N 160 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN N 148 OD1
REMARK 620 2 GLN P 151 OE1 75.8
REMARK 620 3 GLN R 151 OE1 142.3 73.7
REMARK 620 4 GLN T 151 OE1 142.1 118.4 73.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM P 159 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET O 52 SD
REMARK 620 2 HEM P 159 NA 85.5
REMARK 620 3 HEM P 159 NB 98.4 85.7
REMARK 620 4 HEM P 159 NC 97.9 175.8 91.5
REMARK 620 5 HEM P 159 ND 86.3 97.3 174.7 85.4
REMARK 620 6 MET P 52 SD 165.2 83.8 91.0 93.2 84.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM Q 159 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET Q 52 SD
REMARK 620 2 HEM Q 159 NA 86.5
REMARK 620 3 HEM Q 159 NB 95.2 82.9
REMARK 620 4 HEM Q 159 NC 94.8 176.9 94.2
REMARK 620 5 HEM Q 159 ND 83.6 95.4 178.0 87.5
REMARK 620 6 MET R 52 SD 169.1 89.0 94.0 90.2 87.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM S 159 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET S 52 SD
REMARK 620 2 HEM S 159 NA 86.7
REMARK 620 3 HEM S 159 NB 94.9 84.7
REMARK 620 4 HEM S 159 NC 90.9 176.7 97.8
REMARK 620 5 HEM S 159 ND 84.4 97.1 178.0 80.4
REMARK 620 6 MET T 52 SD 170.6 85.9 90.3 96.2 90.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM V 159 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET U 52 SD
REMARK 620 2 HEM V 159 NA 87.6
REMARK 620 3 HEM V 159 NB 93.6 85.2
REMARK 620 4 HEM V 159 NC 92.8 178.5 93.3
REMARK 620 5 HEM V 159 ND 85.6 96.0 178.6 85.5
REMARK 620 6 MET V 52 SD 168.9 84.5 93.4 95.3 87.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM X 159 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET W 52 SD
REMARK 620 2 HEM X 159 NA 87.2
REMARK 620 3 HEM X 159 NB 94.1 94.0
REMARK 620 4 HEM X 159 NC 95.0 177.7 86.8
REMARK 620 5 HEM X 159 ND 87.0 90.4 175.5 88.8
REMARK 620 6 MET X 52 SD 166.6 84.8 97.2 92.9 82.3
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 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM H 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM J 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM K 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM N 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K N 160
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM P 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM Q 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM S 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM V 159
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM X 159
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3IS8 RELATED DB: PDB
REMARK 900 RELATED ID: 3ISE RELATED DB: PDB
REMARK 900 RELATED ID: 3ISF RELATED DB: PDB
DBREF 3IS7 A 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 B 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 C 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 D 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 E 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 F 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 G 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 H 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 I 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 J 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 K 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 L 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 M 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 N 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 O 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 P 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 Q 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 R 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 S 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 T 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 U 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 V 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 W 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
DBREF 3IS7 X 1 158 UNP Q9HY79 Q9HY79_PSEAE 1 158
SEQRES 1 A 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 A 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 A 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 A 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 A 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 A 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 A 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 A 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 A 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 A 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 A 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 A 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 A 158 ASP ASP
SEQRES 1 B 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 B 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 B 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 B 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 B 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 B 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 B 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 B 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 B 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 B 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 B 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 B 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 B 158 ASP ASP
SEQRES 1 C 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 C 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 C 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 C 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 C 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 C 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 C 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 C 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 C 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 C 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 C 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 C 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 C 158 ASP ASP
SEQRES 1 D 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 D 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 D 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 D 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 D 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 D 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 D 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 D 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 D 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 D 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 D 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 D 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 D 158 ASP ASP
SEQRES 1 E 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 E 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 E 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 E 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 E 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 E 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 E 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 E 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 E 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 E 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 E 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 E 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 E 158 ASP ASP
SEQRES 1 F 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 F 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 F 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 F 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 F 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 F 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 F 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 F 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 F 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 F 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 F 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 F 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 F 158 ASP ASP
SEQRES 1 G 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 G 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 G 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 G 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 G 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 G 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 G 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 G 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 G 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 G 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 G 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 G 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 G 158 ASP ASP
SEQRES 1 H 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 H 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 H 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 H 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 H 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 H 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 H 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 H 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 H 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 H 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 H 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 H 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 H 158 ASP ASP
SEQRES 1 I 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 I 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 I 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 I 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 I 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 I 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 I 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 I 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 I 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 I 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 I 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 I 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 I 158 ASP ASP
SEQRES 1 J 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 J 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 J 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 J 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 J 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 J 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 J 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 J 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 J 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 J 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 J 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 J 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 J 158 ASP ASP
SEQRES 1 K 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 K 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 K 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 K 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 K 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 K 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 K 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 K 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 K 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 K 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 K 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 K 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 K 158 ASP ASP
SEQRES 1 L 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 L 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 L 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 L 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 L 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 L 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 L 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 L 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 L 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 L 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 L 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 L 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 L 158 ASP ASP
SEQRES 1 M 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 M 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 M 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 M 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 M 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 M 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 M 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 M 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 M 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 M 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 M 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 M 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 M 158 ASP ASP
SEQRES 1 N 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 N 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 N 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 N 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 N 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 N 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 N 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 N 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 N 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 N 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 N 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 N 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 N 158 ASP ASP
SEQRES 1 O 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 O 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 O 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 O 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 O 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 O 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 O 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 O 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 O 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 O 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 O 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 O 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 O 158 ASP ASP
SEQRES 1 P 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 P 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 P 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 P 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 P 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 P 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 P 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 P 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 P 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 P 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 P 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 P 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 P 158 ASP ASP
SEQRES 1 Q 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 Q 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 Q 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 Q 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 Q 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 Q 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 Q 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 Q 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 Q 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 Q 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 Q 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 Q 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 Q 158 ASP ASP
SEQRES 1 R 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 R 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 R 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 R 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 R 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 R 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 R 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 R 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 R 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 R 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 R 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 R 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 R 158 ASP ASP
SEQRES 1 S 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 S 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 S 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 S 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 S 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 S 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 S 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 S 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 S 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 S 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 S 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 S 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 S 158 ASP ASP
SEQRES 1 T 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 T 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 T 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 T 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 T 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 T 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 T 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 T 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 T 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 T 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 T 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 T 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 T 158 ASP ASP
SEQRES 1 U 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 U 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 U 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 U 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 U 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 U 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 U 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 U 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 U 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 U 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 U 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 U 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 U 158 ASP ASP
SEQRES 1 V 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 V 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 V 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 V 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 V 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 V 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 V 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 V 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 V 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 V 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 V 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 V 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 V 158 ASP ASP
SEQRES 1 W 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 W 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 W 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 W 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 W 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 W 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 W 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 W 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 W 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 W 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 W 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 W 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 W 158 ASP ASP
SEQRES 1 X 158 MET LYS GLY ASP LYS LYS VAL ILE GLN HIS LEU ASN LYS
SEQRES 2 X 158 ILE LEU GLY ASN GLU LEU ILE ALA ILE ASN GLN TYR PHE
SEQRES 3 X 158 LEU HIS SER ARG MET TRP ASN ASP TRP GLY LEU LYS ARG
SEQRES 4 X 158 LEU GLY ALA HIS GLU TYR HIS GLU SER ILE ASP GLU MET
SEQRES 5 X 158 LYS HIS ALA ASP LYS LEU ILE GLU ARG ILE LEU PHE LEU
SEQRES 6 X 158 GLU GLY LEU PRO ASN LEU GLN ASP LEU GLY LYS LEU LEU
SEQRES 7 X 158 ILE GLY GLU ASN THR GLN GLU MET LEU GLN CYS ASP LEU
SEQRES 8 X 158 ASN LEU GLU LEU LYS ALA THR LYS ASP LEU ARG GLU ALA
SEQRES 9 X 158 ILE VAL HIS CYS GLU GLN VAL HIS ASP TYR VAL SER ARG
SEQRES 10 X 158 ASP LEU LEU LYS ASP ILE LEU GLU SER GLU GLU GLU HIS
SEQRES 11 X 158 ILE ASP TYR LEU GLU THR GLN LEU GLY LEU ILE GLN LYS
SEQRES 12 X 158 VAL GLY LEU GLU ASN TYR LEU GLN SER HIS MET HIS GLU
SEQRES 13 X 158 ASP ASP
HET HEM A 159 43
HET K A 160 1
HET K B 159 1
HET HEM C 159 43
HET K C 160 1
HET K E 159 1
HET HEM F 159 43
HET K G 159 1
HET HEM H 159 43
HET HEM J 159 43
HET HEM K 159 43
HET HEM N 159 43
HET K N 160 1
HET HEM P 159 43
HET HEM Q 159 43
HET HEM S 159 43
HET HEM V 159 43
HET HEM X 159 43
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM K POTASSIUM ION
HETSYN HEM HEME
FORMUL 25 HEM 12(C34 H32 FE N4 O4)
FORMUL 26 K 6(K 1+)
FORMUL 43 HOH *1512(H2 O)
HELIX 1 1 ASP A 4 GLY A 36 1 33
HELIX 2 2 LEU A 37 LEU A 65 1 29
HELIX 3 3 ASN A 82 VAL A 111 1 30
HELIX 4 4 ASP A 113 GLY A 145 1 33
HELIX 5 5 GLY A 145 SER A 152 1 8
HELIX 6 6 ASP B 4 TRP B 35 1 32
HELIX 7 7 LEU B 37 LEU B 65 1 29
HELIX 8 8 ASN B 82 VAL B 111 1 30
HELIX 9 9 ASP B 113 GLY B 145 1 33
HELIX 10 10 GLY B 145 SER B 152 1 8
HELIX 11 11 ASP C 4 GLY C 36 1 33
HELIX 12 12 LEU C 37 LEU C 65 1 29
HELIX 13 13 ASN C 82 HIS C 112 1 31
HELIX 14 14 ASP C 113 GLY C 145 1 33
HELIX 15 15 GLY C 145 SER C 152 1 8
HELIX 16 16 ASP D 4 TRP D 35 1 32
HELIX 17 17 LEU D 37 LEU D 65 1 29
HELIX 18 18 ASN D 82 VAL D 111 1 30
HELIX 19 19 ASP D 113 GLY D 145 1 33
HELIX 20 20 GLY D 145 SER D 152 1 8
HELIX 21 21 ASP E 4 TRP E 35 1 32
HELIX 22 22 LEU E 37 LEU E 65 1 29
HELIX 23 23 ASN E 82 VAL E 111 1 30
HELIX 24 24 ASP E 113 GLY E 145 1 33
HELIX 25 25 GLY E 145 SER E 152 1 8
HELIX 26 26 ASP F 4 TRP F 35 1 32
HELIX 27 27 LEU F 37 LEU F 65 1 29
HELIX 28 28 ASN F 82 VAL F 111 1 30
HELIX 29 29 ASP F 113 GLY F 145 1 33
HELIX 30 30 GLY F 145 SER F 152 1 8
HELIX 31 31 ASP G 4 GLY G 36 1 33
HELIX 32 32 LEU G 37 LEU G 65 1 29
HELIX 33 33 ASN G 82 VAL G 111 1 30
HELIX 34 34 ASP G 113 GLY G 145 1 33
HELIX 35 35 GLY G 145 SER G 152 1 8
HELIX 36 36 ASP H 4 GLY H 36 1 33
HELIX 37 37 LEU H 37 LEU H 65 1 29
HELIX 38 38 ASN H 82 VAL H 111 1 30
HELIX 39 39 ASP H 113 GLY H 145 1 33
HELIX 40 40 GLY H 145 HIS H 153 1 9
HELIX 41 41 ASP I 4 TRP I 35 1 32
HELIX 42 42 LEU I 37 LEU I 65 1 29
HELIX 43 43 ASN I 82 VAL I 111 1 30
HELIX 44 44 ASP I 113 GLY I 145 1 33
HELIX 45 45 GLY I 145 SER I 152 1 8
HELIX 46 46 ASP J 4 GLY J 36 1 33
HELIX 47 47 LEU J 37 LEU J 65 1 29
HELIX 48 48 ASN J 82 VAL J 111 1 30
HELIX 49 49 ASP J 113 GLY J 145 1 33
HELIX 50 50 GLY J 145 SER J 152 1 8
HELIX 51 51 ASP K 4 TRP K 35 1 32
HELIX 52 52 LEU K 37 LEU K 65 1 29
HELIX 53 53 ASN K 82 HIS K 112 1 31
HELIX 54 54 ASP K 113 GLY K 145 1 33
HELIX 55 55 GLY K 145 SER K 152 1 8
HELIX 56 56 ASP L 4 TRP L 35 1 32
HELIX 57 57 LEU L 37 LEU L 65 1 29
HELIX 58 58 ASN L 82 VAL L 111 1 30
HELIX 59 59 ASP L 113 GLY L 145 1 33
HELIX 60 60 GLY L 145 SER L 152 1 8
HELIX 61 61 ASP M 4 TRP M 35 1 32
HELIX 62 62 LEU M 37 LEU M 65 1 29
HELIX 63 63 ASN M 82 VAL M 111 1 30
HELIX 64 64 ASP M 113 GLY M 145 1 33
HELIX 65 65 GLY M 145 SER M 152 1 8
HELIX 66 66 ASP N 4 TRP N 35 1 32
HELIX 67 67 LEU N 37 LEU N 65 1 29
HELIX 68 68 ASN N 82 HIS N 112 1 31
HELIX 69 69 ASP N 113 GLY N 145 1 33
HELIX 70 70 GLY N 145 SER N 152 1 8
HELIX 71 71 ASP O 4 TRP O 35 1 32
HELIX 72 72 LEU O 37 LEU O 65 1 29
HELIX 73 73 ASN O 82 VAL O 111 1 30
HELIX 74 74 ASP O 113 GLY O 145 1 33
HELIX 75 75 GLY O 145 SER O 152 1 8
HELIX 76 76 ASP P 4 TRP P 35 1 32
HELIX 77 77 LEU P 37 LEU P 65 1 29
HELIX 78 78 ASN P 82 HIS P 112 1 31
HELIX 79 79 ASP P 113 GLY P 145 1 33
HELIX 80 80 GLY P 145 SER P 152 1 8
HELIX 81 81 ASP Q 4 TRP Q 35 1 32
HELIX 82 82 LEU Q 37 LEU Q 65 1 29
HELIX 83 83 ASN Q 82 VAL Q 111 1 30
HELIX 84 84 ASP Q 113 GLY Q 145 1 33
HELIX 85 85 GLY Q 145 SER Q 152 1 8
HELIX 86 86 ASP R 4 TRP R 35 1 32
HELIX 87 87 LEU R 37 LEU R 65 1 29
HELIX 88 88 ASN R 82 HIS R 112 1 31
HELIX 89 89 ASP R 113 GLY R 145 1 33
HELIX 90 90 GLY R 145 SER R 152 1 8
HELIX 91 91 ASP S 4 GLY S 36 1 33
HELIX 92 92 LEU S 37 LEU S 65 1 29
HELIX 93 93 ASN S 82 VAL S 111 1 30
HELIX 94 94 ASP S 113 GLY S 145 1 33
HELIX 95 95 GLY S 145 SER S 152 1 8
HELIX 96 96 ASP T 4 GLY T 36 1 33
HELIX 97 97 LEU T 37 LEU T 65 1 29
HELIX 98 98 ASN T 82 VAL T 111 1 30
HELIX 99 99 ASP T 113 GLY T 145 1 33
HELIX 100 100 GLY T 145 SER T 152 1 8
HELIX 101 101 ASP U 4 GLY U 36 1 33
HELIX 102 102 LEU U 37 LEU U 65 1 29
HELIX 103 103 ASN U 82 VAL U 111 1 30
HELIX 104 104 ASP U 113 GLY U 145 1 33
HELIX 105 105 GLY U 145 SER U 152 1 8
HELIX 106 106 ASP V 4 GLY V 36 1 33
HELIX 107 107 LEU V 37 LEU V 65 1 29
HELIX 108 108 ASN V 82 HIS V 112 1 31
HELIX 109 109 ASP V 113 GLY V 145 1 33
HELIX 110 110 GLY V 145 SER V 152 1 8
HELIX 111 111 ASP W 4 TRP W 35 1 32
HELIX 112 112 LEU W 37 LEU W 65 1 29
HELIX 113 113 ASN W 82 VAL W 111 1 30
HELIX 114 114 ASP W 113 GLY W 145 1 33
HELIX 115 115 GLY W 145 SER W 152 1 8
HELIX 116 116 ASP X 4 TRP X 35 1 32
HELIX 117 117 LEU X 37 LEU X 65 1 29
HELIX 118 118 ASN X 82 VAL X 111 1 30
HELIX 119 119 ASP X 113 GLY X 145 1 33
HELIX 120 120 GLY X 145 SER X 152 1 8
LINK SD MET A 52 FE HEM A 159 1555 1555 2.32
LINK OD1 ASN A 148 K K A 160 1555 1555 2.86
LINK OE1 GLN A 151 K K A 160 1555 1555 2.89
LINK FE HEM A 159 SD MET B 52 1555 1555 2.27
LINK K K A 160 OD1 ASN L 148 1555 1555 2.97
LINK K K A 160 OE1 GLN L 151 1555 1555 2.86
LINK K K A 160 OE1 GLN M 151 1555 1555 2.86
LINK K K A 160 OE1 GLN X 151 1555 1555 2.92
LINK OD1 ASN B 148 K K B 159 1555 1555 2.97
LINK OE1 GLN B 151 K K B 159 1555 1555 2.87
LINK K K B 159 OD1 ASN D 148 1555 1555 2.99
LINK K K B 159 OE1 GLN D 151 1555 1555 2.89
LINK K K B 159 OD1 ASN F 148 1555 1555 3.00
LINK K K B 159 OE1 GLN F 151 1555 1555 2.97
LINK K K B 159 OE1 GLN H 151 1555 1555 2.90
LINK SD MET C 52 FE HEM C 159 1555 1555 2.30
LINK OE1 GLN C 151 K K C 160 1555 1555 2.88
LINK FE HEM C 159 SD MET D 52 1555 1555 2.33
LINK K K C 160 OD1 ASN K 148 1555 1555 2.94
LINK K K C 160 OE1 GLN K 151 1555 1555 2.87
LINK K K C 160 OE1 GLN S 151 1555 1555 2.88
LINK K K C 160 OE1 GLN U 151 1555 1555 2.88
LINK SD MET E 52 FE HEM F 159 1555 1555 2.30
LINK OD1 ASN E 148 K K E 159 1555 1555 2.88
LINK OE1 GLN E 151 K K E 159 1555 1555 2.88
LINK K K E 159 OE1 GLN J 151 1555 1555 2.81
LINK K K E 159 OE1 GLN Q 151 1555 1555 2.88
LINK K K E 159 OE1 GLN V 151 1555 1555 2.92
LINK SD MET F 52 FE HEM F 159 1555 1555 2.28
LINK SD MET G 52 FE HEM H 159 1555 1555 2.33
LINK OE1 GLN G 151 K K G 159 1555 1555 2.87
LINK K K G 159 OE1 GLN I 151 1555 1555 2.93
LINK K K G 159 OE1 GLN O 151 1555 1555 2.83
LINK K K G 159 OE1 GLN W 151 1555 1555 2.84
LINK SD MET H 52 FE HEM H 159 1555 1555 2.26
LINK SD MET I 52 FE HEM J 159 1555 1555 2.34
LINK SD MET J 52 FE HEM J 159 1555 1555 2.23
LINK SD MET K 52 FE HEM K 159 1555 1555 2.19
LINK FE HEM K 159 SD MET L 52 1555 1555 2.26
LINK SD MET M 52 FE HEM N 159 1555 1555 2.33
LINK SD MET N 52 FE HEM N 159 1555 1555 2.24
LINK OD1 ASN N 148 K K N 160 1555 1555 2.90
LINK K K N 160 OE1 GLN P 151 1555 1555 2.96
LINK K K N 160 OE1 GLN R 151 1555 1555 2.89
LINK K K N 160 OE1 GLN T 151 1555 1555 2.95
LINK SD MET O 52 FE HEM P 159 1555 1555 2.32
LINK SD MET P 52 FE HEM P 159 1555 1555 2.20
LINK SD MET Q 52 FE HEM Q 159 1555 1555 2.30
LINK FE HEM Q 159 SD MET R 52 1555 1555 2.20
LINK SD MET S 52 FE HEM S 159 1555 1555 2.32
LINK FE HEM S 159 SD MET T 52 1555 1555 2.31
LINK SD MET U 52 FE HEM V 159 1555 1555 2.34
LINK SD MET V 52 FE HEM V 159 1555 1555 2.25
LINK SD MET W 52 FE HEM X 159 1555 1555 2.34
LINK SD MET X 52 FE HEM X 159 1555 1555 2.31
SITE 1 AC1 15 ASN A 23 PHE A 26 TYR A 45 ILE A 49
SITE 2 AC1 15 MET A 52 LYS A 53 HOH A1053 LEU B 19
SITE 3 AC1 15 ILE B 22 ASN B 23 PHE B 26 TYR B 45
SITE 4 AC1 15 ILE B 49 MET B 52 LYS B 53
SITE 1 AC2 8 ASN A 148 GLN A 151 ASN L 148 GLN L 151
SITE 2 AC2 8 ASN M 148 GLN M 151 ASN X 148 GLN X 151
SITE 1 AC3 8 ASN B 148 GLN B 151 ASN D 148 GLN D 151
SITE 2 AC3 8 ASN F 148 GLN F 151 ASN H 148 GLN H 151
SITE 1 AC4 14 ASN C 23 PHE C 26 TYR C 45 MET C 52
SITE 2 AC4 14 LYS C 53 HOH C 198 HOH C 378 LEU D 19
SITE 3 AC4 14 ASN D 23 PHE D 26 TYR D 45 ILE D 49
SITE 4 AC4 14 MET D 52 LYS D 53
SITE 1 AC5 8 ASN C 148 GLN C 151 ASN K 148 GLN K 151
SITE 2 AC5 8 ASN S 148 GLN S 151 ASN U 148 GLN U 151
SITE 1 AC6 8 ASN E 148 GLN E 151 ASN J 148 GLN J 151
SITE 2 AC6 8 ASN Q 148 GLN Q 151 ASN V 148 GLN V 151
SITE 1 AC7 16 ILE E 22 ASN E 23 PHE E 26 TYR E 45
SITE 2 AC7 16 MET E 52 LYS E 53 LEU F 19 ASN F 23
SITE 3 AC7 16 PHE F 26 TYR F 45 ILE F 49 MET F 52
SITE 4 AC7 16 LYS F 53 HOH F1019 HOH F1204 HOH F1330
SITE 1 AC8 8 ASN G 148 GLN G 151 ASN I 148 GLN I 151
SITE 2 AC8 8 ASN O 148 GLN O 151 ASN W 148 GLN W 151
SITE 1 AC9 14 ASN G 23 PHE G 26 TYR G 45 ILE G 49
SITE 2 AC9 14 MET G 52 LYS G 53 LEU H 19 ASN H 23
SITE 3 AC9 14 TYR H 45 ILE H 49 MET H 52 LYS H 53
SITE 4 AC9 14 HOH H1336 HOH H1373
SITE 1 BC1 12 ASN I 23 PHE I 26 TYR I 45 MET I 52
SITE 2 BC1 12 LYS I 53 LEU J 19 ASN J 23 PHE J 26
SITE 3 BC1 12 TYR J 45 MET J 52 LYS J 53 HOH J1326
SITE 1 BC2 14 ASN K 23 PHE K 26 TYR K 45 ILE K 49
SITE 2 BC2 14 MET K 52 LYS K 53 ASP K 56 HOH K1022
SITE 3 BC2 14 HOH K1394 ASN L 23 PHE L 26 TYR L 45
SITE 4 BC2 14 MET L 52 LYS L 53
SITE 1 BC3 17 ILE M 22 ASN M 23 PHE M 26 TYR M 45
SITE 2 BC3 17 ILE M 49 MET M 52 LYS M 53 LEU N 19
SITE 3 BC3 17 ASN N 23 PHE N 26 TYR N 45 ILE N 49
SITE 4 BC3 17 MET N 52 LYS N 53 HOH N 557 HOH N 860
SITE 5 BC3 17 HOH N1359
SITE 1 BC4 8 ASN N 148 GLN N 151 ASN P 148 GLN P 151
SITE 2 BC4 8 ASN R 148 GLN R 151 ASN T 148 GLN T 151
SITE 1 BC5 14 ASN O 23 PHE O 26 TYR O 45 ILE O 49
SITE 2 BC5 14 MET O 52 LYS O 53 LEU P 19 ILE P 22
SITE 3 BC5 14 ASN P 23 PHE P 26 TYR P 45 MET P 52
SITE 4 BC5 14 LYS P 53 HOH P1219
SITE 1 BC6 15 ILE Q 22 ASN Q 23 PHE Q 26 TYR Q 45
SITE 2 BC6 15 MET Q 52 LYS Q 53 HOH Q1241 HOH Q1270
SITE 3 BC6 15 HOH Q1399 ASN R 23 PHE R 26 TYR R 45
SITE 4 BC6 15 ILE R 49 MET R 52 LYS R 53
SITE 1 BC7 17 ASN S 23 PHE S 26 TYR S 45 ILE S 49
SITE 2 BC7 17 MET S 52 LYS S 53 ALA S 55 HOH S1149
SITE 3 BC7 17 HOH S1286 HOH S1393 LEU T 19 ASN T 23
SITE 4 BC7 17 PHE T 26 TYR T 45 MET T 52 LYS T 53
SITE 5 BC7 17 HOH T1411
SITE 1 BC8 12 ASN U 23 PHE U 26 TYR U 45 ILE U 49
SITE 2 BC8 12 MET U 52 LYS U 53 ASN V 23 PHE V 26
SITE 3 BC8 12 TYR V 45 MET V 52 LYS V 53 HOH V1148
SITE 1 BC9 14 LEU W 19 ILE W 22 ASN W 23 PHE W 26
SITE 2 BC9 14 TYR W 45 ILE W 49 MET W 52 ASN X 23
SITE 3 BC9 14 TYR X 45 ILE X 49 MET X 52 LYS X 53
SITE 4 BC9 14 HOH X 232 HOH X1220
CRYST1 125.806 202.756 207.546 90.00 90.00 90.00 P 21 21 21 96
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 0.007949 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004932 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004818 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
