HEADER OXIDOREDUCTASE 23-FEB-12 4DVQ
TITLE STRUCTURE OF HUMAN ALDOSTERONE SYNTHASE, CYP11B2, IN COMPLEX WITH
TITLE 2 DEOXYCORTICOSTERONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME P450 11B2, MITOCHONDRIAL;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 SYNONYM: ALDOSTERONE SYNTHASE, ALDOS, ALDOSTERONE-SYNTHESIZING
COMPND 5 ENZYME, CYPXIB2, CYTOCHROME P-450ALDO, CYTOCHROME P-450C18, STEROID
COMPND 6 18-HYDROXYLASE;
COMPND 7 EC: 1.14.15.4, 1.14.15.5;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ALDOSTERONE SYNTHASE, CYP11B2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5A;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCW
KEYWDS CYTOCHROME P450, CYP11B2, ALDOSTERONE SYNTHASE, MONOOXYGENASE, HEME
KEYWDS 2 PROTEIN, MINERALOCORTICOID, CORTICOSTEROID, MITOCHONDRIA, MEMBRANE,
KEYWDS 3 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.STRUSHKEVICH,L.SHEN,W.TEMPEL,C.ARROWSMITH,A.EDWARDS,S.A.USANOV,H.-
AUTHOR 2 W.PARK
REVDAT 2 13-FEB-13 4DVQ 1 JRNL
REVDAT 1 30-JAN-13 4DVQ 0
JRNL AUTH N.STRUSHKEVICH,A.A.GILEP,L.SHEN,C.H.ARROWSMITH,A.M.EDWARDS,
JRNL AUTH 2 S.A.USANOV,H.W.PARK
JRNL TITL STRUCTURAL INSIGHTS INTO ALDOSTERONE SYNTHASE SUBSTRATE
JRNL TITL 2 SPECIFICITY AND TARGETED INHIBITION.
JRNL REF MOL.ENDOCRINOL. V. 27 315 2013
JRNL REFN ISSN 0888-8809
JRNL PMID 23322723
JRNL DOI 10.1210/ME.2012-1287
REMARK 2
REMARK 2 RESOLUTION. 2.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 245706
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.973
REMARK 3 FREE R VALUE TEST SET COUNT : 12220
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.49
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 15486
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.3280
REMARK 3 BIN FREE R VALUE SET COUNT : 838
REMARK 3 BIN FREE R VALUE : 0.3780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 45085
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 849
REMARK 3 SOLVENT ATOMS : 260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.33600
REMARK 3 B22 (A**2) : 0.56500
REMARK 3 B33 (A**2) : -0.46400
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.57900
REMARK 3 B23 (A**2) : 0.00000
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): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.240
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.859
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 47254 ; 0.011 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 32605 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 64368 ; 1.319 ; 2.005
REMARK 3 BOND ANGLES OTHERS (DEGREES): 78990 ; 0.886 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 5526 ; 5.899 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 2183 ;34.081 ;22.863
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 7953 ;17.844 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 384 ;16.480 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 7000 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 51416 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 9936 ; 0.002 ; 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): 27816 ; 0.739 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 44974 ; 1.452 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 19403 ; 2.295 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 19341 ; 3.784 ; 4.500
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 : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 4
REMARK 4 4DVQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-12.
REMARK 100 THE RCSB ID CODE IS RCSB070842.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JAN-12
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 245749
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.490
REMARK 200 RESOLUTION RANGE LOW (A) : 48.550
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 4.240
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7435
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.94000
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 4000, 0.1M TRIS, PH 8.5, 0.2M
REMARK 280 LITHIUM SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 99.81450
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 24100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 106890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -199.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, F, D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 24520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 106590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -188.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, L, H, K, I, J
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 27
REMARK 465 ALA A 28
REMARK 465 LYS A 29
REMARK 465 LYS A 30
REMARK 465 THR A 31
REMARK 465 SER A 32
REMARK 465 SER A 33
REMARK 465 ARG A 432
REMARK 465 GLY A 433
REMARK 465 SER A 434
REMARK 465 GLY A 435
REMARK 465 ARG A 436
REMARK 465 ASN A 437
REMARK 465 ASN A 503
REMARK 465 HIS A 504
REMARK 465 HIS A 505
REMARK 465 HIS A 506
REMARK 465 HIS A 507
REMARK 465 HIS A 508
REMARK 465 HIS A 509
REMARK 465 MET B 27
REMARK 465 ALA B 28
REMARK 465 LYS B 29
REMARK 465 LYS B 30
REMARK 465 THR B 31
REMARK 465 SER B 32
REMARK 465 SER B 33
REMARK 465 ARG B 432
REMARK 465 GLY B 433
REMARK 465 SER B 434
REMARK 465 GLY B 435
REMARK 465 ARG B 436
REMARK 465 ASN B 437
REMARK 465 ASN B 503
REMARK 465 HIS B 504
REMARK 465 HIS B 505
REMARK 465 HIS B 506
REMARK 465 HIS B 507
REMARK 465 HIS B 508
REMARK 465 HIS B 509
REMARK 465 MET C 27
REMARK 465 ALA C 28
REMARK 465 LYS C 29
REMARK 465 LYS C 30
REMARK 465 THR C 31
REMARK 465 SER C 32
REMARK 465 SER C 33
REMARK 465 ILE C 431
REMARK 465 ARG C 432
REMARK 465 GLY C 433
REMARK 465 SER C 434
REMARK 465 GLY C 435
REMARK 465 ARG C 436
REMARK 465 ASN C 437
REMARK 465 ASN C 503
REMARK 465 HIS C 504
REMARK 465 HIS C 505
REMARK 465 HIS C 506
REMARK 465 HIS C 507
REMARK 465 HIS C 508
REMARK 465 HIS C 509
REMARK 465 MET D 27
REMARK 465 ALA D 28
REMARK 465 LYS D 29
REMARK 465 LYS D 30
REMARK 465 THR D 31
REMARK 465 SER D 32
REMARK 465 SER D 33
REMARK 465 ILE D 431
REMARK 465 ARG D 432
REMARK 465 GLY D 433
REMARK 465 SER D 434
REMARK 465 GLY D 435
REMARK 465 ARG D 436
REMARK 465 ASN D 437
REMARK 465 ASN D 503
REMARK 465 HIS D 504
REMARK 465 HIS D 505
REMARK 465 HIS D 506
REMARK 465 HIS D 507
REMARK 465 HIS D 508
REMARK 465 HIS D 509
REMARK 465 MET E 27
REMARK 465 ALA E 28
REMARK 465 LYS E 29
REMARK 465 LYS E 30
REMARK 465 THR E 31
REMARK 465 SER E 32
REMARK 465 SER E 33
REMARK 465 ILE E 431
REMARK 465 ARG E 432
REMARK 465 GLY E 433
REMARK 465 SER E 434
REMARK 465 GLY E 435
REMARK 465 ARG E 436
REMARK 465 MET F 27
REMARK 465 ALA F 28
REMARK 465 LYS F 29
REMARK 465 LYS F 30
REMARK 465 THR F 31
REMARK 465 SER F 32
REMARK 465 SER F 33
REMARK 465 ILE F 431
REMARK 465 ARG F 432
REMARK 465 GLY F 433
REMARK 465 SER F 434
REMARK 465 GLY F 435
REMARK 465 ARG F 436
REMARK 465 ASN F 437
REMARK 465 MET G 27
REMARK 465 ALA G 28
REMARK 465 LYS G 29
REMARK 465 LYS G 30
REMARK 465 THR G 31
REMARK 465 SER G 32
REMARK 465 SER G 33
REMARK 465 ILE G 431
REMARK 465 ARG G 432
REMARK 465 GLY G 433
REMARK 465 SER G 434
REMARK 465 GLY G 435
REMARK 465 ARG G 436
REMARK 465 ASN G 437
REMARK 465 ASN G 503
REMARK 465 HIS G 504
REMARK 465 HIS G 505
REMARK 465 HIS G 506
REMARK 465 HIS G 507
REMARK 465 HIS G 508
REMARK 465 HIS G 509
REMARK 465 MET H 27
REMARK 465 ALA H 28
REMARK 465 LYS H 29
REMARK 465 LYS H 30
REMARK 465 THR H 31
REMARK 465 SER H 32
REMARK 465 SER H 33
REMARK 465 ILE H 431
REMARK 465 ARG H 432
REMARK 465 GLY H 433
REMARK 465 SER H 434
REMARK 465 GLY H 435
REMARK 465 ARG H 436
REMARK 465 ASN H 437
REMARK 465 ASN H 503
REMARK 465 HIS H 504
REMARK 465 HIS H 505
REMARK 465 HIS H 506
REMARK 465 HIS H 507
REMARK 465 HIS H 508
REMARK 465 HIS H 509
REMARK 465 MET I 27
REMARK 465 ALA I 28
REMARK 465 LYS I 29
REMARK 465 LYS I 30
REMARK 465 THR I 31
REMARK 465 SER I 32
REMARK 465 SER I 33
REMARK 465 ILE I 431
REMARK 465 ARG I 432
REMARK 465 GLY I 433
REMARK 465 SER I 434
REMARK 465 GLY I 435
REMARK 465 ARG I 436
REMARK 465 ASN I 437
REMARK 465 ASN I 503
REMARK 465 HIS I 504
REMARK 465 HIS I 505
REMARK 465 HIS I 506
REMARK 465 HIS I 507
REMARK 465 HIS I 508
REMARK 465 HIS I 509
REMARK 465 MET J 27
REMARK 465 ALA J 28
REMARK 465 LYS J 29
REMARK 465 LYS J 30
REMARK 465 THR J 31
REMARK 465 SER J 32
REMARK 465 SER J 33
REMARK 465 ILE J 431
REMARK 465 ARG J 432
REMARK 465 GLY J 433
REMARK 465 SER J 434
REMARK 465 GLY J 435
REMARK 465 ARG J 436
REMARK 465 ASN J 437
REMARK 465 ASN J 503
REMARK 465 HIS J 504
REMARK 465 HIS J 505
REMARK 465 HIS J 506
REMARK 465 HIS J 507
REMARK 465 HIS J 508
REMARK 465 HIS J 509
REMARK 465 MET K 27
REMARK 465 ALA K 28
REMARK 465 LYS K 29
REMARK 465 LYS K 30
REMARK 465 THR K 31
REMARK 465 SER K 32
REMARK 465 SER K 33
REMARK 465 LEU K 429
REMARK 465 ASP K 430
REMARK 465 ILE K 431
REMARK 465 ARG K 432
REMARK 465 GLY K 433
REMARK 465 SER K 434
REMARK 465 GLY K 435
REMARK 465 ARG K 436
REMARK 465 ASN K 437
REMARK 465 ASN K 503
REMARK 465 HIS K 504
REMARK 465 HIS K 505
REMARK 465 HIS K 506
REMARK 465 HIS K 507
REMARK 465 HIS K 508
REMARK 465 HIS K 509
REMARK 465 MET L 27
REMARK 465 ALA L 28
REMARK 465 LYS L 29
REMARK 465 LYS L 30
REMARK 465 THR L 31
REMARK 465 SER L 32
REMARK 465 SER L 33
REMARK 465 THR L 34
REMARK 465 VAL L 35
REMARK 465 ASN L 82
REMARK 465 LEU L 83
REMARK 465 GLY L 84
REMARK 465 GLY L 85
REMARK 465 ILE L 431
REMARK 465 ARG L 432
REMARK 465 GLY L 433
REMARK 465 SER L 434
REMARK 465 GLY L 435
REMARK 465 ARG L 436
REMARK 465 ASN L 437
REMARK 465 PHE L 438
REMARK 465 HIS L 439
REMARK 465 ASN L 503
REMARK 465 HIS L 504
REMARK 465 HIS L 505
REMARK 465 HIS L 506
REMARK 465 HIS L 507
REMARK 465 HIS L 508
REMARK 465 HIS L 509
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 63 CG HIS A 63 CD2 0.057
REMARK 500 HIS B 225 CG HIS B 225 CD2 0.058
REMARK 500 HIS D 63 CG HIS D 63 CD2 0.056
REMARK 500 HIS F 225 CG HIS F 225 CD2 0.056
REMARK 500 HIS G 440 CG HIS G 440 CD2 0.061
REMARK 500 HIS K 440 CG HIS K 440 CD2 0.058
REMARK 500 HIS L 440 CG HIS L 440 CD2 0.058
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 TYR A 61 53.11 -155.27
REMARK 500 PRO A 77 21.72 -77.36
REMARK 500 MET A 92 11.08 -149.97
REMARK 500 SER A 105 -167.28 -69.02
REMARK 500 SER A 249 55.00 -140.99
REMARK 500 LEU A 362 57.13 -118.22
REMARK 500 ALA A 399 131.85 -34.31
REMARK 500 CYS A 450 128.05 -36.95
REMARK 500 THR A 477 81.01 -62.31
REMARK 500 SER A 486 57.03 -149.39
REMARK 500 PHE A 487 -49.39 72.58
REMARK 500 ARG B 48 -38.54 -36.10
REMARK 500 TYR B 61 54.41 -150.23
REMARK 500 ASN B 82 96.67 -62.41
REMARK 500 MET B 92 24.85 -160.51
REMARK 500 SER B 105 -164.60 -69.26
REMARK 500 SER B 243 -59.07 -29.68
REMARK 500 VAL B 316 -79.01 -100.19
REMARK 500 ALA B 349 -71.03 -37.97
REMARK 500 ARG B 427 -37.70 -24.61
REMARK 500 GLN B 449 151.82 -47.92
REMARK 500 CYS B 450 120.79 -37.44
REMARK 500 PHE B 487 -59.17 68.93
REMARK 500 TYR C 61 53.00 -163.33
REMARK 500 MET C 92 10.66 -151.21
REMARK 500 GLU C 95 -55.82 -22.42
REMARK 500 SER C 105 -159.33 -77.09
REMARK 500 SER C 249 53.63 -142.14
REMARK 500 ASN C 413 96.43 -65.65
REMARK 500 PHE C 487 -59.75 66.84
REMARK 500 TYR D 61 54.78 -157.25
REMARK 500 SER D 249 45.62 -142.23
REMARK 500 ALA D 297 29.76 46.99
REMARK 500 VAL D 316 -68.03 -104.93
REMARK 500 ASN D 333 74.42 -110.74
REMARK 500 ASN D 413 93.76 -64.98
REMARK 500 ARG D 419 71.25 56.70
REMARK 500 ARG D 427 -3.67 -57.53
REMARK 500 GLN D 449 152.97 -46.40
REMARK 500 PHE D 487 -46.93 71.04
REMARK 500 TYR E 61 61.50 -159.20
REMARK 500 PRO E 77 0.58 -66.79
REMARK 500 ASN E 82 88.07 -63.49
REMARK 500 MET E 92 10.75 -151.15
REMARK 500 GLU E 95 -50.54 -25.25
REMARK 500 SER E 105 -162.75 -73.48
REMARK 500 VAL E 316 -68.12 -100.23
REMARK 500 ARG E 419 60.76 66.79
REMARK 500 PHE E 438 29.30 -71.23
REMARK 500 CYS E 450 122.46 -37.96
REMARK 500
REMARK 500 THIS ENTRY HAS 126 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM G 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 450 SG
REMARK 620 2 HEM G 601 NA 99.8
REMARK 620 3 HEM G 601 NB 89.9 88.9
REMARK 620 4 HEM G 601 NC 84.0 176.0 89.8
REMARK 620 5 HEM G 601 ND 94.2 90.8 175.9 90.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 450 SG
REMARK 620 2 HEM A 601 NA 98.9
REMARK 620 3 HEM A 601 NB 89.3 88.8
REMARK 620 4 HEM A 601 NC 83.7 177.1 90.0
REMARK 620 5 HEM A 601 ND 94.0 91.8 176.5 89.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM F 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 450 SG
REMARK 620 2 HEM F 601 NA 93.3
REMARK 620 3 HEM F 601 NB 80.8 87.8
REMARK 620 4 HEM F 601 NC 89.6 176.5 90.8
REMARK 620 5 HEM F 601 ND 102.4 91.8 176.8 89.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM H 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 450 SG
REMARK 620 2 HEM H 601 NA 97.9
REMARK 620 3 HEM H 601 NB 88.2 90.1
REMARK 620 4 HEM H 601 NC 85.4 176.6 89.0
REMARK 620 5 HEM H 601 ND 95.7 89.5 176.2 91.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM I 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 450 SG
REMARK 620 2 HEM I 601 NA 95.9
REMARK 620 3 HEM I 601 NB 86.3 86.7
REMARK 620 4 HEM I 601 NC 86.3 177.7 92.8
REMARK 620 5 HEM I 601 ND 96.5 93.5 177.1 86.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM E 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 450 SG
REMARK 620 2 HEM E 601 NA 99.6
REMARK 620 3 HEM E 601 NB 85.2 89.9
REMARK 620 4 HEM E 601 NC 83.7 176.4 89.2
REMARK 620 5 HEM E 601 ND 99.5 89.1 175.3 91.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM D 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 450 SG
REMARK 620 2 HEM D 601 NA 97.1
REMARK 620 3 HEM D 601 NB 89.8 92.5
REMARK 620 4 HEM D 601 NC 85.9 177.0 87.0
REMARK 620 5 HEM D 601 ND 93.8 87.0 176.4 93.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 450 SG
REMARK 620 2 HEM C 601 NA 98.6
REMARK 620 3 HEM C 601 NB 90.0 93.7
REMARK 620 4 HEM C 601 NC 84.7 176.7 86.2
REMARK 620 5 HEM C 601 ND 93.9 86.3 176.1 93.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM L 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 450 SG
REMARK 620 2 HEM L 601 NA 98.4
REMARK 620 3 HEM L 601 NB 88.4 89.7
REMARK 620 4 HEM L 601 NC 83.1 178.3 89.7
REMARK 620 5 HEM L 601 ND 93.6 90.2 178.0 90.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 450 SG
REMARK 620 2 HEM B 601 NA 99.3
REMARK 620 3 HEM B 601 NB 88.3 91.0
REMARK 620 4 HEM B 601 NC 83.4 177.0 87.7
REMARK 620 5 HEM B 601 ND 94.5 89.8 176.9 91.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM K 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 450 SG
REMARK 620 2 HEM K 601 NA 99.8
REMARK 620 3 HEM K 601 NB 82.9 89.7
REMARK 620 4 HEM K 601 NC 81.4 178.7 89.9
REMARK 620 5 HEM K 601 ND 98.1 90.8 178.8 89.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM J 601 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 450 SG
REMARK 620 2 HEM J 601 NA 96.2
REMARK 620 3 HEM J 601 NB 86.6 86.4
REMARK 620 4 HEM J 601 NC 84.8 178.5 92.6
REMARK 620 5 HEM J 601 ND 95.2 92.9 178.1 88.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA C 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA D 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM E 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA E 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM F 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA F 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM G 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA G 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM H 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA H 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM I 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA I 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM J 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA J 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM K 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA K 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 K 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM L 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CA L 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 603
DBREF 4DVQ A 34 503 UNP P19099 C11B2_HUMAN 34 503
DBREF 4DVQ B 34 503 UNP P19099 C11B2_HUMAN 34 503
DBREF 4DVQ C 34 503 UNP P19099 C11B2_HUMAN 34 503
DBREF 4DVQ D 34 503 UNP P19099 C11B2_HUMAN 34 503
DBREF 4DVQ E 34 503 UNP P19099 C11B2_HUMAN 34 503
DBREF 4DVQ F 34 503 UNP P19099 C11B2_HUMAN 34 503
DBREF 4DVQ G 34 503 UNP P19099 C11B2_HUMAN 34 503
DBREF 4DVQ H 34 503 UNP P19099 C11B2_HUMAN 34 503
DBREF 4DVQ I 34 503 UNP P19099 C11B2_HUMAN 34 503
DBREF 4DVQ J 34 503 UNP P19099 C11B2_HUMAN 34 503
DBREF 4DVQ K 34 503 UNP P19099 C11B2_HUMAN 34 503
DBREF 4DVQ L 34 503 UNP P19099 C11B2_HUMAN 34 503
SEQADV 4DVQ MET A 27 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ ALA A 28 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS A 29 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS A 30 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ THR A 31 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER A 32 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER A 33 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS A 504 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS A 505 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS A 506 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS A 507 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS A 508 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS A 509 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ MET B 27 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ ALA B 28 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS B 29 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS B 30 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ THR B 31 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER B 32 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER B 33 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS B 504 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS B 505 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS B 506 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS B 507 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS B 508 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS B 509 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ MET C 27 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ ALA C 28 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS C 29 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS C 30 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ THR C 31 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER C 32 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER C 33 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS C 504 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS C 505 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS C 506 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS C 507 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS C 508 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS C 509 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ MET D 27 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ ALA D 28 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS D 29 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS D 30 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ THR D 31 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER D 32 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER D 33 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS D 504 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS D 505 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS D 506 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS D 507 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS D 508 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS D 509 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ MET E 27 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ ALA E 28 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS E 29 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS E 30 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ THR E 31 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER E 32 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER E 33 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS E 504 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS E 505 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS E 506 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS E 507 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS E 508 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS E 509 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ MET F 27 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ ALA F 28 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS F 29 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS F 30 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ THR F 31 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER F 32 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER F 33 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS F 504 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS F 505 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS F 506 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS F 507 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS F 508 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS F 509 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ MET G 27 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ ALA G 28 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS G 29 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS G 30 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ THR G 31 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER G 32 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER G 33 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS G 504 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS G 505 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS G 506 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS G 507 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS G 508 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS G 509 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ MET H 27 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ ALA H 28 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS H 29 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS H 30 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ THR H 31 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER H 32 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER H 33 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS H 504 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS H 505 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS H 506 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS H 507 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS H 508 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS H 509 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ MET I 27 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ ALA I 28 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS I 29 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS I 30 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ THR I 31 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER I 32 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER I 33 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS I 504 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS I 505 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS I 506 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS I 507 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS I 508 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS I 509 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ MET J 27 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ ALA J 28 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS J 29 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS J 30 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ THR J 31 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER J 32 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER J 33 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS J 504 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS J 505 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS J 506 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS J 507 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS J 508 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS J 509 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ MET K 27 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ ALA K 28 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS K 29 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS K 30 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ THR K 31 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER K 32 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER K 33 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS K 504 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS K 505 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS K 506 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS K 507 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS K 508 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS K 509 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ MET L 27 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ ALA L 28 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS L 29 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ LYS L 30 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ THR L 31 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER L 32 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ SER L 33 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS L 504 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS L 505 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS L 506 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS L 507 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS L 508 UNP P19099 EXPRESSION TAG
SEQADV 4DVQ HIS L 509 UNP P19099 EXPRESSION TAG
SEQRES 1 A 483 MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU
SEQRES 2 A 483 ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU
SEQRES 3 A 483 LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS
SEQRES 4 A 483 LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE
SEQRES 5 A 483 PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL
SEQRES 6 A 483 MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP
SEQRES 7 A 483 SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL
SEQRES 8 A 483 ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE
SEQRES 9 A 483 LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG
SEQRES 10 A 483 LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG
SEQRES 11 A 483 PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER
SEQRES 12 A 483 GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY
SEQRES 13 A 483 SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR
SEQRES 14 A 483 THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG
SEQRES 15 A 483 LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU
SEQRES 16 A 483 ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR
SEQRES 17 A 483 VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP
SEQRES 18 A 483 ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP
SEQRES 19 A 483 ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS
SEQRES 20 A 483 ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR
SEQRES 21 A 483 THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU
SEQRES 22 A 483 SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR
SEQRES 23 A 483 ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET
SEQRES 24 A 483 THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN
SEQRES 25 A 483 ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE
SEQRES 26 A 483 SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU
SEQRES 27 A 483 LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO
SEQRES 28 A 483 VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU
SEQRES 29 A 483 VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL
SEQRES 30 A 483 GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU
SEQRES 31 A 483 PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU
SEQRES 32 A 483 ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO
SEQRES 33 A 483 PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU
SEQRES 34 A 483 ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU
SEQRES 35 A 483 LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE
SEQRES 36 A 483 LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER
SEQRES 37 A 483 PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS
SEQRES 38 A 483 HIS HIS
SEQRES 1 B 483 MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU
SEQRES 2 B 483 ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU
SEQRES 3 B 483 LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS
SEQRES 4 B 483 LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE
SEQRES 5 B 483 PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL
SEQRES 6 B 483 MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP
SEQRES 7 B 483 SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL
SEQRES 8 B 483 ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE
SEQRES 9 B 483 LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG
SEQRES 10 B 483 LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG
SEQRES 11 B 483 PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER
SEQRES 12 B 483 GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY
SEQRES 13 B 483 SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR
SEQRES 14 B 483 THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG
SEQRES 15 B 483 LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU
SEQRES 16 B 483 ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR
SEQRES 17 B 483 VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP
SEQRES 18 B 483 ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP
SEQRES 19 B 483 ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS
SEQRES 20 B 483 ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR
SEQRES 21 B 483 THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU
SEQRES 22 B 483 SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR
SEQRES 23 B 483 ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET
SEQRES 24 B 483 THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN
SEQRES 25 B 483 ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE
SEQRES 26 B 483 SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU
SEQRES 27 B 483 LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO
SEQRES 28 B 483 VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU
SEQRES 29 B 483 VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL
SEQRES 30 B 483 GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU
SEQRES 31 B 483 PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU
SEQRES 32 B 483 ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO
SEQRES 33 B 483 PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU
SEQRES 34 B 483 ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU
SEQRES 35 B 483 LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE
SEQRES 36 B 483 LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER
SEQRES 37 B 483 PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS
SEQRES 38 B 483 HIS HIS
SEQRES 1 C 483 MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU
SEQRES 2 C 483 ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU
SEQRES 3 C 483 LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS
SEQRES 4 C 483 LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE
SEQRES 5 C 483 PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL
SEQRES 6 C 483 MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP
SEQRES 7 C 483 SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL
SEQRES 8 C 483 ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE
SEQRES 9 C 483 LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG
SEQRES 10 C 483 LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG
SEQRES 11 C 483 PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER
SEQRES 12 C 483 GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY
SEQRES 13 C 483 SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR
SEQRES 14 C 483 THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG
SEQRES 15 C 483 LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU
SEQRES 16 C 483 ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR
SEQRES 17 C 483 VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP
SEQRES 18 C 483 ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP
SEQRES 19 C 483 ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS
SEQRES 20 C 483 ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR
SEQRES 21 C 483 THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU
SEQRES 22 C 483 SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR
SEQRES 23 C 483 ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET
SEQRES 24 C 483 THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN
SEQRES 25 C 483 ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE
SEQRES 26 C 483 SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU
SEQRES 27 C 483 LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO
SEQRES 28 C 483 VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU
SEQRES 29 C 483 VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL
SEQRES 30 C 483 GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU
SEQRES 31 C 483 PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU
SEQRES 32 C 483 ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO
SEQRES 33 C 483 PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU
SEQRES 34 C 483 ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU
SEQRES 35 C 483 LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE
SEQRES 36 C 483 LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER
SEQRES 37 C 483 PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS
SEQRES 38 C 483 HIS HIS
SEQRES 1 D 483 MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU
SEQRES 2 D 483 ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU
SEQRES 3 D 483 LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS
SEQRES 4 D 483 LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE
SEQRES 5 D 483 PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL
SEQRES 6 D 483 MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP
SEQRES 7 D 483 SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL
SEQRES 8 D 483 ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE
SEQRES 9 D 483 LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG
SEQRES 10 D 483 LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG
SEQRES 11 D 483 PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER
SEQRES 12 D 483 GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY
SEQRES 13 D 483 SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR
SEQRES 14 D 483 THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG
SEQRES 15 D 483 LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU
SEQRES 16 D 483 ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR
SEQRES 17 D 483 VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP
SEQRES 18 D 483 ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP
SEQRES 19 D 483 ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS
SEQRES 20 D 483 ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR
SEQRES 21 D 483 THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU
SEQRES 22 D 483 SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR
SEQRES 23 D 483 ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET
SEQRES 24 D 483 THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN
SEQRES 25 D 483 ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE
SEQRES 26 D 483 SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU
SEQRES 27 D 483 LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO
SEQRES 28 D 483 VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU
SEQRES 29 D 483 VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL
SEQRES 30 D 483 GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU
SEQRES 31 D 483 PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU
SEQRES 32 D 483 ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO
SEQRES 33 D 483 PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU
SEQRES 34 D 483 ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU
SEQRES 35 D 483 LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE
SEQRES 36 D 483 LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER
SEQRES 37 D 483 PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS
SEQRES 38 D 483 HIS HIS
SEQRES 1 E 483 MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU
SEQRES 2 E 483 ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU
SEQRES 3 E 483 LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS
SEQRES 4 E 483 LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE
SEQRES 5 E 483 PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL
SEQRES 6 E 483 MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP
SEQRES 7 E 483 SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL
SEQRES 8 E 483 ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE
SEQRES 9 E 483 LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG
SEQRES 10 E 483 LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG
SEQRES 11 E 483 PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER
SEQRES 12 E 483 GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY
SEQRES 13 E 483 SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR
SEQRES 14 E 483 THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG
SEQRES 15 E 483 LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU
SEQRES 16 E 483 ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR
SEQRES 17 E 483 VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP
SEQRES 18 E 483 ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP
SEQRES 19 E 483 ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS
SEQRES 20 E 483 ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR
SEQRES 21 E 483 THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU
SEQRES 22 E 483 SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR
SEQRES 23 E 483 ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET
SEQRES 24 E 483 THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN
SEQRES 25 E 483 ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE
SEQRES 26 E 483 SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU
SEQRES 27 E 483 LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO
SEQRES 28 E 483 VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU
SEQRES 29 E 483 VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL
SEQRES 30 E 483 GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU
SEQRES 31 E 483 PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU
SEQRES 32 E 483 ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO
SEQRES 33 E 483 PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU
SEQRES 34 E 483 ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU
SEQRES 35 E 483 LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE
SEQRES 36 E 483 LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER
SEQRES 37 E 483 PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS
SEQRES 38 E 483 HIS HIS
SEQRES 1 F 483 MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU
SEQRES 2 F 483 ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU
SEQRES 3 F 483 LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS
SEQRES 4 F 483 LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE
SEQRES 5 F 483 PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL
SEQRES 6 F 483 MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP
SEQRES 7 F 483 SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL
SEQRES 8 F 483 ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE
SEQRES 9 F 483 LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG
SEQRES 10 F 483 LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG
SEQRES 11 F 483 PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER
SEQRES 12 F 483 GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY
SEQRES 13 F 483 SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR
SEQRES 14 F 483 THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG
SEQRES 15 F 483 LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU
SEQRES 16 F 483 ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR
SEQRES 17 F 483 VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP
SEQRES 18 F 483 ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP
SEQRES 19 F 483 ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS
SEQRES 20 F 483 ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR
SEQRES 21 F 483 THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU
SEQRES 22 F 483 SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR
SEQRES 23 F 483 ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET
SEQRES 24 F 483 THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN
SEQRES 25 F 483 ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE
SEQRES 26 F 483 SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU
SEQRES 27 F 483 LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO
SEQRES 28 F 483 VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU
SEQRES 29 F 483 VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL
SEQRES 30 F 483 GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU
SEQRES 31 F 483 PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU
SEQRES 32 F 483 ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO
SEQRES 33 F 483 PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU
SEQRES 34 F 483 ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU
SEQRES 35 F 483 LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE
SEQRES 36 F 483 LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER
SEQRES 37 F 483 PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS
SEQRES 38 F 483 HIS HIS
SEQRES 1 G 483 MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU
SEQRES 2 G 483 ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU
SEQRES 3 G 483 LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS
SEQRES 4 G 483 LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE
SEQRES 5 G 483 PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL
SEQRES 6 G 483 MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP
SEQRES 7 G 483 SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL
SEQRES 8 G 483 ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE
SEQRES 9 G 483 LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG
SEQRES 10 G 483 LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG
SEQRES 11 G 483 PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER
SEQRES 12 G 483 GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY
SEQRES 13 G 483 SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR
SEQRES 14 G 483 THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG
SEQRES 15 G 483 LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU
SEQRES 16 G 483 ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR
SEQRES 17 G 483 VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP
SEQRES 18 G 483 ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP
SEQRES 19 G 483 ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS
SEQRES 20 G 483 ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR
SEQRES 21 G 483 THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU
SEQRES 22 G 483 SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR
SEQRES 23 G 483 ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET
SEQRES 24 G 483 THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN
SEQRES 25 G 483 ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE
SEQRES 26 G 483 SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU
SEQRES 27 G 483 LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO
SEQRES 28 G 483 VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU
SEQRES 29 G 483 VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL
SEQRES 30 G 483 GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU
SEQRES 31 G 483 PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU
SEQRES 32 G 483 ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO
SEQRES 33 G 483 PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU
SEQRES 34 G 483 ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU
SEQRES 35 G 483 LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE
SEQRES 36 G 483 LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER
SEQRES 37 G 483 PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS
SEQRES 38 G 483 HIS HIS
SEQRES 1 H 483 MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU
SEQRES 2 H 483 ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU
SEQRES 3 H 483 LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS
SEQRES 4 H 483 LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE
SEQRES 5 H 483 PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL
SEQRES 6 H 483 MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP
SEQRES 7 H 483 SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL
SEQRES 8 H 483 ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE
SEQRES 9 H 483 LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG
SEQRES 10 H 483 LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG
SEQRES 11 H 483 PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER
SEQRES 12 H 483 GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY
SEQRES 13 H 483 SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR
SEQRES 14 H 483 THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG
SEQRES 15 H 483 LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU
SEQRES 16 H 483 ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR
SEQRES 17 H 483 VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP
SEQRES 18 H 483 ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP
SEQRES 19 H 483 ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS
SEQRES 20 H 483 ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR
SEQRES 21 H 483 THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU
SEQRES 22 H 483 SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR
SEQRES 23 H 483 ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET
SEQRES 24 H 483 THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN
SEQRES 25 H 483 ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE
SEQRES 26 H 483 SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU
SEQRES 27 H 483 LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO
SEQRES 28 H 483 VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU
SEQRES 29 H 483 VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL
SEQRES 30 H 483 GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU
SEQRES 31 H 483 PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU
SEQRES 32 H 483 ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO
SEQRES 33 H 483 PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU
SEQRES 34 H 483 ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU
SEQRES 35 H 483 LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE
SEQRES 36 H 483 LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER
SEQRES 37 H 483 PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS
SEQRES 38 H 483 HIS HIS
SEQRES 1 I 483 MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU
SEQRES 2 I 483 ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU
SEQRES 3 I 483 LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS
SEQRES 4 I 483 LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE
SEQRES 5 I 483 PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL
SEQRES 6 I 483 MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP
SEQRES 7 I 483 SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL
SEQRES 8 I 483 ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE
SEQRES 9 I 483 LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG
SEQRES 10 I 483 LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG
SEQRES 11 I 483 PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER
SEQRES 12 I 483 GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY
SEQRES 13 I 483 SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR
SEQRES 14 I 483 THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG
SEQRES 15 I 483 LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU
SEQRES 16 I 483 ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR
SEQRES 17 I 483 VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP
SEQRES 18 I 483 ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP
SEQRES 19 I 483 ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS
SEQRES 20 I 483 ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR
SEQRES 21 I 483 THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU
SEQRES 22 I 483 SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR
SEQRES 23 I 483 ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET
SEQRES 24 I 483 THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN
SEQRES 25 I 483 ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE
SEQRES 26 I 483 SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU
SEQRES 27 I 483 LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO
SEQRES 28 I 483 VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU
SEQRES 29 I 483 VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL
SEQRES 30 I 483 GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU
SEQRES 31 I 483 PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU
SEQRES 32 I 483 ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO
SEQRES 33 I 483 PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU
SEQRES 34 I 483 ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU
SEQRES 35 I 483 LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE
SEQRES 36 I 483 LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER
SEQRES 37 I 483 PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS
SEQRES 38 I 483 HIS HIS
SEQRES 1 J 483 MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU
SEQRES 2 J 483 ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU
SEQRES 3 J 483 LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS
SEQRES 4 J 483 LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE
SEQRES 5 J 483 PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL
SEQRES 6 J 483 MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP
SEQRES 7 J 483 SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL
SEQRES 8 J 483 ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE
SEQRES 9 J 483 LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG
SEQRES 10 J 483 LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG
SEQRES 11 J 483 PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER
SEQRES 12 J 483 GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY
SEQRES 13 J 483 SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR
SEQRES 14 J 483 THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG
SEQRES 15 J 483 LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU
SEQRES 16 J 483 ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR
SEQRES 17 J 483 VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP
SEQRES 18 J 483 ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP
SEQRES 19 J 483 ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS
SEQRES 20 J 483 ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR
SEQRES 21 J 483 THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU
SEQRES 22 J 483 SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR
SEQRES 23 J 483 ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET
SEQRES 24 J 483 THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN
SEQRES 25 J 483 ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE
SEQRES 26 J 483 SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU
SEQRES 27 J 483 LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO
SEQRES 28 J 483 VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU
SEQRES 29 J 483 VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL
SEQRES 30 J 483 GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU
SEQRES 31 J 483 PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU
SEQRES 32 J 483 ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO
SEQRES 33 J 483 PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU
SEQRES 34 J 483 ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU
SEQRES 35 J 483 LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE
SEQRES 36 J 483 LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER
SEQRES 37 J 483 PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS
SEQRES 38 J 483 HIS HIS
SEQRES 1 K 483 MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU
SEQRES 2 K 483 ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU
SEQRES 3 K 483 LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS
SEQRES 4 K 483 LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE
SEQRES 5 K 483 PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL
SEQRES 6 K 483 MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP
SEQRES 7 K 483 SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL
SEQRES 8 K 483 ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE
SEQRES 9 K 483 LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG
SEQRES 10 K 483 LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG
SEQRES 11 K 483 PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER
SEQRES 12 K 483 GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY
SEQRES 13 K 483 SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR
SEQRES 14 K 483 THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG
SEQRES 15 K 483 LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU
SEQRES 16 K 483 ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR
SEQRES 17 K 483 VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP
SEQRES 18 K 483 ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP
SEQRES 19 K 483 ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS
SEQRES 20 K 483 ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR
SEQRES 21 K 483 THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU
SEQRES 22 K 483 SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR
SEQRES 23 K 483 ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET
SEQRES 24 K 483 THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN
SEQRES 25 K 483 ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE
SEQRES 26 K 483 SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU
SEQRES 27 K 483 LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO
SEQRES 28 K 483 VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU
SEQRES 29 K 483 VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL
SEQRES 30 K 483 GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU
SEQRES 31 K 483 PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU
SEQRES 32 K 483 ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO
SEQRES 33 K 483 PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU
SEQRES 34 K 483 ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU
SEQRES 35 K 483 LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE
SEQRES 36 K 483 LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER
SEQRES 37 K 483 PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS
SEQRES 38 K 483 HIS HIS
SEQRES 1 L 483 MET ALA LYS LYS THR SER SER THR VAL LEU PRO PHE GLU
SEQRES 2 L 483 ALA MET PRO GLN HIS PRO GLY ASN ARG TRP LEU ARG LEU
SEQRES 3 L 483 LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU HIS LEU HIS
SEQRES 4 L 483 LEU GLU MET HIS GLN THR PHE GLN GLU LEU GLY PRO ILE
SEQRES 5 L 483 PHE ARG TYR ASN LEU GLY GLY PRO ARG MET VAL CYS VAL
SEQRES 6 L 483 MET LEU PRO GLU ASP VAL GLU LYS LEU GLN GLN VAL ASP
SEQRES 7 L 483 SER LEU HIS PRO CYS ARG MET ILE LEU GLU PRO TRP VAL
SEQRES 8 L 483 ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS GLY VAL PHE
SEQRES 9 L 483 LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN ARG LEU ARG
SEQRES 10 L 483 LEU ASN PRO ASP VAL LEU SER PRO LYS ALA VAL GLN ARG
SEQRES 11 L 483 PHE LEU PRO MET VAL ASP ALA VAL ALA ARG ASP PHE SER
SEQRES 12 L 483 GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN ALA ARG GLY
SEQRES 13 L 483 SER LEU THR LEU ASP VAL GLN PRO SER ILE PHE HIS TYR
SEQRES 14 L 483 THR ILE GLU ALA SER ASN LEU ALA LEU PHE GLY GLU ARG
SEQRES 15 L 483 LEU GLY LEU VAL GLY HIS SER PRO SER SER ALA SER LEU
SEQRES 16 L 483 ASN PHE LEU HIS ALA LEU GLU VAL MET PHE LYS SER THR
SEQRES 17 L 483 VAL GLN LEU MET PHE MET PRO ARG SER LEU SER ARG TRP
SEQRES 18 L 483 ILE SER PRO LYS VAL TRP LYS GLU HIS PHE GLU ALA TRP
SEQRES 19 L 483 ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS ILE GLN LYS
SEQRES 20 L 483 ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO GLN HIS TYR
SEQRES 21 L 483 THR GLY ILE VAL ALA GLU LEU LEU LEU LYS ALA GLU LEU
SEQRES 22 L 483 SER LEU GLU ALA ILE LYS ALA ASN SER MET GLU LEU THR
SEQRES 23 L 483 ALA GLY SER VAL ASP THR THR ALA PHE PRO LEU LEU MET
SEQRES 24 L 483 THR LEU PHE GLU LEU ALA ARG ASN PRO ASP VAL GLN GLN
SEQRES 25 L 483 ILE LEU ARG GLN GLU SER LEU ALA ALA ALA ALA SER ILE
SEQRES 26 L 483 SER GLU HIS PRO GLN LYS ALA THR THR GLU LEU PRO LEU
SEQRES 27 L 483 LEU ARG ALA ALA LEU LYS GLU THR LEU ARG LEU TYR PRO
SEQRES 28 L 483 VAL GLY LEU PHE LEU GLU ARG VAL VAL SER SER ASP LEU
SEQRES 29 L 483 VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY THR LEU VAL
SEQRES 30 L 483 GLN VAL PHE LEU TYR SER LEU GLY ARG ASN ALA ALA LEU
SEQRES 31 L 483 PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN ARG TRP LEU
SEQRES 32 L 483 ASP ILE ARG GLY SER GLY ARG ASN PHE HIS HIS VAL PRO
SEQRES 33 L 483 PHE GLY PHE GLY MET ARG GLN CYS LEU GLY ARG ARG LEU
SEQRES 34 L 483 ALA GLU ALA GLU MET LEU LEU LEU LEU HIS HIS VAL LEU
SEQRES 35 L 483 LYS HIS PHE LEU VAL GLU THR LEU THR GLN GLU ASP ILE
SEQRES 36 L 483 LYS MET VAL TYR SER PHE ILE LEU ARG PRO GLY THR SER
SEQRES 37 L 483 PRO LEU LEU THR PHE ARG ALA ILE ASN HIS HIS HIS HIS
SEQRES 38 L 483 HIS HIS
HET HEM A 601 43
HET 1CA A 602 24
HET HEM B 601 43
HET SO4 A 603 5
HET 1CA B 602 24
HET HEM C 601 43
HET 1CA C 602 24
HET SO4 B 603 5
HET HEM D 601 43
HET 1CA D 602 24
HET HEM E 601 43
HET SO4 C 603 5
HET 1CA E 602 24
HET HEM F 601 43
HET 1CA F 602 24
HET SO4 D 603 5
HET HEM G 601 43
HET 1CA G 602 24
HET HEM H 601 43
HET SO4 E 603 5
HET 1CA H 602 24
HET HEM I 601 43
HET 1CA I 602 24
HET SO4 F 603 5
HET HEM J 601 43
HET 1CA J 602 24
HET HEM K 601 43
HET SO4 G 603 5
HET 1CA K 602 24
HET HEM L 601 43
HET 1CA L 602 24
HET SO4 K 603 5
HET SO4 L 603 5
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM 1CA DESOXYCORTICOSTERONE
HETNAM SO4 SULFATE ION
HETSYN HEM HEME
HETSYN 1CA 4-PREGNEN-21-OL-3,20-DIONE; DOC; 21-HYDROXYPROGESTERONE
FORMUL 13 HEM 12(C34 H32 FE N4 O4)
FORMUL 14 1CA 12(C21 H30 O3)
FORMUL 16 SO4 9(O4 S 2-)
FORMUL 46 HOH *260(H2 O)
HELIX 1 1 PRO A 37 MET A 41 5 5
HELIX 2 2 ASN A 47 GLN A 59 1 13
HELIX 3 3 HIS A 63 GLY A 76 1 14
HELIX 4 4 LEU A 93 ASP A 104 1 12
HELIX 5 5 LEU A 113 GLY A 124 1 12
HELIX 6 6 GLY A 128 LEU A 132 5 5
HELIX 7 7 ASN A 133 ARG A 143 1 11
HELIX 8 8 LEU A 144 LEU A 149 1 6
HELIX 9 9 SER A 150 ASN A 179 1 30
HELIX 10 10 VAL A 188 GLY A 206 1 19
HELIX 11 11 SER A 217 PHE A 239 1 23
HELIX 12 12 PRO A 241 SER A 249 1 9
HELIX 13 13 SER A 249 ASN A 281 1 33
HELIX 14 14 GLY A 288 ALA A 297 1 10
HELIX 15 15 SER A 300 GLY A 314 1 15
HELIX 16 16 VAL A 316 ASN A 333 1 18
HELIX 17 17 ASN A 333 HIS A 354 1 22
HELIX 18 18 LYS A 357 LEU A 362 1 6
HELIX 19 19 LEU A 362 TYR A 376 1 15
HELIX 20 20 LEU A 407 GLY A 411 1 5
HELIX 21 21 GLN A 426 ILE A 431 1 6
HELIX 22 22 GLY A 452 HIS A 470 1 19
HELIX 23 23 PRO B 37 MET B 41 5 5
HELIX 24 24 ASN B 47 GLN B 59 1 13
HELIX 25 25 HIS B 63 GLY B 76 1 14
HELIX 26 26 LEU B 93 GLN B 102 1 10
HELIX 27 27 LEU B 113 GLY B 124 1 12
HELIX 28 28 GLY B 128 LEU B 132 5 5
HELIX 29 29 ASN B 133 ARG B 143 1 11
HELIX 30 30 LEU B 144 LEU B 149 1 6
HELIX 31 31 SER B 150 GLN B 178 1 29
HELIX 32 32 VAL B 188 GLY B 206 1 19
HELIX 33 33 SER B 217 PHE B 239 1 23
HELIX 34 34 PRO B 241 SER B 249 1 9
HELIX 35 35 SER B 249 ASN B 281 1 33
HELIX 36 36 GLY B 288 ALA B 297 1 10
HELIX 37 37 SER B 300 SER B 315 1 16
HELIX 38 38 VAL B 316 ASN B 333 1 18
HELIX 39 39 ASN B 333 HIS B 354 1 22
HELIX 40 40 LYS B 357 LEU B 362 1 6
HELIX 41 41 LEU B 362 TYR B 376 1 15
HELIX 42 42 LEU B 407 ARG B 412 1 6
HELIX 43 43 PRO B 425 ILE B 431 1 7
HELIX 44 44 GLY B 452 HIS B 470 1 19
HELIX 45 45 PRO C 37 MET C 41 5 5
HELIX 46 46 ASN C 47 GLN C 59 1 13
HELIX 47 47 HIS C 63 GLY C 76 1 14
HELIX 48 48 LEU C 93 VAL C 103 1 11
HELIX 49 49 LEU C 113 GLY C 124 1 12
HELIX 50 50 GLY C 128 LEU C 132 5 5
HELIX 51 51 ASN C 133 LEU C 149 1 17
HELIX 52 52 SER C 150 ASN C 179 1 30
HELIX 53 53 VAL C 188 GLY C 206 1 19
HELIX 54 54 SER C 217 PHE C 239 1 23
HELIX 55 55 PRO C 241 SER C 249 1 9
HELIX 56 56 SER C 249 ASN C 281 1 33
HELIX 57 57 GLY C 288 ALA C 297 1 10
HELIX 58 58 SER C 300 GLY C 314 1 15
HELIX 59 59 VAL C 316 ASN C 333 1 18
HELIX 60 60 ASN C 333 ALA C 347 1 15
HELIX 61 61 ALA C 347 HIS C 354 1 8
HELIX 62 62 LYS C 357 LEU C 362 1 6
HELIX 63 63 LEU C 362 TYR C 376 1 15
HELIX 64 64 LEU C 407 ASN C 413 1 7
HELIX 65 65 ASN C 424 LEU C 429 5 6
HELIX 66 66 PHE C 445 GLN C 449 5 5
HELIX 67 67 GLY C 452 HIS C 470 1 19
HELIX 68 68 ASN D 47 GLN D 59 1 13
HELIX 69 69 HIS D 63 GLY D 76 1 14
HELIX 70 70 LEU D 93 VAL D 103 1 11
HELIX 71 71 LEU D 113 GLY D 124 1 12
HELIX 72 72 GLY D 128 LEU D 132 5 5
HELIX 73 73 ASN D 133 LEU D 149 1 17
HELIX 74 74 SER D 150 GLN D 178 1 29
HELIX 75 75 VAL D 188 GLY D 206 1 19
HELIX 76 76 SER D 217 PHE D 239 1 23
HELIX 77 77 PRO D 241 SER D 249 1 9
HELIX 78 78 SER D 249 ASN D 281 1 33
HELIX 79 79 GLY D 288 ALA D 297 1 10
HELIX 80 80 SER D 300 GLY D 314 1 15
HELIX 81 81 VAL D 316 ASN D 333 1 18
HELIX 82 82 ASN D 333 HIS D 354 1 22
HELIX 83 83 LYS D 357 LEU D 362 1 6
HELIX 84 84 LEU D 362 TYR D 376 1 15
HELIX 85 85 LEU D 407 GLY D 411 1 5
HELIX 86 86 ASN D 424 LEU D 429 5 6
HELIX 87 87 PHE D 445 GLN D 449 5 5
HELIX 88 88 GLY D 452 HIS D 470 1 19
HELIX 89 89 PRO E 37 MET E 41 5 5
HELIX 90 90 ASN E 47 GLN E 59 1 13
HELIX 91 91 HIS E 63 GLY E 76 1 14
HELIX 92 92 LEU E 93 VAL E 103 1 11
HELIX 93 93 LEU E 113 GLY E 124 1 12
HELIX 94 94 GLY E 128 LEU E 132 5 5
HELIX 95 95 ASN E 133 LEU E 149 1 17
HELIX 96 96 SER E 150 ASN E 179 1 30
HELIX 97 97 VAL E 188 GLY E 206 1 19
HELIX 98 98 SER E 217 PHE E 239 1 23
HELIX 99 99 PRO E 241 SER E 249 1 9
HELIX 100 100 SER E 249 ASN E 281 1 33
HELIX 101 101 GLY E 288 ALA E 297 1 10
HELIX 102 102 SER E 300 SER E 315 1 16
HELIX 103 103 VAL E 316 ASN E 333 1 18
HELIX 104 104 ASN E 333 HIS E 354 1 22
HELIX 105 105 LYS E 357 LEU E 362 1 6
HELIX 106 106 LEU E 362 TYR E 376 1 15
HELIX 107 107 LEU E 407 GLY E 411 1 5
HELIX 108 108 ASN E 424 LEU E 429 5 6
HELIX 109 109 PHE E 445 GLN E 449 5 5
HELIX 110 110 GLY E 452 HIS E 470 1 19
HELIX 111 111 PRO F 37 MET F 41 5 5
HELIX 112 112 ASN F 47 GLN F 59 1 13
HELIX 113 113 HIS F 63 GLY F 76 1 14
HELIX 114 114 LEU F 93 VAL F 103 1 11
HELIX 115 115 LEU F 113 ARG F 123 1 11
HELIX 116 116 ASN F 133 ARG F 143 1 11
HELIX 117 117 LEU F 144 LEU F 149 1 6
HELIX 118 118 SER F 150 ASN F 179 1 30
HELIX 119 119 VAL F 188 GLY F 206 1 19
HELIX 120 120 SER F 217 PHE F 239 1 23
HELIX 121 121 PRO F 241 SER F 249 1 9
HELIX 122 122 SER F 249 ASN F 281 1 33
HELIX 123 123 GLY F 288 ALA F 297 1 10
HELIX 124 124 SER F 300 SER F 315 1 16
HELIX 125 125 VAL F 316 ASN F 333 1 18
HELIX 126 126 ASN F 333 HIS F 354 1 22
HELIX 127 127 LYS F 357 LEU F 362 1 6
HELIX 128 128 LEU F 362 TYR F 376 1 15
HELIX 129 129 LEU F 407 GLY F 411 1 5
HELIX 130 130 ASN F 424 LEU F 429 5 6
HELIX 131 131 PHE F 445 GLN F 449 5 5
HELIX 132 132 GLY F 452 HIS F 470 1 19
HELIX 133 133 PRO G 37 MET G 41 5 5
HELIX 134 134 ASN G 47 GLN G 59 1 13
HELIX 135 135 HIS G 63 GLY G 76 1 14
HELIX 136 136 LEU G 93 GLN G 102 1 10
HELIX 137 137 LEU G 113 ARG G 123 1 11
HELIX 138 138 GLY G 128 LEU G 132 5 5
HELIX 139 139 ASN G 133 LEU G 149 1 17
HELIX 140 140 SER G 150 LEU G 177 1 28
HELIX 141 141 VAL G 188 GLY G 206 1 19
HELIX 142 142 SER G 217 PHE G 239 1 23
HELIX 143 143 PRO G 241 SER G 249 1 9
HELIX 144 144 SER G 249 ASN G 281 1 33
HELIX 145 145 GLY G 288 ALA G 297 1 10
HELIX 146 146 SER G 300 SER G 315 1 16
HELIX 147 147 VAL G 316 ASN G 333 1 18
HELIX 148 148 ASN G 333 HIS G 354 1 22
HELIX 149 149 PRO G 355 THR G 360 5 6
HELIX 150 150 LEU G 362 TYR G 376 1 15
HELIX 151 151 LEU G 407 GLY G 411 1 5
HELIX 152 152 ASN G 424 LEU G 429 5 6
HELIX 153 153 PHE G 445 GLN G 449 5 5
HELIX 154 154 GLY G 452 HIS G 470 1 19
HELIX 155 155 PRO H 37 MET H 41 5 5
HELIX 156 156 ASN H 47 GLN H 59 1 13
HELIX 157 157 HIS H 63 GLY H 76 1 14
HELIX 158 158 LEU H 93 VAL H 103 1 11
HELIX 159 159 LEU H 113 ARG H 123 1 11
HELIX 160 160 GLY H 128 LEU H 132 5 5
HELIX 161 161 ASN H 133 LEU H 149 1 17
HELIX 162 162 SER H 150 GLN H 178 1 29
HELIX 163 163 VAL H 188 GLY H 206 1 19
HELIX 164 164 SER H 217 GLN H 236 1 20
HELIX 165 165 PRO H 241 SER H 249 1 9
HELIX 166 166 SER H 249 ASN H 281 1 33
HELIX 167 167 GLY H 288 ALA H 297 1 10
HELIX 168 168 SER H 300 SER H 315 1 16
HELIX 169 169 VAL H 316 ASN H 333 1 18
HELIX 170 170 ASN H 333 HIS H 354 1 22
HELIX 171 171 LYS H 357 LEU H 362 1 6
HELIX 172 172 LEU H 362 TYR H 376 1 15
HELIX 173 173 LEU H 407 ARG H 412 1 6
HELIX 174 174 ASN H 424 LEU H 429 5 6
HELIX 175 175 PHE H 445 GLN H 449 5 5
HELIX 176 176 GLY H 452 HIS H 470 1 19
HELIX 177 177 PRO I 37 MET I 41 5 5
HELIX 178 178 ASN I 47 GLN I 59 1 13
HELIX 179 179 HIS I 63 PHE I 72 1 10
HELIX 180 180 LEU I 93 VAL I 103 1 11
HELIX 181 181 LEU I 113 GLY I 124 1 12
HELIX 182 182 ASN I 133 ARG I 143 1 11
HELIX 183 183 LEU I 144 LEU I 149 1 6
HELIX 184 184 SER I 150 ASN I 179 1 30
HELIX 185 185 VAL I 188 GLY I 206 1 19
HELIX 186 186 SER I 217 PHE I 239 1 23
HELIX 187 187 PRO I 241 SER I 249 1 9
HELIX 188 188 SER I 249 ASN I 281 1 33
HELIX 189 189 GLY I 288 ALA I 297 1 10
HELIX 190 190 SER I 300 SER I 315 1 16
HELIX 191 191 VAL I 316 ASN I 333 1 18
HELIX 192 192 ASN I 333 ALA I 347 1 15
HELIX 193 193 ALA I 347 HIS I 354 1 8
HELIX 194 194 LYS I 357 LEU I 362 1 6
HELIX 195 195 LEU I 362 TYR I 376 1 15
HELIX 196 196 LEU I 407 ASN I 413 1 7
HELIX 197 197 ASN I 424 LEU I 429 5 6
HELIX 198 198 PHE I 445 GLN I 449 5 5
HELIX 199 199 GLY I 452 HIS I 470 1 19
HELIX 200 200 PRO J 37 MET J 41 5 5
HELIX 201 201 ARG J 48 LEU J 53 1 6
HELIX 202 202 LEU J 53 GLN J 59 1 7
HELIX 203 203 HIS J 63 GLY J 76 1 14
HELIX 204 204 LEU J 93 VAL J 103 1 11
HELIX 205 205 LEU J 113 ARG J 123 1 11
HELIX 206 206 GLY J 128 LEU J 132 5 5
HELIX 207 207 ASN J 133 ARG J 143 1 11
HELIX 208 208 LEU J 144 LEU J 149 1 6
HELIX 209 209 SER J 150 ASN J 179 1 30
HELIX 210 210 VAL J 188 GLY J 206 1 19
HELIX 211 211 SER J 217 PHE J 239 1 23
HELIX 212 212 PRO J 241 SER J 249 1 9
HELIX 213 213 SER J 249 ASN J 281 1 33
HELIX 214 214 GLY J 288 ALA J 297 1 10
HELIX 215 215 SER J 300 SER J 315 1 16
HELIX 216 216 VAL J 316 ASN J 333 1 18
HELIX 217 217 ASN J 333 HIS J 354 1 22
HELIX 218 218 LYS J 357 LEU J 362 1 6
HELIX 219 219 LEU J 362 TYR J 376 1 15
HELIX 220 220 LEU J 407 ASN J 413 1 7
HELIX 221 221 ASN J 424 ASP J 430 5 7
HELIX 222 222 PHE J 445 GLN J 449 5 5
HELIX 223 223 GLY J 452 HIS J 470 1 19
HELIX 224 224 PRO K 37 MET K 41 5 5
HELIX 225 225 ASN K 47 GLN K 59 1 13
HELIX 226 226 HIS K 63 GLY K 76 1 14
HELIX 227 227 LEU K 93 VAL K 103 1 11
HELIX 228 228 LEU K 113 GLY K 124 1 12
HELIX 229 229 GLY K 134 ARG K 143 1 10
HELIX 230 230 LEU K 144 LEU K 149 1 6
HELIX 231 231 SER K 150 LEU K 177 1 28
HELIX 232 232 VAL K 188 GLY K 206 1 19
HELIX 233 233 SER K 217 PHE K 239 1 23
HELIX 234 234 PRO K 241 SER K 249 1 9
HELIX 235 235 SER K 249 ALA K 279 1 31
HELIX 236 236 GLY K 288 ALA K 297 1 10
HELIX 237 237 SER K 300 SER K 315 1 16
HELIX 238 238 VAL K 316 ASN K 333 1 18
HELIX 239 239 ASN K 333 ALA K 346 1 14
HELIX 240 240 ALA K 347 HIS K 354 1 8
HELIX 241 241 PRO K 355 THR K 360 5 6
HELIX 242 242 LEU K 362 TYR K 376 1 15
HELIX 243 243 LEU K 407 ARG K 412 1 6
HELIX 244 244 ASN K 424 TRP K 428 5 5
HELIX 245 245 PHE K 445 GLN K 449 5 5
HELIX 246 246 GLY K 452 HIS K 470 1 19
HELIX 247 247 PRO L 37 MET L 41 5 5
HELIX 248 248 TRP L 49 GLN L 59 1 11
HELIX 249 249 HIS L 63 GLY L 76 1 14
HELIX 250 250 LEU L 93 VAL L 103 1 11
HELIX 251 251 LEU L 113 ARG L 123 1 11
HELIX 252 252 ASN L 133 ARG L 143 1 11
HELIX 253 253 LEU L 144 LEU L 149 1 6
HELIX 254 254 SER L 150 GLN L 178 1 29
HELIX 255 255 VAL L 188 GLY L 206 1 19
HELIX 256 256 SER L 217 MET L 238 1 22
HELIX 257 257 PRO L 241 SER L 249 1 9
HELIX 258 258 SER L 249 ASN L 281 1 33
HELIX 259 259 GLY L 288 ALA L 297 1 10
HELIX 260 260 SER L 300 SER L 315 1 16
HELIX 261 261 VAL L 316 ASN L 333 1 18
HELIX 262 262 ASN L 333 HIS L 354 1 22
HELIX 263 263 LYS L 357 LEU L 362 1 6
HELIX 264 264 LEU L 362 TYR L 376 1 15
HELIX 265 265 LEU L 407 GLY L 411 1 5
HELIX 266 266 ASN L 424 LEU L 429 5 6
HELIX 267 267 PHE L 445 GLN L 449 5 5
HELIX 268 268 GLY L 452 LYS L 469 1 18
SHEET 1 A 4 ILE A 78 ARG A 80 0
SHEET 2 A 4 MET A 88 VAL A 91 -1 O CYS A 90 N PHE A 79
SHEET 3 A 4 LEU A 402 PHE A 406 1 O LEU A 402 N VAL A 89
SHEET 4 A 4 PHE A 381 VAL A 385 -1 N ARG A 384 O VAL A 403
SHEET 1 B 3 SER A 183 LEU A 186 0
SHEET 2 B 3 LEU A 497 ALA A 501 -1 O PHE A 499 N LEU A 184
SHEET 3 B 3 PHE A 471 GLU A 474 -1 N LEU A 472 O ARG A 500
SHEET 1 C 2 LEU A 390 LEU A 392 0
SHEET 2 C 2 TYR A 395 ILE A 397 -1 O ILE A 397 N LEU A 390
SHEET 1 D 2 MET A 483 TYR A 485 0
SHEET 2 D 2 LEU A 489 PRO A 491 -1 O ARG A 490 N VAL A 484
SHEET 1 E 4 ILE B 78 ASN B 82 0
SHEET 2 E 4 ARG B 87 VAL B 91 -1 O CYS B 90 N PHE B 79
SHEET 3 E 4 LEU B 402 PHE B 406 1 O LEU B 402 N ARG B 87
SHEET 4 E 4 PHE B 381 VAL B 385 -1 N ARG B 384 O VAL B 403
SHEET 1 F 3 SER B 183 LEU B 186 0
SHEET 2 F 3 LEU B 497 ALA B 501 -1 O PHE B 499 N LEU B 184
SHEET 3 F 3 PHE B 471 GLU B 474 -1 N LEU B 472 O ARG B 500
SHEET 1 G 2 LEU B 390 LEU B 392 0
SHEET 2 G 2 TYR B 395 ILE B 397 -1 O ILE B 397 N LEU B 390
SHEET 1 H 2 MET B 483 TYR B 485 0
SHEET 2 H 2 LEU B 489 PRO B 491 -1 O ARG B 490 N VAL B 484
SHEET 1 I 4 ILE C 78 ASN C 82 0
SHEET 2 I 4 ARG C 87 VAL C 91 -1 O CYS C 90 N PHE C 79
SHEET 3 I 4 LEU C 402 PHE C 406 1 O GLN C 404 N VAL C 89
SHEET 4 I 4 PHE C 381 VAL C 385 -1 N ARG C 384 O VAL C 403
SHEET 1 J 3 SER C 183 LEU C 186 0
SHEET 2 J 3 LEU C 497 ALA C 501 -1 O PHE C 499 N LEU C 184
SHEET 3 J 3 PHE C 471 GLU C 474 -1 N LEU C 472 O ARG C 500
SHEET 1 K 2 LEU C 390 LEU C 392 0
SHEET 2 K 2 TYR C 395 ILE C 397 -1 O ILE C 397 N LEU C 390
SHEET 1 L 2 MET C 483 TYR C 485 0
SHEET 2 L 2 LEU C 489 PRO C 491 -1 O ARG C 490 N VAL C 484
SHEET 1 M 4 ILE D 78 ASN D 82 0
SHEET 2 M 4 ARG D 87 VAL D 91 -1 O CYS D 90 N PHE D 79
SHEET 3 M 4 LEU D 402 PHE D 406 1 O GLN D 404 N VAL D 89
SHEET 4 M 4 PHE D 381 VAL D 385 -1 N ARG D 384 O VAL D 403
SHEET 1 N 3 SER D 183 LEU D 186 0
SHEET 2 N 3 LEU D 497 ALA D 501 -1 O LEU D 497 N LEU D 186
SHEET 3 N 3 PHE D 471 GLU D 474 -1 N LEU D 472 O ARG D 500
SHEET 1 O 2 LEU D 390 LEU D 392 0
SHEET 2 O 2 TYR D 395 ILE D 397 -1 O ILE D 397 N LEU D 390
SHEET 1 P 2 MET D 483 TYR D 485 0
SHEET 2 P 2 LEU D 489 PRO D 491 -1 O ARG D 490 N VAL D 484
SHEET 1 Q 5 GLN E 43 HIS E 44 0
SHEET 2 Q 5 ILE E 78 TYR E 81 1 O ARG E 80 N HIS E 44
SHEET 3 Q 5 MET E 88 VAL E 91 -1 O CYS E 90 N PHE E 79
SHEET 4 Q 5 LEU E 402 PHE E 406 1 O GLN E 404 N VAL E 89
SHEET 5 Q 5 PHE E 381 VAL E 385 -1 N ARG E 384 O VAL E 403
SHEET 1 R 3 SER E 183 LEU E 186 0
SHEET 2 R 3 LEU E 497 ALA E 501 -1 O PHE E 499 N LEU E 184
SHEET 3 R 3 PHE E 471 GLU E 474 -1 N LEU E 472 O ARG E 500
SHEET 1 S 2 LEU E 390 LEU E 392 0
SHEET 2 S 2 TYR E 395 ILE E 397 -1 O ILE E 397 N LEU E 390
SHEET 1 T 2 MET E 483 TYR E 485 0
SHEET 2 T 2 LEU E 489 PRO E 491 -1 O ARG E 490 N VAL E 484
SHEET 1 U 4 ILE F 78 ARG F 80 0
SHEET 2 U 4 MET F 88 VAL F 91 -1 O CYS F 90 N PHE F 79
SHEET 3 U 4 LEU F 402 PHE F 406 1 O LEU F 402 N VAL F 89
SHEET 4 U 4 PHE F 381 VAL F 385 -1 N ARG F 384 O VAL F 403
SHEET 1 V 3 SER F 183 LEU F 186 0
SHEET 2 V 3 LEU F 497 ALA F 501 -1 O PHE F 499 N LEU F 184
SHEET 3 V 3 PHE F 471 GLU F 474 -1 N GLU F 474 O THR F 498
SHEET 1 W 2 LEU F 390 LEU F 392 0
SHEET 2 W 2 TYR F 395 ILE F 397 -1 O ILE F 397 N LEU F 390
SHEET 1 X 2 MET F 483 TYR F 485 0
SHEET 2 X 2 LEU F 489 PRO F 491 -1 O ARG F 490 N VAL F 484
SHEET 1 Y 4 ILE G 78 TYR G 81 0
SHEET 2 Y 4 MET G 88 VAL G 91 -1 O CYS G 90 N PHE G 79
SHEET 3 Y 4 LEU G 402 PHE G 406 1 O GLN G 404 N VAL G 89
SHEET 4 Y 4 PHE G 381 VAL G 385 -1 N ARG G 384 O VAL G 403
SHEET 1 Z 3 SER G 183 LEU G 186 0
SHEET 2 Z 3 LEU G 497 ALA G 501 -1 O PHE G 499 N LEU G 184
SHEET 3 Z 3 PHE G 471 GLU G 474 -1 N GLU G 474 O THR G 498
SHEET 1 AA 2 LEU G 390 LEU G 392 0
SHEET 2 AA 2 TYR G 395 ILE G 397 -1 O ILE G 397 N LEU G 390
SHEET 1 AB 2 MET G 483 TYR G 485 0
SHEET 2 AB 2 LEU G 489 PRO G 491 -1 O ARG G 490 N VAL G 484
SHEET 1 AC 4 ILE H 78 TYR H 81 0
SHEET 2 AC 4 MET H 88 VAL H 91 -1 O CYS H 90 N PHE H 79
SHEET 3 AC 4 LEU H 402 PHE H 406 1 O GLN H 404 N VAL H 89
SHEET 4 AC 4 PHE H 381 VAL H 385 -1 N ARG H 384 O VAL H 403
SHEET 1 AD 3 SER H 183 LEU H 186 0
SHEET 2 AD 3 LEU H 497 ALA H 501 -1 O PHE H 499 N LEU H 184
SHEET 3 AD 3 PHE H 471 GLU H 474 -1 N GLU H 474 O THR H 498
SHEET 1 AE 2 LEU H 390 LEU H 392 0
SHEET 2 AE 2 TYR H 395 ILE H 397 -1 O ILE H 397 N LEU H 390
SHEET 1 AF 2 MET H 483 TYR H 485 0
SHEET 2 AF 2 LEU H 489 PRO H 491 -1 O ARG H 490 N VAL H 484
SHEET 1 AG 4 ILE I 78 TYR I 81 0
SHEET 2 AG 4 MET I 88 VAL I 91 -1 O CYS I 90 N PHE I 79
SHEET 3 AG 4 LEU I 402 PHE I 406 1 O LEU I 402 N VAL I 89
SHEET 4 AG 4 PHE I 381 VAL I 385 -1 N ARG I 384 O VAL I 403
SHEET 1 AH 3 SER I 183 LEU I 186 0
SHEET 2 AH 3 LEU I 497 ALA I 501 -1 O PHE I 499 N LEU I 184
SHEET 3 AH 3 PHE I 471 GLU I 474 -1 N GLU I 474 O THR I 498
SHEET 1 AI 2 LEU I 390 VAL I 391 0
SHEET 2 AI 2 HIS I 396 ILE I 397 -1 O ILE I 397 N LEU I 390
SHEET 1 AJ 2 MET I 483 TYR I 485 0
SHEET 2 AJ 2 LEU I 489 PRO I 491 -1 O ARG I 490 N VAL I 484
SHEET 1 AK 4 ILE J 78 TYR J 81 0
SHEET 2 AK 4 MET J 88 VAL J 91 -1 O CYS J 90 N PHE J 79
SHEET 3 AK 4 LEU J 402 PHE J 406 1 O LEU J 402 N VAL J 89
SHEET 4 AK 4 PHE J 381 VAL J 385 -1 N ARG J 384 O VAL J 403
SHEET 1 AL 3 SER J 183 LEU J 186 0
SHEET 2 AL 3 LEU J 497 ALA J 501 -1 O PHE J 499 N LEU J 184
SHEET 3 AL 3 PHE J 471 GLU J 474 -1 N GLU J 474 O THR J 498
SHEET 1 AM 2 LEU J 390 LEU J 392 0
SHEET 2 AM 2 TYR J 395 ILE J 397 -1 O ILE J 397 N LEU J 390
SHEET 1 AN 2 MET J 483 TYR J 485 0
SHEET 2 AN 2 LEU J 489 PRO J 491 -1 O ARG J 490 N VAL J 484
SHEET 1 AO 4 ILE K 78 ASN K 82 0
SHEET 2 AO 4 ARG K 87 VAL K 91 -1 O CYS K 90 N PHE K 79
SHEET 3 AO 4 LEU K 402 PHE K 406 1 O LEU K 402 N ARG K 87
SHEET 4 AO 4 PHE K 381 VAL K 385 -1 N ARG K 384 O VAL K 403
SHEET 1 AP 3 SER K 183 LEU K 186 0
SHEET 2 AP 3 LEU K 497 ALA K 501 -1 O PHE K 499 N LEU K 184
SHEET 3 AP 3 PHE K 471 GLU K 474 -1 N LEU K 472 O ARG K 500
SHEET 1 AQ 2 LEU K 390 LEU K 392 0
SHEET 2 AQ 2 TYR K 395 ILE K 397 -1 O ILE K 397 N LEU K 390
SHEET 1 AR 2 MET K 483 TYR K 485 0
SHEET 2 AR 2 LEU K 489 PRO K 491 -1 O ARG K 490 N VAL K 484
SHEET 1 AS 4 ILE L 78 ARG L 80 0
SHEET 2 AS 4 MET L 88 VAL L 91 -1 O CYS L 90 N PHE L 79
SHEET 3 AS 4 LEU L 402 PHE L 406 1 O GLN L 404 N VAL L 89
SHEET 4 AS 4 PHE L 381 VAL L 385 -1 N ARG L 384 O VAL L 403
SHEET 1 AT 3 SER L 183 LEU L 186 0
SHEET 2 AT 3 LEU L 497 ALA L 501 -1 O PHE L 499 N LEU L 184
SHEET 3 AT 3 PHE L 471 GLU L 474 -1 N GLU L 474 O THR L 498
SHEET 1 AU 2 LEU L 390 LEU L 392 0
SHEET 2 AU 2 TYR L 395 ILE L 397 -1 O ILE L 397 N LEU L 390
SHEET 1 AV 2 MET L 483 TYR L 485 0
SHEET 2 AV 2 LEU L 489 PRO L 491 -1 O ARG L 490 N VAL L 484
LINK SG CYS G 450 FE HEM G 601 1555 1555 2.24
LINK SG CYS A 450 FE HEM A 601 1555 1555 2.25
LINK SG CYS F 450 FE HEM F 601 1555 1555 2.25
LINK SG CYS H 450 FE HEM H 601 1555 1555 2.26
LINK SG CYS I 450 FE HEM I 601 1555 1555 2.31
LINK SG CYS E 450 FE HEM E 601 1555 1555 2.32
LINK SG CYS D 450 FE HEM D 601 1555 1555 2.32
LINK SG CYS C 450 FE HEM C 601 1555 1555 2.34
LINK SG CYS L 450 FE HEM L 601 1555 1555 2.37
LINK SG CYS B 450 FE HEM B 601 1555 1555 2.38
LINK SG CYS K 450 FE HEM K 601 1555 1555 2.47
LINK SG CYS J 450 FE HEM J 601 1555 1555 2.52
SITE 1 AC1 17 ARG A 110 TRP A 137 ARG A 141 LEU A 311
SITE 2 AC1 17 GLY A 314 SER A 315 THR A 318 LEU A 382
SITE 3 AC1 17 ARG A 384 PRO A 442 PHE A 443 GLY A 444
SITE 4 AC1 17 PHE A 445 ARG A 448 CYS A 450 GLY A 452
SITE 5 AC1 17 1CA A 602
SITE 1 AC2 7 GLU A 310 GLY A 314 GLY A 379 PHE A 381
SITE 2 AC2 7 PHE A 487 ILE A 488 HEM A 601
SITE 1 AC3 4 ARG A 366 ARG A 453 ARG A 454 HOH A 728
SITE 1 AC4 16 ARG B 110 VAL B 129 TRP B 137 ARG B 141
SITE 2 AC4 16 GLY B 314 SER B 315 THR B 318 LEU B 382
SITE 3 AC4 16 ARG B 384 PRO B 442 PHE B 443 GLY B 444
SITE 4 AC4 16 PHE B 445 ARG B 448 CYS B 450 1CA B 602
SITE 1 AC5 8 TRP B 116 PHE B 130 GLU B 310 GLY B 314
SITE 2 AC5 8 GLY B 379 PHE B 381 PHE B 487 HEM B 601
SITE 1 AC6 3 ARG B 366 ARG B 453 ARG B 454
SITE 1 AC7 20 ARG C 110 VAL C 129 TRP C 137 ARG C 141
SITE 2 AC7 20 LEU C 311 GLY C 314 SER C 315 THR C 318
SITE 3 AC7 20 THR C 319 LEU C 382 ARG C 384 PRO C 442
SITE 4 AC7 20 PHE C 443 GLY C 444 PHE C 445 ARG C 448
SITE 5 AC7 20 CYS C 450 LEU C 451 GLY C 452 1CA C 602
SITE 1 AC8 6 TRP C 116 GLU C 310 GLY C 379 PHE C 381
SITE 2 AC8 6 PHE C 487 HEM C 601
SITE 1 AC9 3 ARG C 366 ARG C 453 ARG C 454
SITE 1 BC1 19 ARG D 110 TRP D 137 ARG D 141 LEU D 311
SITE 2 BC1 19 GLY D 314 SER D 315 THR D 318 THR D 319
SITE 3 BC1 19 VAL D 378 ARG D 384 PRO D 442 PHE D 443
SITE 4 BC1 19 GLY D 444 PHE D 445 ARG D 448 CYS D 450
SITE 5 BC1 19 GLY D 452 1CA D 602 HOH D 713
SITE 1 BC2 8 TRP D 116 PHE D 130 GLU D 310 GLY D 379
SITE 2 BC2 8 PHE D 381 PHE D 487 HEM D 601 HOH D 713
SITE 1 BC3 3 ARG D 366 ARG D 453 ARG D 454
SITE 1 BC4 18 ARG E 110 VAL E 129 TRP E 137 ARG E 141
SITE 2 BC4 18 LEU E 311 SER E 315 THR E 318 VAL E 378
SITE 3 BC4 18 LEU E 382 ARG E 384 PRO E 442 PHE E 443
SITE 4 BC4 18 GLY E 444 PHE E 445 ARG E 448 CYS E 450
SITE 5 BC4 18 GLY E 452 1CA E 602
SITE 1 BC5 7 TRP E 116 PHE E 130 GLU E 310 GLY E 379
SITE 2 BC5 7 PHE E 381 PHE E 487 HEM E 601
SITE 1 BC6 3 ARG E 366 ARG E 453 ARG E 454
SITE 1 BC7 20 ARG F 110 VAL F 129 TRP F 137 ARG F 141
SITE 2 BC7 20 GLU F 310 LEU F 311 GLY F 314 SER F 315
SITE 3 BC7 20 THR F 318 LEU F 382 ARG F 384 PRO F 442
SITE 4 BC7 20 PHE F 443 GLY F 444 PHE F 445 ARG F 448
SITE 5 BC7 20 GLN F 449 CYS F 450 GLY F 452 1CA F 602
SITE 1 BC8 7 TRP F 116 PHE F 130 GLU F 310 GLY F 379
SITE 2 BC8 7 PHE F 381 PHE F 487 HEM F 601
SITE 1 BC9 3 ARG F 366 ARG F 453 ARG F 454
SITE 1 CC1 18 ARG G 110 VAL G 129 TRP G 137 ARG G 141
SITE 2 CC1 18 LEU G 311 SER G 315 THR G 318 LEU G 382
SITE 3 CC1 18 ARG G 384 PRO G 442 PHE G 443 GLY G 444
SITE 4 CC1 18 PHE G 445 ARG G 448 CYS G 450 GLY G 452
SITE 5 CC1 18 1CA G 602 HOH G 716
SITE 1 CC2 9 TRP G 116 GLU G 310 GLY G 314 GLY G 379
SITE 2 CC2 9 PHE G 381 PHE G 487 ILE G 488 HEM G 601
SITE 3 CC2 9 HOH G 716
SITE 1 CC3 3 ARG G 366 ARG G 453 ARG G 454
SITE 1 CC4 19 ARG H 110 VAL H 129 PHE H 130 TRP H 137
SITE 2 CC4 19 ARG H 141 GLU H 310 GLY H 314 SER H 315
SITE 3 CC4 19 THR H 318 VAL H 378 LEU H 382 ARG H 384
SITE 4 CC4 19 PRO H 442 PHE H 443 GLY H 444 PHE H 445
SITE 5 CC4 19 ARG H 448 CYS H 450 1CA H 602
SITE 1 CC5 7 TRP H 116 PHE H 130 GLU H 310 GLY H 379
SITE 2 CC5 7 PHE H 381 PHE H 487 HEM H 601
SITE 1 CC6 17 ARG I 110 VAL I 129 TRP I 137 ARG I 141
SITE 2 CC6 17 GLY I 314 SER I 315 THR I 318 LEU I 382
SITE 3 CC6 17 ARG I 384 PRO I 442 PHE I 443 GLY I 444
SITE 4 CC6 17 PHE I 445 ARG I 448 CYS I 450 GLY I 452
SITE 5 CC6 17 1CA I 602
SITE 1 CC7 8 TRP I 116 PHE I 130 GLU I 310 GLY I 379
SITE 2 CC7 8 LEU I 380 PHE I 381 PHE I 487 HEM I 601
SITE 1 CC8 16 ARG J 110 VAL J 129 TRP J 137 ARG J 141
SITE 2 CC8 16 GLY J 314 SER J 315 THR J 318 LEU J 382
SITE 3 CC8 16 ARG J 384 PRO J 442 PHE J 443 GLY J 444
SITE 4 CC8 16 PHE J 445 ARG J 448 CYS J 450 1CA J 602
SITE 1 CC9 7 GLU J 310 GLY J 314 GLY J 379 LEU J 380
SITE 2 CC9 7 PHE J 381 PHE J 487 HEM J 601
SITE 1 DC1 20 ARG K 110 VAL K 129 TRP K 137 ARG K 141
SITE 2 DC1 20 SER K 315 THR K 318 VAL K 378 LEU K 382
SITE 3 DC1 20 ARG K 384 PRO K 442 PHE K 443 GLY K 444
SITE 4 DC1 20 PHE K 445 ARG K 448 GLN K 449 CYS K 450
SITE 5 DC1 20 LEU K 451 GLY K 452 1CA K 602 HOH K 704
SITE 1 DC2 9 ARG K 110 GLU K 310 GLY K 314 GLY K 379
SITE 2 DC2 9 PHE K 381 PHE K 487 ILE K 488 HEM K 601
SITE 3 DC2 9 HOH K 704
SITE 1 DC3 3 ARG K 366 ARG K 453 ARG K 454
SITE 1 DC4 17 ARG L 110 VAL L 129 TRP L 137 ARG L 141
SITE 2 DC4 17 SER L 315 THR L 318 VAL L 378 LEU L 382
SITE 3 DC4 17 ARG L 384 PRO L 442 PHE L 443 GLY L 444
SITE 4 DC4 17 PHE L 445 ARG L 448 CYS L 450 GLY L 452
SITE 5 DC4 17 1CA L 602
SITE 1 DC5 10 TRP L 116 PHE L 130 GLU L 310 GLY L 314
SITE 2 DC5 10 GLY L 379 PHE L 381 LEU L 382 PHE L 487
SITE 3 DC5 10 ILE L 488 HEM L 601
SITE 1 DC6 3 ARG L 366 ARG L 453 ARG L 454
CRYST1 130.347 199.629 150.153 90.00 112.18 90.00 P 1 21 1 24
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 0.007672 0.000000 0.003128 0.00000
SCALE2 0.000000 0.005009 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007192 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
