HEADER OXIDOREDUCTASE 13-APR-12 4ENW
TITLE STRUCTURE OF THE S234N VARIANT OF E. COLI KATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATALASE HPII;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: HYDROXYPEROXIDASE II;
COMPND 5 EC: 1.11.1.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B1732, JW1721, KATE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: UM255;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PKS
KEYWDS CATALASE FOLD, KATE, S234N VARIANT, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.C.LOEWEN,V.JHA
REVDAT 3 13-SEP-23 4ENW 1 REMARK SEQADV LINK
REVDAT 2 27-FEB-13 4ENW 1 JRNL
REVDAT 1 02-MAY-12 4ENW 0
JRNL AUTH V.JHA,P.CHELIKANI,X.CARPENA,I.FITA,P.C.LOEWEN
JRNL TITL INFLUENCE OF MAIN CHANNEL STRUCTURE ON H(2)O(2) ACCESS TO
JRNL TITL 2 THE HEME CAVITY OF CATALASE KATE OF ESCHERICHIA COLI.
JRNL REF ARCH.BIOCHEM.BIOPHYS. V. 526 54 2012
JRNL REFN ISSN 0003-9861
JRNL PMID 22820098
JRNL DOI 10.1016/J.ABB.2012.06.010
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.13
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 206533
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10355
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 12674
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.4090
REMARK 3 BIN FREE R VALUE SET COUNT : 662
REMARK 3 BIN FREE R VALUE : 0.4400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 22960
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 176
REMARK 3 SOLVENT ATOMS : 2752
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.12000
REMARK 3 B22 (A**2) : -0.26000
REMARK 3 B33 (A**2) : 0.68000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.46000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.183
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.159
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.092
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.900
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 23841 ; 0.019 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 32505 ; 2.068 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2912 ; 6.568 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1181 ;36.757 ;23.870
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3768 ;14.966 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 176 ;15.161 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3427 ; 0.151 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18836 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 28 A 753 4
REMARK 3 1 B 28 B 753 4
REMARK 3 1 C 28 C 753 4
REMARK 3 1 D 28 D 753 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 5736 ; 0.310 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 5736 ; 0.310 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 5736 ; 0.320 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 5736 ; 0.350 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 5736 ; 2.270 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 5736 ; 2.060 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 5736 ; 1.990 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 5736 ; 1.810 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 28 A 753
REMARK 3 RESIDUE RANGE : A 801 A 801
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5142 -9.1911 31.7428
REMARK 3 T TENSOR
REMARK 3 T11: 0.0100 T22: 0.0096
REMARK 3 T33: 0.0235 T12: 0.0035
REMARK 3 T13: 0.0108 T23: 0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 0.0575 L22: 0.0814
REMARK 3 L33: 0.0459 L12: 0.0005
REMARK 3 L13: 0.0246 L23: -0.0186
REMARK 3 S TENSOR
REMARK 3 S11: -0.0056 S12: -0.0150 S13: -0.0245
REMARK 3 S21: 0.0225 S22: 0.0121 S23: 0.0247
REMARK 3 S31: 0.0012 S32: -0.0100 S33: -0.0065
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 28 B 753
REMARK 3 RESIDUE RANGE : B 801 B 801
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4521 11.7914 -18.8396
REMARK 3 T TENSOR
REMARK 3 T11: 0.0272 T22: 0.0087
REMARK 3 T33: 0.0218 T12: 0.0001
REMARK 3 T13: -0.0137 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 0.0656 L22: 0.1033
REMARK 3 L33: 0.0513 L12: -0.0355
REMARK 3 L13: -0.0257 L23: -0.0113
REMARK 3 S TENSOR
REMARK 3 S11: 0.0055 S12: 0.0136 S13: 0.0229
REMARK 3 S21: -0.0474 S22: -0.0027 S23: 0.0093
REMARK 3 S31: 0.0004 S32: -0.0123 S33: -0.0029
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 28 C 753
REMARK 3 RESIDUE RANGE : C 801 C 801
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1321 -11.6795 -19.4655
REMARK 3 T TENSOR
REMARK 3 T11: 0.0335 T22: 0.0092
REMARK 3 T33: 0.0176 T12: -0.0057
REMARK 3 T13: 0.0151 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.0610 L22: 0.0942
REMARK 3 L33: 0.0552 L12: -0.0071
REMARK 3 L13: 0.0031 L23: -0.0030
REMARK 3 S TENSOR
REMARK 3 S11: -0.0091 S12: 0.0101 S13: -0.0241
REMARK 3 S21: -0.0500 S22: 0.0044 S23: -0.0100
REMARK 3 S31: 0.0117 S32: 0.0110 S33: 0.0047
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 28 D 753
REMARK 3 RESIDUE RANGE : D 801 D 801
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6027 9.0432 31.1587
REMARK 3 T TENSOR
REMARK 3 T11: 0.0111 T22: 0.0190
REMARK 3 T33: 0.0145 T12: -0.0032
REMARK 3 T13: -0.0038 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.0800 L22: 0.0865
REMARK 3 L33: 0.0357 L12: 0.0412
REMARK 3 L13: -0.0232 L23: 0.0050
REMARK 3 S TENSOR
REMARK 3 S11: 0.0106 S12: -0.0181 S13: 0.0135
REMARK 3 S21: 0.0226 S22: -0.0031 S23: -0.0057
REMARK 3 S31: -0.0078 S32: 0.0216 S33: -0.0075
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 4ENW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071852.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
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) : 0.98
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 206796
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 35.131
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.6
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.23800
REMARK 200 R SYM FOR SHELL (I) : 0.23800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1GGE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG3350, 1.6 M LICL, 0.1 M TRIS,
REMARK 280 PH 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 66.28500
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 58830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 78160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -277.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLN A 3
REMARK 465 HIS A 4
REMARK 465 ASN A 5
REMARK 465 GLU A 6
REMARK 465 LYS A 7
REMARK 465 ASN A 8
REMARK 465 PRO A 9
REMARK 465 HIS A 10
REMARK 465 GLN A 11
REMARK 465 HIS A 12
REMARK 465 GLN A 13
REMARK 465 SER A 14
REMARK 465 PRO A 15
REMARK 465 LEU A 16
REMARK 465 HIS A 17
REMARK 465 ASP A 18
REMARK 465 SER A 19
REMARK 465 SER A 20
REMARK 465 GLU A 21
REMARK 465 ALA A 22
REMARK 465 LYS A 23
REMARK 465 PRO A 24
REMARK 465 GLY A 25
REMARK 465 MET A 26
REMARK 465 ASP A 27
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLN B 3
REMARK 465 HIS B 4
REMARK 465 ASN B 5
REMARK 465 GLU B 6
REMARK 465 LYS B 7
REMARK 465 ASN B 8
REMARK 465 PRO B 9
REMARK 465 HIS B 10
REMARK 465 GLN B 11
REMARK 465 HIS B 12
REMARK 465 GLN B 13
REMARK 465 SER B 14
REMARK 465 PRO B 15
REMARK 465 LEU B 16
REMARK 465 HIS B 17
REMARK 465 ASP B 18
REMARK 465 SER B 19
REMARK 465 SER B 20
REMARK 465 GLU B 21
REMARK 465 ALA B 22
REMARK 465 LYS B 23
REMARK 465 PRO B 24
REMARK 465 GLY B 25
REMARK 465 MET B 26
REMARK 465 ASP B 27
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLN C 3
REMARK 465 HIS C 4
REMARK 465 ASN C 5
REMARK 465 GLU C 6
REMARK 465 LYS C 7
REMARK 465 ASN C 8
REMARK 465 PRO C 9
REMARK 465 HIS C 10
REMARK 465 GLN C 11
REMARK 465 HIS C 12
REMARK 465 GLN C 13
REMARK 465 SER C 14
REMARK 465 PRO C 15
REMARK 465 LEU C 16
REMARK 465 HIS C 17
REMARK 465 ASP C 18
REMARK 465 SER C 19
REMARK 465 SER C 20
REMARK 465 GLU C 21
REMARK 465 ALA C 22
REMARK 465 LYS C 23
REMARK 465 PRO C 24
REMARK 465 GLY C 25
REMARK 465 MET C 26
REMARK 465 ASP C 27
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 GLN D 3
REMARK 465 HIS D 4
REMARK 465 ASN D 5
REMARK 465 GLU D 6
REMARK 465 LYS D 7
REMARK 465 ASN D 8
REMARK 465 PRO D 9
REMARK 465 HIS D 10
REMARK 465 GLN D 11
REMARK 465 HIS D 12
REMARK 465 GLN D 13
REMARK 465 SER D 14
REMARK 465 PRO D 15
REMARK 465 LEU D 16
REMARK 465 HIS D 17
REMARK 465 ASP D 18
REMARK 465 SER D 19
REMARK 465 SER D 20
REMARK 465 GLU D 21
REMARK 465 ALA D 22
REMARK 465 LYS D 23
REMARK 465 PRO D 24
REMARK 465 GLY D 25
REMARK 465 MET D 26
REMARK 465 ASP D 27
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 ND1 HIS D 392 CB TYR D 415 1.69
REMARK 500 ND1 HIS A 392 CB TYR A 415 1.71
REMARK 500 ND1 HIS C 392 CB TYR C 415 1.71
REMARK 500 ND1 HIS B 392 CB TYR B 415 1.72
REMARK 500 O HOH D 1252 O HOH D 1306 1.93
REMARK 500 O HOH C 1260 O HOH C 1549 2.01
REMARK 500 O HOH D 1326 O HOH D 1541 2.02
REMARK 500 O HOH A 1536 O HOH C 1133 2.05
REMARK 500 OE1 GLN D 368 O HOH D 1555 2.07
REMARK 500 O HOH D 1640 O HOH D 1641 2.14
REMARK 500 O HOH C 1436 O HOH C 1547 2.15
REMARK 500 CD LYS D 73 O HOH B 1463 2.16
REMARK 500 O HOH B 1352 O HOH B 1401 2.17
REMARK 500 CG GLU A 716 O HOH A 1302 2.18
REMARK 500 O HOH D 1492 O HOH D 1540 2.19
REMARK 500 O HOH A 1151 O HOH A 1353 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CB ASP C 59 O HOH B 1526 2545 2.00
REMARK 500
REMARK 500 REMARK: NULL
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 135 CG HIS A 135 CD2 0.063
REMARK 500 HIS A 318 CG HIS A 318 CD2 0.058
REMARK 500 GLU A 321 CD GLU A 321 OE1 0.074
REMARK 500 TRP A 323 CE2 TRP A 323 CD2 0.074
REMARK 500 TYR A 440 CE1 TYR A 440 CZ 0.094
REMARK 500 HIS A 549 CG HIS A 549 CD2 0.063
REMARK 500 TRP A 742 CE2 TRP A 742 CD2 0.076
REMARK 500 TRP B 255 CE2 TRP B 255 CD2 0.089
REMARK 500 TYR B 440 CE1 TYR B 440 CZ 0.102
REMARK 500 HIS B 449 CG HIS B 449 CD2 0.077
REMARK 500 HIS C 449 CG HIS C 449 CD2 0.059
REMARK 500 TRP C 469 CE2 TRP C 469 CD2 0.077
REMARK 500 HIS C 522 CG HIS C 522 CD2 0.056
REMARK 500 HIS D 236 CG HIS D 236 CD2 0.060
REMARK 500 HIS D 251 CG HIS D 251 CD2 0.061
REMARK 500 TRP D 293 CE2 TRP D 293 CD2 0.084
REMARK 500 TRP D 323 CE2 TRP D 323 CD2 0.078
REMARK 500 HIS D 522 CG HIS D 522 CD2 0.071
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 ARG A 130 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP A 350 CB - CG - OD1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG A 377 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG A 471 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 479 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 740 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 121 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 LEU B 375 CB - CG - CD1 ANGL. DEV. = 12.0 DEGREES
REMARK 500 ASP B 401 CB - CG - OD1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP B 401 CB - CG - OD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG B 422 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 LEU B 590 CB - CG - CD2 ANGL. DEV. = -11.2 DEGREES
REMARK 500 ARG C 471 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 LEU C 552 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
REMARK 500 ARG C 636 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG C 636 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP D 401 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 LYS D 478 CD - CE - NZ ANGL. DEV. = 23.1 DEGREES
REMARK 500 LEU D 582 CB - CG - CD1 ANGL. DEV. = 10.7 DEGREES
REMARK 500 ARG D 740 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 75 -37.39 -165.95
REMARK 500 THR A 178 36.32 -90.85
REMARK 500 ILE A 274 -64.75 71.72
REMARK 500 ASP A 314 86.06 -155.01
REMARK 500 ASP A 405 113.46 -32.41
REMARK 500 ASP A 446 -153.63 70.66
REMARK 500 ASP A 595 36.86 -159.04
REMARK 500 GLU A 610 58.35 -148.97
REMARK 500 ASP A 725 -169.61 -78.55
REMARK 500 HIS A 739 -64.98 77.64
REMARK 500 VAL A 741 77.21 -102.34
REMARK 500 SER B 35 3.55 -69.88
REMARK 500 SER B 75 -39.69 -163.37
REMARK 500 THR B 178 38.66 -87.37
REMARK 500 ILE B 274 -61.30 68.98
REMARK 500 ASP B 314 88.24 -153.72
REMARK 500 ASN B 442 -167.93 -163.82
REMARK 500 ASP B 446 -151.84 65.24
REMARK 500 HIS B 449 31.57 70.63
REMARK 500 ASP B 595 31.94 -148.67
REMARK 500 GLU B 610 61.22 -152.25
REMARK 500 ARG B 612 89.96 -59.05
REMARK 500 ALA B 724 30.87 -88.66
REMARK 500 ASP B 725 -179.63 -33.18
REMARK 500 HIS B 739 -61.19 67.52
REMARK 500 SER C 75 -36.75 -164.50
REMARK 500 THR C 178 40.95 -91.42
REMARK 500 ILE C 274 -62.17 65.21
REMARK 500 PHE C 277 -169.98 -112.60
REMARK 500 ASP C 314 82.12 -154.49
REMARK 500 ASN C 442 -168.30 -165.32
REMARK 500 ASP C 446 -154.81 67.94
REMARK 500 LYS C 584 155.71 171.95
REMARK 500 ASP C 595 33.63 -150.61
REMARK 500 ASP C 725 -134.81 -144.81
REMARK 500 HIS C 739 -65.86 78.45
REMARK 500 SER D 75 -35.79 -166.80
REMARK 500 VAL D 169 -51.96 -121.19
REMARK 500 THR D 178 38.52 -88.46
REMARK 500 ILE D 274 -60.38 65.41
REMARK 500 ASP D 405 116.22 -37.88
REMARK 500 ASN D 442 -167.73 -163.19
REMARK 500 ASP D 446 -151.47 73.85
REMARK 500 ASP D 595 34.93 -142.58
REMARK 500 GLU D 610 71.49 -154.76
REMARK 500 HIS D 739 -64.62 73.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA C 724 ASP C 725 146.14
REMARK 500 ASP C 725 GLY C 726 -142.50
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 HDD A 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 415 OH
REMARK 620 2 HDD A 801 NA 95.1
REMARK 620 3 HDD A 801 NB 86.5 88.7
REMARK 620 4 HDD A 801 NC 94.8 170.0 90.7
REMARK 620 5 HDD A 801 ND 95.0 91.0 178.5 89.4
REMARK 620 6 HOH A1506 O 160.8 81.7 74.6 88.5 104.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HDD B 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 415 OH
REMARK 620 2 HDD B 801 NA 93.5
REMARK 620 3 HDD B 801 NB 83.6 91.1
REMARK 620 4 HDD B 801 NC 94.0 172.3 91.2
REMARK 620 5 HDD B 801 ND 97.7 88.5 178.6 89.0
REMARK 620 6 HOH B1460 O 163.7 84.6 80.2 88.6 98.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HDD C 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR C 415 OH
REMARK 620 2 HDD C 801 NA 93.1
REMARK 620 3 HDD C 801 NB 86.5 89.8
REMARK 620 4 HDD C 801 NC 94.2 172.5 92.4
REMARK 620 5 HDD C 801 ND 94.8 89.6 178.5 88.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HDD D 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR D 415 OH
REMARK 620 2 HDD D 801 NA 95.9
REMARK 620 3 HDD D 801 NB 87.3 90.7
REMARK 620 4 HDD D 801 NC 93.7 170.3 90.5
REMARK 620 5 HDD D 801 ND 94.3 89.0 178.3 89.5
REMARK 620 6 HOH D1643 O 160.0 84.9 72.7 86.4 105.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD C 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HDD D 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ENP RELATED DB: PDB
REMARK 900 RELATED ID: 4ENQ RELATED DB: PDB
REMARK 900 RELATED ID: 4ENR RELATED DB: PDB
REMARK 900 RELATED ID: 4ENS RELATED DB: PDB
REMARK 900 RELATED ID: 4ENT RELATED DB: PDB
REMARK 900 RELATED ID: 4ENU RELATED DB: PDB
REMARK 900 RELATED ID: 4ENV RELATED DB: PDB
DBREF 4ENW A 1 753 UNP P21179 CATE_ECOLI 1 753
DBREF 4ENW B 1 753 UNP P21179 CATE_ECOLI 1 753
DBREF 4ENW C 1 753 UNP P21179 CATE_ECOLI 1 753
DBREF 4ENW D 1 753 UNP P21179 CATE_ECOLI 1 753
SEQADV 4ENW ASN A 234 UNP P21179 SER 234 ENGINEERED MUTATION
SEQADV 4ENW ASN B 234 UNP P21179 SER 234 ENGINEERED MUTATION
SEQADV 4ENW ASN C 234 UNP P21179 SER 234 ENGINEERED MUTATION
SEQADV 4ENW ASN D 234 UNP P21179 SER 234 ENGINEERED MUTATION
SEQRES 1 A 753 MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES 2 A 753 SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES 3 A 753 ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES 4 A 753 ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES 5 A 753 GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES 6 A 753 ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES 7 A 753 ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES 8 A 753 GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES 9 A 753 LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES 10 A 753 ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES 11 A 753 GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES 12 A 753 LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES 13 A 753 ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 14 A 753 GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES 15 A 753 ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES 16 A 753 PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES 17 A 753 GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES 18 A 753 LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN ASN
SEQRES 19 A 753 ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES 20 A 753 GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES 21 A 753 GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES 22 A 753 ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES 23 A 753 THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES 24 A 753 ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES 25 A 753 ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES 26 A 753 ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES 27 A 753 GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES 28 A 753 ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES 29 A 753 VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES 30 A 753 ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES 31 A 753 PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES 32 A 753 ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES 33 A 753 ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES 34 A 753 GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES 35 A 753 PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES 36 A 753 ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES 37 A 753 TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES 38 A 753 PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES 39 A 753 ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES 40 A 753 PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES 41 A 753 ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES 42 A 753 VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES 43 A 753 LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES 44 A 753 LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES 45 A 753 ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES 46 A 753 PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES 47 A 753 LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES 48 A 753 ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES 49 A 753 ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES 50 A 753 GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES 51 A 753 ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES 52 A 753 ALA VAL ILE VAL PRO CYS GLY ASN ILE ALA ASP ILE ALA
SEQRES 53 A 753 ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES 54 A 753 LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES 55 A 753 LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES 56 A 753 GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES 57 A 753 MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES 58 A 753 TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
SEQRES 1 B 753 MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES 2 B 753 SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES 3 B 753 ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES 4 B 753 ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES 5 B 753 GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES 6 B 753 ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES 7 B 753 ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES 8 B 753 GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES 9 B 753 LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES 10 B 753 ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES 11 B 753 GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES 12 B 753 LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES 13 B 753 ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 14 B 753 GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES 15 B 753 ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES 16 B 753 PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES 17 B 753 GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES 18 B 753 LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN ASN
SEQRES 19 B 753 ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES 20 B 753 GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES 21 B 753 GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES 22 B 753 ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES 23 B 753 THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES 24 B 753 ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES 25 B 753 ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES 26 B 753 ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES 27 B 753 GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES 28 B 753 ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES 29 B 753 VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES 30 B 753 ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES 31 B 753 PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES 32 B 753 ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES 33 B 753 ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES 34 B 753 GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES 35 B 753 PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES 36 B 753 ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES 37 B 753 TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES 38 B 753 PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES 39 B 753 ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES 40 B 753 PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES 41 B 753 ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES 42 B 753 VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES 43 B 753 LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES 44 B 753 LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES 45 B 753 ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES 46 B 753 PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES 47 B 753 LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES 48 B 753 ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES 49 B 753 ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES 50 B 753 GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES 51 B 753 ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES 52 B 753 ALA VAL ILE VAL PRO CYS GLY ASN ILE ALA ASP ILE ALA
SEQRES 53 B 753 ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES 54 B 753 LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES 55 B 753 LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES 56 B 753 GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES 57 B 753 MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES 58 B 753 TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
SEQRES 1 C 753 MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES 2 C 753 SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES 3 C 753 ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES 4 C 753 ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES 5 C 753 GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES 6 C 753 ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES 7 C 753 ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES 8 C 753 GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES 9 C 753 LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES 10 C 753 ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES 11 C 753 GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES 12 C 753 LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES 13 C 753 ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 14 C 753 GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES 15 C 753 ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES 16 C 753 PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES 17 C 753 GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES 18 C 753 LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN ASN
SEQRES 19 C 753 ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES 20 C 753 GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES 21 C 753 GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES 22 C 753 ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES 23 C 753 THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES 24 C 753 ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES 25 C 753 ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES 26 C 753 ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES 27 C 753 GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES 28 C 753 ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES 29 C 753 VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES 30 C 753 ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES 31 C 753 PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES 32 C 753 ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES 33 C 753 ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES 34 C 753 GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES 35 C 753 PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES 36 C 753 ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES 37 C 753 TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES 38 C 753 PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES 39 C 753 ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES 40 C 753 PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES 41 C 753 ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES 42 C 753 VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES 43 C 753 LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES 44 C 753 LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES 45 C 753 ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES 46 C 753 PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES 47 C 753 LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES 48 C 753 ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES 49 C 753 ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES 50 C 753 GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES 51 C 753 ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES 52 C 753 ALA VAL ILE VAL PRO CYS GLY ASN ILE ALA ASP ILE ALA
SEQRES 53 C 753 ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES 54 C 753 LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES 55 C 753 LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES 56 C 753 GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES 57 C 753 MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES 58 C 753 TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
SEQRES 1 D 753 MET SER GLN HIS ASN GLU LYS ASN PRO HIS GLN HIS GLN
SEQRES 2 D 753 SER PRO LEU HIS ASP SER SER GLU ALA LYS PRO GLY MET
SEQRES 3 D 753 ASP SER LEU ALA PRO GLU ASP GLY SER HIS ARG PRO ALA
SEQRES 4 D 753 ALA GLU PRO THR PRO PRO GLY ALA GLN PRO THR ALA PRO
SEQRES 5 D 753 GLY SER LEU LYS ALA PRO ASP THR ARG ASN GLU LYS LEU
SEQRES 6 D 753 ASN SER LEU GLU ASP VAL ARG LYS GLY SER GLU ASN TYR
SEQRES 7 D 753 ALA LEU THR THR ASN GLN GLY VAL ARG ILE ALA ASP ASP
SEQRES 8 D 753 GLN ASN SER LEU ARG ALA GLY SER ARG GLY PRO THR LEU
SEQRES 9 D 753 LEU GLU ASP PHE ILE LEU ARG GLU LYS ILE THR HIS PHE
SEQRES 10 D 753 ASP HIS GLU ARG ILE PRO GLU ARG ILE VAL HIS ALA ARG
SEQRES 11 D 753 GLY SER ALA ALA HIS GLY TYR PHE GLN PRO TYR LYS SER
SEQRES 12 D 753 LEU SER ASP ILE THR LYS ALA ASP PHE LEU SER ASP PRO
SEQRES 13 D 753 ASN LYS ILE THR PRO VAL PHE VAL ARG PHE SER THR VAL
SEQRES 14 D 753 GLN GLY GLY ALA GLY SER ALA ASP THR VAL ARG ASP ILE
SEQRES 15 D 753 ARG GLY PHE ALA THR LYS PHE TYR THR GLU GLU GLY ILE
SEQRES 16 D 753 PHE ASP LEU VAL GLY ASN ASN THR PRO ILE PHE PHE ILE
SEQRES 17 D 753 GLN ASP ALA HIS LYS PHE PRO ASP PHE VAL HIS ALA VAL
SEQRES 18 D 753 LYS PRO GLU PRO HIS TRP ALA ILE PRO GLN GLY GLN ASN
SEQRES 19 D 753 ALA HIS ASP THR PHE TRP ASP TYR VAL SER LEU GLN PRO
SEQRES 20 D 753 GLU THR LEU HIS ASN VAL MET TRP ALA MET SER ASP ARG
SEQRES 21 D 753 GLY ILE PRO ARG SER TYR ARG THR MET GLU GLY PHE GLY
SEQRES 22 D 753 ILE HIS THR PHE ARG LEU ILE ASN ALA GLU GLY LYS ALA
SEQRES 23 D 753 THR PHE VAL ARG PHE HIS TRP LYS PRO LEU ALA GLY LYS
SEQRES 24 D 753 ALA SER LEU VAL TRP ASP GLU ALA GLN LYS LEU THR GLY
SEQRES 25 D 753 ARG ASP PRO ASP PHE HIS ARG ARG GLU LEU TRP GLU ALA
SEQRES 26 D 753 ILE GLU ALA GLY ASP PHE PRO GLU TYR GLU LEU GLY PHE
SEQRES 27 D 753 GLN LEU ILE PRO GLU GLU ASP GLU PHE LYS PHE ASP PHE
SEQRES 28 D 753 ASP LEU LEU ASP PRO THR LYS LEU ILE PRO GLU GLU LEU
SEQRES 29 D 753 VAL PRO VAL GLN ARG VAL GLY LYS MET VAL LEU ASN ARG
SEQRES 30 D 753 ASN PRO ASP ASN PHE PHE ALA GLU ASN GLU GLN ALA ALA
SEQRES 31 D 753 PHE HIS PRO GLY HIS ILE VAL PRO GLY LEU ASP PHE THR
SEQRES 32 D 753 ASN ASP PRO LEU LEU GLN GLY ARG LEU PHE SER TYR THR
SEQRES 33 D 753 ASP THR GLN ILE SER ARG LEU GLY GLY PRO ASN PHE HIS
SEQRES 34 D 753 GLU ILE PRO ILE ASN ARG PRO THR CYS PRO TYR HIS ASN
SEQRES 35 D 753 PHE GLN ARG ASP GLY MET HIS ARG MET GLY ILE ASP THR
SEQRES 36 D 753 ASN PRO ALA ASN TYR GLU PRO ASN SER ILE ASN ASP ASN
SEQRES 37 D 753 TRP PRO ARG GLU THR PRO PRO GLY PRO LYS ARG GLY GLY
SEQRES 38 D 753 PHE GLU SER TYR GLN GLU ARG VAL GLU GLY ASN LYS VAL
SEQRES 39 D 753 ARG GLU ARG SER PRO SER PHE GLY GLU TYR TYR SER HIS
SEQRES 40 D 753 PRO ARG LEU PHE TRP LEU SER GLN THR PRO PHE GLU GLN
SEQRES 41 D 753 ARG HIS ILE VAL ASP GLY PHE SER PHE GLU LEU SER LYS
SEQRES 42 D 753 VAL VAL ARG PRO TYR ILE ARG GLU ARG VAL VAL ASP GLN
SEQRES 43 D 753 LEU ALA HIS ILE ASP LEU THR LEU ALA GLN ALA VAL ALA
SEQRES 44 D 753 LYS ASN LEU GLY ILE GLU LEU THR ASP ASP GLN LEU ASN
SEQRES 45 D 753 ILE THR PRO PRO PRO ASP VAL ASN GLY LEU LYS LYS ASP
SEQRES 46 D 753 PRO SER LEU SER LEU TYR ALA ILE PRO ASP GLY ASP VAL
SEQRES 47 D 753 LYS GLY ARG VAL VAL ALA ILE LEU LEU ASN ASP GLU VAL
SEQRES 48 D 753 ARG SER ALA ASP LEU LEU ALA ILE LEU LYS ALA LEU LYS
SEQRES 49 D 753 ALA LYS GLY VAL HIS ALA LYS LEU LEU TYR SER ARG MET
SEQRES 50 D 753 GLY GLU VAL THR ALA ASP ASP GLY THR VAL LEU PRO ILE
SEQRES 51 D 753 ALA ALA THR PHE ALA GLY ALA PRO SER LEU THR VAL ASP
SEQRES 52 D 753 ALA VAL ILE VAL PRO CYS GLY ASN ILE ALA ASP ILE ALA
SEQRES 53 D 753 ASP ASN GLY ASP ALA ASN TYR TYR LEU MET GLU ALA TYR
SEQRES 54 D 753 LYS HIS LEU LYS PRO ILE ALA LEU ALA GLY ASP ALA ARG
SEQRES 55 D 753 LYS PHE LYS ALA THR ILE LYS ILE ALA ASP GLN GLY GLU
SEQRES 56 D 753 GLU GLY ILE VAL GLU ALA ASP SER ALA ASP GLY SER PHE
SEQRES 57 D 753 MET ASP GLU LEU LEU THR LEU MET ALA ALA HIS ARG VAL
SEQRES 58 D 753 TRP SER ARG ILE PRO LYS ILE ASP LYS ILE PRO ALA
HET HDD A 801 44
HET HDD B 801 44
HET HDD C 801 44
HET HDD D 801 44
HETNAM HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE
HETSYN HDD HEME
FORMUL 5 HDD 4(C34 H32 FE N4 O5)
FORMUL 9 HOH *2752(H2 O)
HELIX 1 1 PRO A 52 ALA A 57 1 6
HELIX 2 2 ASN A 62 LEU A 68 1 7
HELIX 3 3 ASP A 107 HIS A 119 1 13
HELIX 4 4 ALA A 150 SER A 154 5 5
HELIX 5 5 ASP A 210 HIS A 212 5 3
HELIX 6 6 LYS A 213 LYS A 222 1 10
HELIX 7 7 HIS A 236 GLN A 246 1 11
HELIX 8 8 THR A 249 SER A 258 1 10
HELIX 9 9 ASP A 259 ILE A 262 5 4
HELIX 10 10 SER A 265 MET A 269 5 5
HELIX 11 11 VAL A 303 ASP A 314 1 12
HELIX 12 12 ASP A 316 GLY A 329 1 14
HELIX 13 13 GLU A 344 GLU A 346 5 3
HELIX 14 14 ASN A 381 ASN A 386 1 6
HELIX 15 15 ASP A 405 THR A 418 1 14
HELIX 16 16 THR A 418 LEU A 423 1 6
HELIX 17 17 ASN A 427 ARG A 435 5 9
HELIX 18 18 SER A 498 GLY A 502 5 5
HELIX 19 19 TYR A 505 SER A 514 1 10
HELIX 20 20 THR A 516 LYS A 533 1 18
HELIX 21 21 ARG A 536 ASP A 551 1 16
HELIX 22 22 ASP A 551 LEU A 562 1 12
HELIX 23 23 THR A 567 ASN A 572 1 6
HELIX 24 24 ASP A 585 SER A 589 5 5
HELIX 25 25 ARG A 612 LYS A 626 1 15
HELIX 26 26 PRO A 658 VAL A 662 5 5
HELIX 27 27 ILE A 672 ASP A 677 1 6
HELIX 28 28 ASN A 678 HIS A 691 1 14
HELIX 29 29 ASP A 700 LYS A 709 5 10
HELIX 30 30 ASP A 725 ALA A 738 1 14
HELIX 31 31 VAL A 741 SER A 743 5 3
HELIX 32 32 ARG A 744 ASP A 749 1 6
HELIX 33 33 PRO B 52 ALA B 57 1 6
HELIX 34 34 ASN B 62 LEU B 68 1 7
HELIX 35 35 ASP B 107 HIS B 119 1 13
HELIX 36 36 ALA B 150 SER B 154 5 5
HELIX 37 37 ASP B 210 HIS B 212 5 3
HELIX 38 38 LYS B 213 LYS B 222 1 10
HELIX 39 39 HIS B 236 GLN B 246 1 11
HELIX 40 40 THR B 249 SER B 258 1 10
HELIX 41 41 ASP B 259 ILE B 262 5 4
HELIX 42 42 SER B 265 MET B 269 5 5
HELIX 43 43 VAL B 303 ASP B 314 1 12
HELIX 44 44 ASP B 316 GLY B 329 1 14
HELIX 45 45 GLU B 344 GLU B 346 5 3
HELIX 46 46 ASN B 381 ASN B 386 1 6
HELIX 47 47 ASP B 405 THR B 418 1 14
HELIX 48 48 THR B 418 LEU B 423 1 6
HELIX 49 49 ASN B 427 ARG B 435 5 9
HELIX 50 50 SER B 498 GLY B 502 5 5
HELIX 51 51 TYR B 505 SER B 514 1 10
HELIX 52 52 THR B 516 LYS B 533 1 18
HELIX 53 53 ARG B 536 ALA B 548 1 13
HELIX 54 54 ASP B 551 LEU B 562 1 12
HELIX 55 55 THR B 567 ASN B 572 1 6
HELIX 56 56 ASP B 585 SER B 589 5 5
HELIX 57 57 ARG B 612 LYS B 626 1 15
HELIX 58 58 PRO B 658 VAL B 662 5 5
HELIX 59 59 ILE B 672 ASP B 677 1 6
HELIX 60 60 ASN B 678 HIS B 691 1 14
HELIX 61 61 ASP B 700 THR B 707 5 8
HELIX 62 62 ASP B 725 ALA B 738 1 14
HELIX 63 63 VAL B 741 SER B 743 5 3
HELIX 64 64 ARG B 744 ASP B 749 1 6
HELIX 65 65 PRO C 52 ALA C 57 1 6
HELIX 66 66 ASN C 62 LEU C 68 1 7
HELIX 67 67 ASP C 107 HIS C 119 1 13
HELIX 68 68 ALA C 150 SER C 154 5 5
HELIX 69 69 ASP C 210 HIS C 212 5 3
HELIX 70 70 LYS C 213 LYS C 222 1 10
HELIX 71 71 HIS C 236 GLN C 246 1 11
HELIX 72 72 THR C 249 SER C 258 1 10
HELIX 73 73 ASP C 259 ILE C 262 5 4
HELIX 74 74 SER C 265 MET C 269 5 5
HELIX 75 75 VAL C 303 ASP C 314 1 12
HELIX 76 76 ASP C 316 GLY C 329 1 14
HELIX 77 77 GLU C 344 GLU C 346 5 3
HELIX 78 78 ASN C 381 ASN C 386 1 6
HELIX 79 79 ASP C 405 THR C 418 1 14
HELIX 80 80 THR C 418 LEU C 423 1 6
HELIX 81 81 ASN C 427 ARG C 435 5 9
HELIX 82 82 SER C 498 GLY C 502 5 5
HELIX 83 83 TYR C 505 SER C 514 1 10
HELIX 84 84 THR C 516 LYS C 533 1 18
HELIX 85 85 ARG C 536 HIS C 549 1 14
HELIX 86 86 ASP C 551 LEU C 562 1 12
HELIX 87 87 THR C 567 ASN C 572 1 6
HELIX 88 88 ASP C 585 SER C 589 5 5
HELIX 89 89 ARG C 612 GLY C 627 1 16
HELIX 90 90 PRO C 658 VAL C 662 5 5
HELIX 91 91 ILE C 672 ASP C 677 1 6
HELIX 92 92 ASN C 678 HIS C 691 1 14
HELIX 93 93 ASP C 700 ALA C 706 5 7
HELIX 94 94 SER C 727 ALA C 738 1 12
HELIX 95 95 VAL C 741 ILE C 748 5 8
HELIX 96 96 PRO D 52 ALA D 57 1 6
HELIX 97 97 ASN D 62 LEU D 68 1 7
HELIX 98 98 ASP D 107 HIS D 119 1 13
HELIX 99 99 ALA D 150 SER D 154 5 5
HELIX 100 100 ASP D 210 HIS D 212 5 3
HELIX 101 101 LYS D 213 LYS D 222 1 10
HELIX 102 102 HIS D 236 GLN D 246 1 11
HELIX 103 103 THR D 249 SER D 258 1 10
HELIX 104 104 ASP D 259 ILE D 262 5 4
HELIX 105 105 SER D 265 MET D 269 5 5
HELIX 106 106 VAL D 303 ASP D 314 1 12
HELIX 107 107 ASP D 316 GLY D 329 1 14
HELIX 108 108 GLU D 344 GLU D 346 5 3
HELIX 109 109 ASN D 381 ASN D 386 1 6
HELIX 110 110 ASP D 405 LEU D 423 1 19
HELIX 111 111 ASN D 427 ARG D 435 5 9
HELIX 112 112 SER D 498 GLY D 502 5 5
HELIX 113 113 TYR D 505 GLN D 515 1 11
HELIX 114 114 THR D 516 LYS D 533 1 18
HELIX 115 115 ARG D 536 HIS D 549 1 14
HELIX 116 116 ASP D 551 LEU D 562 1 12
HELIX 117 117 THR D 567 ASN D 572 1 6
HELIX 118 118 ASP D 585 SER D 589 5 5
HELIX 119 119 ARG D 612 LYS D 626 1 15
HELIX 120 120 PRO D 658 VAL D 662 5 5
HELIX 121 121 ILE D 672 ASP D 677 1 6
HELIX 122 122 ASN D 678 HIS D 691 1 14
HELIX 123 123 ASP D 700 THR D 707 5 8
HELIX 124 124 SER D 727 ALA D 738 1 12
HELIX 125 125 VAL D 741 SER D 743 5 3
HELIX 126 126 ARG D 744 ASP D 749 1 6
SHEET 1 A 2 ARG A 72 LYS A 73 0
SHEET 2 A 2 ILE C 453 ASP C 454 1 O ILE C 453 N LYS A 73
SHEET 1 B 4 LEU A 95 ALA A 97 0
SHEET 2 B 4 ARG D 488 ARG D 495 -1 O VAL D 494 N ARG A 96
SHEET 3 B 4 ARG C 488 ARG C 495 -1 N VAL C 489 O GLY D 491
SHEET 4 B 4 LEU B 95 ALA B 97 -1 N ARG B 96 O VAL C 494
SHEET 1 C11 LEU A 400 ASP A 401 0
SHEET 2 C11 PHE A 277 ILE A 280 -1 N ARG A 278 O ASP A 401
SHEET 3 C11 ALA A 286 PRO A 295 -1 O VAL A 289 N PHE A 277
SHEET 4 C11 GLU A 333 PRO A 342 -1 O GLU A 335 N LYS A 294
SHEET 5 C11 GLN A 368 ARG A 377 -1 O VAL A 370 N LEU A 336
SHEET 6 C11 GLY A 131 PRO A 140 -1 N HIS A 135 O ARG A 377
SHEET 7 C11 THR A 160 SER A 167 -1 O THR A 160 N PHE A 138
SHEET 8 C11 GLY A 184 THR A 191 -1 O LYS A 188 N PHE A 163
SHEET 9 C11 GLY A 194 ASN A 201 -1 O PHE A 196 N PHE A 189
SHEET 10 C11 GLY A 271 PHE A 272 -1 O PHE A 272 N ASN A 201
SHEET 11 C11 ALA A 286 PRO A 295 -1 O TRP A 293 N GLY A 271
SHEET 1 D 2 ILE A 453 ASP A 454 0
SHEET 2 D 2 ARG C 72 LYS C 73 1 O LYS C 73 N ILE A 453
SHEET 1 E 4 LEU C 95 ALA C 97 0
SHEET 2 E 4 ARG B 488 ARG B 495 -1 N VAL B 494 O ARG C 96
SHEET 3 E 4 ARG A 488 VAL A 494 -1 N GLY A 491 O VAL B 489
SHEET 4 E 4 ARG D 96 ALA D 97 -1 O ARG D 96 N VAL A 494
SHEET 1 F 6 ALA A 652 THR A 653 0
SHEET 2 F 6 HIS A 629 TYR A 634 1 N TYR A 634 O ALA A 652
SHEET 3 F 6 VAL A 602 LEU A 606 1 N ILE A 605 O LEU A 633
SHEET 4 F 6 ALA A 664 VAL A 667 1 O ILE A 666 N ALA A 604
SHEET 5 F 6 ILE A 695 ALA A 698 1 O ALA A 696 N VAL A 665
SHEET 6 F 6 ILE A 718 ALA A 721 1 O VAL A 719 N LEU A 697
SHEET 1 G 2 GLU A 639 THR A 641 0
SHEET 2 G 2 VAL A 647 PRO A 649 -1 O LEU A 648 N VAL A 640
SHEET 1 H 2 ARG B 72 LYS B 73 0
SHEET 2 H 2 ILE D 453 ASP D 454 1 O ILE D 453 N LYS B 73
SHEET 1 I11 LEU B 400 ASP B 401 0
SHEET 2 I11 PHE B 277 ILE B 280 -1 N ARG B 278 O ASP B 401
SHEET 3 I11 ALA B 286 PRO B 295 -1 O VAL B 289 N PHE B 277
SHEET 4 I11 GLU B 333 PRO B 342 -1 O GLU B 335 N LYS B 294
SHEET 5 I11 GLN B 368 ARG B 377 -1 O VAL B 370 N LEU B 336
SHEET 6 I11 GLY B 131 PRO B 140 -1 N HIS B 135 O ARG B 377
SHEET 7 I11 THR B 160 SER B 167 -1 O PHE B 166 N SER B 132
SHEET 8 I11 GLY B 184 THR B 191 -1 O LYS B 188 N PHE B 163
SHEET 9 I11 GLY B 194 ASN B 201 -1 O PHE B 196 N PHE B 189
SHEET 10 I11 GLY B 271 PHE B 272 -1 O PHE B 272 N ASN B 201
SHEET 11 I11 ALA B 286 PRO B 295 -1 O TRP B 293 N GLY B 271
SHEET 1 J 2 ILE B 453 ASP B 454 0
SHEET 2 J 2 ARG D 72 LYS D 73 1 O LYS D 73 N ILE B 453
SHEET 1 K 6 ALA B 652 THR B 653 0
SHEET 2 K 6 HIS B 629 TYR B 634 1 N TYR B 634 O ALA B 652
SHEET 3 K 6 VAL B 602 LEU B 606 1 N ILE B 605 O LEU B 633
SHEET 4 K 6 ALA B 664 VAL B 667 1 O ILE B 666 N ALA B 604
SHEET 5 K 6 ILE B 695 ALA B 698 1 O ALA B 696 N VAL B 667
SHEET 6 K 6 ILE B 718 ALA B 721 1 O VAL B 719 N LEU B 697
SHEET 1 L 2 GLU B 639 THR B 641 0
SHEET 2 L 2 VAL B 647 PRO B 649 -1 O LEU B 648 N VAL B 640
SHEET 1 M10 LEU C 400 ASP C 401 0
SHEET 2 M10 GLY C 271 ILE C 280 -1 N ARG C 278 O ASP C 401
SHEET 3 M10 ALA C 286 PRO C 295 -1 O TRP C 293 N GLY C 271
SHEET 4 M10 GLU C 333 PRO C 342 -1 O GLU C 335 N LYS C 294
SHEET 5 M10 VAL C 367 ARG C 377 -1 O VAL C 370 N LEU C 336
SHEET 6 M10 GLY C 131 PRO C 140 -1 N HIS C 135 O ARG C 377
SHEET 7 M10 THR C 160 SER C 167 -1 O PHE C 166 N SER C 132
SHEET 8 M10 GLY C 184 THR C 191 -1 O LYS C 188 N PHE C 163
SHEET 9 M10 GLY C 194 ASN C 201 -1 O PHE C 196 N PHE C 189
SHEET 10 M10 GLY C 271 ILE C 280 -1 O PHE C 272 N ASN C 201
SHEET 1 N 6 ALA C 652 THR C 653 0
SHEET 2 N 6 HIS C 629 TYR C 634 1 N TYR C 634 O ALA C 652
SHEET 3 N 6 VAL C 602 LEU C 606 1 N ILE C 605 O LYS C 631
SHEET 4 N 6 ALA C 664 VAL C 667 1 O ILE C 666 N ALA C 604
SHEET 5 N 6 ILE C 695 ALA C 698 1 O ALA C 696 N VAL C 667
SHEET 6 N 6 ILE C 718 ALA C 721 1 O VAL C 719 N LEU C 697
SHEET 1 O 2 GLU C 639 THR C 641 0
SHEET 2 O 2 VAL C 647 PRO C 649 -1 O LEU C 648 N VAL C 640
SHEET 1 P11 LEU D 400 ASP D 401 0
SHEET 2 P11 PHE D 277 ILE D 280 -1 N ARG D 278 O ASP D 401
SHEET 3 P11 ALA D 286 PRO D 295 -1 O VAL D 289 N PHE D 277
SHEET 4 P11 GLU D 333 PRO D 342 -1 O GLU D 335 N LYS D 294
SHEET 5 P11 GLN D 368 ARG D 377 -1 O MET D 373 N TYR D 334
SHEET 6 P11 GLY D 131 PRO D 140 -1 N HIS D 135 O ARG D 377
SHEET 7 P11 THR D 160 SER D 167 -1 O THR D 160 N PHE D 138
SHEET 8 P11 GLY D 184 THR D 191 -1 O ALA D 186 N ARG D 165
SHEET 9 P11 GLY D 194 ASN D 201 -1 O PHE D 196 N PHE D 189
SHEET 10 P11 GLY D 271 PHE D 272 -1 O PHE D 272 N ASN D 201
SHEET 11 P11 ALA D 286 PRO D 295 -1 O TRP D 293 N GLY D 271
SHEET 1 Q 6 ALA D 652 THR D 653 0
SHEET 2 Q 6 HIS D 629 TYR D 634 1 N TYR D 634 O ALA D 652
SHEET 3 Q 6 VAL D 602 LEU D 606 1 N ILE D 605 O LEU D 633
SHEET 4 Q 6 ALA D 664 VAL D 667 1 O ILE D 666 N ALA D 604
SHEET 5 Q 6 ILE D 695 ALA D 698 1 O ALA D 696 N VAL D 667
SHEET 6 Q 6 ILE D 718 ALA D 721 1 O VAL D 719 N ILE D 695
SHEET 1 R 2 GLU D 639 THR D 641 0
SHEET 2 R 2 VAL D 647 PRO D 649 -1 O LEU D 648 N VAL D 640
LINK OH TYR A 415 FE HDD A 801 1555 1555 1.98
LINK FE HDD A 801 O HOH A1506 1555 1555 2.52
LINK OH TYR B 415 FE HDD B 801 1555 1555 2.02
LINK FE HDD B 801 O HOH B1460 1555 1555 2.29
LINK OH TYR C 415 FE HDD C 801 1555 1555 1.93
LINK OH TYR D 415 FE HDD D 801 1555 1555 1.98
LINK FE HDD D 801 O HOH D1643 1555 1555 2.74
CISPEP 1 ILE A 229 PRO A 230 0 1.83
CISPEP 2 GLU A 461 PRO A 462 0 3.87
CISPEP 3 TRP A 469 PRO A 470 0 -3.18
CISPEP 4 ILE B 229 PRO B 230 0 4.29
CISPEP 5 GLU B 461 PRO B 462 0 8.51
CISPEP 6 TRP B 469 PRO B 470 0 -5.65
CISPEP 7 ILE C 229 PRO C 230 0 5.53
CISPEP 8 GLU C 461 PRO C 462 0 8.20
CISPEP 9 TRP C 469 PRO C 470 0 -3.70
CISPEP 10 ILE D 229 PRO D 230 0 3.61
CISPEP 11 GLU D 461 PRO D 462 0 7.24
CISPEP 12 TRP D 469 PRO D 470 0 -5.22
SITE 1 AC1 24 ARG A 125 VAL A 127 HIS A 128 ARG A 165
SITE 2 AC1 24 GLY A 184 VAL A 199 GLY A 200 ASN A 201
SITE 3 AC1 24 PHE A 206 PHE A 214 ILE A 274 HIS A 275
SITE 4 AC1 24 PHE A 391 LEU A 407 ARG A 411 SER A 414
SITE 5 AC1 24 TYR A 415 THR A 418 GLN A 419 ARG A 422
SITE 6 AC1 24 HOH A 924 HOH A 968 HOH A 996 HOH A1506
SITE 1 AC2 23 ARG B 125 VAL B 127 HIS B 128 ARG B 165
SITE 2 AC2 23 GLY B 184 VAL B 199 GLY B 200 ASN B 201
SITE 3 AC2 23 PHE B 206 PHE B 214 ILE B 274 HIS B 275
SITE 4 AC2 23 PHE B 391 LEU B 407 ARG B 411 SER B 414
SITE 5 AC2 23 TYR B 415 THR B 418 GLN B 419 ARG B 422
SITE 6 AC2 23 HOH B 963 HOH B1010 HOH B1460
SITE 1 AC3 24 ASP B 118 ARG C 125 VAL C 127 HIS C 128
SITE 2 AC3 24 ARG C 165 GLY C 184 VAL C 199 GLY C 200
SITE 3 AC3 24 ASN C 201 PHE C 206 PHE C 214 ILE C 274
SITE 4 AC3 24 HIS C 275 PHE C 391 LEU C 407 ARG C 411
SITE 5 AC3 24 SER C 414 TYR C 415 THR C 418 GLN C 419
SITE 6 AC3 24 ARG C 422 HOH C1010 HOH C1054 HOH C1083
SITE 1 AC4 23 ARG D 125 VAL D 127 HIS D 128 ARG D 165
SITE 2 AC4 23 GLY D 184 VAL D 199 GLY D 200 ASN D 201
SITE 3 AC4 23 PHE D 206 PHE D 214 HIS D 275 PHE D 391
SITE 4 AC4 23 LEU D 407 GLY D 410 ARG D 411 SER D 414
SITE 5 AC4 23 TYR D 415 THR D 418 GLN D 419 HOH D1066
SITE 6 AC4 23 HOH D1109 HOH D1139 HOH D1643
CRYST1 93.393 132.570 122.567 90.00 109.23 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.010707 0.000000 0.003735 0.00000
SCALE2 0.000000 0.007543 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008641 0.00000
(ATOM LINES ARE NOT SHOWN.)
END