HEADER OXIDOREDUCTASE 14-AUG-02 1MG2
TITLE MUTATION OF ALPHA PHE55 OF METHYLAMINE DEHYDROGENASE ALTERS THE
TITLE 2 REORGANIZATION ENERGY AND ELECTRONIC COUPLING FOR ITS ELECTRON
TITLE 3 TRANSFER REACTION WITH AMICYANIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METHYLAMINE DEHYDROGENASE, HEAVY CHAIN;
COMPND 3 CHAIN: A, E, I, M;
COMPND 4 SYNONYM: MADH;
COMPND 5 EC: 1.4.99.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: METHYLAMINE DEHYDROGENASE, LIGHT CHAIN;
COMPND 10 CHAIN: B, F, J, N;
COMPND 11 SYNONYM: MADH;
COMPND 12 EC: 1.4.99.3;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: AMICYANIN;
COMPND 16 CHAIN: C, G, K, O;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: CYTOCHROME C-L;
COMPND 20 CHAIN: D, H, L, P;
COMPND 21 SYNONYM: CYTOCHROME C551I;
COMPND 22 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;
SOURCE 3 ORGANISM_TAXID: 266;
SOURCE 4 EXPRESSION_SYSTEM: RHODOBACTER SPHAEROIDES;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 1063;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;
SOURCE 8 ORGANISM_TAXID: 266;
SOURCE 9 EXPRESSION_SYSTEM: RHODOBACTER SPHAEROIDES;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 1063;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;
SOURCE 13 ORGANISM_TAXID: 266;
SOURCE 14 EXPRESSION_SYSTEM: RHODOBACTER SPHAEROIDES;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 1063;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: PARACOCCUS DENITRIFICANS;
SOURCE 18 ORGANISM_TAXID: 266;
SOURCE 19 EXPRESSION_SYSTEM: RHODOBACTER SPHAEROIDES;
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 1063
KEYWDS ELECTRON TRANSFER, METHYLAMINE DEHYDROGENASE, CYTOCHROME, BLUE COPPER
KEYWDS 2 PROTEIN, ACTIVE SITE MUTANT, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.SUN,Z.W.CHEN,F.S.MATHEWS,V.L.DAVIDSON
REVDAT 5 27-OCT-21 1MG2 1 SEQADV
REVDAT 4 03-MAR-21 1MG2 1 COMPND REMARK SEQADV HET
REVDAT 4 2 1 HETNAM HETSYN FORMUL LINK
REVDAT 4 3 1 ATOM
REVDAT 3 11-OCT-17 1MG2 1 REMARK
REVDAT 2 24-FEB-09 1MG2 1 VERSN
REVDAT 1 11-DEC-02 1MG2 0
JRNL AUTH D.SUN,Z.W.CHEN,F.S.MATHEWS,V.L.DAVIDSON
JRNL TITL MUTATION OF ALPHA PHE55 OF METHYLAMINE DEHYDROGENASE ALTERS
JRNL TITL 2 THE REORGANIZATION ENERGY AND ELECTRONIC COUPLING FOR ITS
JRNL TITL 3 ELECTRON TRANSFER REACTION WITH AMICYANIN
JRNL REF BIOCHEMISTRY V. 41 13926 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 12437349
JRNL DOI 10.1021/BI026654X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.CHEN,R.DURLEY,F.S.MATHEWS,V.L.DAVIDSON
REMARK 1 TITL STRUCTUREOF AN ELECTRON TRANSFER COMPLEX: METHYLAMINE
REMARK 1 TITL 2 DEHYDROGENASE, AMICYANIN, AND CYTOCHROME C551I.
REMARK 1 REF SCIENCE V. 264 86 1994
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.9
REMARK 3 NUMBER OF REFLECTIONS : 150643
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 SET) : 0.173
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 15071
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.39
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 52.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 13523
REMARK 3 BIN R VALUE (WORKING SET) : 0.2231
REMARK 3 BIN FREE R VALUE : 0.2735
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1509
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.007
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23472
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 220
REMARK 3 SOLVENT ATOMS : 1685
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.24
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.31
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.820
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.780 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.660 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.990 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.020 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 35.53
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MG2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-02.
REMARK 100 THE DEPOSITION ID IS D_1000016886.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-AUG-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : R-AXIS
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 150718
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 47.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.20100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 2MTA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PHOSPHATE, PH 5.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 295K
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 94.10050
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 300 REMARK: TWO HETEROOCTAMERIC MOLECULES PER ASYMMETRIC UNIT
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: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L, M, N, O, P
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A -3
REMARK 465 ALA A -2
REMARK 465 SER A -1
REMARK 465 ALA A 0
REMARK 465 GLN A 1
REMARK 465 ASP A 2
REMARK 465 ALA A 3
REMARK 465 PRO A 4
REMARK 465 ALA B 1
REMARK 465 ASP B 2
REMARK 465 ALA B 3
REMARK 465 PRO B 4
REMARK 465 ALA B 5
REMARK 465 GLY B 6
REMARK 465 LYS D 148
REMARK 465 SER D 149
REMARK 465 SER D 150
REMARK 465 GLY D 151
REMARK 465 GLU D 152
REMARK 465 ASP D 153
REMARK 465 GLN D 154
REMARK 465 SER D 155
REMARK 465 ALA E -3
REMARK 465 ALA E -2
REMARK 465 SER E -1
REMARK 465 ALA E 0
REMARK 465 GLN E 1
REMARK 465 ASP E 2
REMARK 465 ALA E 3
REMARK 465 PRO E 4
REMARK 465 ALA F 1
REMARK 465 ASP F 2
REMARK 465 ALA F 3
REMARK 465 PRO F 4
REMARK 465 ALA F 5
REMARK 465 GLY F 6
REMARK 465 LYS H 148
REMARK 465 SER H 149
REMARK 465 SER H 150
REMARK 465 GLY H 151
REMARK 465 GLU H 152
REMARK 465 ASP H 153
REMARK 465 GLN H 154
REMARK 465 SER H 155
REMARK 465 ALA I -3
REMARK 465 ALA I -2
REMARK 465 SER I -1
REMARK 465 ALA I 0
REMARK 465 GLN I 1
REMARK 465 ASP I 2
REMARK 465 ALA I 3
REMARK 465 PRO I 4
REMARK 465 ALA J 1
REMARK 465 ASP J 2
REMARK 465 ALA J 3
REMARK 465 PRO J 4
REMARK 465 ALA J 5
REMARK 465 GLY J 6
REMARK 465 LYS L 148
REMARK 465 SER L 149
REMARK 465 SER L 150
REMARK 465 GLY L 151
REMARK 465 GLU L 152
REMARK 465 ASP L 153
REMARK 465 GLN L 154
REMARK 465 SER L 155
REMARK 465 ALA M -3
REMARK 465 ALA M -2
REMARK 465 SER M -1
REMARK 465 ALA M 0
REMARK 465 GLN M 1
REMARK 465 ASP M 2
REMARK 465 ALA M 3
REMARK 465 PRO M 4
REMARK 465 ALA N 1
REMARK 465 ASP N 2
REMARK 465 ALA N 3
REMARK 465 PRO N 4
REMARK 465 ALA N 5
REMARK 465 GLY N 6
REMARK 465 LYS P 148
REMARK 465 SER P 149
REMARK 465 SER P 150
REMARK 465 GLY P 151
REMARK 465 GLU P 152
REMARK 465 ASP P 153
REMARK 465 GLN P 154
REMARK 465 SER P 155
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 P 61 CE1 HIS P 61 NE2 0.115
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 HIS D 61 CB - CG - CD2 ANGL. DEV. = -10.5 DEGREES
REMARK 500 HIS D 61 ND1 - CG - CD2 ANGL. DEV. = 11.2 DEGREES
REMARK 500 HIS H 61 CB - CG - CD2 ANGL. DEV. = -10.5 DEGREES
REMARK 500 HIS H 61 ND1 - CG - CD2 ANGL. DEV. = 11.1 DEGREES
REMARK 500 HIS L 61 CB - CG - CD2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 HIS L 61 ND1 - CG - CD2 ANGL. DEV. = 11.3 DEGREES
REMARK 500 HIS P 61 CB - CG - CD2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 HIS P 61 ND1 - CG - CD2 ANGL. DEV. = 11.3 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 LEU A 80 54.34 38.14
REMARK 500 ILE A 102 -83.08 65.92
REMARK 500 ALA A 130 68.52 29.44
REMARK 500 THR A 137 109.85 -55.38
REMARK 500 TRP A 140 31.16 -91.78
REMARK 500 LYS A 173 -69.03 -96.82
REMARK 500 PRO A 179 -175.24 -66.65
REMARK 500 HIS A 183 159.43 76.06
REMARK 500 TRP A 282 -84.97 -107.27
REMARK 500 LYS A 343 74.87 -110.09
REMARK 500 PRO A 344 153.55 -49.52
REMARK 500 SER B 30 35.61 -144.91
REMARK 500 ALA B 130 -167.65 -121.15
REMARK 500 ILE D 8 -60.18 -96.27
REMARK 500 CYS D 57 -34.24 -130.66
REMARK 500 LYS D 68 -97.56 -162.39
REMARK 500 PRO D 81 -35.28 -37.90
REMARK 500 ASN D 83 3.24 -68.87
REMARK 500 ALA D 97 -126.47 -108.16
REMARK 500 ALA E 55 32.86 70.86
REMARK 500 LEU E 80 50.79 39.85
REMARK 500 ILE E 102 -82.54 66.37
REMARK 500 ALA E 130 66.36 34.97
REMARK 500 LYS E 173 -64.69 -98.60
REMARK 500 HIS E 183 158.67 76.88
REMARK 500 TRP E 282 -84.58 -109.24
REMARK 500 LYS E 343 77.02 -112.71
REMARK 500 ASN E 371 -168.93 -103.77
REMARK 500 GLN E 378 -26.89 -140.75
REMARK 500 SER F 30 36.48 -144.53
REMARK 500 ALA F 130 -167.74 -120.77
REMARK 500 GLU G 34 74.25 -119.50
REMARK 500 THR H 25 152.93 -49.55
REMARK 500 LYS H 68 -100.40 -165.20
REMARK 500 ALA H 97 -134.54 -114.79
REMARK 500 SER H 107 -10.78 -147.77
REMARK 500 ALA H 131 75.09 -69.49
REMARK 500 SER H 132 -6.96 -59.70
REMARK 500 PRO H 144 132.04 -39.26
REMARK 500 LEU I 80 54.52 39.94
REMARK 500 ILE I 102 -82.25 63.63
REMARK 500 ALA I 130 65.45 32.73
REMARK 500 LYS I 173 -65.85 -99.04
REMARK 500 HIS I 183 157.09 73.70
REMARK 500 HIS I 230 65.90 -118.69
REMARK 500 TRP I 282 -87.17 -106.78
REMARK 500 LYS I 343 77.17 -108.87
REMARK 500 SER J 30 35.70 -143.82
REMARK 500 ALA J 130 -167.38 -120.61
REMARK 500 CYS L 57 -33.30 -136.42
REMARK 500
REMARK 500 THIS ENTRY HAS 72 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH I2582 DISTANCE = 6.56 ANGSTROMS
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 CU C 107 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 53 ND1
REMARK 620 2 CYS C 92 SG 124.8
REMARK 620 3 HIS C 95 ND1 103.7 127.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC D 200 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 61 NE2
REMARK 620 2 HEC D 200 NA 91.4
REMARK 620 3 HEC D 200 NB 87.4 89.7
REMARK 620 4 HEC D 200 NC 87.9 179.1 89.7
REMARK 620 5 HEC D 200 ND 91.8 90.5 179.2 90.1
REMARK 620 6 MET D 101 SD 177.8 90.0 90.8 90.7 89.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 604 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 75 OD2
REMARK 620 2 TYR D 77 O 75.4
REMARK 620 3 HOH D1002 O 80.8 66.4
REMARK 620 4 HOH D1409 O 81.8 154.5 98.9
REMARK 620 5 HOH D1768 O 146.8 93.7 124.0 111.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU G 107 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 53 ND1
REMARK 620 2 CYS G 92 SG 128.2
REMARK 620 3 HIS G 95 ND1 105.0 119.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC H 200 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 61 NE2
REMARK 620 2 HEC H 200 NA 89.9
REMARK 620 3 HEC H 200 NB 87.4 90.1
REMARK 620 4 HEC H 200 NC 90.1 179.2 89.1
REMARK 620 5 HEC H 200 ND 91.9 90.8 178.8 90.0
REMARK 620 6 MET H 101 SD 176.4 93.2 90.9 86.7 89.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA H 603 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY H 72 O
REMARK 620 2 ASP H 75 OD2 147.9
REMARK 620 3 TYR H 77 O 124.6 80.2
REMARK 620 4 HOH H1158 O 88.3 81.5 69.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA L 601 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU K 31 OE2
REMARK 620 2 HOH K1348 O 60.3
REMARK 620 3 GLY L 72 O 88.4 74.8
REMARK 620 4 ASP L 75 OD2 95.2 74.2 141.8
REMARK 620 5 TYR L 77 O 133.2 146.4 128.2 73.9
REMARK 620 6 HOH L1273 O 154.8 95.0 89.1 71.9 65.1
REMARK 620 7 HOH L1529 O 85.8 124.4 60.6 157.6 89.1 114.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU K 107 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS K 53 ND1
REMARK 620 2 CYS K 92 SG 129.6
REMARK 620 3 HIS K 95 ND1 111.8 108.2
REMARK 620 4 MET K 98 SD 86.2 116.2 99.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC L 200 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS L 61 NE2
REMARK 620 2 HEC L 200 NA 89.4
REMARK 620 3 HEC L 200 NB 87.1 90.2
REMARK 620 4 HEC L 200 NC 90.2 179.5 89.4
REMARK 620 5 HEC L 200 ND 92.2 90.6 178.9 89.8
REMARK 620 6 MET L 101 SD 179.1 90.2 92.1 90.2 88.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU O 107 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS O 53 ND1
REMARK 620 2 CYS O 92 SG 131.4
REMARK 620 3 HIS O 95 ND1 104.8 115.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA P 602 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH O1352 O
REMARK 620 2 GLY P 72 O 76.7
REMARK 620 3 ASP P 75 OD2 71.2 141.3
REMARK 620 4 TYR P 77 O 142.2 127.7 73.5
REMARK 620 5 HOH P1276 O 89.0 87.2 71.4 67.0
REMARK 620 6 HOH P2639 O 122.2 58.3 160.2 95.4 120.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC P 200 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS P 61 NE2
REMARK 620 2 HEC P 200 NA 95.0
REMARK 620 3 HEC P 200 NB 88.7 90.4
REMARK 620 4 HEC P 200 NC 84.4 179.3 89.2
REMARK 620 5 HEC P 200 ND 90.5 90.7 178.7 89.7
REMARK 620 6 MET P 101 SD 171.0 93.0 95.6 87.7 85.1
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 CU C 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU G 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU K 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU O 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 F 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 J 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 N 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 I 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 M 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA L 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA P 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC D 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC H 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC L 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC P 200
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2MTA RELATED DB: PDB
REMARK 900 STRUCTURE OF AN ELECTRON TRANSFER COMPLEX: METHYLAMINE
REMARK 900 DEHYDROGENASE, AMICYANIN, AND CYTOCHROME C551I.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS MAINTAIN THAT THE SEQUENCE IN THE SEQUENCE
REMARK 999 DATABASE IS WRONG.
DBREF 1MG2 A -3 386 UNP P29894 DHMH_PARDE 28 417
DBREF 1MG2 B 1 131 UNP P22619 DHML_PARDE 58 188
DBREF 1MG2 C 1 105 UNP P22364 AMCY_PARDE 27 131
DBREF 1MG2 D 1 155 UNP P29889 VF12_VACCP 631 635
DBREF 1MG2 E -3 386 UNP P29894 DHMH_PARDE 28 417
DBREF 1MG2 F 1 131 UNP P22619 DHML_PARDE 58 188
DBREF 1MG2 G 1 105 UNP P22364 AMCY_PARDE 27 131
DBREF 1MG2 H 1 155 UNP P29889 VF12_VACCP 631 635
DBREF 1MG2 I -3 386 UNP P29894 DHMH_PARDE 28 417
DBREF 1MG2 J 1 131 UNP P22619 DHML_PARDE 58 188
DBREF 1MG2 K 1 105 UNP P22364 AMCY_PARDE 27 131
DBREF 1MG2 L 1 155 UNP P29889 VF12_VACCP 631 635
DBREF 1MG2 M -3 386 UNP P29894 DHMH_PARDE 28 417
DBREF 1MG2 N 1 131 UNP P22619 DHML_PARDE 58 188
DBREF 1MG2 O 1 105 UNP P22364 AMCY_PARDE 27 131
DBREF 1MG2 P 1 155 UNP P29889 VF12_VACCP 631 635
SEQADV 1MG2 ALA A 55 UNP P29894 PHE 86 ENGINEERED MUTATION
SEQADV 1MG2 PHE A 312 UNP P29894 LEU 343 SEE REMARK 999
SEQADV 1MG2 VAL A 313 UNP P29894 LEU 344 SEE REMARK 999
SEQADV 1MG2 ALA E 55 UNP P29894 PHE 86 ENGINEERED MUTATION
SEQADV 1MG2 PHE E 312 UNP P29894 LEU 343 SEE REMARK 999
SEQADV 1MG2 VAL E 313 UNP P29894 LEU 344 SEE REMARK 999
SEQADV 1MG2 ALA I 55 UNP P29894 PHE 86 ENGINEERED MUTATION
SEQADV 1MG2 PHE I 312 UNP P29894 LEU 343 SEE REMARK 999
SEQADV 1MG2 VAL I 313 UNP P29894 LEU 344 SEE REMARK 999
SEQADV 1MG2 ALA M 55 UNP P29894 PHE 86 ENGINEERED MUTATION
SEQADV 1MG2 PHE M 312 UNP P29894 LEU 343 SEE REMARK 999
SEQADV 1MG2 VAL M 313 UNP P29894 LEU 344 SEE REMARK 999
SEQADV 1MG2 TRQ B 57 UNP P22619 TRP 114 MODIFIED RESIDUE
SEQADV 1MG2 TRQ F 57 UNP P22619 TRP 114 MODIFIED RESIDUE
SEQADV 1MG2 TRQ J 57 UNP P22619 TRP 114 MODIFIED RESIDUE
SEQADV 1MG2 TRQ N 57 UNP P22619 TRP 114 MODIFIED RESIDUE
SEQRES 1 A 390 ALA ALA SER ALA GLN ASP ALA PRO GLU ALA GLU THR GLN
SEQRES 2 A 390 ALA GLN GLU THR GLN GLY GLN ALA ALA ALA ARG ALA ALA
SEQRES 3 A 390 ALA ALA ASP LEU ALA ALA GLY GLN ASP ASP GLU PRO ARG
SEQRES 4 A 390 ILE LEU GLU ALA PRO ALA PRO ASP ALA ARG ARG VAL TYR
SEQRES 5 A 390 VAL ASN ASP PRO ALA HIS ALA ALA ALA VAL THR GLN GLN
SEQRES 6 A 390 PHE VAL ILE ASP GLY GLU ALA GLY ARG VAL ILE GLY MET
SEQRES 7 A 390 ILE ASP GLY GLY PHE LEU PRO ASN PRO VAL VAL ALA ASP
SEQRES 8 A 390 ASP GLY SER PHE ILE ALA HIS ALA SER THR VAL PHE SER
SEQRES 9 A 390 ARG ILE ALA ARG GLY GLU ARG THR ASP TYR VAL GLU VAL
SEQRES 10 A 390 PHE ASP PRO VAL THR LEU LEU PRO THR ALA ASP ILE GLU
SEQRES 11 A 390 LEU PRO ASP ALA PRO ARG PHE LEU VAL GLY THR TYR PRO
SEQRES 12 A 390 TRP MET THR SER LEU THR PRO ASP GLY LYS THR LEU LEU
SEQRES 13 A 390 PHE TYR GLN PHE SER PRO ALA PRO ALA VAL GLY VAL VAL
SEQRES 14 A 390 ASP LEU GLU GLY LYS ALA PHE LYS ARG MET LEU ASP VAL
SEQRES 15 A 390 PRO ASP CYS TYR HIS ILE PHE PRO THR ALA PRO ASP THR
SEQRES 16 A 390 PHE PHE MET HIS CYS ARG ASP GLY SER LEU ALA LYS VAL
SEQRES 17 A 390 ALA PHE GLY THR GLU GLY THR PRO GLU ILE THR HIS THR
SEQRES 18 A 390 GLU VAL PHE HIS PRO GLU ASP GLU PHE LEU ILE ASN HIS
SEQRES 19 A 390 PRO ALA TYR SER GLN LYS ALA GLY ARG LEU VAL TRP PRO
SEQRES 20 A 390 THR TYR THR GLY LYS ILE HIS GLN ILE ASP LEU SER SER
SEQRES 21 A 390 GLY ASP ALA LYS PHE LEU PRO ALA VAL GLU ALA LEU THR
SEQRES 22 A 390 GLU ALA GLU ARG ALA ASP GLY TRP ARG PRO GLY GLY TRP
SEQRES 23 A 390 GLN GLN VAL ALA TYR HIS ARG ALA LEU ASP ARG ILE TYR
SEQRES 24 A 390 LEU LEU VAL ASP GLN ARG ASP GLU TRP ARG HIS LYS THR
SEQRES 25 A 390 ALA SER ARG PHE VAL VAL VAL LEU ASP ALA LYS THR GLY
SEQRES 26 A 390 GLU ARG LEU ALA LYS PHE GLU MET GLY HIS GLU ILE ASP
SEQRES 27 A 390 SER ILE ASN VAL SER GLN ASP GLU LYS PRO LEU LEU TYR
SEQRES 28 A 390 ALA LEU SER THR GLY ASP LYS THR LEU TYR ILE HIS ASP
SEQRES 29 A 390 ALA GLU SER GLY GLU GLU LEU ARG SER VAL ASN GLN LEU
SEQRES 30 A 390 GLY HIS GLY PRO GLN VAL ILE THR THR ALA ASP MET GLY
SEQRES 1 B 131 ALA ASP ALA PRO ALA GLY THR ASP PRO ARG ALA LYS TRP
SEQRES 2 B 131 VAL PRO GLN ASP ASN ASP ILE GLN ALA CYS ASP TYR TRP
SEQRES 3 B 131 ARG HIS CYS SER ILE ASP GLY ASN ILE CYS ASP CYS SER
SEQRES 4 B 131 GLY GLY SER LEU THR ASN CYS PRO PRO GLY THR LYS LEU
SEQRES 5 B 131 ALA THR ALA SER TRQ VAL ALA SER CYS TYR ASN PRO THR
SEQRES 6 B 131 ASP GLY GLN SER TYR LEU ILE ALA TYR ARG ASP CYS CYS
SEQRES 7 B 131 GLY TYR ASN VAL SER GLY ARG CYS PRO CYS LEU ASN THR
SEQRES 8 B 131 GLU GLY GLU LEU PRO VAL TYR ARG PRO GLU PHE ALA ASN
SEQRES 9 B 131 ASP ILE ILE TRP CYS PHE GLY ALA GLU ASP ASP ALA MET
SEQRES 10 B 131 THR TYR HIS CYS THR ILE SER PRO ILE VAL GLY LYS ALA
SEQRES 11 B 131 SER
SEQRES 1 C 105 ASP LYS ALA THR ILE PRO SER GLU SER PRO PHE ALA ALA
SEQRES 2 C 105 ALA GLU VAL ALA ASP GLY ALA ILE VAL VAL ASP ILE ALA
SEQRES 3 C 105 LYS MET LYS TYR GLU THR PRO GLU LEU HIS VAL LYS VAL
SEQRES 4 C 105 GLY ASP THR VAL THR TRP ILE ASN ARG GLU ALA MET PRO
SEQRES 5 C 105 HIS ASN VAL HIS PHE VAL ALA GLY VAL LEU GLY GLU ALA
SEQRES 6 C 105 ALA LEU LYS GLY PRO MET MET LYS LYS GLU GLN ALA TYR
SEQRES 7 C 105 SER LEU THR PHE THR GLU ALA GLY THR TYR ASP TYR HIS
SEQRES 8 C 105 CYS THR PRO HIS PRO PHE MET ARG GLY LYS VAL VAL VAL
SEQRES 9 C 105 GLU
SEQRES 1 D 155 ALA PRO GLN PHE PHE ASN ILE ILE ASP GLY SER PRO LEU
SEQRES 2 D 155 ASN PHE ASP ASP ALA MET GLU GLU GLY ARG ASP THR GLU
SEQRES 3 D 155 ALA VAL LYS HIS PHE LEU GLU THR GLY GLU ASN VAL TYR
SEQRES 4 D 155 ASN GLU ASP PRO GLU ILE LEU PRO GLU ALA GLU GLU LEU
SEQRES 5 D 155 TYR ALA GLY MET CYS SER GLY CYS HIS GLY HIS TYR ALA
SEQRES 6 D 155 GLU GLY LYS ILE GLY PRO GLY LEU ASN ASP ALA TYR TRP
SEQRES 7 D 155 THR TYR PRO GLY ASN GLU THR ASP VAL GLY LEU PHE SER
SEQRES 8 D 155 THR LEU TYR GLY GLY ALA THR GLY GLN MET GLY PRO MET
SEQRES 9 D 155 TRP GLY SER LEU THR LEU ASP GLU MET LEU ARG THR MET
SEQRES 10 D 155 ALA TRP VAL ARG HIS LEU TYR THR GLY ASP PRO LYS ASP
SEQRES 11 D 155 ALA SER TRP LEU THR ASP GLU GLN LYS ALA GLY PHE THR
SEQRES 12 D 155 PRO PHE GLN PRO LYS SER SER GLY GLU ASP GLN SER
SEQRES 1 E 390 ALA ALA SER ALA GLN ASP ALA PRO GLU ALA GLU THR GLN
SEQRES 2 E 390 ALA GLN GLU THR GLN GLY GLN ALA ALA ALA ARG ALA ALA
SEQRES 3 E 390 ALA ALA ASP LEU ALA ALA GLY GLN ASP ASP GLU PRO ARG
SEQRES 4 E 390 ILE LEU GLU ALA PRO ALA PRO ASP ALA ARG ARG VAL TYR
SEQRES 5 E 390 VAL ASN ASP PRO ALA HIS ALA ALA ALA VAL THR GLN GLN
SEQRES 6 E 390 PHE VAL ILE ASP GLY GLU ALA GLY ARG VAL ILE GLY MET
SEQRES 7 E 390 ILE ASP GLY GLY PHE LEU PRO ASN PRO VAL VAL ALA ASP
SEQRES 8 E 390 ASP GLY SER PHE ILE ALA HIS ALA SER THR VAL PHE SER
SEQRES 9 E 390 ARG ILE ALA ARG GLY GLU ARG THR ASP TYR VAL GLU VAL
SEQRES 10 E 390 PHE ASP PRO VAL THR LEU LEU PRO THR ALA ASP ILE GLU
SEQRES 11 E 390 LEU PRO ASP ALA PRO ARG PHE LEU VAL GLY THR TYR PRO
SEQRES 12 E 390 TRP MET THR SER LEU THR PRO ASP GLY LYS THR LEU LEU
SEQRES 13 E 390 PHE TYR GLN PHE SER PRO ALA PRO ALA VAL GLY VAL VAL
SEQRES 14 E 390 ASP LEU GLU GLY LYS ALA PHE LYS ARG MET LEU ASP VAL
SEQRES 15 E 390 PRO ASP CYS TYR HIS ILE PHE PRO THR ALA PRO ASP THR
SEQRES 16 E 390 PHE PHE MET HIS CYS ARG ASP GLY SER LEU ALA LYS VAL
SEQRES 17 E 390 ALA PHE GLY THR GLU GLY THR PRO GLU ILE THR HIS THR
SEQRES 18 E 390 GLU VAL PHE HIS PRO GLU ASP GLU PHE LEU ILE ASN HIS
SEQRES 19 E 390 PRO ALA TYR SER GLN LYS ALA GLY ARG LEU VAL TRP PRO
SEQRES 20 E 390 THR TYR THR GLY LYS ILE HIS GLN ILE ASP LEU SER SER
SEQRES 21 E 390 GLY ASP ALA LYS PHE LEU PRO ALA VAL GLU ALA LEU THR
SEQRES 22 E 390 GLU ALA GLU ARG ALA ASP GLY TRP ARG PRO GLY GLY TRP
SEQRES 23 E 390 GLN GLN VAL ALA TYR HIS ARG ALA LEU ASP ARG ILE TYR
SEQRES 24 E 390 LEU LEU VAL ASP GLN ARG ASP GLU TRP ARG HIS LYS THR
SEQRES 25 E 390 ALA SER ARG PHE VAL VAL VAL LEU ASP ALA LYS THR GLY
SEQRES 26 E 390 GLU ARG LEU ALA LYS PHE GLU MET GLY HIS GLU ILE ASP
SEQRES 27 E 390 SER ILE ASN VAL SER GLN ASP GLU LYS PRO LEU LEU TYR
SEQRES 28 E 390 ALA LEU SER THR GLY ASP LYS THR LEU TYR ILE HIS ASP
SEQRES 29 E 390 ALA GLU SER GLY GLU GLU LEU ARG SER VAL ASN GLN LEU
SEQRES 30 E 390 GLY HIS GLY PRO GLN VAL ILE THR THR ALA ASP MET GLY
SEQRES 1 F 131 ALA ASP ALA PRO ALA GLY THR ASP PRO ARG ALA LYS TRP
SEQRES 2 F 131 VAL PRO GLN ASP ASN ASP ILE GLN ALA CYS ASP TYR TRP
SEQRES 3 F 131 ARG HIS CYS SER ILE ASP GLY ASN ILE CYS ASP CYS SER
SEQRES 4 F 131 GLY GLY SER LEU THR ASN CYS PRO PRO GLY THR LYS LEU
SEQRES 5 F 131 ALA THR ALA SER TRQ VAL ALA SER CYS TYR ASN PRO THR
SEQRES 6 F 131 ASP GLY GLN SER TYR LEU ILE ALA TYR ARG ASP CYS CYS
SEQRES 7 F 131 GLY TYR ASN VAL SER GLY ARG CYS PRO CYS LEU ASN THR
SEQRES 8 F 131 GLU GLY GLU LEU PRO VAL TYR ARG PRO GLU PHE ALA ASN
SEQRES 9 F 131 ASP ILE ILE TRP CYS PHE GLY ALA GLU ASP ASP ALA MET
SEQRES 10 F 131 THR TYR HIS CYS THR ILE SER PRO ILE VAL GLY LYS ALA
SEQRES 11 F 131 SER
SEQRES 1 G 105 ASP LYS ALA THR ILE PRO SER GLU SER PRO PHE ALA ALA
SEQRES 2 G 105 ALA GLU VAL ALA ASP GLY ALA ILE VAL VAL ASP ILE ALA
SEQRES 3 G 105 LYS MET LYS TYR GLU THR PRO GLU LEU HIS VAL LYS VAL
SEQRES 4 G 105 GLY ASP THR VAL THR TRP ILE ASN ARG GLU ALA MET PRO
SEQRES 5 G 105 HIS ASN VAL HIS PHE VAL ALA GLY VAL LEU GLY GLU ALA
SEQRES 6 G 105 ALA LEU LYS GLY PRO MET MET LYS LYS GLU GLN ALA TYR
SEQRES 7 G 105 SER LEU THR PHE THR GLU ALA GLY THR TYR ASP TYR HIS
SEQRES 8 G 105 CYS THR PRO HIS PRO PHE MET ARG GLY LYS VAL VAL VAL
SEQRES 9 G 105 GLU
SEQRES 1 H 155 ALA PRO GLN PHE PHE ASN ILE ILE ASP GLY SER PRO LEU
SEQRES 2 H 155 ASN PHE ASP ASP ALA MET GLU GLU GLY ARG ASP THR GLU
SEQRES 3 H 155 ALA VAL LYS HIS PHE LEU GLU THR GLY GLU ASN VAL TYR
SEQRES 4 H 155 ASN GLU ASP PRO GLU ILE LEU PRO GLU ALA GLU GLU LEU
SEQRES 5 H 155 TYR ALA GLY MET CYS SER GLY CYS HIS GLY HIS TYR ALA
SEQRES 6 H 155 GLU GLY LYS ILE GLY PRO GLY LEU ASN ASP ALA TYR TRP
SEQRES 7 H 155 THR TYR PRO GLY ASN GLU THR ASP VAL GLY LEU PHE SER
SEQRES 8 H 155 THR LEU TYR GLY GLY ALA THR GLY GLN MET GLY PRO MET
SEQRES 9 H 155 TRP GLY SER LEU THR LEU ASP GLU MET LEU ARG THR MET
SEQRES 10 H 155 ALA TRP VAL ARG HIS LEU TYR THR GLY ASP PRO LYS ASP
SEQRES 11 H 155 ALA SER TRP LEU THR ASP GLU GLN LYS ALA GLY PHE THR
SEQRES 12 H 155 PRO PHE GLN PRO LYS SER SER GLY GLU ASP GLN SER
SEQRES 1 I 390 ALA ALA SER ALA GLN ASP ALA PRO GLU ALA GLU THR GLN
SEQRES 2 I 390 ALA GLN GLU THR GLN GLY GLN ALA ALA ALA ARG ALA ALA
SEQRES 3 I 390 ALA ALA ASP LEU ALA ALA GLY GLN ASP ASP GLU PRO ARG
SEQRES 4 I 390 ILE LEU GLU ALA PRO ALA PRO ASP ALA ARG ARG VAL TYR
SEQRES 5 I 390 VAL ASN ASP PRO ALA HIS ALA ALA ALA VAL THR GLN GLN
SEQRES 6 I 390 PHE VAL ILE ASP GLY GLU ALA GLY ARG VAL ILE GLY MET
SEQRES 7 I 390 ILE ASP GLY GLY PHE LEU PRO ASN PRO VAL VAL ALA ASP
SEQRES 8 I 390 ASP GLY SER PHE ILE ALA HIS ALA SER THR VAL PHE SER
SEQRES 9 I 390 ARG ILE ALA ARG GLY GLU ARG THR ASP TYR VAL GLU VAL
SEQRES 10 I 390 PHE ASP PRO VAL THR LEU LEU PRO THR ALA ASP ILE GLU
SEQRES 11 I 390 LEU PRO ASP ALA PRO ARG PHE LEU VAL GLY THR TYR PRO
SEQRES 12 I 390 TRP MET THR SER LEU THR PRO ASP GLY LYS THR LEU LEU
SEQRES 13 I 390 PHE TYR GLN PHE SER PRO ALA PRO ALA VAL GLY VAL VAL
SEQRES 14 I 390 ASP LEU GLU GLY LYS ALA PHE LYS ARG MET LEU ASP VAL
SEQRES 15 I 390 PRO ASP CYS TYR HIS ILE PHE PRO THR ALA PRO ASP THR
SEQRES 16 I 390 PHE PHE MET HIS CYS ARG ASP GLY SER LEU ALA LYS VAL
SEQRES 17 I 390 ALA PHE GLY THR GLU GLY THR PRO GLU ILE THR HIS THR
SEQRES 18 I 390 GLU VAL PHE HIS PRO GLU ASP GLU PHE LEU ILE ASN HIS
SEQRES 19 I 390 PRO ALA TYR SER GLN LYS ALA GLY ARG LEU VAL TRP PRO
SEQRES 20 I 390 THR TYR THR GLY LYS ILE HIS GLN ILE ASP LEU SER SER
SEQRES 21 I 390 GLY ASP ALA LYS PHE LEU PRO ALA VAL GLU ALA LEU THR
SEQRES 22 I 390 GLU ALA GLU ARG ALA ASP GLY TRP ARG PRO GLY GLY TRP
SEQRES 23 I 390 GLN GLN VAL ALA TYR HIS ARG ALA LEU ASP ARG ILE TYR
SEQRES 24 I 390 LEU LEU VAL ASP GLN ARG ASP GLU TRP ARG HIS LYS THR
SEQRES 25 I 390 ALA SER ARG PHE VAL VAL VAL LEU ASP ALA LYS THR GLY
SEQRES 26 I 390 GLU ARG LEU ALA LYS PHE GLU MET GLY HIS GLU ILE ASP
SEQRES 27 I 390 SER ILE ASN VAL SER GLN ASP GLU LYS PRO LEU LEU TYR
SEQRES 28 I 390 ALA LEU SER THR GLY ASP LYS THR LEU TYR ILE HIS ASP
SEQRES 29 I 390 ALA GLU SER GLY GLU GLU LEU ARG SER VAL ASN GLN LEU
SEQRES 30 I 390 GLY HIS GLY PRO GLN VAL ILE THR THR ALA ASP MET GLY
SEQRES 1 J 131 ALA ASP ALA PRO ALA GLY THR ASP PRO ARG ALA LYS TRP
SEQRES 2 J 131 VAL PRO GLN ASP ASN ASP ILE GLN ALA CYS ASP TYR TRP
SEQRES 3 J 131 ARG HIS CYS SER ILE ASP GLY ASN ILE CYS ASP CYS SER
SEQRES 4 J 131 GLY GLY SER LEU THR ASN CYS PRO PRO GLY THR LYS LEU
SEQRES 5 J 131 ALA THR ALA SER TRQ VAL ALA SER CYS TYR ASN PRO THR
SEQRES 6 J 131 ASP GLY GLN SER TYR LEU ILE ALA TYR ARG ASP CYS CYS
SEQRES 7 J 131 GLY TYR ASN VAL SER GLY ARG CYS PRO CYS LEU ASN THR
SEQRES 8 J 131 GLU GLY GLU LEU PRO VAL TYR ARG PRO GLU PHE ALA ASN
SEQRES 9 J 131 ASP ILE ILE TRP CYS PHE GLY ALA GLU ASP ASP ALA MET
SEQRES 10 J 131 THR TYR HIS CYS THR ILE SER PRO ILE VAL GLY LYS ALA
SEQRES 11 J 131 SER
SEQRES 1 K 105 ASP LYS ALA THR ILE PRO SER GLU SER PRO PHE ALA ALA
SEQRES 2 K 105 ALA GLU VAL ALA ASP GLY ALA ILE VAL VAL ASP ILE ALA
SEQRES 3 K 105 LYS MET LYS TYR GLU THR PRO GLU LEU HIS VAL LYS VAL
SEQRES 4 K 105 GLY ASP THR VAL THR TRP ILE ASN ARG GLU ALA MET PRO
SEQRES 5 K 105 HIS ASN VAL HIS PHE VAL ALA GLY VAL LEU GLY GLU ALA
SEQRES 6 K 105 ALA LEU LYS GLY PRO MET MET LYS LYS GLU GLN ALA TYR
SEQRES 7 K 105 SER LEU THR PHE THR GLU ALA GLY THR TYR ASP TYR HIS
SEQRES 8 K 105 CYS THR PRO HIS PRO PHE MET ARG GLY LYS VAL VAL VAL
SEQRES 9 K 105 GLU
SEQRES 1 L 155 ALA PRO GLN PHE PHE ASN ILE ILE ASP GLY SER PRO LEU
SEQRES 2 L 155 ASN PHE ASP ASP ALA MET GLU GLU GLY ARG ASP THR GLU
SEQRES 3 L 155 ALA VAL LYS HIS PHE LEU GLU THR GLY GLU ASN VAL TYR
SEQRES 4 L 155 ASN GLU ASP PRO GLU ILE LEU PRO GLU ALA GLU GLU LEU
SEQRES 5 L 155 TYR ALA GLY MET CYS SER GLY CYS HIS GLY HIS TYR ALA
SEQRES 6 L 155 GLU GLY LYS ILE GLY PRO GLY LEU ASN ASP ALA TYR TRP
SEQRES 7 L 155 THR TYR PRO GLY ASN GLU THR ASP VAL GLY LEU PHE SER
SEQRES 8 L 155 THR LEU TYR GLY GLY ALA THR GLY GLN MET GLY PRO MET
SEQRES 9 L 155 TRP GLY SER LEU THR LEU ASP GLU MET LEU ARG THR MET
SEQRES 10 L 155 ALA TRP VAL ARG HIS LEU TYR THR GLY ASP PRO LYS ASP
SEQRES 11 L 155 ALA SER TRP LEU THR ASP GLU GLN LYS ALA GLY PHE THR
SEQRES 12 L 155 PRO PHE GLN PRO LYS SER SER GLY GLU ASP GLN SER
SEQRES 1 M 390 ALA ALA SER ALA GLN ASP ALA PRO GLU ALA GLU THR GLN
SEQRES 2 M 390 ALA GLN GLU THR GLN GLY GLN ALA ALA ALA ARG ALA ALA
SEQRES 3 M 390 ALA ALA ASP LEU ALA ALA GLY GLN ASP ASP GLU PRO ARG
SEQRES 4 M 390 ILE LEU GLU ALA PRO ALA PRO ASP ALA ARG ARG VAL TYR
SEQRES 5 M 390 VAL ASN ASP PRO ALA HIS ALA ALA ALA VAL THR GLN GLN
SEQRES 6 M 390 PHE VAL ILE ASP GLY GLU ALA GLY ARG VAL ILE GLY MET
SEQRES 7 M 390 ILE ASP GLY GLY PHE LEU PRO ASN PRO VAL VAL ALA ASP
SEQRES 8 M 390 ASP GLY SER PHE ILE ALA HIS ALA SER THR VAL PHE SER
SEQRES 9 M 390 ARG ILE ALA ARG GLY GLU ARG THR ASP TYR VAL GLU VAL
SEQRES 10 M 390 PHE ASP PRO VAL THR LEU LEU PRO THR ALA ASP ILE GLU
SEQRES 11 M 390 LEU PRO ASP ALA PRO ARG PHE LEU VAL GLY THR TYR PRO
SEQRES 12 M 390 TRP MET THR SER LEU THR PRO ASP GLY LYS THR LEU LEU
SEQRES 13 M 390 PHE TYR GLN PHE SER PRO ALA PRO ALA VAL GLY VAL VAL
SEQRES 14 M 390 ASP LEU GLU GLY LYS ALA PHE LYS ARG MET LEU ASP VAL
SEQRES 15 M 390 PRO ASP CYS TYR HIS ILE PHE PRO THR ALA PRO ASP THR
SEQRES 16 M 390 PHE PHE MET HIS CYS ARG ASP GLY SER LEU ALA LYS VAL
SEQRES 17 M 390 ALA PHE GLY THR GLU GLY THR PRO GLU ILE THR HIS THR
SEQRES 18 M 390 GLU VAL PHE HIS PRO GLU ASP GLU PHE LEU ILE ASN HIS
SEQRES 19 M 390 PRO ALA TYR SER GLN LYS ALA GLY ARG LEU VAL TRP PRO
SEQRES 20 M 390 THR TYR THR GLY LYS ILE HIS GLN ILE ASP LEU SER SER
SEQRES 21 M 390 GLY ASP ALA LYS PHE LEU PRO ALA VAL GLU ALA LEU THR
SEQRES 22 M 390 GLU ALA GLU ARG ALA ASP GLY TRP ARG PRO GLY GLY TRP
SEQRES 23 M 390 GLN GLN VAL ALA TYR HIS ARG ALA LEU ASP ARG ILE TYR
SEQRES 24 M 390 LEU LEU VAL ASP GLN ARG ASP GLU TRP ARG HIS LYS THR
SEQRES 25 M 390 ALA SER ARG PHE VAL VAL VAL LEU ASP ALA LYS THR GLY
SEQRES 26 M 390 GLU ARG LEU ALA LYS PHE GLU MET GLY HIS GLU ILE ASP
SEQRES 27 M 390 SER ILE ASN VAL SER GLN ASP GLU LYS PRO LEU LEU TYR
SEQRES 28 M 390 ALA LEU SER THR GLY ASP LYS THR LEU TYR ILE HIS ASP
SEQRES 29 M 390 ALA GLU SER GLY GLU GLU LEU ARG SER VAL ASN GLN LEU
SEQRES 30 M 390 GLY HIS GLY PRO GLN VAL ILE THR THR ALA ASP MET GLY
SEQRES 1 N 131 ALA ASP ALA PRO ALA GLY THR ASP PRO ARG ALA LYS TRP
SEQRES 2 N 131 VAL PRO GLN ASP ASN ASP ILE GLN ALA CYS ASP TYR TRP
SEQRES 3 N 131 ARG HIS CYS SER ILE ASP GLY ASN ILE CYS ASP CYS SER
SEQRES 4 N 131 GLY GLY SER LEU THR ASN CYS PRO PRO GLY THR LYS LEU
SEQRES 5 N 131 ALA THR ALA SER TRQ VAL ALA SER CYS TYR ASN PRO THR
SEQRES 6 N 131 ASP GLY GLN SER TYR LEU ILE ALA TYR ARG ASP CYS CYS
SEQRES 7 N 131 GLY TYR ASN VAL SER GLY ARG CYS PRO CYS LEU ASN THR
SEQRES 8 N 131 GLU GLY GLU LEU PRO VAL TYR ARG PRO GLU PHE ALA ASN
SEQRES 9 N 131 ASP ILE ILE TRP CYS PHE GLY ALA GLU ASP ASP ALA MET
SEQRES 10 N 131 THR TYR HIS CYS THR ILE SER PRO ILE VAL GLY LYS ALA
SEQRES 11 N 131 SER
SEQRES 1 O 105 ASP LYS ALA THR ILE PRO SER GLU SER PRO PHE ALA ALA
SEQRES 2 O 105 ALA GLU VAL ALA ASP GLY ALA ILE VAL VAL ASP ILE ALA
SEQRES 3 O 105 LYS MET LYS TYR GLU THR PRO GLU LEU HIS VAL LYS VAL
SEQRES 4 O 105 GLY ASP THR VAL THR TRP ILE ASN ARG GLU ALA MET PRO
SEQRES 5 O 105 HIS ASN VAL HIS PHE VAL ALA GLY VAL LEU GLY GLU ALA
SEQRES 6 O 105 ALA LEU LYS GLY PRO MET MET LYS LYS GLU GLN ALA TYR
SEQRES 7 O 105 SER LEU THR PHE THR GLU ALA GLY THR TYR ASP TYR HIS
SEQRES 8 O 105 CYS THR PRO HIS PRO PHE MET ARG GLY LYS VAL VAL VAL
SEQRES 9 O 105 GLU
SEQRES 1 P 155 ALA PRO GLN PHE PHE ASN ILE ILE ASP GLY SER PRO LEU
SEQRES 2 P 155 ASN PHE ASP ASP ALA MET GLU GLU GLY ARG ASP THR GLU
SEQRES 3 P 155 ALA VAL LYS HIS PHE LEU GLU THR GLY GLU ASN VAL TYR
SEQRES 4 P 155 ASN GLU ASP PRO GLU ILE LEU PRO GLU ALA GLU GLU LEU
SEQRES 5 P 155 TYR ALA GLY MET CYS SER GLY CYS HIS GLY HIS TYR ALA
SEQRES 6 P 155 GLU GLY LYS ILE GLY PRO GLY LEU ASN ASP ALA TYR TRP
SEQRES 7 P 155 THR TYR PRO GLY ASN GLU THR ASP VAL GLY LEU PHE SER
SEQRES 8 P 155 THR LEU TYR GLY GLY ALA THR GLY GLN MET GLY PRO MET
SEQRES 9 P 155 TRP GLY SER LEU THR LEU ASP GLU MET LEU ARG THR MET
SEQRES 10 P 155 ALA TRP VAL ARG HIS LEU TYR THR GLY ASP PRO LYS ASP
SEQRES 11 P 155 ALA SER TRP LEU THR ASP GLU GLN LYS ALA GLY PHE THR
SEQRES 12 P 155 PRO PHE GLN PRO LYS SER SER GLY GLU ASP GLN SER
MODRES 1MG2 TRQ B 57 TRP
MODRES 1MG2 TRQ F 57 TRP
MODRES 1MG2 TRQ J 57 TRP
MODRES 1MG2 TRQ N 57 TRP
HET TRQ B 57 16
HET TRQ F 57 16
HET TRQ J 57 16
HET TRQ N 57 16
HET PO4 A 408 5
HET PO4 B 402 5
HET CU C 107 1
HET NA D 604 1
HET HEC D 200 43
HET PO4 E 406 5
HET PO4 F 401 5
HET CU G 107 1
HET NA H 603 1
HET HEC H 200 43
HET PO4 I 405 5
HET PO4 J 403 5
HET CU K 107 1
HET NA L 601 1
HET HEC L 200 43
HET PO4 M 407 5
HET PO4 N 404 5
HET CU O 107 1
HET NA P 602 1
HET HEC P 200 43
HETNAM TRQ 2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-
HETNAM 2 TRQ PROPIONIC ACID
HETNAM PO4 PHOSPHATE ION
HETNAM CU COPPER (II) ION
HETNAM NA SODIUM ION
HETNAM HEC HEME C
FORMUL 2 TRQ 4(C11 H10 N2 O4)
FORMUL 17 PO4 8(O4 P 3-)
FORMUL 19 CU 4(CU 2+)
FORMUL 20 NA 4(NA 1+)
FORMUL 21 HEC 4(C34 H34 FE N4 O4)
FORMUL 37 HOH *1685(H2 O)
HELIX 1 1 THR A 8 GLY A 29 1 22
HELIX 2 2 PRO A 52 ALA A 56 5 5
HELIX 3 3 TYR A 138 TRP A 140 5 3
HELIX 4 4 THR A 269 ASP A 275 1 7
HELIX 5 5 TYR B 25 CYS B 29 5 5
HELIX 6 6 CYS B 36 SER B 39 5 4
HELIX 7 7 ARG B 99 ALA B 103 5 5
HELIX 8 8 ALA B 112 ALA B 116 5 5
HELIX 9 9 ALA C 14 VAL C 16 5 3
HELIX 10 10 ASN D 14 ALA D 18 5 5
HELIX 11 11 THR D 25 GLY D 35 1 11
HELIX 12 12 ILE D 45 CYS D 57 1 13
HELIX 13 13 CYS D 57 GLY D 62 1 6
HELIX 14 14 TYR D 80 GLU D 84 5 5
HELIX 15 15 THR D 85 GLY D 96 1 12
HELIX 16 16 THR D 109 LEU D 123 1 15
HELIX 17 17 ASP D 127 ALA D 131 5 5
HELIX 18 18 THR D 135 PHE D 142 1 8
HELIX 19 19 ALA E 10 ALA E 28 1 19
HELIX 20 20 PRO E 52 ALA E 56 5 5
HELIX 21 21 TYR E 138 TRP E 140 5 3
HELIX 22 22 THR E 269 ASP E 275 1 7
HELIX 23 23 TYR F 25 CYS F 29 5 5
HELIX 24 24 CYS F 36 SER F 39 5 4
HELIX 25 25 ARG F 99 ALA F 103 5 5
HELIX 26 26 ALA F 112 ALA F 116 5 5
HELIX 27 27 ALA G 14 VAL G 16 5 3
HELIX 28 28 ASN H 14 ALA H 18 5 5
HELIX 29 29 THR H 25 GLY H 35 1 11
HELIX 30 30 ILE H 45 CYS H 57 1 13
HELIX 31 31 CYS H 57 GLY H 62 1 6
HELIX 32 32 TYR H 80 GLU H 84 5 5
HELIX 33 33 THR H 85 GLY H 96 1 12
HELIX 34 34 THR H 109 LEU H 123 1 15
HELIX 35 35 ASP H 127 ALA H 131 5 5
HELIX 36 36 THR H 135 PHE H 142 1 8
HELIX 37 37 THR I 8 GLY I 29 1 22
HELIX 38 38 TYR I 138 TRP I 140 5 3
HELIX 39 39 THR I 269 ASP I 275 1 7
HELIX 40 40 TYR J 25 CYS J 29 5 5
HELIX 41 41 CYS J 36 SER J 39 5 4
HELIX 42 42 ARG J 99 ALA J 103 5 5
HELIX 43 43 ALA J 112 ALA J 116 5 5
HELIX 44 44 ALA K 14 VAL K 16 5 3
HELIX 45 45 ASN L 14 ALA L 18 5 5
HELIX 46 46 THR L 25 GLY L 35 1 11
HELIX 47 47 ILE L 45 CYS L 57 1 13
HELIX 48 48 CYS L 57 GLY L 62 1 6
HELIX 49 49 TYR L 80 GLU L 84 5 5
HELIX 50 50 THR L 85 GLY L 96 1 12
HELIX 51 51 THR L 109 LEU L 123 1 15
HELIX 52 52 ASP L 127 ALA L 131 5 5
HELIX 53 53 THR L 135 PHE L 142 1 8
HELIX 54 54 THR M 8 ALA M 28 1 21
HELIX 55 55 TYR M 138 TRP M 140 5 3
HELIX 56 56 THR M 269 ASP M 275 1 7
HELIX 57 57 TYR N 25 CYS N 29 5 5
HELIX 58 58 CYS N 36 SER N 39 5 4
HELIX 59 59 ARG N 99 ALA N 103 5 5
HELIX 60 60 ALA N 112 ALA N 116 5 5
HELIX 61 61 ALA O 14 VAL O 16 5 3
HELIX 62 62 ASN P 14 ALA P 18 5 5
HELIX 63 63 THR P 25 GLY P 35 1 11
HELIX 64 64 ILE P 45 CYS P 57 1 13
HELIX 65 65 CYS P 57 GLY P 62 1 6
HELIX 66 66 TYR P 80 GLU P 84 5 5
HELIX 67 67 THR P 85 GLY P 96 1 12
HELIX 68 68 THR P 109 LEU P 123 1 15
HELIX 69 69 THR P 135 GLY P 141 1 7
SHEET 1 A 4 ARG A 70 GLY A 77 0
SHEET 2 A 4 THR A 59 ASP A 65 -1 N VAL A 63 O GLY A 73
SHEET 3 A 4 ARG A 46 ASP A 51 -1 N VAL A 47 O ILE A 64
SHEET 4 A 4 VAL A 379 THR A 382 -1 O VAL A 379 N ASN A 50
SHEET 1 B 4 ASN A 82 VAL A 85 0
SHEET 2 B 4 ILE A 92 ARG A 101 -1 O ALA A 93 N VAL A 84
SHEET 3 B 4 ARG A 104 PHE A 114 -1 O PHE A 114 N ILE A 92
SHEET 4 B 4 PRO A 121 LEU A 127 -1 O ILE A 125 N VAL A 111
SHEET 1 C 4 THR A 142 LEU A 144 0
SHEET 2 C 4 THR A 150 GLN A 155 -1 O LEU A 152 N SER A 143
SHEET 3 C 4 ALA A 161 ASP A 166 -1 O ALA A 161 N GLN A 155
SHEET 4 C 4 ALA A 171 ASP A 177 -1 O ALA A 171 N ASP A 166
SHEET 1 D 4 CYS A 181 ALA A 188 0
SHEET 2 D 4 THR A 191 CYS A 196 -1 O HIS A 195 N TYR A 182
SHEET 3 D 4 LEU A 201 ALA A 205 -1 O ALA A 202 N MET A 194
SHEET 4 D 4 GLU A 213 HIS A 216 -1 O THR A 215 N LYS A 203
SHEET 1 E 4 ALA A 232 SER A 234 0
SHEET 2 E 4 ARG A 239 PRO A 243 -1 O VAL A 241 N ALA A 232
SHEET 3 E 4 LYS A 248 ASP A 253 -1 O HIS A 250 N TRP A 242
SHEET 4 E 4 LYS A 260 PHE A 261 -1 O LYS A 260 N ASP A 253
SHEET 1 F 4 ALA A 232 SER A 234 0
SHEET 2 F 4 ARG A 239 PRO A 243 -1 O VAL A 241 N ALA A 232
SHEET 3 F 4 LYS A 248 ASP A 253 -1 O HIS A 250 N TRP A 242
SHEET 4 F 4 VAL A 265 GLU A 266 -1 O VAL A 265 N ILE A 249
SHEET 1 G 4 ARG A 323 ILE A 333 0
SHEET 2 G 4 SER A 310 ASP A 317 -1 N VAL A 313 O PHE A 327
SHEET 3 G 4 ARG A 293 GLN A 300 -1 N ILE A 294 O LEU A 316
SHEET 4 G 4 TRP A 277 PRO A 279 -1 N ARG A 278 O ASP A 299
SHEET 1 H 4 ARG A 323 ILE A 333 0
SHEET 2 H 4 SER A 310 ASP A 317 -1 N VAL A 313 O PHE A 327
SHEET 3 H 4 ARG A 293 GLN A 300 -1 N ILE A 294 O LEU A 316
SHEET 4 H 4 VAL A 285 HIS A 288 -1 N ALA A 286 O TYR A 295
SHEET 1 I 4 SER A 335 VAL A 338 0
SHEET 2 I 4 LEU A 345 SER A 350 -1 O TYR A 347 N ASN A 337
SHEET 3 I 4 THR A 355 ASP A 360 -1 O HIS A 359 N LEU A 346
SHEET 4 I 4 GLU A 366 VAL A 370 -1 O ARG A 368 N ILE A 358
SHEET 1 J 2 ASP B 32 ASN B 34 0
SHEET 2 J 2 PRO B 87 LEU B 89 -1 O CYS B 88 N GLY B 33
SHEET 1 K 3 LYS B 51 LEU B 52 0
SHEET 2 K 3 ASP B 76 CYS B 78 -1 O CYS B 78 N LYS B 51
SHEET 3 K 3 TYR B 119 THR B 122 -1 O CYS B 121 N CYS B 77
SHEET 1 L 3 TRQ B 57 ASN B 63 0
SHEET 2 L 3 GLN B 68 TYR B 74 -1 O TYR B 70 N CYS B 61
SHEET 3 L 3 ILE B 126 LYS B 129 -1 O GLY B 128 N LEU B 71
SHEET 1 M 5 LYS C 29 TYR C 30 0
SHEET 2 M 5 ILE C 21 ALA C 26 -1 N ALA C 26 O LYS C 29
SHEET 3 M 5 THR C 42 ASN C 47 1 O ILE C 46 N ILE C 25
SHEET 4 M 5 GLN C 76 PHE C 82 -1 O TYR C 78 N TRP C 45
SHEET 5 M 5 ALA C 3 THR C 4 -1 N THR C 4 O THR C 81
SHEET 1 N 5 LYS C 29 TYR C 30 0
SHEET 2 N 5 ILE C 21 ALA C 26 -1 N ALA C 26 O LYS C 29
SHEET 3 N 5 THR C 42 ASN C 47 1 O ILE C 46 N ILE C 25
SHEET 4 N 5 GLN C 76 PHE C 82 -1 O TYR C 78 N TRP C 45
SHEET 5 N 5 PHE C 11 ALA C 12 -1 N PHE C 11 O ALA C 77
SHEET 1 O 3 GLU C 34 VAL C 37 0
SHEET 2 O 3 HIS C 95 VAL C 104 1 O VAL C 103 N LEU C 35
SHEET 3 O 3 GLY C 86 CYS C 92 -1 N GLY C 86 O VAL C 104
SHEET 1 P 2 HIS C 56 PHE C 57 0
SHEET 2 P 2 LEU C 67 LYS C 68 -1 O LEU C 67 N PHE C 57
SHEET 1 Q 4 ARG E 70 GLY E 77 0
SHEET 2 Q 4 THR E 59 ASP E 65 -1 N ASP E 65 O ARG E 70
SHEET 3 Q 4 ARG E 46 ASP E 51 -1 N VAL E 47 O ILE E 64
SHEET 4 Q 4 VAL E 379 THR E 382 -1 O VAL E 379 N ASN E 50
SHEET 1 R 4 ASN E 82 VAL E 85 0
SHEET 2 R 4 ILE E 92 ARG E 101 -1 O ALA E 93 N VAL E 84
SHEET 3 R 4 ARG E 104 PHE E 114 -1 O PHE E 114 N ILE E 92
SHEET 4 R 4 PRO E 121 LEU E 127 -1 O ILE E 125 N VAL E 111
SHEET 1 S 4 THR E 142 LEU E 144 0
SHEET 2 S 4 THR E 150 GLN E 155 -1 O LEU E 152 N SER E 143
SHEET 3 S 4 ALA E 161 ASP E 166 -1 O ALA E 161 N GLN E 155
SHEET 4 S 4 ALA E 171 ASP E 177 -1 O ARG E 174 N VAL E 164
SHEET 1 T 4 CYS E 181 ALA E 188 0
SHEET 2 T 4 THR E 191 CYS E 196 -1 O HIS E 195 N TYR E 182
SHEET 3 T 4 LEU E 201 ALA E 205 -1 O ALA E 202 N MET E 194
SHEET 4 T 4 GLU E 213 HIS E 216 -1 O THR E 215 N LYS E 203
SHEET 1 U 4 ALA E 232 SER E 234 0
SHEET 2 U 4 ARG E 239 PRO E 243 -1 O VAL E 241 N ALA E 232
SHEET 3 U 4 LYS E 248 ASP E 253 -1 O HIS E 250 N TRP E 242
SHEET 4 U 4 LYS E 260 PHE E 261 -1 O LYS E 260 N ASP E 253
SHEET 1 V 4 ALA E 232 SER E 234 0
SHEET 2 V 4 ARG E 239 PRO E 243 -1 O VAL E 241 N ALA E 232
SHEET 3 V 4 LYS E 248 ASP E 253 -1 O HIS E 250 N TRP E 242
SHEET 4 V 4 VAL E 265 GLU E 266 -1 O VAL E 265 N ILE E 249
SHEET 1 W 4 ARG E 323 ILE E 333 0
SHEET 2 W 4 SER E 310 ASP E 317 -1 N VAL E 315 O LEU E 324
SHEET 3 W 4 ARG E 293 GLN E 300 -1 N ILE E 294 O LEU E 316
SHEET 4 W 4 TRP E 277 PRO E 279 -1 N ARG E 278 O ASP E 299
SHEET 1 X 4 ARG E 323 ILE E 333 0
SHEET 2 X 4 SER E 310 ASP E 317 -1 N VAL E 315 O LEU E 324
SHEET 3 X 4 ARG E 293 GLN E 300 -1 N ILE E 294 O LEU E 316
SHEET 4 X 4 VAL E 285 HIS E 288 -1 N HIS E 288 O ARG E 293
SHEET 1 Y 4 SER E 335 VAL E 338 0
SHEET 2 Y 4 LEU E 345 SER E 350 -1 O TYR E 347 N ASN E 337
SHEET 3 Y 4 THR E 355 ASP E 360 -1 O TYR E 357 N ALA E 348
SHEET 4 Y 4 GLU E 366 VAL E 370 -1 O VAL E 370 N LEU E 356
SHEET 1 Z 2 ASP F 32 ASN F 34 0
SHEET 2 Z 2 PRO F 87 LEU F 89 -1 O CYS F 88 N GLY F 33
SHEET 1 AA 3 LYS F 51 LEU F 52 0
SHEET 2 AA 3 ASP F 76 CYS F 78 -1 O CYS F 78 N LYS F 51
SHEET 3 AA 3 TYR F 119 THR F 122 -1 O CYS F 121 N CYS F 77
SHEET 1 AB 3 TRQ F 57 ASN F 63 0
SHEET 2 AB 3 GLN F 68 TYR F 74 -1 O TYR F 70 N CYS F 61
SHEET 3 AB 3 ILE F 126 LYS F 129 -1 O GLY F 128 N LEU F 71
SHEET 1 AC 5 LYS G 29 TYR G 30 0
SHEET 2 AC 5 ILE G 21 ALA G 26 -1 N ALA G 26 O LYS G 29
SHEET 3 AC 5 THR G 42 ASN G 47 1 O ILE G 46 N ILE G 25
SHEET 4 AC 5 GLN G 76 PHE G 82 -1 O TYR G 78 N TRP G 45
SHEET 5 AC 5 ALA G 3 THR G 4 -1 N THR G 4 O THR G 81
SHEET 1 AD 5 LYS G 29 TYR G 30 0
SHEET 2 AD 5 ILE G 21 ALA G 26 -1 N ALA G 26 O LYS G 29
SHEET 3 AD 5 THR G 42 ASN G 47 1 O ILE G 46 N ILE G 25
SHEET 4 AD 5 GLN G 76 PHE G 82 -1 O TYR G 78 N TRP G 45
SHEET 5 AD 5 PHE G 11 ALA G 12 -1 N PHE G 11 O ALA G 77
SHEET 1 AE 3 GLU G 34 VAL G 37 0
SHEET 2 AE 3 HIS G 95 VAL G 104 1 O VAL G 103 N LEU G 35
SHEET 3 AE 3 GLY G 86 CYS G 92 -1 N GLY G 86 O VAL G 104
SHEET 1 AF 2 HIS G 56 PHE G 57 0
SHEET 2 AF 2 LEU G 67 LYS G 68 -1 O LEU G 67 N PHE G 57
SHEET 1 AG 4 ARG I 70 GLY I 77 0
SHEET 2 AG 4 THR I 59 ASP I 65 -1 N ASP I 65 O ARG I 70
SHEET 3 AG 4 ARG I 46 ASP I 51 -1 N ASP I 51 O GLN I 60
SHEET 4 AG 4 VAL I 379 THR I 382 -1 O VAL I 379 N ASN I 50
SHEET 1 AH 4 ASN I 82 VAL I 85 0
SHEET 2 AH 4 ILE I 92 ARG I 101 -1 O ALA I 93 N VAL I 84
SHEET 3 AH 4 ARG I 104 PHE I 114 -1 O PHE I 114 N ILE I 92
SHEET 4 AH 4 PRO I 121 LEU I 127 -1 O LEU I 127 N ASP I 109
SHEET 1 AI 4 THR I 142 LEU I 144 0
SHEET 2 AI 4 THR I 150 GLN I 155 -1 O LEU I 152 N SER I 143
SHEET 3 AI 4 ALA I 161 ASP I 166 -1 O GLY I 163 N PHE I 153
SHEET 4 AI 4 ALA I 171 ASP I 177 -1 O LYS I 173 N VAL I 164
SHEET 1 AJ 4 CYS I 181 ALA I 188 0
SHEET 2 AJ 4 THR I 191 CYS I 196 -1 O HIS I 195 N TYR I 182
SHEET 3 AJ 4 SER I 200 ALA I 205 -1 O ALA I 202 N MET I 194
SHEET 4 AJ 4 GLU I 213 VAL I 219 -1 O THR I 215 N LYS I 203
SHEET 1 AK 4 ALA I 232 SER I 234 0
SHEET 2 AK 4 ARG I 239 PRO I 243 -1 O VAL I 241 N ALA I 232
SHEET 3 AK 4 LYS I 248 ASP I 253 -1 O HIS I 250 N TRP I 242
SHEET 4 AK 4 LYS I 260 PHE I 261 -1 O LYS I 260 N ASP I 253
SHEET 1 AL 4 ALA I 232 SER I 234 0
SHEET 2 AL 4 ARG I 239 PRO I 243 -1 O VAL I 241 N ALA I 232
SHEET 3 AL 4 LYS I 248 ASP I 253 -1 O HIS I 250 N TRP I 242
SHEET 4 AL 4 VAL I 265 GLU I 266 -1 O VAL I 265 N ILE I 249
SHEET 1 AM 4 ARG I 323 ILE I 333 0
SHEET 2 AM 4 SER I 310 ASP I 317 -1 N VAL I 315 O LEU I 324
SHEET 3 AM 4 ARG I 293 GLN I 300 -1 N VAL I 298 O PHE I 312
SHEET 4 AM 4 TRP I 277 PRO I 279 -1 N ARG I 278 O ASP I 299
SHEET 1 AN 4 ARG I 323 ILE I 333 0
SHEET 2 AN 4 SER I 310 ASP I 317 -1 N VAL I 315 O LEU I 324
SHEET 3 AN 4 ARG I 293 GLN I 300 -1 N VAL I 298 O PHE I 312
SHEET 4 AN 4 VAL I 285 HIS I 288 -1 N ALA I 286 O TYR I 295
SHEET 1 AO 4 SER I 335 VAL I 338 0
SHEET 2 AO 4 LEU I 345 SER I 350 -1 O LEU I 349 N SER I 335
SHEET 3 AO 4 THR I 355 ASP I 360 -1 O TYR I 357 N ALA I 348
SHEET 4 AO 4 GLU I 366 VAL I 370 -1 O ARG I 368 N ILE I 358
SHEET 1 AP 2 ASP J 32 ASN J 34 0
SHEET 2 AP 2 PRO J 87 LEU J 89 -1 O CYS J 88 N GLY J 33
SHEET 1 AQ 3 LYS J 51 LEU J 52 0
SHEET 2 AQ 3 ASP J 76 CYS J 78 -1 O CYS J 78 N LYS J 51
SHEET 3 AQ 3 TYR J 119 THR J 122 -1 O CYS J 121 N CYS J 77
SHEET 1 AR 3 TRQ J 57 TYR J 62 0
SHEET 2 AR 3 SER J 69 TYR J 74 -1 O TYR J 70 N CYS J 61
SHEET 3 AR 3 ILE J 126 LYS J 129 -1 O GLY J 128 N LEU J 71
SHEET 1 AS 5 LYS K 29 TYR K 30 0
SHEET 2 AS 5 ILE K 21 ALA K 26 -1 N ALA K 26 O LYS K 29
SHEET 3 AS 5 THR K 42 ASN K 47 1 O THR K 44 N VAL K 23
SHEET 4 AS 5 GLN K 76 PHE K 82 -1 O TYR K 78 N TRP K 45
SHEET 5 AS 5 ALA K 3 THR K 4 -1 N THR K 4 O THR K 81
SHEET 1 AT 5 LYS K 29 TYR K 30 0
SHEET 2 AT 5 ILE K 21 ALA K 26 -1 N ALA K 26 O LYS K 29
SHEET 3 AT 5 THR K 42 ASN K 47 1 O THR K 44 N VAL K 23
SHEET 4 AT 5 GLN K 76 PHE K 82 -1 O TYR K 78 N TRP K 45
SHEET 5 AT 5 PHE K 11 ALA K 12 -1 N PHE K 11 O ALA K 77
SHEET 1 AU 3 GLU K 34 VAL K 37 0
SHEET 2 AU 3 HIS K 95 VAL K 104 1 O VAL K 103 N LEU K 35
SHEET 3 AU 3 GLY K 86 CYS K 92 -1 N GLY K 86 O VAL K 104
SHEET 1 AV 2 HIS K 56 PHE K 57 0
SHEET 2 AV 2 LEU K 67 LYS K 68 -1 O LEU K 67 N PHE K 57
SHEET 1 AW 4 ARG M 70 GLY M 77 0
SHEET 2 AW 4 THR M 59 ASP M 65 -1 N VAL M 63 O GLY M 73
SHEET 3 AW 4 ARG M 46 ASP M 51 -1 N VAL M 47 O ILE M 64
SHEET 4 AW 4 VAL M 379 THR M 382 -1 O THR M 381 N TYR M 48
SHEET 1 AX 4 ASN M 82 VAL M 85 0
SHEET 2 AX 4 ILE M 92 ARG M 101 -1 O ALA M 93 N VAL M 84
SHEET 3 AX 4 ARG M 104 PHE M 114 -1 O PHE M 114 N ILE M 92
SHEET 4 AX 4 PRO M 121 LEU M 127 -1 O LEU M 127 N ASP M 109
SHEET 1 AY 4 THR M 142 LEU M 144 0
SHEET 2 AY 4 THR M 150 GLN M 155 -1 O LEU M 152 N SER M 143
SHEET 3 AY 4 ALA M 161 ASP M 166 -1 O ALA M 161 N GLN M 155
SHEET 4 AY 4 ALA M 171 ASP M 177 -1 O LYS M 173 N VAL M 164
SHEET 1 AZ 4 CYS M 181 ALA M 188 0
SHEET 2 AZ 4 THR M 191 CYS M 196 -1 O HIS M 195 N TYR M 182
SHEET 3 AZ 4 LEU M 201 ALA M 205 -1 O VAL M 204 N PHE M 192
SHEET 4 AZ 4 GLU M 213 HIS M 216 -1 O THR M 215 N LYS M 203
SHEET 1 BA 4 ALA M 232 SER M 234 0
SHEET 2 BA 4 ARG M 239 PRO M 243 -1 O VAL M 241 N ALA M 232
SHEET 3 BA 4 LYS M 248 ASP M 253 -1 O HIS M 250 N TRP M 242
SHEET 4 BA 4 LYS M 260 PHE M 261 -1 O LYS M 260 N ASP M 253
SHEET 1 BB 4 ALA M 232 SER M 234 0
SHEET 2 BB 4 ARG M 239 PRO M 243 -1 O VAL M 241 N ALA M 232
SHEET 3 BB 4 LYS M 248 ASP M 253 -1 O HIS M 250 N TRP M 242
SHEET 4 BB 4 VAL M 265 GLU M 266 -1 O VAL M 265 N ILE M 249
SHEET 1 BC 4 ARG M 323 ILE M 333 0
SHEET 2 BC 4 SER M 310 ASP M 317 -1 N VAL M 315 O LEU M 324
SHEET 3 BC 4 ARG M 293 GLN M 300 -1 N ILE M 294 O LEU M 316
SHEET 4 BC 4 TRP M 277 PRO M 279 -1 N ARG M 278 O ASP M 299
SHEET 1 BD 4 ARG M 323 ILE M 333 0
SHEET 2 BD 4 SER M 310 ASP M 317 -1 N VAL M 315 O LEU M 324
SHEET 3 BD 4 ARG M 293 GLN M 300 -1 N ILE M 294 O LEU M 316
SHEET 4 BD 4 VAL M 285 HIS M 288 -1 N ALA M 286 O TYR M 295
SHEET 1 BE 4 SER M 335 VAL M 338 0
SHEET 2 BE 4 LEU M 345 SER M 350 -1 O LEU M 349 N SER M 335
SHEET 3 BE 4 THR M 355 ASP M 360 -1 O TYR M 357 N ALA M 348
SHEET 4 BE 4 GLU M 366 VAL M 370 -1 O ARG M 368 N ILE M 358
SHEET 1 BF 2 ASP N 32 ASN N 34 0
SHEET 2 BF 2 PRO N 87 LEU N 89 -1 O CYS N 88 N GLY N 33
SHEET 1 BG 3 LYS N 51 LEU N 52 0
SHEET 2 BG 3 ASP N 76 CYS N 78 -1 O CYS N 78 N LYS N 51
SHEET 3 BG 3 TYR N 119 THR N 122 -1 O CYS N 121 N CYS N 77
SHEET 1 BH 3 TRQ N 57 ASN N 63 0
SHEET 2 BH 3 GLN N 68 TYR N 74 -1 O TYR N 70 N CYS N 61
SHEET 3 BH 3 ILE N 126 LYS N 129 -1 O GLY N 128 N LEU N 71
SHEET 1 BI 5 LYS O 29 TYR O 30 0
SHEET 2 BI 5 ILE O 21 ALA O 26 -1 N ALA O 26 O LYS O 29
SHEET 3 BI 5 THR O 42 ASN O 47 1 O ILE O 46 N ILE O 25
SHEET 4 BI 5 GLN O 76 PHE O 82 -1 O LEU O 80 N VAL O 43
SHEET 5 BI 5 ALA O 3 THR O 4 -1 N THR O 4 O THR O 81
SHEET 1 BJ 5 LYS O 29 TYR O 30 0
SHEET 2 BJ 5 ILE O 21 ALA O 26 -1 N ALA O 26 O LYS O 29
SHEET 3 BJ 5 THR O 42 ASN O 47 1 O ILE O 46 N ILE O 25
SHEET 4 BJ 5 GLN O 76 PHE O 82 -1 O LEU O 80 N VAL O 43
SHEET 5 BJ 5 PHE O 11 ALA O 12 -1 N PHE O 11 O ALA O 77
SHEET 1 BK 3 GLU O 34 LYS O 38 0
SHEET 2 BK 3 ARG O 99 GLU O 105 1 O VAL O 103 N LEU O 35
SHEET 3 BK 3 GLY O 86 HIS O 91 -1 N GLY O 86 O VAL O 104
SHEET 1 BL 2 HIS O 56 PHE O 57 0
SHEET 2 BL 2 LEU O 67 LYS O 68 -1 O LEU O 67 N PHE O 57
SSBOND 1 CYS A 181 CYS A 196 1555 1555 2.48
SSBOND 2 CYS B 23 CYS B 88 1555 1555 2.49
SSBOND 3 CYS B 29 CYS B 61 1555 1555 2.48
SSBOND 4 CYS B 36 CYS B 121 1555 1555 2.48
SSBOND 5 CYS B 38 CYS B 86 1555 1555 2.45
SSBOND 6 CYS B 46 CYS B 77 1555 1555 2.51
SSBOND 7 CYS B 78 CYS B 109 1555 1555 2.45
SSBOND 8 CYS E 181 CYS E 196 1555 1555 2.46
SSBOND 9 CYS F 23 CYS F 88 1555 1555 2.49
SSBOND 10 CYS F 29 CYS F 61 1555 1555 2.43
SSBOND 11 CYS F 36 CYS F 121 1555 1555 2.45
SSBOND 12 CYS F 38 CYS F 86 1555 1555 2.41
SSBOND 13 CYS F 46 CYS F 77 1555 1555 2.41
SSBOND 14 CYS F 78 CYS F 109 1555 1555 2.42
SSBOND 15 CYS I 181 CYS I 196 1555 1555 2.44
SSBOND 16 CYS J 23 CYS J 88 1555 1555 2.48
SSBOND 17 CYS J 29 CYS J 61 1555 1555 2.44
SSBOND 18 CYS J 36 CYS J 121 1555 1555 2.45
SSBOND 19 CYS J 38 CYS J 86 1555 1555 2.45
SSBOND 20 CYS J 46 CYS J 77 1555 1555 2.48
SSBOND 21 CYS J 78 CYS J 109 1555 1555 2.41
SSBOND 22 CYS M 181 CYS M 196 1555 1555 2.47
SSBOND 23 CYS N 23 CYS N 88 1555 1555 2.48
SSBOND 24 CYS N 29 CYS N 61 1555 1555 2.48
SSBOND 25 CYS N 36 CYS N 121 1555 1555 2.51
SSBOND 26 CYS N 38 CYS N 86 1555 1555 2.44
SSBOND 27 CYS N 46 CYS N 77 1555 1555 2.54
SSBOND 28 CYS N 78 CYS N 109 1555 1555 2.44
LINK C SER B 56 N TRQ B 57 1555 1555 1.32
LINK C TRQ B 57 N VAL B 58 1555 1555 1.33
LINK CE3 TRQ B 57 CD1 TRP B 108 1555 1555 1.41
LINK SG CYS D 57 CAB HEC D 200 1555 1555 1.80
LINK SG CYS D 60 CAC HEC D 200 1555 1555 1.85
LINK C SER F 56 N TRQ F 57 1555 1555 1.32
LINK C TRQ F 57 N VAL F 58 1555 1555 1.33
LINK CE3 TRQ F 57 CD1 TRP F 108 1555 1555 1.41
LINK SG CYS H 57 CAB HEC H 200 1555 1555 1.80
LINK SG CYS H 60 CAC HEC H 200 1555 1555 1.84
LINK C SER J 56 N TRQ J 57 1555 1555 1.32
LINK C TRQ J 57 N VAL J 58 1555 1555 1.33
LINK CE3 TRQ J 57 CD1 TRP J 108 1555 1555 1.41
LINK SG CYS L 57 CAB HEC L 200 1555 1555 1.81
LINK SG CYS L 60 CAC HEC L 200 1555 1555 1.84
LINK C SER N 56 N TRQ N 57 1555 1555 1.33
LINK C TRQ N 57 N VAL N 58 1555 1555 1.33
LINK CE3 TRQ N 57 CD1 TRP N 108 1555 1555 1.41
LINK SG CYS P 57 CAB HEC P 200 1555 1555 1.81
LINK SG CYS P 60 CAC HEC P 200 1555 1555 1.82
LINK ND1 HIS C 53 CU CU C 107 1555 1555 2.16
LINK SG CYS C 92 CU CU C 107 1555 1555 2.21
LINK ND1 HIS C 95 CU CU C 107 1555 1555 2.20
LINK NE2 HIS D 61 FE HEC D 200 1555 1555 2.00
LINK OD2 ASP D 75 NA NA D 604 1555 1555 2.40
LINK O TYR D 77 NA NA D 604 1555 1555 2.62
LINK SD MET D 101 FE HEC D 200 1555 1555 2.31
LINK NA NA D 604 O HOH D1002 1555 1555 2.79
LINK NA NA D 604 O HOH D1409 1555 1555 2.49
LINK NA NA D 604 O HOH D1768 1555 1555 2.70
LINK ND1 HIS G 53 CU CU G 107 1555 1555 2.08
LINK SG CYS G 92 CU CU G 107 1555 1555 2.23
LINK ND1 HIS G 95 CU CU G 107 1555 1555 2.09
LINK NE2 HIS H 61 FE HEC H 200 1555 1555 2.00
LINK O GLY H 72 NA NA H 603 1555 1555 2.78
LINK OD2 ASP H 75 NA NA H 603 1555 1555 2.39
LINK O TYR H 77 NA NA H 603 1555 1555 2.75
LINK SD MET H 101 FE HEC H 200 1555 1555 2.25
LINK NA NA H 603 O HOH H1158 1555 1555 2.82
LINK OE2 GLU K 31 NA NA L 601 1555 1555 2.94
LINK ND1 HIS K 53 CU CU K 107 1555 1555 2.08
LINK SG CYS K 92 CU CU K 107 1555 1555 2.33
LINK ND1 HIS K 95 CU CU K 107 1555 1555 2.15
LINK SD MET K 98 CU CU K 107 1555 1555 2.76
LINK O HOH K1348 NA NA L 601 1555 1555 2.74
LINK NE2 HIS L 61 FE HEC L 200 1555 1555 2.05
LINK O GLY L 72 NA NA L 601 1555 1555 2.79
LINK OD2 ASP L 75 NA NA L 601 1555 1555 2.46
LINK O TYR L 77 NA NA L 601 1555 1555 2.68
LINK SD MET L 101 FE HEC L 200 1555 1555 2.25
LINK NA NA L 601 O HOH L1273 1555 1555 2.58
LINK NA NA L 601 O HOH L1529 1555 1555 2.45
LINK ND1 HIS O 53 CU CU O 107 1555 1555 2.13
LINK SG CYS O 92 CU CU O 107 1555 1555 2.31
LINK ND1 HIS O 95 CU CU O 107 1555 1555 2.19
LINK O HOH O1352 NA NA P 602 1555 1555 2.56
LINK NE2 HIS P 61 FE HEC P 200 1555 1555 2.00
LINK O GLY P 72 NA NA P 602 1555 1555 2.86
LINK OD2 ASP P 75 NA NA P 602 1555 1555 2.39
LINK O TYR P 77 NA NA P 602 1555 1555 2.71
LINK SD MET P 101 FE HEC P 200 1555 1555 2.29
LINK NA NA P 602 O HOH P1276 1555 1555 2.83
LINK NA NA P 602 O HOH P2639 1555 1555 2.82
CISPEP 1 SER A 157 PRO A 158 0 -0.02
CISPEP 2 SER E 157 PRO E 158 0 0.25
CISPEP 3 SER I 157 PRO I 158 0 0.01
CISPEP 4 SER M 157 PRO M 158 0 0.21
SITE 1 AC1 4 HIS C 53 CYS C 92 HIS C 95 MET C 98
SITE 1 AC2 4 HIS G 53 CYS G 92 HIS G 95 MET G 98
SITE 1 AC3 4 HIS K 53 CYS K 92 HIS K 95 MET K 98
SITE 1 AC4 4 HIS O 53 CYS O 92 HIS O 95 MET O 98
SITE 1 AC5 6 PHE F 110 GLY F 111 ASP F 115 HOH F1690
SITE 2 AC5 6 HOH F2285 LYS G 68
SITE 1 AC6 5 PHE B 110 GLY B 111 ASP B 115 HOH B2517
SITE 2 AC6 5 LYS C 68
SITE 1 AC7 10 PHE J 110 GLY J 111 ASP J 115 MET J 117
SITE 2 AC7 10 HOH J1065 HOH J1223 HOH J1615 HOH J1902
SITE 3 AC7 10 HOH J2558 LYS K 68
SITE 1 AC8 9 HOH M2677 PHE N 110 GLY N 111 ASP N 115
SITE 2 AC8 9 MET N 117 HOH N1282 HOH N1925 HOH N2529
SITE 3 AC8 9 LYS O 68
SITE 1 AC9 6 ALA I 86 ASP I 87 ASP I 88 PRO I 146
SITE 2 AC9 6 ASP I 147 HOH I2612
SITE 1 BC1 6 ALA E 86 ASP E 87 ASP E 88 PRO E 146
SITE 2 BC1 6 GLY E 148 HOH E2614
SITE 1 BC2 6 ASP G 18 ASP M 87 ASP M 88 PRO M 146
SITE 2 BC2 6 GLY M 148 HOH M1206
SITE 1 BC3 4 ALA A 86 ASP A 87 ASP A 88 PRO A 146
SITE 1 BC4 7 GLU K 31 HOH K1348 GLY L 72 ASP L 75
SITE 2 BC4 7 TYR L 77 HOH L1273 HOH L1529
SITE 1 BC5 7 GLU O 31 HOH O1352 GLY P 72 ASP P 75
SITE 2 BC5 7 TYR P 77 HOH P1276 HOH P2639
SITE 1 BC6 5 GLU G 31 GLY H 72 ASP H 75 TYR H 77
SITE 2 BC6 5 HOH H1158
SITE 1 BC7 7 GLU C 31 GLY D 72 ASP D 75 TYR D 77
SITE 2 BC7 7 HOH D1002 HOH D1409 HOH D1768
SITE 1 BC8 16 MET D 56 CYS D 57 CYS D 60 HIS D 61
SITE 2 BC8 16 PRO D 71 TRP D 78 THR D 79 TYR D 80
SITE 3 BC8 16 ASN D 83 LEU D 89 LEU D 93 ALA D 97
SITE 4 BC8 16 THR D 98 GLN D 100 MET D 101 HOH D1852
SITE 1 BC9 17 MET H 56 CYS H 57 CYS H 60 HIS H 61
SITE 2 BC9 17 PRO H 71 TRP H 78 THR H 79 TYR H 80
SITE 3 BC9 17 ASN H 83 LEU H 89 LEU H 93 ALA H 97
SITE 4 BC9 17 THR H 98 GLN H 100 MET H 101 HOH H1646
SITE 5 BC9 17 HOH H1903
SITE 1 CC1 17 MET L 56 CYS L 57 CYS L 60 HIS L 61
SITE 2 CC1 17 PRO L 71 TRP L 78 THR L 79 TYR L 80
SITE 3 CC1 17 ASN L 83 LEU L 89 LEU L 93 ALA L 97
SITE 4 CC1 17 THR L 98 GLN L 100 MET L 101 MET L 104
SITE 5 CC1 17 HOH L2369
SITE 1 CC2 16 MET P 56 CYS P 57 CYS P 60 HIS P 61
SITE 2 CC2 16 PRO P 71 TRP P 78 THR P 79 TYR P 80
SITE 3 CC2 16 ASN P 83 THR P 92 LEU P 93 ALA P 97
SITE 4 CC2 16 THR P 98 GLN P 100 MET P 101 HOH P2639
CRYST1 79.122 188.201 127.100 90.00 99.24 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 0.012639 0.000000 0.002056 0.00000
SCALE2 0.000000 0.005313 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007971 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
