HEADER LYASE 03-SEP-01 1IR2
TITLE CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5-BISPHOSPHATE
TITLE 2 CARBOXYLASE/OXYGENASE (RUBISCO) FROM GREEN ALGA, CHLAMYDOMONAS
TITLE 3 REINHARDTII COMPLEXED WITH 2-CARBOXYARABINITOL-1,5-BISPHOSPHATE (2-
TITLE 4 CABP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LARGE SUBUNIT OF RUBISCO;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, S, T, U, V, W, X, Y, Z;
COMPND 4 SYNONYM: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;
COMPND 5 EC: 4.1.1.39;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: SMALL SUBUNIT OF RUBISCO;
COMPND 8 CHAIN: I, J, K, L, M, N, O, P, 1, 2, 3, 4, 5, 6, 7, 8;
COMPND 9 SYNONYM: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 2;
COMPND 10 EC: 4.1.1.39
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE 3 ORGANISM_TAXID: 3055;
SOURCE 4 STRAIN: 137C MT+;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;
SOURCE 7 ORGANISM_TAXID: 3055;
SOURCE 8 STRAIN: 137C MT+
KEYWDS N-METHYLMETHIONINE, 4-HYDROXYPROLINE, S-METHYLCYSTEINE, ALPHA/BETA
KEYWDS 2 BARREL, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.MIZOHATA,H.MATSUMURA,Y.OKANO,M.KUMEI,H.TAKUMA,J.ONODERA,K.KATO,
AUTHOR 2 N.SHIBATA,T.INOUE,A.YOKOTA,Y.KAI
REVDAT 6 15-NOV-23 1IR2 1 REMARK
REVDAT 5 25-OCT-23 1IR2 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 1IR2 1 VERSN
REVDAT 3 24-FEB-09 1IR2 1 VERSN
REVDAT 2 14-JAN-03 1IR2 1 REMARK
REVDAT 1 20-MAR-02 1IR2 0
JRNL AUTH E.MIZOHATA,H.MATSUMURA,Y.OKANO,M.KUMEI,H.TAKUMA,J.ONODERA,
JRNL AUTH 2 K.KATO,N.SHIBATA,T.INOUE,A.YOKOTA,Y.KAI
JRNL TITL CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5-BISPHOSPHATE
JRNL TITL 2 CARBOXYLASE/OXYGENASE FROM GREEN ALGA CHLAMYDOMONAS
JRNL TITL 3 REINHARDTII COMPLEXED WITH
JRNL TITL 4 2-CARBOXYARABINITOL-1,5-BISPHOSPHATE.
JRNL REF J.MOL.BIOL. V. 316 679 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 11866526
JRNL DOI 10.1006/JMBI.2001.5381
REMARK 2
REMARK 2 RESOLUTION. 1.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.89
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) (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 762301
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) : 0.152
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 37921
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 2859
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.005
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 76496
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 592
REMARK 3 SOLVENT ATOMS : 9999
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.10
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) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : 0.21
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) : 0.20
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.22
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.320
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 1IR2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000005202.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-18B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : DIFFRACTOMETER
REMARK 200 DETECTOR MANUFACTURER : WEISSENBERG
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 763078
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.84
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.22900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ID: 1BUR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, HEPES-KOH, GLYCEROL, NAHCO3,
REMARK 280 MGCL2, DTT, 2-CARBOXYARABINITOL-1,5-BISPHOSPHATE (2-CABP), EDTA,
REMARK 280 PH 8.0, 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 87.37500
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: THE BIOLOGICAL ASSEMBLY IS A HEXADECAMER COMPRISED OF 8
REMARK 300 LARGE AND 8 SMALL SUBUNITS. TWO HEXADECAMER EXIST IN THE ASYMMETRIC
REMARK 300 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: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 123440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 115880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -617.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I, B, J, C, K, D, L, E, M,
REMARK 350 AND CHAINS: F, N, G, O, H, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 123270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 116460 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -611.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, 1, T, 2, U, 3, V, 4, W, 5,
REMARK 350 AND CHAINS: X, 6, Y, 7, Z, 8
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 VAL A 2
REMARK 465 PRO A 3
REMARK 465 GLN A 4
REMARK 465 THR A 5
REMARK 465 GLU A 6
REMARK 465 THR A 7
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 PRO B 3
REMARK 465 GLN B 4
REMARK 465 THR B 5
REMARK 465 GLU B 6
REMARK 465 THR B 7
REMARK 465 LYS B 8
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 PRO C 3
REMARK 465 GLN C 4
REMARK 465 THR C 5
REMARK 465 GLU C 6
REMARK 465 THR C 7
REMARK 465 LYS C 8
REMARK 465 ALA C 9
REMARK 465 MET D 1
REMARK 465 VAL D 2
REMARK 465 PRO D 3
REMARK 465 GLN D 4
REMARK 465 THR D 5
REMARK 465 GLU D 6
REMARK 465 THR D 7
REMARK 465 LYS D 8
REMARK 465 MET E 1
REMARK 465 VAL E 2
REMARK 465 PRO E 3
REMARK 465 GLN E 4
REMARK 465 THR E 5
REMARK 465 GLU E 6
REMARK 465 THR E 7
REMARK 465 LYS E 8
REMARK 465 ALA E 9
REMARK 465 GLY E 10
REMARK 465 MET F 1
REMARK 465 VAL F 2
REMARK 465 PRO F 3
REMARK 465 GLN F 4
REMARK 465 THR F 5
REMARK 465 GLU F 6
REMARK 465 THR F 7
REMARK 465 LYS F 8
REMARK 465 ALA F 9
REMARK 465 GLY F 10
REMARK 465 MET G 1
REMARK 465 VAL G 2
REMARK 465 PRO G 3
REMARK 465 GLN G 4
REMARK 465 THR G 5
REMARK 465 GLU G 6
REMARK 465 THR G 7
REMARK 465 LYS G 8
REMARK 465 ALA G 9
REMARK 465 MET H 1
REMARK 465 VAL H 2
REMARK 465 PRO H 3
REMARK 465 GLN H 4
REMARK 465 THR H 5
REMARK 465 GLU H 6
REMARK 465 THR H 7
REMARK 465 MET S 1
REMARK 465 VAL S 2
REMARK 465 PRO S 3
REMARK 465 GLN S 4
REMARK 465 THR S 5
REMARK 465 GLU S 6
REMARK 465 THR S 7
REMARK 465 LYS S 8
REMARK 465 ALA S 9
REMARK 465 GLY S 10
REMARK 465 MET T 1
REMARK 465 VAL T 2
REMARK 465 PRO T 3
REMARK 465 GLN T 4
REMARK 465 THR T 5
REMARK 465 GLU T 6
REMARK 465 THR T 7
REMARK 465 LYS T 8
REMARK 465 ALA T 9
REMARK 465 MET U 1
REMARK 465 VAL U 2
REMARK 465 PRO U 3
REMARK 465 GLN U 4
REMARK 465 THR U 5
REMARK 465 GLU U 6
REMARK 465 MET V 1
REMARK 465 VAL V 2
REMARK 465 PRO V 3
REMARK 465 GLN V 4
REMARK 465 THR V 5
REMARK 465 GLU V 6
REMARK 465 MET W 1
REMARK 465 VAL W 2
REMARK 465 PRO W 3
REMARK 465 GLN W 4
REMARK 465 THR W 5
REMARK 465 GLU W 6
REMARK 465 THR W 7
REMARK 465 LYS W 8
REMARK 465 ALA W 9
REMARK 465 MET X 1
REMARK 465 VAL X 2
REMARK 465 PRO X 3
REMARK 465 GLN X 4
REMARK 465 THR X 5
REMARK 465 GLU X 6
REMARK 465 THR X 7
REMARK 465 LYS X 8
REMARK 465 ALA X 9
REMARK 465 MET Y 1
REMARK 465 VAL Y 2
REMARK 465 PRO Y 3
REMARK 465 GLN Y 4
REMARK 465 THR Y 5
REMARK 465 GLU Y 6
REMARK 465 THR Y 7
REMARK 465 LYS Y 8
REMARK 465 ALA Y 9
REMARK 465 GLY Y 10
REMARK 465 MET Z 1
REMARK 465 VAL Z 2
REMARK 465 PRO Z 3
REMARK 465 GLN Z 4
REMARK 465 THR Z 5
REMARK 465 GLU Z 6
REMARK 465 THR Z 7
REMARK 465 LYS Z 8
REMARK 465 ALA Z 9
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 GLY M 61 N - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 GLY 3 61 N - CA - C ANGL. DEV. = -15.1 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 ALA A 9 114.60 155.16
REMARK 500 SER A 62 -77.91 -141.00
REMARK 500 THR A 75 -164.11 -124.95
REMARK 500 HIS A 153 -57.72 -133.23
REMARK 500 CYS A 172 123.04 -175.53
REMARK 500 ASN A 207 -91.21 -121.53
REMARK 500 MET A 212 109.31 -165.94
REMARK 500 MET A 297 -10.72 86.29
REMARK 500 VAL A 331 -50.45 78.53
REMARK 500 ASP A 357 91.40 -160.97
REMARK 500 THR A 406 -56.56 -121.87
REMARK 500 PHE I 12 49.18 -140.05
REMARK 500 GLU I 13 -149.71 60.14
REMARK 500 PHE I 15 -2.28 80.98
REMARK 500 LYS I 77 -122.09 52.60
REMARK 500 SER B 62 -78.26 -142.45
REMARK 500 THR B 75 -168.20 -124.09
REMARK 500 ASN B 95 21.88 -149.30
REMARK 500 HIS B 153 -51.96 -135.56
REMARK 500 CYS B 172 124.47 -174.70
REMARK 500 ASN B 207 -92.17 -120.42
REMARK 500 MET B 212 109.66 -165.39
REMARK 500 ARG B 295 30.87 -94.66
REMARK 500 MET B 297 -10.64 89.91
REMARK 500 VAL B 331 -53.05 78.75
REMARK 500 ASP B 357 91.52 -163.26
REMARK 500 THR B 406 -55.69 -124.79
REMARK 500 GLU J 13 -149.68 60.66
REMARK 500 THR J 14 120.05 -39.05
REMARK 500 LYS J 77 -120.43 56.08
REMARK 500 GLN J 115 74.67 48.71
REMARK 500 ALA C 11 -106.56 39.47
REMARK 500 SER C 62 -74.78 -143.52
REMARK 500 THR C 75 -164.69 -125.51
REMARK 500 HIS C 153 -55.64 -135.46
REMARK 500 CYS C 172 125.76 -172.89
REMARK 500 ASN C 207 -90.55 -121.08
REMARK 500 MET C 212 108.85 -163.83
REMARK 500 MET C 297 -12.38 86.29
REMARK 500 VAL C 331 -52.28 77.65
REMARK 500 ASP C 357 89.55 -158.12
REMARK 500 GLU K 13 -149.43 61.10
REMARK 500 PHE K 15 -1.01 81.10
REMARK 500 LYS K 77 -124.78 55.47
REMARK 500 GLN K 115 73.91 49.67
REMARK 500 ARG K 130 27.63 -143.52
REMARK 500 SER D 62 -75.63 -143.90
REMARK 500 THR D 75 -164.18 -124.09
REMARK 500 ASN D 95 19.16 -147.91
REMARK 500 HIS D 153 -55.85 -136.21
REMARK 500
REMARK 500 THIS ENTRY HAS 250 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX A 201 OQ1
REMARK 620 2 ASP A 203 OD1 89.3
REMARK 620 3 GLU A 204 OE1 91.9 92.7
REMARK 620 4 CAP A 501 O6 169.0 95.6 97.7
REMARK 620 5 CAP A 501 O2 91.2 104.9 162.2 78.0
REMARK 620 6 CAP A 501 O3 87.6 176.7 86.3 87.6 76.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX B 201 OQ1
REMARK 620 2 ASP B 203 OD1 86.7
REMARK 620 3 GLU B 204 OE1 92.8 95.7
REMARK 620 4 CAP B 501 O3 87.9 174.0 87.2
REMARK 620 5 CAP B 501 O2 88.0 99.8 164.6 77.4
REMARK 620 6 CAP B 501 O6 163.6 94.7 103.4 89.7 75.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX C 201 OQ1
REMARK 620 2 ASP C 203 OD1 89.6
REMARK 620 3 GLU C 204 OE1 92.4 90.9
REMARK 620 4 CAP C 501 O6 163.0 96.5 103.3
REMARK 620 5 CAP C 501 O2 87.5 104.6 164.5 75.6
REMARK 620 6 CAP C 501 O3 83.8 173.2 88.2 90.3 76.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX D 201 OQ1
REMARK 620 2 ASP D 203 OD1 88.7
REMARK 620 3 GLU D 204 OE1 96.2 92.4
REMARK 620 4 CAP D 501 O6 163.0 94.6 100.2
REMARK 620 5 CAP D 501 O2 86.3 104.8 162.7 76.8
REMARK 620 6 CAP D 501 O3 87.2 175.0 85.2 90.1 77.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX E 201 OQ1
REMARK 620 2 ASP E 203 OD1 88.6
REMARK 620 3 GLU E 204 OE1 91.4 89.0
REMARK 620 4 CAP E 501 O6 171.7 92.8 96.7
REMARK 620 5 CAP E 501 O3 90.3 173.9 85.0 89.0
REMARK 620 6 CAP E 501 O2 94.3 108.0 162.1 77.5 78.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX F 201 OQ1
REMARK 620 2 ASP F 203 OD1 89.0
REMARK 620 3 GLU F 204 OE1 91.7 90.1
REMARK 620 4 CAP F 501 O3 89.5 175.7 85.9
REMARK 620 5 CAP F 501 O6 169.0 94.8 98.5 87.4
REMARK 620 6 CAP F 501 O2 93.4 106.7 162.5 77.5 75.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX G 201 OQ1
REMARK 620 2 ASP G 203 OD1 91.7
REMARK 620 3 GLU G 204 OE1 94.0 88.9
REMARK 620 4 CAP G 501 O2 89.8 107.5 163.0
REMARK 620 5 CAP G 501 O3 85.8 175.3 87.3 76.5
REMARK 620 6 CAP G 501 O6 164.7 95.5 99.5 75.2 87.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX H 201 OQ1
REMARK 620 2 ASP H 203 OD1 87.1
REMARK 620 3 GLU H 204 OE1 92.0 90.5
REMARK 620 4 CAP H 501 O3 87.1 174.1 88.6
REMARK 620 5 CAP H 501 O6 166.7 94.2 101.2 91.7
REMARK 620 6 CAP H 501 O2 88.8 102.4 167.1 78.6 78.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG S 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX S 201 OQ1
REMARK 620 2 ASP S 203 OD1 86.9
REMARK 620 3 GLU S 204 OE1 92.6 95.7
REMARK 620 4 CAP S 501 O3 89.1 175.8 83.5
REMARK 620 5 CAP S 501 O2 90.8 103.0 161.2 78.1
REMARK 620 6 CAP S 501 O6 166.4 94.3 100.8 89.9 75.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG T 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX T 201 OQ1
REMARK 620 2 ASP T 203 OD1 89.1
REMARK 620 3 GLU T 204 OE1 91.1 88.1
REMARK 620 4 CAP T 501 O6 170.1 95.1 98.0
REMARK 620 5 CAP T 501 O3 88.5 175.0 87.5 88.0
REMARK 620 6 CAP T 501 O2 92.1 106.5 165.1 78.1 78.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG U 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX U 201 OQ1
REMARK 620 2 ASP U 203 OD1 89.9
REMARK 620 3 GLU U 204 OE1 90.9 93.4
REMARK 620 4 CAP U 501 O3 86.4 176.0 85.1
REMARK 620 5 CAP U 501 O6 164.7 97.0 102.2 87.0
REMARK 620 6 CAP U 501 O2 89.3 104.6 162.0 77.0 75.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG V 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX V 201 OQ1
REMARK 620 2 ASP V 203 OD1 86.2
REMARK 620 3 GLU V 204 OE1 88.2 91.2
REMARK 620 4 CAP V 501 O6 170.0 98.9 100.2
REMARK 620 5 CAP V 501 O2 92.3 107.5 161.3 78.0
REMARK 620 6 CAP V 501 O3 86.5 171.8 84.8 88.8 76.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG W 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX W 201 OQ1
REMARK 620 2 ASP W 203 OD1 88.9
REMARK 620 3 GLU W 204 OE1 96.9 90.6
REMARK 620 4 CAP W 501 O3 91.2 177.6 87.0
REMARK 620 5 CAP W 501 O6 166.2 94.0 96.6 86.5
REMARK 620 6 CAP W 501 O2 90.9 104.9 162.9 77.5 75.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX X 201 OQ1
REMARK 620 2 ASP X 203 OD1 87.5
REMARK 620 3 GLU X 204 OE1 93.6 96.0
REMARK 620 4 CAP X 501 O6 165.8 96.4 99.5
REMARK 620 5 CAP X 501 O3 87.4 174.7 85.8 88.2
REMARK 620 6 CAP X 501 O2 89.0 102.9 161.1 76.8 75.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Y 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX Y 201 OQ1
REMARK 620 2 ASP Y 203 OD1 90.5
REMARK 620 3 GLU Y 204 OE1 93.2 94.6
REMARK 620 4 CAP Y 501 O6 166.3 95.9 98.4
REMARK 620 5 CAP Y 501 O3 87.8 178.2 84.9 85.9
REMARK 620 6 CAP Y 501 O2 90.7 104.4 160.5 76.0 76.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Z 476 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 KCX Z 201 OQ1
REMARK 620 2 ASP Z 203 OD1 89.5
REMARK 620 3 GLU Z 204 OE1 97.2 93.8
REMARK 620 4 CAP Z 501 O3 89.5 178.5 87.5
REMARK 620 5 CAP Z 501 O6 163.9 94.7 98.1 85.9
REMARK 620 6 CAP Z 501 O2 89.1 103.1 162.1 75.8 74.8
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 MG A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG S 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG T 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG U 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG V 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG W 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Y 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Z 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP S 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP T 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP U 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP V 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP W 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP X 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP Y 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP Z 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 620
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL W 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL X 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Y 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Z 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL S 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL T 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL U 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL V 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL S 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL X 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Y 611
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Z 612
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL S 613
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL T 614
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL U 615
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL V 616
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL X 617
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Y 618
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Z 619
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL W 620
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IR1 RELATED DB: PDB
REMARK 900 1IR1 CONTAINS SPINACH RUBISCO COMPLEXED WITH CO2, MG2+ AND 2-
REMARK 900 CARBOXYARABINITOL-1,5-BISPHOSPHATE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE IS A DIFFERENCE BETWEEN SEQRES(PRO46) AND
REMARK 999 SEQUENCE DATABASE(LEU46) IN LARGE SUBUNIT.
REMARK 999 THERE IS NO QUESTION FROM THE ELECTRON
REMARK 999 DENSITY THAT THE 46TH RESIDUE IS PRO.
DBREF 1IR2 A 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 B 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 C 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 D 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 E 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 F 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 G 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 H 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 S 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 T 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 U 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 V 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 W 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 X 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 Y 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 Z 1 475 UNP P00877 RBL_CHLRE 1 475
DBREF 1IR2 I 1 140 UNP P08475 RBS2_CHLRE 46 185
DBREF 1IR2 J 1 140 UNP P08475 RBS2_CHLRE 46 185
DBREF 1IR2 K 1 140 UNP P08475 RBS2_CHLRE 46 185
DBREF 1IR2 L 1 140 UNP P08475 RBS2_CHLRE 46 185
DBREF 1IR2 M 1 140 UNP P08475 RBS2_CHLRE 46 185
DBREF 1IR2 N 1 140 UNP P08475 RBS2_CHLRE 46 185
DBREF 1IR2 O 1 140 UNP P08475 RBS2_CHLRE 46 185
DBREF 1IR2 P 1 140 UNP P08475 RBS2_CHLRE 46 185
DBREF 1IR2 1 1 140 UNP P08475 RBS2_CHLRE 46 185
DBREF 1IR2 2 1 140 UNP P08475 RBS2_CHLRE 46 185
DBREF 1IR2 3 1 140 UNP P08475 RBS2_CHLRE 46 185
DBREF 1IR2 4 1 140 UNP P08475 RBS2_CHLRE 46 185
DBREF 1IR2 5 1 140 UNP P08475 RBS2_CHLRE 46 185
DBREF 1IR2 6 1 140 UNP P08475 RBS2_CHLRE 46 185
DBREF 1IR2 7 1 140 UNP P08475 RBS2_CHLRE 46 185
DBREF 1IR2 8 1 140 UNP P08475 RBS2_CHLRE 46 185
SEQADV 1IR2 PRO A 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP A 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP A 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX A 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC A 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC A 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 PRO B 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP B 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP B 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX B 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC B 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC B 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 PRO C 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP C 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP C 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX C 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC C 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC C 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 PRO D 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP D 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP D 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX D 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC D 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC D 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 PRO E 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP E 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP E 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX E 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC E 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC E 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 PRO F 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP F 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP F 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX F 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC F 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC F 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 PRO G 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP G 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP G 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX G 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC G 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC G 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 PRO H 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP H 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP H 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX H 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC H 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC H 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 PRO S 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP S 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP S 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX S 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC S 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC S 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 PRO T 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP T 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP T 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX T 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC T 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC T 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 PRO U 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP U 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP U 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX U 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC U 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC U 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 PRO V 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP V 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP V 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX V 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC V 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC V 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 PRO W 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP W 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP W 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX W 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC W 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC W 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 PRO X 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP X 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP X 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX X 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC X 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC X 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 PRO Y 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP Y 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP Y 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX Y 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC Y 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC Y 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 PRO Z 46 UNP P00877 LEU 46 SEE REMARK 999
SEQADV 1IR2 HYP Z 104 UNP P00877 PRO 104 MODIFIED RESIDUE
SEQADV 1IR2 HYP Z 151 UNP P00877 PRO 151 MODIFIED RESIDUE
SEQADV 1IR2 KCX Z 201 UNP P00877 LYS 201 MODIFIED RESIDUE
SEQADV 1IR2 SMC Z 256 UNP P00877 CYS 256 MODIFIED RESIDUE
SEQADV 1IR2 SMC Z 369 UNP P00877 CYS 369 MODIFIED RESIDUE
SEQADV 1IR2 MME I 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQADV 1IR2 MME J 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQADV 1IR2 MME K 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQADV 1IR2 MME L 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQADV 1IR2 MME M 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQADV 1IR2 MME N 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQADV 1IR2 MME O 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQADV 1IR2 MME P 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQADV 1IR2 MME 1 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQADV 1IR2 MME 2 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQADV 1IR2 MME 3 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQADV 1IR2 MME 4 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQADV 1IR2 MME 5 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQADV 1IR2 MME 6 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQADV 1IR2 MME 7 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQADV 1IR2 MME 8 1 UNP P08475 MET 46 MODIFIED RESIDUE
SEQRES 1 A 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 A 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 A 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 A 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 A 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 A 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 A 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 A 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 A 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 A 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 A 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 A 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 A 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 A 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 A 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 A 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 A 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 A 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 A 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 A 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 A 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 A 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 A 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 A 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 A 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 A 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 A 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 A 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 A 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 A 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 A 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 A 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 A 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 A 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 A 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 A 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 A 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 I 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 I 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 I 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 I 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 I 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 I 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 I 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 I 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 I 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 I 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 I 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 B 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 B 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 B 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 B 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 B 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 B 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 B 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 B 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 B 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 B 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 B 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 B 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 B 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 B 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 B 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 B 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 B 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 B 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 B 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 B 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 B 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 B 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 B 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 B 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 B 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 B 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 B 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 B 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 B 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 B 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 B 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 B 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 B 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 B 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 B 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 B 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 B 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 J 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 J 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 J 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 J 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 J 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 J 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 J 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 J 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 J 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 J 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 J 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 C 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 C 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 C 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 C 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 C 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 C 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 C 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 C 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 C 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 C 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 C 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 C 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 C 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 C 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 C 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 C 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 C 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 C 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 C 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 C 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 C 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 C 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 C 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 C 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 C 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 C 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 C 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 C 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 C 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 C 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 C 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 C 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 C 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 C 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 C 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 C 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 C 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 K 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 K 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 K 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 K 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 K 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 K 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 K 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 K 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 K 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 K 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 K 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 D 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 D 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 D 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 D 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 D 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 D 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 D 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 D 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 D 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 D 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 D 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 D 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 D 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 D 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 D 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 D 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 D 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 D 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 D 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 D 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 D 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 D 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 D 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 D 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 D 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 D 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 D 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 D 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 D 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 D 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 D 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 D 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 D 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 D 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 D 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 D 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 D 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 L 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 L 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 L 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 L 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 L 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 L 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 L 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 L 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 L 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 L 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 L 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 E 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 E 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 E 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 E 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 E 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 E 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 E 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 E 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 E 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 E 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 E 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 E 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 E 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 E 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 E 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 E 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 E 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 E 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 E 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 E 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 E 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 E 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 E 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 E 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 E 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 E 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 E 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 E 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 E 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 E 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 E 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 E 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 E 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 E 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 E 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 E 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 E 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 M 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 M 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 M 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 M 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 M 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 M 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 M 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 M 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 M 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 M 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 M 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 F 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 F 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 F 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 F 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 F 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 F 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 F 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 F 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 F 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 F 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 F 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 F 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 F 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 F 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 F 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 F 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 F 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 F 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 F 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 F 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 F 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 F 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 F 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 F 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 F 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 F 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 F 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 F 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 F 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 F 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 F 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 F 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 F 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 F 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 F 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 F 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 F 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 N 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 N 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 N 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 N 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 N 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 N 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 N 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 N 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 N 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 N 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 N 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 G 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 G 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 G 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 G 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 G 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 G 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 G 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 G 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 G 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 G 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 G 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 G 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 G 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 G 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 G 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 G 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 G 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 G 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 G 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 G 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 G 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 G 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 G 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 G 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 G 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 G 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 G 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 G 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 G 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 G 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 G 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 G 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 G 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 G 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 G 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 G 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 G 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 O 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 O 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 O 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 O 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 O 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 O 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 O 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 O 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 O 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 O 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 O 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 H 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 H 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 H 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 H 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 H 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 H 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 H 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 H 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 H 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 H 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 H 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 H 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 H 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 H 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 H 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 H 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 H 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 H 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 H 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 H 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 H 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 H 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 H 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 H 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 H 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 H 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 H 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 H 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 H 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 H 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 H 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 H 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 H 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 H 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 H 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 H 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 H 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 P 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 P 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 P 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 P 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 P 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 P 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 P 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 P 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 P 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 P 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 P 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 S 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 S 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 S 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 S 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 S 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 S 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 S 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 S 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 S 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 S 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 S 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 S 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 S 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 S 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 S 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 S 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 S 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 S 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 S 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 S 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 S 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 S 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 S 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 S 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 S 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 S 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 S 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 S 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 S 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 S 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 S 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 S 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 S 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 S 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 S 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 S 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 S 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 1 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 1 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 1 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 1 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 1 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 1 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 1 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 1 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 1 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 1 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 1 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 T 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 T 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 T 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 T 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 T 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 T 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 T 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 T 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 T 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 T 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 T 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 T 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 T 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 T 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 T 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 T 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 T 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 T 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 T 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 T 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 T 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 T 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 T 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 T 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 T 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 T 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 T 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 T 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 T 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 T 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 T 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 T 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 T 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 T 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 T 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 T 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 T 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 2 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 2 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 2 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 2 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 2 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 2 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 2 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 2 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 2 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 2 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 2 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 U 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 U 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 U 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 U 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 U 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 U 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 U 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 U 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 U 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 U 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 U 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 U 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 U 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 U 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 U 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 U 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 U 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 U 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 U 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 U 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 U 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 U 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 U 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 U 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 U 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 U 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 U 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 U 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 U 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 U 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 U 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 U 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 U 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 U 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 U 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 U 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 U 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 3 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 3 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 3 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 3 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 3 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 3 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 3 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 3 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 3 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 3 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 3 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 V 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 V 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 V 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 V 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 V 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 V 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 V 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 V 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 V 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 V 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 V 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 V 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 V 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 V 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 V 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 V 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 V 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 V 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 V 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 V 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 V 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 V 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 V 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 V 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 V 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 V 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 V 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 V 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 V 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 V 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 V 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 V 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 V 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 V 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 V 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 V 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 V 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 4 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 4 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 4 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 4 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 4 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 4 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 4 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 4 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 4 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 4 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 4 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 W 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 W 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 W 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 W 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 W 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 W 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 W 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 W 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 W 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 W 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 W 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 W 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 W 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 W 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 W 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 W 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 W 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 W 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 W 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 W 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 W 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 W 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 W 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 W 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 W 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 W 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 W 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 W 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 W 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 W 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 W 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 W 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 W 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 W 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 W 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 W 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 W 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 5 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 5 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 5 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 5 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 5 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 5 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 5 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 5 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 5 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 5 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 5 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 X 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 X 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 X 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 X 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 X 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 X 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 X 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 X 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 X 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 X 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 X 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 X 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 X 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 X 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 X 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 X 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 X 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 X 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 X 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 X 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 X 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 X 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 X 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 X 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 X 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 X 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 X 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 X 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 X 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 X 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 X 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 X 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 X 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 X 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 X 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 X 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 X 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 6 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 6 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 6 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 6 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 6 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 6 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 6 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 6 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 6 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 6 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 6 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 Y 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 Y 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 Y 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 Y 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 Y 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 Y 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 Y 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 Y 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 Y 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 Y 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 Y 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 Y 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 Y 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 Y 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 Y 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 Y 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 Y 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 Y 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 Y 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 Y 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 Y 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 Y 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 Y 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 Y 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 Y 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 Y 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 Y 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 Y 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 Y 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 Y 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 Y 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 Y 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 Y 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 Y 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 Y 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 Y 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 Y 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 7 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 7 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 7 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 7 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 7 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 7 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 7 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 7 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 7 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 7 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 7 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
SEQRES 1 Z 475 MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE
SEQRES 2 Z 475 LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR
SEQRES 3 Z 475 PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA
SEQRES 4 Z 475 PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU
SEQRES 5 Z 475 CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR
SEQRES 6 Z 475 TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP
SEQRES 7 Z 475 ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO
SEQRES 8 Z 475 GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP
SEQRES 9 Z 475 ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE
SEQRES 10 Z 475 THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU
SEQRES 11 Z 475 ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA
SEQRES 12 Z 475 TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN
SEQRES 13 Z 475 VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU
SEQRES 14 Z 475 LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA
SEQRES 15 Z 475 LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY
SEQRES 16 Z 475 GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER
SEQRES 17 Z 475 GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL
SEQRES 18 Z 475 ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU
SEQRES 19 Z 475 VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS
SEQRES 20 Z 475 GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU
SEQRES 21 Z 475 GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY
SEQRES 22 Z 475 PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP
SEQRES 23 Z 475 ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA
SEQRES 24 Z 475 VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG
SEQRES 25 Z 475 VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS
SEQRES 26 Z 475 LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU
SEQRES 27 Z 475 ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP
SEQRES 28 Z 475 ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE
SEQRES 29 Z 475 THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL
SEQRES 30 Z 475 ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU
SEQRES 31 Z 475 VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY
SEQRES 32 Z 475 GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY
SEQRES 33 Z 475 ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN
SEQRES 34 Z 475 ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY
SEQRES 35 Z 475 ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU
SEQRES 36 Z 475 ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU
SEQRES 37 Z 475 PHE ASP THR ILE ASP LYS LEU
SEQRES 1 8 140 MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU
SEQRES 2 8 140 THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE
SEQRES 3 8 140 ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE
SEQRES 4 8 140 PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL
SEQRES 5 8 140 SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS
SEQRES 6 8 140 LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU
SEQRES 7 8 140 PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG
SEQRES 8 8 140 GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR
SEQRES 9 8 140 VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN
SEQRES 10 8 140 ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG
SEQRES 11 8 140 ASP TRP GLN PRO ALA ASN LYS ARG SER VAL
MODRES 1IR2 HYP A 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP A 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX A 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC A 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC A 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME I 1 MET N-METHYL METHIONINE
MODRES 1IR2 HYP B 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP B 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX B 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC B 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC B 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME J 1 MET N-METHYL METHIONINE
MODRES 1IR2 HYP C 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP C 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX C 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC C 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC C 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME K 1 MET N-METHYL METHIONINE
MODRES 1IR2 HYP D 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP D 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX D 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC D 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC D 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME L 1 MET N-METHYL METHIONINE
MODRES 1IR2 HYP E 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP E 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX E 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC E 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC E 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME M 1 MET N-METHYL METHIONINE
MODRES 1IR2 HYP F 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP F 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX F 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC F 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC F 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME N 1 MET N-METHYL METHIONINE
MODRES 1IR2 HYP G 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP G 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX G 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC G 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC G 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME O 1 MET N-METHYL METHIONINE
MODRES 1IR2 HYP H 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP H 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX H 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC H 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC H 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME P 1 MET N-METHYL METHIONINE
MODRES 1IR2 HYP S 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP S 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX S 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC S 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC S 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME 1 1 MET N-METHYL METHIONINE
MODRES 1IR2 HYP T 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP T 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX T 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC T 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC T 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME 2 1 MET N-METHYL METHIONINE
MODRES 1IR2 HYP U 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP U 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX U 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC U 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC U 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME 3 1 MET N-METHYL METHIONINE
MODRES 1IR2 HYP V 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP V 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX V 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC V 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC V 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME 4 1 MET N-METHYL METHIONINE
MODRES 1IR2 HYP W 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP W 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX W 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC W 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC W 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME 5 1 MET N-METHYL METHIONINE
MODRES 1IR2 HYP X 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP X 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX X 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC X 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC X 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME 6 1 MET N-METHYL METHIONINE
MODRES 1IR2 HYP Y 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP Y 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX Y 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC Y 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC Y 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME 7 1 MET N-METHYL METHIONINE
MODRES 1IR2 HYP Z 104 PRO 4-HYDROXYPROLINE
MODRES 1IR2 HYP Z 151 PRO 4-HYDROXYPROLINE
MODRES 1IR2 KCX Z 201 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 1IR2 SMC Z 256 CYS S-METHYLCYSTEINE
MODRES 1IR2 SMC Z 369 CYS S-METHYLCYSTEINE
MODRES 1IR2 MME 8 1 MET N-METHYL METHIONINE
HET HYP A 104 8
HET HYP A 151 8
HET KCX A 201 12
HET SMC A 256 7
HET SMC A 369 7
HET MME I 1 9
HET HYP B 104 8
HET HYP B 151 8
HET KCX B 201 12
HET SMC B 256 7
HET SMC B 369 7
HET MME J 1 9
HET HYP C 104 8
HET HYP C 151 8
HET KCX C 201 12
HET SMC C 256 7
HET SMC C 369 7
HET MME K 1 9
HET HYP D 104 8
HET HYP D 151 8
HET KCX D 201 12
HET SMC D 256 7
HET SMC D 369 7
HET MME L 1 9
HET HYP E 104 8
HET HYP E 151 8
HET KCX E 201 12
HET SMC E 256 7
HET SMC E 369 7
HET MME M 1 9
HET HYP F 104 8
HET HYP F 151 8
HET KCX F 201 12
HET SMC F 256 7
HET SMC F 369 7
HET MME N 1 9
HET HYP G 104 8
HET HYP G 151 8
HET KCX G 201 12
HET SMC G 256 7
HET SMC G 369 7
HET MME O 1 9
HET HYP H 104 8
HET HYP H 151 8
HET KCX H 201 12
HET SMC H 256 7
HET SMC H 369 7
HET MME P 1 9
HET HYP S 104 8
HET HYP S 151 8
HET KCX S 201 12
HET SMC S 256 7
HET SMC S 369 7
HET MME 1 1 9
HET HYP T 104 8
HET HYP T 151 8
HET KCX T 201 12
HET SMC T 256 7
HET SMC T 369 7
HET MME 2 1 9
HET HYP U 104 8
HET HYP U 151 8
HET KCX U 201 12
HET SMC U 256 7
HET SMC U 369 7
HET MME 3 1 9
HET HYP V 104 8
HET HYP V 151 8
HET KCX V 201 12
HET SMC V 256 7
HET SMC V 369 7
HET MME 4 1 9
HET HYP W 104 8
HET HYP W 151 8
HET KCX W 201 12
HET SMC W 256 7
HET SMC W 369 7
HET MME 5 1 9
HET HYP X 104 8
HET HYP X 151 8
HET KCX X 201 12
HET SMC X 256 7
HET SMC X 369 7
HET MME 6 1 9
HET HYP Y 104 8
HET HYP Y 151 8
HET KCX Y 201 12
HET SMC Y 256 7
HET SMC Y 369 7
HET MME 7 1 9
HET HYP Z 104 8
HET HYP Z 151 8
HET KCX Z 201 12
HET SMC Z 256 7
HET SMC Z 369 7
HET MME 8 1 9
HET MG A 476 1
HET CAP A 501 21
HET GOL A 605 6
HET GOL A 613 6
HET MG B 476 1
HET CAP B 501 21
HET GOL B 606 6
HET GOL B 610 6
HET GOL B 614 6
HET MG C 476 1
HET CAP C 501 21
HET GOL C 607 6
HET GOL C 615 6
HET MG D 476 1
HET CAP D 501 21
HET GOL D 608 6
HET GOL D 616 6
HET MG E 476 1
HET CAP E 501 21
HET GOL E 601 6
HET GOL E 609 6
HET GOL E 620 6
HET MG F 476 1
HET CAP F 501 21
HET GOL F 602 6
HET GOL F 617 6
HET MG G 476 1
HET CAP G 501 21
HET GOL G 603 6
HET GOL G 611 6
HET GOL G 618 6
HET MG H 476 1
HET CAP H 501 21
HET GOL H 604 6
HET GOL H 612 6
HET GOL H 619 6
HET MG S 476 1
HET CAP S 501 21
HET GOL S 605 6
HET GOL S 609 6
HET GOL S 613 6
HET MG T 476 1
HET CAP T 501 21
HET GOL T 606 6
HET GOL T 614 6
HET MG U 476 1
HET CAP U 501 21
HET GOL U 607 6
HET GOL U 615 6
HET MG V 476 1
HET CAP V 501 21
HET GOL V 608 6
HET GOL V 616 6
HET MG W 476 1
HET CAP W 501 21
HET GOL W 601 6
HET GOL W 620 6
HET MG X 476 1
HET CAP X 501 21
HET GOL X 602 6
HET GOL X 610 6
HET GOL X 617 6
HET MG Y 476 1
HET CAP Y 501 21
HET GOL Y 603 6
HET GOL Y 611 6
HET GOL Y 618 6
HET MG Z 476 1
HET CAP Z 501 21
HET GOL Z 604 6
HET GOL Z 612 6
HET GOL Z 619 6
HETNAM HYP 4-HYDROXYPROLINE
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM SMC S-METHYLCYSTEINE
HETNAM MME N-METHYL METHIONINE
HETNAM MG MAGNESIUM ION
HETNAM CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
HETNAM GOL GLYCEROL
HETSYN HYP HYDROXYPROLINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 HYP 32(C5 H9 N O3)
FORMUL 1 KCX 16(C7 H14 N2 O4)
FORMUL 1 SMC 32(C4 H9 N O2 S)
FORMUL 2 MME 16(C6 H13 N O2 S)
FORMUL 33 MG 16(MG 2+)
FORMUL 34 CAP 16(C6 H14 O13 P2)
FORMUL 35 GOL 40(C3 H8 O3)
FORMUL 05 HOH *9999(H2 O)
HELIX 1 1 TYR A 20 TYR A 25 1 6
HELIX 2 2 PRO A 49 GLU A 60 1 12
HELIX 3 3 VAL A 69 THR A 75 5 7
HELIX 4 4 SER A 76 LYS A 81 1 6
HELIX 5 5 HYP A 104 PHE A 108 5 5
HELIX 6 6 SER A 112 GLY A 122 1 11
HELIX 7 7 ASN A 123 PHE A 127 5 5
HELIX 8 8 PRO A 141 LYS A 146 1 6
HELIX 9 9 GLY A 154 ASN A 163 1 10
HELIX 10 10 SER A 181 GLY A 195 1 15
HELIX 11 11 ARG A 213 GLY A 233 1 21
HELIX 12 12 THR A 246 GLY A 261 1 16
HELIX 13 13 TYR A 269 GLY A 273 1 5
HELIX 14 14 GLY A 273 GLY A 288 1 16
HELIX 15 15 MET A 297 ARG A 303 1 7
HELIX 16 16 HIS A 310 GLY A 322 1 13
HELIX 17 17 GLU A 338 ASP A 351 1 14
HELIX 18 18 ASP A 357 GLY A 361 5 5
HELIX 19 19 HIS A 383 TRP A 385 5 3
HELIX 20 20 HIS A 386 GLY A 395 1 10
HELIX 21 21 GLY A 403 GLY A 408 1 6
HELIX 22 22 GLY A 412 GLU A 433 1 22
HELIX 23 23 ASP A 436 LYS A 450 1 15
HELIX 24 24 SER A 452 LYS A 463 1 12
HELIX 25 25 SER I 22 ASN I 36 1 15
HELIX 26 26 GLU I 46 ALA I 50 5 5
HELIX 27 27 ASN I 54 PHE I 60 5 7
HELIX 28 28 ASP I 85 PHE I 100 1 16
HELIX 29 29 PRO I 134 ARG I 138 5 5
HELIX 30 30 TYR B 20 TYR B 25 1 6
HELIX 31 31 PRO B 49 GLU B 60 1 12
HELIX 32 32 VAL B 69 THR B 75 5 7
HELIX 33 33 SER B 76 LYS B 81 1 6
HELIX 34 34 HYP B 104 PHE B 108 5 5
HELIX 35 35 SER B 112 VAL B 121 1 10
HELIX 36 36 ASN B 123 PHE B 127 5 5
HELIX 37 37 PRO B 141 LYS B 146 1 6
HELIX 38 38 GLY B 154 ASN B 163 1 10
HELIX 39 39 SER B 181 GLY B 195 1 15
HELIX 40 40 ARG B 213 GLY B 233 1 21
HELIX 41 41 THR B 246 GLY B 261 1 16
HELIX 42 42 TYR B 269 GLY B 273 1 5
HELIX 43 43 GLY B 273 GLY B 288 1 16
HELIX 44 44 MET B 297 ARG B 303 1 7
HELIX 45 45 HIS B 310 GLY B 322 1 13
HELIX 46 46 GLU B 338 ASP B 351 1 14
HELIX 47 47 ASP B 357 GLY B 361 5 5
HELIX 48 48 HIS B 383 TRP B 385 5 3
HELIX 49 49 HIS B 386 GLY B 395 1 10
HELIX 50 50 GLY B 403 GLY B 408 1 6
HELIX 51 51 GLY B 412 GLU B 433 1 22
HELIX 52 52 ASP B 436 LYS B 450 1 15
HELIX 53 53 SER B 452 LYS B 463 1 12
HELIX 54 54 SER J 22 ASN J 36 1 15
HELIX 55 55 GLU J 46 ALA J 50 5 5
HELIX 56 56 ASN J 54 PHE J 60 5 7
HELIX 57 57 ASP J 85 PHE J 100 1 16
HELIX 58 58 PRO J 134 LYS J 137 5 4
HELIX 59 59 TYR C 20 TYR C 25 1 6
HELIX 60 60 PRO C 49 SER C 61 1 13
HELIX 61 61 VAL C 69 THR C 75 5 7
HELIX 62 62 SER C 76 LYS C 81 1 6
HELIX 63 63 HYP C 104 PHE C 108 5 5
HELIX 64 64 SER C 112 GLY C 122 1 11
HELIX 65 65 ASN C 123 PHE C 127 5 5
HELIX 66 66 PRO C 141 LYS C 146 1 6
HELIX 67 67 GLY C 154 ASN C 163 1 10
HELIX 68 68 SER C 181 GLY C 195 1 15
HELIX 69 69 ARG C 213 GLY C 233 1 21
HELIX 70 70 THR C 246 GLY C 261 1 16
HELIX 71 71 TYR C 269 GLY C 273 1 5
HELIX 72 72 GLY C 273 GLY C 288 1 16
HELIX 73 73 MET C 297 ARG C 303 1 7
HELIX 74 74 HIS C 310 GLY C 322 1 13
HELIX 75 75 GLU C 338 ASP C 351 1 14
HELIX 76 76 ASP C 357 GLY C 361 5 5
HELIX 77 77 HIS C 383 TRP C 385 5 3
HELIX 78 78 HIS C 386 GLY C 395 1 10
HELIX 79 79 GLY C 403 GLY C 408 1 6
HELIX 80 80 GLY C 412 GLU C 433 1 22
HELIX 81 81 ASP C 436 LYS C 450 1 15
HELIX 82 82 SER C 452 LYS C 463 1 12
HELIX 83 83 SER K 22 ASN K 36 1 15
HELIX 84 84 GLU K 46 ALA K 50 5 5
HELIX 85 85 ASN K 54 PHE K 60 5 7
HELIX 86 86 ASP K 85 PHE K 100 1 16
HELIX 87 87 PRO K 134 LYS K 137 5 4
HELIX 88 88 TYR D 20 TYR D 25 1 6
HELIX 89 89 PRO D 49 SER D 61 1 13
HELIX 90 90 VAL D 69 THR D 75 5 7
HELIX 91 91 SER D 76 LYS D 81 1 6
HELIX 92 92 HYP D 104 PHE D 108 5 5
HELIX 93 93 SER D 112 VAL D 121 1 10
HELIX 94 94 ASN D 123 PHE D 127 5 5
HELIX 95 95 PRO D 141 LYS D 146 1 6
HELIX 96 96 GLY D 154 ASN D 163 1 10
HELIX 97 97 SER D 181 GLY D 195 1 15
HELIX 98 98 ARG D 213 GLY D 233 1 21
HELIX 99 99 THR D 246 GLY D 261 1 16
HELIX 100 100 TYR D 269 GLY D 273 1 5
HELIX 101 101 GLY D 273 GLY D 288 1 16
HELIX 102 102 MET D 297 ARG D 303 1 7
HELIX 103 103 HIS D 310 GLY D 322 1 13
HELIX 104 104 GLU D 338 ASP D 351 1 14
HELIX 105 105 ASP D 357 GLY D 361 5 5
HELIX 106 106 HIS D 383 TRP D 385 5 3
HELIX 107 107 HIS D 386 GLY D 395 1 10
HELIX 108 108 GLY D 403 GLY D 408 1 6
HELIX 109 109 GLY D 412 GLU D 433 1 22
HELIX 110 110 ASP D 436 LYS D 450 1 15
HELIX 111 111 SER D 452 LYS D 463 1 12
HELIX 112 112 SER L 22 ASN L 36 1 15
HELIX 113 113 GLU L 46 ALA L 50 5 5
HELIX 114 114 ASN L 54 PHE L 60 5 7
HELIX 115 115 ASP L 85 PHE L 100 1 16
HELIX 116 116 PRO L 134 LYS L 137 5 4
HELIX 117 117 TYR E 20 TYR E 25 1 6
HELIX 118 118 PRO E 49 SER E 61 1 13
HELIX 119 119 VAL E 69 THR E 75 5 7
HELIX 120 120 SER E 76 LYS E 81 1 6
HELIX 121 121 HYP E 104 PHE E 108 5 5
HELIX 122 122 SER E 112 VAL E 121 1 10
HELIX 123 123 ASN E 123 PHE E 127 5 5
HELIX 124 124 PRO E 141 LYS E 146 1 6
HELIX 125 125 GLY E 154 ASN E 163 1 10
HELIX 126 126 SER E 181 GLY E 195 1 15
HELIX 127 127 ARG E 213 GLY E 233 1 21
HELIX 128 128 THR E 246 GLY E 261 1 16
HELIX 129 129 TYR E 269 GLY E 273 1 5
HELIX 130 130 GLY E 273 GLY E 288 1 16
HELIX 131 131 MET E 297 ARG E 303 1 7
HELIX 132 132 HIS E 310 GLY E 322 1 13
HELIX 133 133 GLU E 338 ASP E 351 1 14
HELIX 134 134 ASP E 357 GLY E 361 5 5
HELIX 135 135 HIS E 383 TRP E 385 5 3
HELIX 136 136 HIS E 386 GLY E 395 1 10
HELIX 137 137 GLY E 403 GLY E 408 1 6
HELIX 138 138 GLY E 412 GLU E 433 1 22
HELIX 139 139 ASP E 436 SER E 452 1 17
HELIX 140 140 SER E 452 LYS E 463 1 12
HELIX 141 141 SER M 22 ASN M 36 1 15
HELIX 142 142 GLU M 46 ALA M 50 5 5
HELIX 143 143 ASN M 54 PHE M 60 5 7
HELIX 144 144 ASP M 85 PHE M 100 1 16
HELIX 145 145 PRO M 134 LYS M 137 5 4
HELIX 146 146 TYR F 20 TYR F 25 1 6
HELIX 147 147 PRO F 49 GLU F 60 1 12
HELIX 148 148 VAL F 69 THR F 75 5 7
HELIX 149 149 SER F 76 LYS F 81 1 6
HELIX 150 150 HYP F 104 PHE F 108 5 5
HELIX 151 151 SER F 112 VAL F 121 1 10
HELIX 152 152 ASN F 123 PHE F 127 5 5
HELIX 153 153 PRO F 141 LYS F 146 1 6
HELIX 154 154 GLY F 154 ASN F 163 1 10
HELIX 155 155 SER F 181 GLY F 195 1 15
HELIX 156 156 ARG F 213 GLY F 233 1 21
HELIX 157 157 THR F 246 GLY F 261 1 16
HELIX 158 158 TYR F 269 GLY F 273 1 5
HELIX 159 159 GLY F 273 GLY F 288 1 16
HELIX 160 160 MET F 297 ARG F 303 1 7
HELIX 161 161 HIS F 310 GLY F 322 1 13
HELIX 162 162 GLU F 338 ASP F 351 1 14
HELIX 163 163 ASP F 357 GLY F 361 5 5
HELIX 164 164 HIS F 383 TRP F 385 5 3
HELIX 165 165 HIS F 386 GLY F 395 1 10
HELIX 166 166 GLY F 403 GLY F 408 1 6
HELIX 167 167 GLY F 412 GLU F 433 1 22
HELIX 168 168 ASP F 436 LYS F 450 1 15
HELIX 169 169 SER F 452 LYS F 463 1 12
HELIX 170 170 SER N 22 ASN N 36 1 15
HELIX 171 171 GLU N 46 ALA N 50 5 5
HELIX 172 172 ASN N 54 PHE N 60 5 7
HELIX 173 173 ASP N 85 PHE N 100 1 16
HELIX 174 174 PRO N 134 LYS N 137 5 4
HELIX 175 175 TYR G 20 TYR G 25 1 6
HELIX 176 176 PRO G 49 GLU G 60 1 12
HELIX 177 177 VAL G 69 THR G 75 5 7
HELIX 178 178 SER G 76 LYS G 81 1 6
HELIX 179 179 HYP G 104 PHE G 108 5 5
HELIX 180 180 SER G 112 GLY G 122 1 11
HELIX 181 181 ASN G 123 PHE G 127 5 5
HELIX 182 182 PRO G 141 LYS G 146 1 6
HELIX 183 183 GLY G 154 ASN G 163 1 10
HELIX 184 184 SER G 181 ARG G 194 1 14
HELIX 185 185 ARG G 213 GLY G 233 1 21
HELIX 186 186 THR G 246 GLY G 261 1 16
HELIX 187 187 TYR G 269 GLY G 273 1 5
HELIX 188 188 GLY G 273 GLY G 288 1 16
HELIX 189 189 MET G 297 ARG G 303 1 7
HELIX 190 190 HIS G 310 GLY G 322 1 13
HELIX 191 191 GLU G 338 ASP G 351 1 14
HELIX 192 192 ASP G 357 GLY G 361 5 5
HELIX 193 193 HIS G 383 TRP G 385 5 3
HELIX 194 194 HIS G 386 GLY G 395 1 10
HELIX 195 195 GLY G 403 GLY G 408 1 6
HELIX 196 196 GLY G 412 GLU G 433 1 22
HELIX 197 197 ASP G 436 LYS G 450 1 15
HELIX 198 198 SER G 452 LYS G 463 1 12
HELIX 199 199 SER O 22 ASN O 36 1 15
HELIX 200 200 GLU O 46 ALA O 50 5 5
HELIX 201 201 ASN O 54 PHE O 60 5 7
HELIX 202 202 ASP O 85 PHE O 100 1 16
HELIX 203 203 PRO O 134 LYS O 137 5 4
HELIX 204 204 TYR H 20 TYR H 25 1 6
HELIX 205 205 PRO H 49 GLU H 60 1 12
HELIX 206 206 VAL H 69 THR H 75 5 7
HELIX 207 207 SER H 76 LYS H 81 1 6
HELIX 208 208 HYP H 104 PHE H 108 5 5
HELIX 209 209 SER H 112 VAL H 121 1 10
HELIX 210 210 ASN H 123 PHE H 127 5 5
HELIX 211 211 PRO H 141 LYS H 146 1 6
HELIX 212 212 GLY H 154 ASN H 163 1 10
HELIX 213 213 SER H 181 GLY H 195 1 15
HELIX 214 214 ARG H 213 GLY H 233 1 21
HELIX 215 215 THR H 246 GLY H 261 1 16
HELIX 216 216 TYR H 269 GLY H 273 1 5
HELIX 217 217 GLY H 273 GLY H 288 1 16
HELIX 218 218 MET H 297 ARG H 303 1 7
HELIX 219 219 HIS H 310 GLY H 322 1 13
HELIX 220 220 GLU H 338 ASP H 351 1 14
HELIX 221 221 ASP H 357 GLY H 361 5 5
HELIX 222 222 HIS H 383 TRP H 385 5 3
HELIX 223 223 HIS H 386 GLY H 395 1 10
HELIX 224 224 GLY H 403 GLY H 408 1 6
HELIX 225 225 GLY H 412 GLU H 433 1 22
HELIX 226 226 ASP H 436 LYS H 450 1 15
HELIX 227 227 SER H 452 LYS H 463 1 12
HELIX 228 228 SER P 22 ASN P 36 1 15
HELIX 229 229 GLU P 46 ALA P 50 5 5
HELIX 230 230 ASN P 54 PHE P 60 5 7
HELIX 231 231 ASP P 85 PHE P 100 1 16
HELIX 232 232 PRO P 134 ARG P 138 5 5
HELIX 233 233 TYR S 20 TYR S 25 1 6
HELIX 234 234 PRO S 49 GLU S 60 1 12
HELIX 235 235 VAL S 69 THR S 75 5 7
HELIX 236 236 SER S 76 LYS S 81 1 6
HELIX 237 237 HYP S 104 PHE S 108 5 5
HELIX 238 238 SER S 112 GLY S 122 1 11
HELIX 239 239 ASN S 123 PHE S 127 5 5
HELIX 240 240 PRO S 141 LYS S 146 1 6
HELIX 241 241 GLY S 154 ASN S 163 1 10
HELIX 242 242 SER S 181 ARG S 194 1 14
HELIX 243 243 ARG S 213 GLY S 233 1 21
HELIX 244 244 THR S 246 GLY S 261 1 16
HELIX 245 245 TYR S 269 GLY S 273 1 5
HELIX 246 246 GLY S 273 GLY S 288 1 16
HELIX 247 247 MET S 297 ARG S 303 1 7
HELIX 248 248 HIS S 310 GLY S 322 1 13
HELIX 249 249 GLU S 338 ASP S 351 1 14
HELIX 250 250 ASP S 357 GLY S 361 5 5
HELIX 251 251 HIS S 383 TRP S 385 5 3
HELIX 252 252 HIS S 386 GLY S 395 1 10
HELIX 253 253 GLY S 403 GLY S 408 1 6
HELIX 254 254 GLY S 412 GLU S 433 1 22
HELIX 255 255 ASP S 436 LYS S 450 1 15
HELIX 256 256 SER S 452 LYS S 463 1 12
HELIX 257 257 SER 1 22 ASN 1 36 1 15
HELIX 258 258 GLU 1 46 ALA 1 50 5 5
HELIX 259 259 ASN 1 54 PHE 1 60 5 7
HELIX 260 260 ASP 1 85 PHE 1 100 1 16
HELIX 261 261 PRO 1 134 LYS 1 137 5 4
HELIX 262 262 TYR T 20 TYR T 25 1 6
HELIX 263 263 PRO T 49 SER T 61 1 13
HELIX 264 264 VAL T 69 THR T 75 5 7
HELIX 265 265 SER T 76 LYS T 81 1 6
HELIX 266 266 HYP T 104 PHE T 108 5 5
HELIX 267 267 SER T 112 VAL T 121 1 10
HELIX 268 268 ASN T 123 PHE T 127 5 5
HELIX 269 269 PRO T 141 LYS T 146 1 6
HELIX 270 270 GLY T 154 ASN T 163 1 10
HELIX 271 271 SER T 181 GLY T 195 1 15
HELIX 272 272 ARG T 213 GLY T 233 1 21
HELIX 273 273 THR T 246 GLY T 261 1 16
HELIX 274 274 TYR T 269 GLY T 273 1 5
HELIX 275 275 GLY T 273 GLY T 288 1 16
HELIX 276 276 MET T 297 ARG T 303 1 7
HELIX 277 277 HIS T 310 GLY T 322 1 13
HELIX 278 278 GLU T 338 ASP T 351 1 14
HELIX 279 279 ASP T 357 GLY T 361 5 5
HELIX 280 280 HIS T 383 TRP T 385 5 3
HELIX 281 281 HIS T 386 GLY T 395 1 10
HELIX 282 282 GLY T 403 GLY T 408 1 6
HELIX 283 283 GLY T 412 GLU T 433 1 22
HELIX 284 284 ASP T 436 LYS T 450 1 15
HELIX 285 285 SER T 452 LYS T 463 1 12
HELIX 286 286 SER 2 22 ASN 2 36 1 15
HELIX 287 287 GLU 2 46 ALA 2 50 5 5
HELIX 288 288 ASN 2 54 PHE 2 60 5 7
HELIX 289 289 ASP 2 85 PHE 2 100 1 16
HELIX 290 290 PRO 2 134 LYS 2 137 5 4
HELIX 291 291 TYR U 20 TYR U 25 1 6
HELIX 292 292 PRO U 49 GLU U 60 1 12
HELIX 293 293 VAL U 69 THR U 75 5 7
HELIX 294 294 SER U 76 LYS U 81 1 6
HELIX 295 295 HYP U 104 PHE U 108 5 5
HELIX 296 296 SER U 112 VAL U 121 1 10
HELIX 297 297 ASN U 123 PHE U 127 5 5
HELIX 298 298 PRO U 141 LYS U 146 1 6
HELIX 299 299 GLY U 154 ASN U 163 1 10
HELIX 300 300 SER U 181 GLY U 195 1 15
HELIX 301 301 ARG U 213 GLY U 233 1 21
HELIX 302 302 THR U 246 GLY U 261 1 16
HELIX 303 303 TYR U 269 GLY U 273 1 5
HELIX 304 304 GLY U 273 GLY U 288 1 16
HELIX 305 305 MET U 297 ARG U 303 1 7
HELIX 306 306 HIS U 310 GLY U 322 1 13
HELIX 307 307 GLU U 338 ASP U 351 1 14
HELIX 308 308 ASP U 357 GLY U 361 5 5
HELIX 309 309 HIS U 383 TRP U 385 5 3
HELIX 310 310 HIS U 386 GLY U 395 1 10
HELIX 311 311 GLY U 403 GLY U 408 1 6
HELIX 312 312 GLY U 412 GLU U 433 1 22
HELIX 313 313 ASP U 436 LYS U 450 1 15
HELIX 314 314 SER U 452 LYS U 463 1 12
HELIX 315 315 SER 3 22 ASN 3 36 1 15
HELIX 316 316 GLU 3 46 ALA 3 50 5 5
HELIX 317 317 ASN 3 54 PHE 3 60 5 7
HELIX 318 318 ASP 3 85 PHE 3 100 1 16
HELIX 319 319 PRO 3 134 LYS 3 137 5 4
HELIX 320 320 TYR V 20 TYR V 25 1 6
HELIX 321 321 PRO V 49 GLU V 60 1 12
HELIX 322 322 VAL V 69 THR V 75 5 7
HELIX 323 323 SER V 76 LYS V 81 1 6
HELIX 324 324 HYP V 104 PHE V 108 5 5
HELIX 325 325 SER V 112 VAL V 121 1 10
HELIX 326 326 ASN V 123 PHE V 127 5 5
HELIX 327 327 PRO V 141 LYS V 146 1 6
HELIX 328 328 GLY V 154 ASN V 163 1 10
HELIX 329 329 SER V 181 GLY V 195 1 15
HELIX 330 330 ARG V 213 GLY V 233 1 21
HELIX 331 331 THR V 246 GLY V 261 1 16
HELIX 332 332 TYR V 269 GLY V 273 1 5
HELIX 333 333 GLY V 273 GLY V 288 1 16
HELIX 334 334 MET V 297 ARG V 303 1 7
HELIX 335 335 HIS V 310 GLY V 322 1 13
HELIX 336 336 GLU V 338 ASP V 351 1 14
HELIX 337 337 ASP V 357 GLY V 361 5 5
HELIX 338 338 HIS V 383 TRP V 385 5 3
HELIX 339 339 HIS V 386 GLY V 395 1 10
HELIX 340 340 GLY V 403 GLY V 408 1 6
HELIX 341 341 GLY V 412 GLU V 433 1 22
HELIX 342 342 ASP V 436 SER V 452 1 17
HELIX 343 343 SER V 452 LYS V 463 1 12
HELIX 344 344 SER 4 22 ASN 4 36 1 15
HELIX 345 345 GLU 4 46 ALA 4 50 5 5
HELIX 346 346 ASN 4 54 PHE 4 60 5 7
HELIX 347 347 ASP 4 85 PHE 4 100 1 16
HELIX 348 348 PRO 4 134 ARG 4 138 5 5
HELIX 349 349 TYR W 20 TYR W 25 1 6
HELIX 350 350 PRO W 49 GLU W 60 1 12
HELIX 351 351 VAL W 69 THR W 75 5 7
HELIX 352 352 SER W 76 LYS W 81 1 6
HELIX 353 353 HYP W 104 PHE W 108 5 5
HELIX 354 354 SER W 112 VAL W 121 1 10
HELIX 355 355 ASN W 123 PHE W 127 5 5
HELIX 356 356 PRO W 141 LYS W 146 1 6
HELIX 357 357 GLY W 154 ASN W 163 1 10
HELIX 358 358 SER W 181 GLY W 195 1 15
HELIX 359 359 ARG W 213 GLY W 233 1 21
HELIX 360 360 THR W 246 GLY W 261 1 16
HELIX 361 361 TYR W 269 GLY W 273 1 5
HELIX 362 362 GLY W 273 GLY W 288 1 16
HELIX 363 363 MET W 297 ARG W 303 1 7
HELIX 364 364 HIS W 310 GLY W 322 1 13
HELIX 365 365 GLU W 338 ASP W 351 1 14
HELIX 366 366 ASP W 357 GLY W 361 5 5
HELIX 367 367 HIS W 383 TRP W 385 5 3
HELIX 368 368 HIS W 386 GLY W 395 1 10
HELIX 369 369 GLY W 403 GLY W 408 1 6
HELIX 370 370 GLY W 412 GLU W 433 1 22
HELIX 371 371 ASP W 436 LYS W 450 1 15
HELIX 372 372 SER W 452 LYS W 463 1 12
HELIX 373 373 SER 5 22 ASN 5 36 1 15
HELIX 374 374 GLU 5 46 ALA 5 50 5 5
HELIX 375 375 ASN 5 54 PHE 5 60 5 7
HELIX 376 376 ASP 5 85 PHE 5 100 1 16
HELIX 377 377 PRO 5 134 ARG 5 138 5 5
HELIX 378 378 TYR X 20 TYR X 25 1 6
HELIX 379 379 PRO X 49 GLU X 60 1 12
HELIX 380 380 VAL X 69 THR X 75 5 7
HELIX 381 381 SER X 76 LYS X 81 1 6
HELIX 382 382 HYP X 104 PHE X 108 5 5
HELIX 383 383 SER X 112 GLY X 122 1 11
HELIX 384 384 ASN X 123 PHE X 127 5 5
HELIX 385 385 PRO X 141 LYS X 146 1 6
HELIX 386 386 GLY X 154 ASN X 163 1 10
HELIX 387 387 SER X 181 GLY X 195 1 15
HELIX 388 388 ARG X 213 GLY X 233 1 21
HELIX 389 389 THR X 246 LEU X 260 1 15
HELIX 390 390 TYR X 269 GLY X 273 1 5
HELIX 391 391 GLY X 273 GLY X 288 1 16
HELIX 392 392 MET X 297 ARG X 303 1 7
HELIX 393 393 HIS X 310 GLY X 322 1 13
HELIX 394 394 GLU X 338 ASP X 351 1 14
HELIX 395 395 ASP X 357 GLY X 361 5 5
HELIX 396 396 HIS X 383 TRP X 385 5 3
HELIX 397 397 HIS X 386 GLY X 395 1 10
HELIX 398 398 GLY X 403 GLY X 408 1 6
HELIX 399 399 GLY X 412 GLU X 433 1 22
HELIX 400 400 ASP X 436 LYS X 450 1 15
HELIX 401 401 SER X 452 LYS X 463 1 12
HELIX 402 402 SER 6 22 ASN 6 36 1 15
HELIX 403 403 GLU 6 46 ALA 6 50 5 5
HELIX 404 404 ASN 6 54 PHE 6 60 5 7
HELIX 405 405 ASP 6 85 PHE 6 100 1 16
HELIX 406 406 PRO 6 134 LYS 6 137 5 4
HELIX 407 407 TYR Y 20 TYR Y 25 1 6
HELIX 408 408 PRO Y 49 SER Y 61 1 13
HELIX 409 409 VAL Y 69 THR Y 75 5 7
HELIX 410 410 SER Y 76 LYS Y 81 1 6
HELIX 411 411 HYP Y 104 PHE Y 108 5 5
HELIX 412 412 SER Y 112 VAL Y 121 1 10
HELIX 413 413 ASN Y 123 PHE Y 127 5 5
HELIX 414 414 PRO Y 141 LYS Y 146 1 6
HELIX 415 415 GLY Y 154 ASN Y 163 1 10
HELIX 416 416 SER Y 181 GLY Y 195 1 15
HELIX 417 417 ARG Y 213 GLY Y 233 1 21
HELIX 418 418 THR Y 246 GLY Y 261 1 16
HELIX 419 419 TYR Y 269 GLY Y 273 1 5
HELIX 420 420 GLY Y 273 GLY Y 288 1 16
HELIX 421 421 MET Y 297 ARG Y 303 1 7
HELIX 422 422 HIS Y 310 GLY Y 322 1 13
HELIX 423 423 GLU Y 338 ASP Y 351 1 14
HELIX 424 424 ASP Y 357 GLY Y 361 5 5
HELIX 425 425 HIS Y 383 TRP Y 385 5 3
HELIX 426 426 HIS Y 386 GLY Y 395 1 10
HELIX 427 427 GLY Y 403 GLY Y 408 1 6
HELIX 428 428 GLY Y 412 GLU Y 433 1 22
HELIX 429 429 ASP Y 436 LYS Y 450 1 15
HELIX 430 430 SER Y 452 LYS Y 463 1 12
HELIX 431 431 SER 7 22 ASN 7 36 1 15
HELIX 432 432 GLU 7 46 ALA 7 50 5 5
HELIX 433 433 ASN 7 54 PHE 7 60 5 7
HELIX 434 434 ASP 7 85 PHE 7 100 1 16
HELIX 435 435 PRO 7 134 LYS 7 137 5 4
HELIX 436 436 TYR Z 20 TYR Z 25 1 6
HELIX 437 437 PRO Z 49 SER Z 61 1 13
HELIX 438 438 VAL Z 69 THR Z 75 5 7
HELIX 439 439 SER Z 76 LYS Z 81 1 6
HELIX 440 440 HYP Z 104 PHE Z 108 5 5
HELIX 441 441 SER Z 112 VAL Z 121 1 10
HELIX 442 442 ASN Z 123 PHE Z 127 5 5
HELIX 443 443 PRO Z 141 LYS Z 146 1 6
HELIX 444 444 GLY Z 154 ASN Z 163 1 10
HELIX 445 445 SER Z 181 GLY Z 195 1 15
HELIX 446 446 ARG Z 213 GLY Z 233 1 21
HELIX 447 447 THR Z 246 GLY Z 261 1 16
HELIX 448 448 TYR Z 269 GLY Z 273 1 5
HELIX 449 449 GLY Z 273 GLY Z 288 1 16
HELIX 450 450 MET Z 297 ARG Z 303 1 7
HELIX 451 451 HIS Z 310 GLY Z 322 1 13
HELIX 452 452 GLU Z 338 ASP Z 351 1 14
HELIX 453 453 ASP Z 357 GLY Z 361 5 5
HELIX 454 454 HIS Z 383 TRP Z 385 5 3
HELIX 455 455 HIS Z 386 GLY Z 395 1 10
HELIX 456 456 GLY Z 403 GLY Z 408 1 6
HELIX 457 457 GLY Z 412 GLU Z 433 1 22
HELIX 458 458 ASP Z 436 SER Z 452 1 17
HELIX 459 459 SER Z 452 LYS Z 463 1 12
HELIX 460 460 SER 8 22 ASN 8 36 1 15
HELIX 461 461 GLU 8 46 ALA 8 50 5 5
HELIX 462 462 ASN 8 54 PHE 8 60 5 7
HELIX 463 463 ASP 8 85 PHE 8 100 1 16
HELIX 464 464 PRO 8 134 LYS 8 137 5 4
SHEET 1 A 5 ARG A 83 PRO A 89 0
SHEET 2 A 5 TYR A 97 TYR A 103 -1 O ILE A 98 N GLU A 88
SHEET 3 A 5 ILE A 36 PRO A 44 -1 N PHE A 40 O ALA A 99
SHEET 4 A 5 LEU A 130 ARG A 139 -1 O ARG A 134 N ARG A 41
SHEET 5 A 5 GLY A 308 ILE A 309 1 O GLY A 308 N LEU A 135
SHEET 1 B 8 LEU A 169 GLY A 171 0
SHEET 2 B 8 CYS A 399 GLN A 401 1 O LEU A 400 N LEU A 169
SHEET 3 B 8 MET A 375 SER A 379 1 N ALA A 378 O GLN A 401
SHEET 4 B 8 HIS A 325 HIS A 327 1 N LEU A 326 O MET A 375
SHEET 5 B 8 LEU A 290 HIS A 294 1 N ILE A 293 O HIS A 327
SHEET 6 B 8 ILE A 264 ASP A 268 1 N ILE A 265 O HIS A 292
SHEET 7 B 8 GLY A 237 ASN A 241 1 N LEU A 240 O MET A 266
SHEET 8 B 8 PHE A 199 KCX A 201 1 N THR A 200 O TYR A 239
SHEET 1 C 2 TYR A 353 VAL A 354 0
SHEET 2 C 2 GLN A 366 ASP A 367 -1 O GLN A 366 N VAL A 354
SHEET 1 D 4 THR I 74 MET I 75 0
SHEET 2 D 4 ILE I 39 ALA I 45 -1 N PHE I 44 O THR I 74
SHEET 3 D 4 TYR I 104 ASP I 111 -1 O VAL I 108 N CYS I 41
SHEET 4 D 4 VAL I 116 GLN I 124 -1 O VAL I 123 N VAL I 105
SHEET 1 E 5 ARG B 83 PRO B 89 0
SHEET 2 E 5 TYR B 97 TYR B 103 -1 O TYR B 100 N ASP B 86
SHEET 3 E 5 ILE B 36 PRO B 44 -1 N MET B 42 O TYR B 97
SHEET 4 E 5 LEU B 130 ARG B 139 -1 O ARG B 134 N ARG B 41
SHEET 5 E 5 GLY B 308 ILE B 309 1 O GLY B 308 N LEU B 135
SHEET 1 F 8 LEU B 169 GLY B 171 0
SHEET 2 F 8 CYS B 399 GLN B 401 1 O LEU B 400 N LEU B 169
SHEET 3 F 8 MET B 375 SER B 379 1 N ALA B 378 O GLN B 401
SHEET 4 F 8 HIS B 325 HIS B 327 1 N LEU B 326 O MET B 375
SHEET 5 F 8 LEU B 290 HIS B 294 1 N ILE B 293 O HIS B 327
SHEET 6 F 8 ILE B 264 ASP B 268 1 N ILE B 265 O HIS B 292
SHEET 7 F 8 GLY B 237 ASN B 241 1 N LEU B 240 O MET B 266
SHEET 8 F 8 PHE B 199 KCX B 201 1 N THR B 200 O TYR B 239
SHEET 1 G 2 TYR B 353 VAL B 354 0
SHEET 2 G 2 GLN B 366 ASP B 367 -1 O GLN B 366 N VAL B 354
SHEET 1 H 2 VAL J 3 TRP J 4 0
SHEET 2 H 2 SER J 139 VAL J 140 -1 O VAL J 140 N VAL J 3
SHEET 1 I 4 THR J 74 TRP J 76 0
SHEET 2 I 4 ILE J 39 ALA J 45 -1 N PHE J 44 O THR J 74
SHEET 3 I 4 TYR J 104 ASP J 111 -1 O TYR J 104 N ALA J 45
SHEET 4 I 4 VAL J 116 GLN J 124 -1 O VAL J 123 N VAL J 105
SHEET 1 J 5 ARG C 83 PRO C 89 0
SHEET 2 J 5 TYR C 97 TYR C 103 -1 O ILE C 98 N GLU C 88
SHEET 3 J 5 ILE C 36 PRO C 44 -1 N MET C 42 O TYR C 97
SHEET 4 J 5 LEU C 130 ARG C 139 -1 O ARG C 131 N THR C 43
SHEET 5 J 5 GLY C 308 ILE C 309 1 O GLY C 308 N LEU C 135
SHEET 1 K 8 LEU C 169 GLY C 171 0
SHEET 2 K 8 CYS C 399 GLN C 401 1 O LEU C 400 N LEU C 169
SHEET 3 K 8 MET C 375 SER C 379 1 N ALA C 378 O GLN C 401
SHEET 4 K 8 HIS C 325 HIS C 327 1 N LEU C 326 O MET C 375
SHEET 5 K 8 LEU C 290 HIS C 294 1 N ILE C 293 O HIS C 327
SHEET 6 K 8 ILE C 264 ASP C 268 1 N ILE C 265 O HIS C 292
SHEET 7 K 8 GLY C 237 ASN C 241 1 N LEU C 240 O MET C 266
SHEET 8 K 8 PHE C 199 KCX C 201 1 N THR C 200 O TYR C 239
SHEET 1 L 2 TYR C 353 VAL C 354 0
SHEET 2 L 2 GLN C 366 ASP C 367 -1 O GLN C 366 N VAL C 354
SHEET 1 M 2 VAL K 3 TRP K 4 0
SHEET 2 M 2 SER K 139 VAL K 140 -1 O VAL K 140 N VAL K 3
SHEET 1 N 4 THR K 74 TRP K 76 0
SHEET 2 N 4 ILE K 39 ALA K 45 -1 N PHE K 44 O THR K 74
SHEET 3 N 4 TYR K 104 ASP K 111 -1 O VAL K 108 N CYS K 41
SHEET 4 N 4 VAL K 116 GLN K 124 -1 O VAL K 123 N VAL K 105
SHEET 1 O 5 ARG D 83 PRO D 89 0
SHEET 2 O 5 TYR D 97 TYR D 103 -1 O TYR D 100 N ASP D 86
SHEET 3 O 5 ILE D 36 PRO D 44 -1 N MET D 42 O TYR D 97
SHEET 4 O 5 LEU D 130 ARG D 139 -1 O ARG D 134 N ARG D 41
SHEET 5 O 5 GLY D 308 ILE D 309 1 O GLY D 308 N LEU D 135
SHEET 1 P 8 LEU D 169 GLY D 171 0
SHEET 2 P 8 CYS D 399 GLN D 401 1 O LEU D 400 N LEU D 169
SHEET 3 P 8 MET D 375 SER D 379 1 N ALA D 378 O GLN D 401
SHEET 4 P 8 HIS D 325 HIS D 327 1 N LEU D 326 O MET D 375
SHEET 5 P 8 LEU D 290 HIS D 294 1 N ILE D 293 O HIS D 327
SHEET 6 P 8 ILE D 264 ASP D 268 1 N ILE D 265 O HIS D 292
SHEET 7 P 8 GLY D 237 ASN D 241 1 N LEU D 240 O MET D 266
SHEET 8 P 8 PHE D 199 KCX D 201 1 N THR D 200 O TYR D 239
SHEET 1 Q 2 TYR D 353 VAL D 354 0
SHEET 2 Q 2 GLN D 366 ASP D 367 -1 O GLN D 366 N VAL D 354
SHEET 1 R 2 VAL L 3 TRP L 4 0
SHEET 2 R 2 SER L 139 VAL L 140 -1 O VAL L 140 N VAL L 3
SHEET 1 S 4 THR L 74 TRP L 76 0
SHEET 2 S 4 ILE L 39 ALA L 45 -1 N PHE L 44 O THR L 74
SHEET 3 S 4 TYR L 104 ASP L 111 -1 O TYR L 104 N ALA L 45
SHEET 4 S 4 VAL L 116 GLN L 124 -1 O VAL L 123 N VAL L 105
SHEET 1 T 5 ARG E 83 PRO E 89 0
SHEET 2 T 5 TYR E 97 TYR E 103 -1 O ILE E 98 N GLU E 88
SHEET 3 T 5 ILE E 36 PRO E 44 -1 N MET E 42 O TYR E 97
SHEET 4 T 5 LEU E 130 ARG E 139 -1 O ARG E 134 N ARG E 41
SHEET 5 T 5 GLY E 308 ILE E 309 1 O GLY E 308 N LEU E 135
SHEET 1 U 8 LEU E 169 GLY E 171 0
SHEET 2 U 8 CYS E 399 GLN E 401 1 O LEU E 400 N LEU E 169
SHEET 3 U 8 MET E 375 SER E 379 1 N ALA E 378 O GLN E 401
SHEET 4 U 8 HIS E 325 HIS E 327 1 N LEU E 326 O MET E 375
SHEET 5 U 8 LEU E 290 HIS E 294 1 N ILE E 293 O HIS E 325
SHEET 6 U 8 ILE E 264 ASP E 268 1 N ILE E 265 O HIS E 292
SHEET 7 U 8 GLY E 237 ASN E 241 1 N LEU E 240 O MET E 266
SHEET 8 U 8 PHE E 199 KCX E 201 1 N THR E 200 O TYR E 239
SHEET 1 V 2 TYR E 353 VAL E 354 0
SHEET 2 V 2 GLN E 366 ASP E 367 -1 O GLN E 366 N VAL E 354
SHEET 1 W 2 VAL M 3 TRP M 4 0
SHEET 2 W 2 SER M 139 VAL M 140 -1 O VAL M 140 N VAL M 3
SHEET 1 X 4 THR M 74 TRP M 76 0
SHEET 2 X 4 ILE M 39 ALA M 45 -1 N PHE M 44 O THR M 74
SHEET 3 X 4 TYR M 104 ASP M 111 -1 O TYR M 104 N ALA M 45
SHEET 4 X 4 VAL M 116 GLN M 124 -1 O ILE M 118 N ALA M 109
SHEET 1 Y 5 ARG F 83 PRO F 89 0
SHEET 2 Y 5 TYR F 97 TYR F 103 -1 O ILE F 98 N GLU F 88
SHEET 3 Y 5 ILE F 36 PRO F 44 -1 N PHE F 40 O ALA F 99
SHEET 4 Y 5 LEU F 130 ARG F 139 -1 O ARG F 134 N ARG F 41
SHEET 5 Y 5 GLY F 308 ILE F 309 1 O GLY F 308 N LEU F 135
SHEET 1 Z 8 LEU F 169 GLY F 171 0
SHEET 2 Z 8 CYS F 399 GLN F 401 1 O LEU F 400 N LEU F 169
SHEET 3 Z 8 MET F 375 SER F 379 1 N ALA F 378 O GLN F 401
SHEET 4 Z 8 HIS F 325 HIS F 327 1 N LEU F 326 O VAL F 377
SHEET 5 Z 8 LEU F 290 HIS F 294 1 N ILE F 293 O HIS F 327
SHEET 6 Z 8 ILE F 264 ASP F 268 1 N ILE F 265 O HIS F 292
SHEET 7 Z 8 GLY F 237 ASN F 241 1 N LEU F 240 O MET F 266
SHEET 8 Z 8 PHE F 199 KCX F 201 1 N THR F 200 O TYR F 239
SHEET 1 AA 2 TYR F 353 VAL F 354 0
SHEET 2 AA 2 GLN F 366 ASP F 367 -1 O GLN F 366 N VAL F 354
SHEET 1 AB 2 VAL N 3 TRP N 4 0
SHEET 2 AB 2 SER N 139 VAL N 140 -1 O VAL N 140 N VAL N 3
SHEET 1 AC 4 THR N 74 TRP N 76 0
SHEET 2 AC 4 ILE N 39 ALA N 45 -1 N LEU N 42 O TRP N 76
SHEET 3 AC 4 TYR N 104 ASP N 111 -1 O TYR N 104 N ALA N 45
SHEET 4 AC 4 VAL N 116 GLN N 124 -1 O VAL N 123 N VAL N 105
SHEET 1 AD 5 ARG G 83 PRO G 89 0
SHEET 2 AD 5 TYR G 97 TYR G 103 -1 O ILE G 98 N GLU G 88
SHEET 3 AD 5 ILE G 36 PRO G 44 -1 N MET G 42 O TYR G 97
SHEET 4 AD 5 LEU G 130 ARG G 139 -1 O ARG G 134 N ARG G 41
SHEET 5 AD 5 GLY G 308 ILE G 309 1 O GLY G 308 N LEU G 135
SHEET 1 AE 8 LEU G 169 GLY G 171 0
SHEET 2 AE 8 CYS G 399 GLN G 401 1 O LEU G 400 N LEU G 169
SHEET 3 AE 8 MET G 375 SER G 379 1 N ALA G 378 O GLN G 401
SHEET 4 AE 8 HIS G 325 HIS G 327 1 N LEU G 326 O MET G 375
SHEET 5 AE 8 LEU G 290 HIS G 294 1 N ILE G 293 O HIS G 327
SHEET 6 AE 8 ILE G 264 ASP G 268 1 N ILE G 265 O HIS G 292
SHEET 7 AE 8 GLY G 237 ASN G 241 1 N LEU G 240 O MET G 266
SHEET 8 AE 8 PHE G 199 KCX G 201 1 N THR G 200 O TYR G 239
SHEET 1 AF 2 TYR G 353 VAL G 354 0
SHEET 2 AF 2 GLN G 366 ASP G 367 -1 O GLN G 366 N VAL G 354
SHEET 1 AG 2 VAL O 3 TRP O 4 0
SHEET 2 AG 2 SER O 139 VAL O 140 -1 O VAL O 140 N VAL O 3
SHEET 1 AH 4 THR O 74 TRP O 76 0
SHEET 2 AH 4 ILE O 39 ALA O 45 -1 N PHE O 44 O THR O 74
SHEET 3 AH 4 TYR O 104 ASP O 111 -1 O VAL O 108 N CYS O 41
SHEET 4 AH 4 VAL O 116 GLN O 124 -1 O VAL O 123 N VAL O 105
SHEET 1 AI 5 ARG H 83 PRO H 89 0
SHEET 2 AI 5 TYR H 97 TYR H 103 -1 O TYR H 100 N ASP H 86
SHEET 3 AI 5 ILE H 36 PRO H 44 -1 N MET H 42 O TYR H 97
SHEET 4 AI 5 LEU H 130 ARG H 139 -1 O ARG H 134 N ARG H 41
SHEET 5 AI 5 GLY H 308 ILE H 309 1 O GLY H 308 N LEU H 135
SHEET 1 AJ 8 LEU H 169 GLY H 171 0
SHEET 2 AJ 8 CYS H 399 GLN H 401 1 O LEU H 400 N LEU H 169
SHEET 3 AJ 8 MET H 375 SER H 379 1 N ALA H 378 O GLN H 401
SHEET 4 AJ 8 HIS H 325 HIS H 327 1 N LEU H 326 O MET H 375
SHEET 5 AJ 8 LEU H 290 HIS H 294 1 N ILE H 293 O HIS H 325
SHEET 6 AJ 8 ILE H 264 ASP H 268 1 N ILE H 265 O HIS H 292
SHEET 7 AJ 8 GLY H 237 ASN H 241 1 N LEU H 240 O MET H 266
SHEET 8 AJ 8 PHE H 199 KCX H 201 1 N THR H 200 O TYR H 239
SHEET 1 AK 2 TYR H 353 VAL H 354 0
SHEET 2 AK 2 GLN H 366 ASP H 367 -1 O GLN H 366 N VAL H 354
SHEET 1 AL 4 THR P 74 TRP P 76 0
SHEET 2 AL 4 ILE P 39 ALA P 45 -1 N PHE P 44 O THR P 74
SHEET 3 AL 4 TYR P 104 ASP P 111 -1 O TYR P 104 N ALA P 45
SHEET 4 AL 4 VAL P 116 GLN P 124 -1 O VAL P 123 N VAL P 105
SHEET 1 BA 5 ARG S 83 PRO S 89 0
SHEET 2 BA 5 TYR S 97 TYR S 103 -1 O TYR S 100 N ASP S 86
SHEET 3 BA 5 ILE S 36 PRO S 44 -1 N MET S 42 O TYR S 97
SHEET 4 BA 5 LEU S 130 ARG S 139 -1 O ARG S 134 N ARG S 41
SHEET 5 BA 5 GLY S 308 ILE S 309 1 O GLY S 308 N LEU S 135
SHEET 1 BB 8 LEU S 169 GLY S 171 0
SHEET 2 BB 8 CYS S 399 GLN S 401 1 O LEU S 400 N LEU S 169
SHEET 3 BB 8 MET S 375 SER S 379 1 N ALA S 378 O GLN S 401
SHEET 4 BB 8 HIS S 325 HIS S 327 1 N LEU S 326 O VAL S 377
SHEET 5 BB 8 LEU S 290 HIS S 294 1 N ILE S 293 O HIS S 325
SHEET 6 BB 8 ILE S 264 ASP S 268 1 N ILE S 265 O HIS S 292
SHEET 7 BB 8 GLY S 237 ASN S 241 1 N LEU S 240 O MET S 266
SHEET 8 BB 8 PHE S 199 KCX S 201 1 N THR S 200 O TYR S 239
SHEET 1 BC 2 TYR S 353 VAL S 354 0
SHEET 2 BC 2 GLN S 366 ASP S 367 -1 O GLN S 366 N VAL S 354
SHEET 1 BD 2 VAL 1 3 TRP 1 4 0
SHEET 2 BD 2 SER 1 139 VAL 1 140 -1 O VAL 1 140 N VAL 1 3
SHEET 1 BE 4 THR 1 74 TRP 1 76 0
SHEET 2 BE 4 ILE 1 39 ALA 1 45 -1 N PHE 1 44 O THR 1 74
SHEET 3 BE 4 TYR 1 104 ASP 1 111 -1 O TYR 1 104 N ALA 1 45
SHEET 4 BE 4 VAL 1 116 GLN 1 124 -1 O VAL 1 123 N VAL 1 105
SHEET 1 BF 5 ARG T 83 PRO T 89 0
SHEET 2 BF 5 TYR T 97 TYR T 103 -1 O ILE T 98 N GLU T 88
SHEET 3 BF 5 ILE T 36 PRO T 44 -1 N MET T 42 O TYR T 97
SHEET 4 BF 5 LEU T 130 ARG T 139 -1 O ARG T 134 N ARG T 41
SHEET 5 BF 5 GLY T 308 ILE T 309 1 O GLY T 308 N LEU T 135
SHEET 1 BG 8 LEU T 169 GLY T 171 0
SHEET 2 BG 8 CYS T 399 GLN T 401 1 O LEU T 400 N LEU T 169
SHEET 3 BG 8 MET T 375 SER T 379 1 N ALA T 378 O GLN T 401
SHEET 4 BG 8 HIS T 325 HIS T 327 1 N LEU T 326 O MET T 375
SHEET 5 BG 8 LEU T 290 HIS T 294 1 N ILE T 293 O HIS T 325
SHEET 6 BG 8 ILE T 264 ASP T 268 1 N ILE T 265 O HIS T 292
SHEET 7 BG 8 GLY T 237 ASN T 241 1 N LEU T 240 O MET T 266
SHEET 8 BG 8 PHE T 199 KCX T 201 1 N THR T 200 O TYR T 239
SHEET 1 BH 2 TYR T 353 VAL T 354 0
SHEET 2 BH 2 GLN T 366 ASP T 367 -1 O GLN T 366 N VAL T 354
SHEET 1 BI 2 VAL 2 3 TRP 2 4 0
SHEET 2 BI 2 SER 2 139 VAL 2 140 -1 O VAL 2 140 N VAL 2 3
SHEET 1 BJ 4 THR 2 74 MET 2 75 0
SHEET 2 BJ 4 ILE 2 39 ALA 2 45 -1 N PHE 2 44 O THR 2 74
SHEET 3 BJ 4 TYR 2 104 ASP 2 111 -1 O TYR 2 104 N ALA 2 45
SHEET 4 BJ 4 VAL 2 116 GLN 2 124 -1 O VAL 2 123 N VAL 2 105
SHEET 1 BK 5 ARG U 83 PRO U 89 0
SHEET 2 BK 5 TYR U 97 TYR U 103 -1 O TYR U 100 N ASP U 86
SHEET 3 BK 5 ILE U 36 PRO U 44 -1 N PHE U 40 O ALA U 99
SHEET 4 BK 5 LEU U 130 ARG U 139 -1 O ARG U 134 N ARG U 41
SHEET 5 BK 5 GLY U 308 ILE U 309 1 O GLY U 308 N LEU U 135
SHEET 1 BL 8 LEU U 169 GLY U 171 0
SHEET 2 BL 8 CYS U 399 GLN U 401 1 O LEU U 400 N LEU U 169
SHEET 3 BL 8 MET U 375 SER U 379 1 N ALA U 378 O GLN U 401
SHEET 4 BL 8 HIS U 325 HIS U 327 1 N LEU U 326 O MET U 375
SHEET 5 BL 8 LEU U 290 HIS U 294 1 N ILE U 293 O HIS U 327
SHEET 6 BL 8 ILE U 264 ASP U 268 1 N ILE U 265 O HIS U 292
SHEET 7 BL 8 GLY U 237 ASN U 241 1 N LEU U 240 O MET U 266
SHEET 8 BL 8 PHE U 199 KCX U 201 1 N THR U 200 O TYR U 239
SHEET 1 BM 2 TYR U 353 VAL U 354 0
SHEET 2 BM 2 GLN U 366 ASP U 367 -1 O GLN U 366 N VAL U 354
SHEET 1 BN 2 VAL 3 3 TRP 3 4 0
SHEET 2 BN 2 SER 3 139 VAL 3 140 -1 O VAL 3 140 N VAL 3 3
SHEET 1 BO 4 THR 3 74 TRP 3 76 0
SHEET 2 BO 4 ILE 3 39 ALA 3 45 -1 N PHE 3 44 O THR 3 74
SHEET 3 BO 4 TYR 3 104 ASP 3 111 -1 O TYR 3 104 N ALA 3 45
SHEET 4 BO 4 VAL 3 116 GLN 3 124 -1 O VAL 3 123 N VAL 3 105
SHEET 1 BP 5 ARG V 83 PRO V 89 0
SHEET 2 BP 5 TYR V 97 TYR V 103 -1 O TYR V 100 N ASP V 86
SHEET 3 BP 5 ILE V 36 PRO V 44 -1 N MET V 42 O TYR V 97
SHEET 4 BP 5 LEU V 130 ARG V 139 -1 O ARG V 134 N ARG V 41
SHEET 5 BP 5 GLY V 308 ILE V 309 1 O GLY V 308 N LEU V 135
SHEET 1 BQ 8 LEU V 169 GLY V 171 0
SHEET 2 BQ 8 CYS V 399 GLN V 401 1 O LEU V 400 N LEU V 169
SHEET 3 BQ 8 MET V 375 SER V 379 1 N ALA V 378 O GLN V 401
SHEET 4 BQ 8 HIS V 325 HIS V 327 1 N LEU V 326 O MET V 375
SHEET 5 BQ 8 LEU V 290 HIS V 294 1 N ILE V 293 O HIS V 327
SHEET 6 BQ 8 ILE V 264 ASP V 268 1 N ILE V 265 O HIS V 292
SHEET 7 BQ 8 GLY V 237 ASN V 241 1 N LEU V 240 O MET V 266
SHEET 8 BQ 8 PHE V 199 KCX V 201 1 N THR V 200 O TYR V 239
SHEET 1 BR 2 TYR V 353 VAL V 354 0
SHEET 2 BR 2 GLN V 366 ASP V 367 -1 O GLN V 366 N VAL V 354
SHEET 1 BS 4 THR 4 74 TRP 4 76 0
SHEET 2 BS 4 ILE 4 39 ALA 4 45 -1 N LEU 4 42 O TRP 4 76
SHEET 3 BS 4 TYR 4 104 ASP 4 111 -1 O TYR 4 104 N ALA 4 45
SHEET 4 BS 4 VAL 4 116 GLN 4 124 -1 O VAL 4 123 N VAL 4 105
SHEET 1 BT 5 ARG W 83 PRO W 89 0
SHEET 2 BT 5 TYR W 97 TYR W 103 -1 O TYR W 100 N ASP W 86
SHEET 3 BT 5 ILE W 36 PRO W 44 -1 N MET W 42 O TYR W 97
SHEET 4 BT 5 LEU W 130 ARG W 139 -1 O ARG W 134 N ARG W 41
SHEET 5 BT 5 GLY W 308 ILE W 309 1 O GLY W 308 N LEU W 135
SHEET 1 BU 8 LEU W 169 GLY W 171 0
SHEET 2 BU 8 CYS W 399 GLN W 401 1 O LEU W 400 N LEU W 169
SHEET 3 BU 8 MET W 375 SER W 379 1 N ALA W 378 O GLN W 401
SHEET 4 BU 8 HIS W 325 HIS W 327 1 N LEU W 326 O MET W 375
SHEET 5 BU 8 LEU W 290 HIS W 294 1 N ILE W 293 O HIS W 327
SHEET 6 BU 8 ILE W 264 ASP W 268 1 N ILE W 265 O HIS W 292
SHEET 7 BU 8 GLY W 237 ASN W 241 1 N LEU W 240 O MET W 266
SHEET 8 BU 8 PHE W 199 KCX W 201 1 N THR W 200 O TYR W 239
SHEET 1 BV 2 TYR W 353 VAL W 354 0
SHEET 2 BV 2 GLN W 366 ASP W 367 -1 O GLN W 366 N VAL W 354
SHEET 1 BW 4 THR 5 74 TRP 5 76 0
SHEET 2 BW 4 ILE 5 39 ALA 5 45 -1 N PHE 5 44 O THR 5 74
SHEET 3 BW 4 TYR 5 104 ASP 5 111 -1 O TYR 5 104 N ALA 5 45
SHEET 4 BW 4 VAL 5 116 GLN 5 124 -1 O VAL 5 123 N VAL 5 105
SHEET 1 BX 5 ARG X 83 PRO X 89 0
SHEET 2 BX 5 TYR X 97 TYR X 103 -1 O TYR X 100 N ASP X 86
SHEET 3 BX 5 ILE X 36 PRO X 44 -1 N MET X 42 O TYR X 97
SHEET 4 BX 5 LEU X 130 ARG X 139 -1 O ARG X 134 N ARG X 41
SHEET 5 BX 5 GLY X 308 ILE X 309 1 O GLY X 308 N LEU X 135
SHEET 1 BY 8 LEU X 169 GLY X 171 0
SHEET 2 BY 8 CYS X 399 GLN X 401 1 O LEU X 400 N LEU X 169
SHEET 3 BY 8 MET X 375 SER X 379 1 N ALA X 378 O GLN X 401
SHEET 4 BY 8 HIS X 325 HIS X 327 1 N LEU X 326 O MET X 375
SHEET 5 BY 8 LEU X 290 HIS X 294 1 N ILE X 293 O HIS X 325
SHEET 6 BY 8 ILE X 264 ASP X 268 1 N ILE X 265 O HIS X 292
SHEET 7 BY 8 GLY X 237 ASN X 241 1 N LEU X 240 O MET X 266
SHEET 8 BY 8 PHE X 199 KCX X 201 1 N THR X 200 O TYR X 239
SHEET 1 BZ 2 TYR X 353 VAL X 354 0
SHEET 2 BZ 2 GLN X 366 ASP X 367 -1 O GLN X 366 N VAL X 354
SHEET 1 CA 2 VAL 6 3 TRP 6 4 0
SHEET 2 CA 2 SER 6 139 VAL 6 140 -1 O VAL 6 140 N VAL 6 3
SHEET 1 CB 4 THR 6 74 TRP 6 76 0
SHEET 2 CB 4 ILE 6 39 ALA 6 45 -1 N PHE 6 44 O THR 6 74
SHEET 3 CB 4 TYR 6 104 ASP 6 111 -1 O VAL 6 108 N CYS 6 41
SHEET 4 CB 4 VAL 6 116 GLN 6 124 -1 O VAL 6 123 N VAL 6 105
SHEET 1 CC 5 ARG Y 83 PRO Y 89 0
SHEET 2 CC 5 TYR Y 97 TYR Y 103 -1 O ILE Y 98 N GLU Y 88
SHEET 3 CC 5 ILE Y 36 PRO Y 44 -1 N MET Y 42 O TYR Y 97
SHEET 4 CC 5 LEU Y 130 ARG Y 139 -1 O ARG Y 134 N ARG Y 41
SHEET 5 CC 5 GLY Y 308 ILE Y 309 1 O GLY Y 308 N LEU Y 135
SHEET 1 CD 8 LEU Y 169 GLY Y 171 0
SHEET 2 CD 8 CYS Y 399 GLN Y 401 1 O LEU Y 400 N LEU Y 169
SHEET 3 CD 8 MET Y 375 SER Y 379 1 N ALA Y 378 O GLN Y 401
SHEET 4 CD 8 HIS Y 325 HIS Y 327 1 N LEU Y 326 O VAL Y 377
SHEET 5 CD 8 LEU Y 290 HIS Y 294 1 N ILE Y 293 O HIS Y 327
SHEET 6 CD 8 ILE Y 264 ASP Y 268 1 N ILE Y 265 O HIS Y 292
SHEET 7 CD 8 GLY Y 237 ASN Y 241 1 N LEU Y 240 O MET Y 266
SHEET 8 CD 8 PHE Y 199 KCX Y 201 1 N THR Y 200 O TYR Y 239
SHEET 1 CE 2 TYR Y 353 VAL Y 354 0
SHEET 2 CE 2 GLN Y 366 ASP Y 367 -1 O GLN Y 366 N VAL Y 354
SHEET 1 CF 2 VAL 7 3 TRP 7 4 0
SHEET 2 CF 2 SER 7 139 VAL 7 140 -1 O VAL 7 140 N VAL 7 3
SHEET 1 CG 4 THR 7 74 TRP 7 76 0
SHEET 2 CG 4 ILE 7 39 ALA 7 45 -1 N PHE 7 44 O THR 7 74
SHEET 3 CG 4 TYR 7 104 ASP 7 111 -1 O TYR 7 104 N ALA 7 45
SHEET 4 CG 4 VAL 7 116 GLN 7 124 -1 O VAL 7 123 N VAL 7 105
SHEET 1 CH 5 ARG Z 83 PRO Z 89 0
SHEET 2 CH 5 TYR Z 97 TYR Z 103 -1 O TYR Z 100 N ASP Z 86
SHEET 3 CH 5 ILE Z 36 PRO Z 44 -1 N PHE Z 40 O ALA Z 99
SHEET 4 CH 5 LEU Z 130 ARG Z 139 -1 O ARG Z 134 N ARG Z 41
SHEET 5 CH 5 GLY Z 308 ILE Z 309 1 O GLY Z 308 N LEU Z 135
SHEET 1 CI 8 LEU Z 169 GLY Z 171 0
SHEET 2 CI 8 CYS Z 399 GLN Z 401 1 O LEU Z 400 N LEU Z 169
SHEET 3 CI 8 MET Z 375 SER Z 379 1 N ALA Z 378 O GLN Z 401
SHEET 4 CI 8 HIS Z 325 HIS Z 327 1 N LEU Z 326 O VAL Z 377
SHEET 5 CI 8 LEU Z 290 HIS Z 294 1 N ILE Z 293 O HIS Z 327
SHEET 6 CI 8 ILE Z 264 ASP Z 268 1 N ILE Z 265 O HIS Z 292
SHEET 7 CI 8 GLY Z 237 ASN Z 241 1 N LEU Z 240 O MET Z 266
SHEET 8 CI 8 PHE Z 199 KCX Z 201 1 N THR Z 200 O TYR Z 239
SHEET 1 CJ 2 TYR Z 353 VAL Z 354 0
SHEET 2 CJ 2 GLN Z 366 ASP Z 367 -1 O GLN Z 366 N VAL Z 354
SHEET 1 CK 2 VAL 8 3 TRP 8 4 0
SHEET 2 CK 2 SER 8 139 VAL 8 140 -1 O VAL 8 140 N VAL 8 3
SHEET 1 CL 4 THR 8 74 TRP 8 76 0
SHEET 2 CL 4 ILE 8 39 ALA 8 45 -1 N LEU 8 42 O TRP 8 76
SHEET 3 CL 4 TYR 8 104 ASP 8 111 -1 O TYR 8 104 N ALA 8 45
SHEET 4 CL 4 VAL 8 116 GLN 8 124 -1 O VAL 8 123 N VAL 8 105
SSBOND 1 CYS A 247 CYS E 247 1555 1555 2.76
SSBOND 2 CYS B 247 CYS F 247 1555 1555 2.79
SSBOND 3 CYS C 247 CYS G 247 1555 1555 2.72
SSBOND 4 CYS D 247 CYS H 247 1555 1555 2.80
SSBOND 5 CYS S 247 CYS W 247 1555 1555 2.77
SSBOND 6 CYS T 247 CYS X 247 1555 1555 2.79
SSBOND 7 CYS U 247 CYS Y 247 1555 1555 2.77
SSBOND 8 CYS V 247 CYS Z 247 1555 1555 2.76
LINK C TYR A 103 N HYP A 104 1555 1555 1.35
LINK C HYP A 104 N ILE A 105 1555 1555 1.33
LINK C GLY A 150 N HYP A 151 1555 1555 1.34
LINK C HYP A 151 N PRO A 152 1555 1555 1.34
LINK C THR A 200 N KCX A 201 1555 1555 1.33
LINK C KCX A 201 N ASP A 202 1555 1555 1.33
LINK C VAL A 255 N SMC A 256 1555 1555 1.33
LINK C SMC A 256 N ALA A 257 1555 1555 1.33
LINK C TRP A 368 N SMC A 369 1555 1555 1.33
LINK C SMC A 369 N SER A 370 1555 1555 1.33
LINK C MME I 1 N MET I 2 1555 1555 1.33
LINK C TYR B 103 N HYP B 104 1555 1555 1.35
LINK C HYP B 104 N ILE B 105 1555 1555 1.33
LINK C GLY B 150 N HYP B 151 1555 1555 1.35
LINK C HYP B 151 N PRO B 152 1555 1555 1.34
LINK C THR B 200 N KCX B 201 1555 1555 1.33
LINK C KCX B 201 N ASP B 202 1555 1555 1.33
LINK C VAL B 255 N SMC B 256 1555 1555 1.33
LINK C SMC B 256 N ALA B 257 1555 1555 1.33
LINK C TRP B 368 N SMC B 369 1555 1555 1.33
LINK C SMC B 369 N SER B 370 1555 1555 1.33
LINK C MME J 1 N MET J 2 1555 1555 1.33
LINK C TYR C 103 N HYP C 104 1555 1555 1.35
LINK C HYP C 104 N ILE C 105 1555 1555 1.33
LINK C GLY C 150 N HYP C 151 1555 1555 1.35
LINK C HYP C 151 N PRO C 152 1555 1555 1.35
LINK C THR C 200 N KCX C 201 1555 1555 1.33
LINK C KCX C 201 N ASP C 202 1555 1555 1.33
LINK C VAL C 255 N SMC C 256 1555 1555 1.33
LINK C SMC C 256 N ALA C 257 1555 1555 1.33
LINK C TRP C 368 N SMC C 369 1555 1555 1.33
LINK C SMC C 369 N SER C 370 1555 1555 1.33
LINK C MME K 1 N MET K 2 1555 1555 1.33
LINK C TYR D 103 N HYP D 104 1555 1555 1.35
LINK C HYP D 104 N ILE D 105 1555 1555 1.33
LINK C GLY D 150 N HYP D 151 1555 1555 1.34
LINK C HYP D 151 N PRO D 152 1555 1555 1.34
LINK C THR D 200 N KCX D 201 1555 1555 1.33
LINK C KCX D 201 N ASP D 202 1555 1555 1.33
LINK C VAL D 255 N SMC D 256 1555 1555 1.33
LINK C SMC D 256 N ALA D 257 1555 1555 1.33
LINK C TRP D 368 N SMC D 369 1555 1555 1.33
LINK C SMC D 369 N SER D 370 1555 1555 1.33
LINK C MME L 1 N MET L 2 1555 1555 1.32
LINK C TYR E 103 N HYP E 104 1555 1555 1.35
LINK C HYP E 104 N ILE E 105 1555 1555 1.33
LINK C GLY E 150 N HYP E 151 1555 1555 1.35
LINK C HYP E 151 N PRO E 152 1555 1555 1.34
LINK C THR E 200 N KCX E 201 1555 1555 1.33
LINK C KCX E 201 N ASP E 202 1555 1555 1.33
LINK C VAL E 255 N SMC E 256 1555 1555 1.33
LINK C SMC E 256 N ALA E 257 1555 1555 1.33
LINK C TRP E 368 N SMC E 369 1555 1555 1.33
LINK C SMC E 369 N SER E 370 1555 1555 1.33
LINK C MME M 1 N MET M 2 1555 1555 1.33
LINK C TYR F 103 N HYP F 104 1555 1555 1.35
LINK C HYP F 104 N ILE F 105 1555 1555 1.33
LINK C GLY F 150 N HYP F 151 1555 1555 1.35
LINK C HYP F 151 N PRO F 152 1555 1555 1.34
LINK C THR F 200 N KCX F 201 1555 1555 1.33
LINK C KCX F 201 N ASP F 202 1555 1555 1.33
LINK C VAL F 255 N SMC F 256 1555 1555 1.33
LINK C SMC F 256 N ALA F 257 1555 1555 1.33
LINK C TRP F 368 N SMC F 369 1555 1555 1.33
LINK C SMC F 369 N SER F 370 1555 1555 1.33
LINK C MME N 1 N MET N 2 1555 1555 1.33
LINK C TYR G 103 N HYP G 104 1555 1555 1.35
LINK C HYP G 104 N ILE G 105 1555 1555 1.33
LINK C GLY G 150 N HYP G 151 1555 1555 1.35
LINK C HYP G 151 N PRO G 152 1555 1555 1.34
LINK C THR G 200 N KCX G 201 1555 1555 1.33
LINK C KCX G 201 N ASP G 202 1555 1555 1.33
LINK C VAL G 255 N SMC G 256 1555 1555 1.33
LINK C SMC G 256 N ALA G 257 1555 1555 1.33
LINK C TRP G 368 N SMC G 369 1555 1555 1.33
LINK C SMC G 369 N SER G 370 1555 1555 1.33
LINK C MME O 1 N MET O 2 1555 1555 1.33
LINK C TYR H 103 N HYP H 104 1555 1555 1.35
LINK C HYP H 104 N ILE H 105 1555 1555 1.33
LINK C GLY H 150 N HYP H 151 1555 1555 1.35
LINK C HYP H 151 N PRO H 152 1555 1555 1.35
LINK C THR H 200 N KCX H 201 1555 1555 1.33
LINK C KCX H 201 N ASP H 202 1555 1555 1.34
LINK C VAL H 255 N SMC H 256 1555 1555 1.33
LINK C SMC H 256 N ALA H 257 1555 1555 1.33
LINK C TRP H 368 N SMC H 369 1555 1555 1.33
LINK C SMC H 369 N SER H 370 1555 1555 1.33
LINK C MME P 1 N MET P 2 1555 1555 1.33
LINK C TYR S 103 N HYP S 104 1555 1555 1.35
LINK C HYP S 104 N ILE S 105 1555 1555 1.33
LINK C GLY S 150 N HYP S 151 1555 1555 1.35
LINK C HYP S 151 N PRO S 152 1555 1555 1.35
LINK C THR S 200 N KCX S 201 1555 1555 1.33
LINK C KCX S 201 N ASP S 202 1555 1555 1.33
LINK C VAL S 255 N SMC S 256 1555 1555 1.33
LINK C SMC S 256 N ALA S 257 1555 1555 1.33
LINK C TRP S 368 N SMC S 369 1555 1555 1.33
LINK C SMC S 369 N SER S 370 1555 1555 1.33
LINK C MME 1 1 N MET 1 2 1555 1555 1.33
LINK C TYR T 103 N HYP T 104 1555 1555 1.35
LINK C HYP T 104 N ILE T 105 1555 1555 1.33
LINK C GLY T 150 N HYP T 151 1555 1555 1.35
LINK C HYP T 151 N PRO T 152 1555 1555 1.35
LINK C THR T 200 N KCX T 201 1555 1555 1.33
LINK C KCX T 201 N ASP T 202 1555 1555 1.33
LINK C VAL T 255 N SMC T 256 1555 1555 1.33
LINK C SMC T 256 N ALA T 257 1555 1555 1.33
LINK C TRP T 368 N SMC T 369 1555 1555 1.33
LINK C SMC T 369 N SER T 370 1555 1555 1.33
LINK C MME 2 1 N MET 2 2 1555 1555 1.33
LINK C TYR U 103 N HYP U 104 1555 1555 1.35
LINK C HYP U 104 N ILE U 105 1555 1555 1.33
LINK C GLY U 150 N HYP U 151 1555 1555 1.35
LINK C HYP U 151 N PRO U 152 1555 1555 1.35
LINK C THR U 200 N KCX U 201 1555 1555 1.33
LINK C KCX U 201 N ASP U 202 1555 1555 1.33
LINK C VAL U 255 N SMC U 256 1555 1555 1.33
LINK C SMC U 256 N ALA U 257 1555 1555 1.33
LINK C TRP U 368 N SMC U 369 1555 1555 1.33
LINK C SMC U 369 N SER U 370 1555 1555 1.33
LINK C MME 3 1 N MET 3 2 1555 1555 1.33
LINK C TYR V 103 N HYP V 104 1555 1555 1.35
LINK C HYP V 104 N ILE V 105 1555 1555 1.33
LINK C GLY V 150 N HYP V 151 1555 1555 1.35
LINK C HYP V 151 N PRO V 152 1555 1555 1.34
LINK C THR V 200 N KCX V 201 1555 1555 1.33
LINK C KCX V 201 N ASP V 202 1555 1555 1.33
LINK C VAL V 255 N SMC V 256 1555 1555 1.33
LINK C SMC V 256 N ALA V 257 1555 1555 1.33
LINK C TRP V 368 N SMC V 369 1555 1555 1.33
LINK C SMC V 369 N SER V 370 1555 1555 1.33
LINK C MME 4 1 N MET 4 2 1555 1555 1.33
LINK C TYR W 103 N HYP W 104 1555 1555 1.35
LINK C HYP W 104 N ILE W 105 1555 1555 1.33
LINK C GLY W 150 N HYP W 151 1555 1555 1.34
LINK C HYP W 151 N PRO W 152 1555 1555 1.34
LINK C THR W 200 N KCX W 201 1555 1555 1.33
LINK C KCX W 201 N ASP W 202 1555 1555 1.33
LINK C VAL W 255 N SMC W 256 1555 1555 1.33
LINK C SMC W 256 N ALA W 257 1555 1555 1.33
LINK C TRP W 368 N SMC W 369 1555 1555 1.33
LINK C SMC W 369 N SER W 370 1555 1555 1.33
LINK C MME 5 1 N MET 5 2 1555 1555 1.33
LINK C TYR X 103 N HYP X 104 1555 1555 1.35
LINK C HYP X 104 N ILE X 105 1555 1555 1.33
LINK C GLY X 150 N HYP X 151 1555 1555 1.35
LINK C HYP X 151 N PRO X 152 1555 1555 1.34
LINK C THR X 200 N KCX X 201 1555 1555 1.33
LINK C KCX X 201 N ASP X 202 1555 1555 1.33
LINK C VAL X 255 N SMC X 256 1555 1555 1.33
LINK C SMC X 256 N ALA X 257 1555 1555 1.33
LINK C TRP X 368 N SMC X 369 1555 1555 1.33
LINK C SMC X 369 N SER X 370 1555 1555 1.33
LINK C MME 6 1 N MET 6 2 1555 1555 1.33
LINK C TYR Y 103 N HYP Y 104 1555 1555 1.35
LINK C HYP Y 104 N ILE Y 105 1555 1555 1.33
LINK C GLY Y 150 N HYP Y 151 1555 1555 1.35
LINK C HYP Y 151 N PRO Y 152 1555 1555 1.34
LINK C THR Y 200 N KCX Y 201 1555 1555 1.33
LINK C KCX Y 201 N ASP Y 202 1555 1555 1.33
LINK C VAL Y 255 N SMC Y 256 1555 1555 1.33
LINK C SMC Y 256 N ALA Y 257 1555 1555 1.33
LINK C TRP Y 368 N SMC Y 369 1555 1555 1.33
LINK C SMC Y 369 N SER Y 370 1555 1555 1.33
LINK C MME 7 1 N MET 7 2 1555 1555 1.33
LINK C TYR Z 103 N HYP Z 104 1555 1555 1.35
LINK C HYP Z 104 N ILE Z 105 1555 1555 1.33
LINK C GLY Z 150 N HYP Z 151 1555 1555 1.35
LINK C HYP Z 151 N PRO Z 152 1555 1555 1.34
LINK C THR Z 200 N KCX Z 201 1555 1555 1.33
LINK C KCX Z 201 N ASP Z 202 1555 1555 1.33
LINK C VAL Z 255 N SMC Z 256 1555 1555 1.33
LINK C SMC Z 256 N ALA Z 257 1555 1555 1.33
LINK C TRP Z 368 N SMC Z 369 1555 1555 1.33
LINK C SMC Z 369 N SER Z 370 1555 1555 1.33
LINK C MME 8 1 N MET 8 2 1555 1555 1.33
LINK OQ1 KCX A 201 MG MG A 476 1555 1555 2.14
LINK OD1 ASP A 203 MG MG A 476 1555 1555 2.02
LINK OE1 GLU A 204 MG MG A 476 1555 1555 2.03
LINK MG MG A 476 O6 CAP A 501 1555 1555 2.15
LINK MG MG A 476 O2 CAP A 501 1555 1555 2.30
LINK MG MG A 476 O3 CAP A 501 1555 1555 2.26
LINK OQ1 KCX B 201 MG MG B 476 1555 1555 2.15
LINK OD1 ASP B 203 MG MG B 476 1555 1555 2.06
LINK OE1 GLU B 204 MG MG B 476 1555 1555 1.97
LINK MG MG B 476 O3 CAP B 501 1555 1555 2.17
LINK MG MG B 476 O2 CAP B 501 1555 1555 2.33
LINK MG MG B 476 O6 CAP B 501 1555 1555 2.21
LINK OQ1 KCX C 201 MG MG C 476 1555 1555 2.16
LINK OD1 ASP C 203 MG MG C 476 1555 1555 2.03
LINK OE1 GLU C 204 MG MG C 476 1555 1555 1.97
LINK MG MG C 476 O6 CAP C 501 1555 1555 2.18
LINK MG MG C 476 O2 CAP C 501 1555 1555 2.33
LINK MG MG C 476 O3 CAP C 501 1555 1555 2.22
LINK OQ1 KCX D 201 MG MG D 476 1555 1555 2.08
LINK OD1 ASP D 203 MG MG D 476 1555 1555 2.00
LINK OE1 GLU D 204 MG MG D 476 1555 1555 2.03
LINK MG MG D 476 O6 CAP D 501 1555 1555 2.19
LINK MG MG D 476 O2 CAP D 501 1555 1555 2.30
LINK MG MG D 476 O3 CAP D 501 1555 1555 2.21
LINK OQ1 KCX E 201 MG MG E 476 1555 1555 2.12
LINK OD1 ASP E 203 MG MG E 476 1555 1555 2.03
LINK OE1 GLU E 204 MG MG E 476 1555 1555 2.11
LINK MG MG E 476 O6 CAP E 501 1555 1555 2.19
LINK MG MG E 476 O3 CAP E 501 1555 1555 2.23
LINK MG MG E 476 O2 CAP E 501 1555 1555 2.25
LINK OQ1 KCX F 201 MG MG F 476 1555 1555 2.08
LINK OD1 ASP F 203 MG MG F 476 1555 1555 2.07
LINK OE1 GLU F 204 MG MG F 476 1555 1555 2.05
LINK MG MG F 476 O3 CAP F 501 1555 1555 2.20
LINK MG MG F 476 O6 CAP F 501 1555 1555 2.27
LINK MG MG F 476 O2 CAP F 501 1555 1555 2.28
LINK OQ1 KCX G 201 MG MG G 476 1555 1555 2.10
LINK OD1 ASP G 203 MG MG G 476 1555 1555 2.05
LINK OE1 GLU G 204 MG MG G 476 1555 1555 1.98
LINK MG MG G 476 O2 CAP G 501 1555 1555 2.32
LINK MG MG G 476 O3 CAP G 501 1555 1555 2.23
LINK MG MG G 476 O6 CAP G 501 1555 1555 2.21
LINK OQ1 KCX H 201 MG MG H 476 1555 1555 2.15
LINK OD1 ASP H 203 MG MG H 476 1555 1555 2.10
LINK OE1 GLU H 204 MG MG H 476 1555 1555 2.02
LINK MG MG H 476 O3 CAP H 501 1555 1555 2.15
LINK MG MG H 476 O6 CAP H 501 1555 1555 2.15
LINK MG MG H 476 O2 CAP H 501 1555 1555 2.29
LINK OQ1 KCX S 201 MG MG S 476 1555 1555 2.13
LINK OD1 ASP S 203 MG MG S 476 1555 1555 2.00
LINK OE1 GLU S 204 MG MG S 476 1555 1555 2.03
LINK MG MG S 476 O3 CAP S 501 1555 1555 2.22
LINK MG MG S 476 O2 CAP S 501 1555 1555 2.28
LINK MG MG S 476 O6 CAP S 501 1555 1555 2.23
LINK OQ1 KCX T 201 MG MG T 476 1555 1555 2.13
LINK OD1 ASP T 203 MG MG T 476 1555 1555 2.06
LINK OE1 GLU T 204 MG MG T 476 1555 1555 2.05
LINK MG MG T 476 O6 CAP T 501 1555 1555 2.17
LINK MG MG T 476 O3 CAP T 501 1555 1555 2.22
LINK MG MG T 476 O2 CAP T 501 1555 1555 2.26
LINK OQ1 KCX U 201 MG MG U 476 1555 1555 2.11
LINK OD1 ASP U 203 MG MG U 476 1555 1555 2.00
LINK OE1 GLU U 204 MG MG U 476 1555 1555 1.96
LINK MG MG U 476 O3 CAP U 501 1555 1555 2.22
LINK MG MG U 476 O6 CAP U 501 1555 1555 2.24
LINK MG MG U 476 O2 CAP U 501 1555 1555 2.31
LINK OQ1 KCX V 201 MG MG V 476 1555 1555 2.18
LINK OD1 ASP V 203 MG MG V 476 1555 1555 1.97
LINK OE1 GLU V 204 MG MG V 476 1555 1555 2.13
LINK MG MG V 476 O6 CAP V 501 1555 1555 2.14
LINK MG MG V 476 O2 CAP V 501 1555 1555 2.28
LINK MG MG V 476 O3 CAP V 501 1555 1555 2.26
LINK OQ1 KCX W 201 MG MG W 476 1555 1555 2.06
LINK OD1 ASP W 203 MG MG W 476 1555 1555 1.99
LINK OE1 GLU W 204 MG MG W 476 1555 1555 2.01
LINK MG MG W 476 O3 CAP W 501 1555 1555 2.19
LINK MG MG W 476 O6 CAP W 501 1555 1555 2.25
LINK MG MG W 476 O2 CAP W 501 1555 1555 2.33
LINK OQ1 KCX X 201 MG MG X 476 1555 1555 2.19
LINK OD1 ASP X 203 MG MG X 476 1555 1555 2.00
LINK OE1 GLU X 204 MG MG X 476 1555 1555 2.03
LINK MG MG X 476 O6 CAP X 501 1555 1555 2.19
LINK MG MG X 476 O3 CAP X 501 1555 1555 2.27
LINK MG MG X 476 O2 CAP X 501 1555 1555 2.32
LINK OQ1 KCX Y 201 MG MG Y 476 1555 1555 2.07
LINK OD1 ASP Y 203 MG MG Y 476 1555 1555 1.99
LINK OE1 GLU Y 204 MG MG Y 476 1555 1555 2.07
LINK MG MG Y 476 O6 CAP Y 501 1555 1555 2.23
LINK MG MG Y 476 O3 CAP Y 501 1555 1555 2.25
LINK MG MG Y 476 O2 CAP Y 501 1555 1555 2.33
LINK OQ1 KCX Z 201 MG MG Z 476 1555 1555 2.10
LINK OD1 ASP Z 203 MG MG Z 476 1555 1555 2.01
LINK OE1 GLU Z 204 MG MG Z 476 1555 1555 2.04
LINK MG MG Z 476 O3 CAP Z 501 1555 1555 2.24
LINK MG MG Z 476 O6 CAP Z 501 1555 1555 2.23
LINK MG MG Z 476 O2 CAP Z 501 1555 1555 2.34
CISPEP 1 LYS A 175 PRO A 176 0 -0.07
CISPEP 2 LYS B 175 PRO B 176 0 -0.05
CISPEP 3 LYS C 175 PRO C 176 0 -0.14
CISPEP 4 LYS D 175 PRO D 176 0 0.01
CISPEP 5 LYS E 175 PRO E 176 0 -0.14
CISPEP 6 LYS F 175 PRO F 176 0 -0.09
CISPEP 7 LYS G 175 PRO G 176 0 -0.06
CISPEP 8 LYS H 175 PRO H 176 0 -0.27
CISPEP 9 LYS S 175 PRO S 176 0 -0.05
CISPEP 10 LYS T 175 PRO T 176 0 -0.09
CISPEP 11 LYS U 175 PRO U 176 0 -0.30
CISPEP 12 LYS V 175 PRO V 176 0 -0.12
CISPEP 13 LYS W 175 PRO W 176 0 -0.16
CISPEP 14 LYS X 175 PRO X 176 0 -0.11
CISPEP 15 LYS Y 175 PRO Y 176 0 -0.19
CISPEP 16 LYS Z 175 PRO Z 176 0 -0.07
SITE 1 AC1 4 KCX A 201 ASP A 203 GLU A 204 CAP A 501
SITE 1 AC2 5 LYS B 177 KCX B 201 ASP B 203 GLU B 204
SITE 2 AC2 5 CAP B 501
SITE 1 AC3 5 LYS C 177 KCX C 201 ASP C 203 GLU C 204
SITE 2 AC3 5 CAP C 501
SITE 1 AC4 4 KCX D 201 ASP D 203 GLU D 204 CAP D 501
SITE 1 AC5 4 KCX E 201 ASP E 203 GLU E 204 CAP E 501
SITE 1 AC6 5 LYS F 177 KCX F 201 ASP F 203 GLU F 204
SITE 2 AC6 5 CAP F 501
SITE 1 AC7 5 LYS G 177 KCX G 201 ASP G 203 GLU G 204
SITE 2 AC7 5 CAP G 501
SITE 1 AC8 4 KCX H 201 ASP H 203 GLU H 204 CAP H 501
SITE 1 AC9 4 KCX S 201 ASP S 203 GLU S 204 CAP S 501
SITE 1 BC1 4 KCX T 201 ASP T 203 GLU T 204 CAP T 501
SITE 1 BC2 5 LYS U 177 KCX U 201 ASP U 203 GLU U 204
SITE 2 BC2 5 CAP U 501
SITE 1 BC3 4 KCX V 201 ASP V 203 GLU V 204 CAP V 501
SITE 1 BC4 5 LYS W 177 KCX W 201 ASP W 203 GLU W 204
SITE 2 BC4 5 CAP W 501
SITE 1 BC5 5 LYS X 177 KCX X 201 ASP X 203 GLU X 204
SITE 2 BC5 5 CAP X 501
SITE 1 BC6 5 LYS Y 177 KCX Y 201 ASP Y 203 GLU Y 204
SITE 2 BC6 5 CAP Y 501
SITE 1 BC7 5 LYS Z 177 KCX Z 201 ASP Z 203 GLU Z 204
SITE 2 BC7 5 CAP Z 501
SITE 1 BC8 29 THR A 173 LYS A 175 LYS A 177 KCX A 201
SITE 2 BC8 29 ASP A 203 GLU A 204 HIS A 294 ARG A 295
SITE 3 BC8 29 HIS A 327 LYS A 334 LEU A 335 SER A 379
SITE 4 BC8 29 GLY A 380 GLY A 381 GLY A 403 GLY A 404
SITE 5 BC8 29 MG A 476 HOH A 616 HOH A 617 HOH A 621
SITE 6 BC8 29 HOH A 630 HOH A 660 HOH A 679 GLU E 60
SITE 7 BC8 29 THR E 65 TRP E 66 ASN E 123 HOH E 678
SITE 8 BC8 29 HOH E 731
SITE 1 BC9 29 THR B 173 LYS B 175 LYS B 177 KCX B 201
SITE 2 BC9 29 ASP B 203 GLU B 204 HIS B 294 ARG B 295
SITE 3 BC9 29 HIS B 327 LYS B 334 LEU B 335 SER B 379
SITE 4 BC9 29 GLY B 380 GLY B 381 GLY B 403 GLY B 404
SITE 5 BC9 29 MG B 476 HOH B 615 HOH B 622 HOH B 653
SITE 6 BC9 29 HOH B 657 HOH B 678 HOH B 700 GLU F 60
SITE 7 BC9 29 THR F 65 TRP F 66 ASN F 123 HOH F 646
SITE 8 BC9 29 HOH F 648
SITE 1 CC1 29 THR C 173 LYS C 175 LYS C 177 KCX C 201
SITE 2 CC1 29 ASP C 203 GLU C 204 HIS C 294 ARG C 295
SITE 3 CC1 29 HIS C 327 LYS C 334 LEU C 335 SER C 379
SITE 4 CC1 29 GLY C 380 GLY C 381 GLY C 403 GLY C 404
SITE 5 CC1 29 MG C 476 HOH C 618 HOH C 625 HOH C 637
SITE 6 CC1 29 HOH C 646 HOH C 657 HOH C 909 GLU G 60
SITE 7 CC1 29 THR G 65 TRP G 66 ASN G 123 HOH G 639
SITE 8 CC1 29 HOH G 675
SITE 1 CC2 29 THR D 173 LYS D 175 LYS D 177 KCX D 201
SITE 2 CC2 29 ASP D 203 GLU D 204 HIS D 294 ARG D 295
SITE 3 CC2 29 HIS D 327 LYS D 334 LEU D 335 SER D 379
SITE 4 CC2 29 GLY D 380 GLY D 381 GLY D 403 GLY D 404
SITE 5 CC2 29 MG D 476 HOH D 617 HOH D 618 HOH D 621
SITE 6 CC2 29 HOH D 658 HOH D 661 HOH D 805 GLU H 60
SITE 7 CC2 29 THR H 65 TRP H 66 ASN H 123 HOH H 621
SITE 8 CC2 29 HOH H 644
SITE 1 CC3 30 GLU A 60 THR A 65 TRP A 66 ASN A 123
SITE 2 CC3 30 HOH A 657 HOH A 779 THR E 173 LYS E 175
SITE 3 CC3 30 LYS E 177 KCX E 201 ASP E 203 GLU E 204
SITE 4 CC3 30 HIS E 294 ARG E 295 HIS E 327 LYS E 334
SITE 5 CC3 30 LEU E 335 SER E 379 GLY E 380 GLY E 381
SITE 6 CC3 30 GLY E 403 GLY E 404 MG E 476 HOH E 623
SITE 7 CC3 30 HOH E 630 HOH E 632 HOH E 635 HOH E 659
SITE 8 CC3 30 HOH E 698 HOH E 778
SITE 1 CC4 29 GLU B 60 THR B 65 TRP B 66 ASN B 123
SITE 2 CC4 29 HOH B 620 HOH B 666 THR F 173 LYS F 175
SITE 3 CC4 29 LYS F 177 KCX F 201 ASP F 203 GLU F 204
SITE 4 CC4 29 HIS F 294 ARG F 295 HIS F 327 LYS F 334
SITE 5 CC4 29 LEU F 335 SER F 379 GLY F 380 GLY F 381
SITE 6 CC4 29 GLY F 403 GLY F 404 MG F 476 HOH F 619
SITE 7 CC4 29 HOH F 625 HOH F 641 HOH F 652 HOH F 704
SITE 8 CC4 29 HOH F 786
SITE 1 CC5 29 GLU C 60 THR C 65 TRP C 66 ASN C 123
SITE 2 CC5 29 HOH C 621 HOH C 645 THR G 173 LYS G 175
SITE 3 CC5 29 LYS G 177 KCX G 201 ASP G 203 GLU G 204
SITE 4 CC5 29 HIS G 294 ARG G 295 HIS G 327 LYS G 334
SITE 5 CC5 29 LEU G 335 SER G 379 GLY G 380 GLY G 381
SITE 6 CC5 29 GLY G 403 GLY G 404 MG G 476 HOH G 620
SITE 7 CC5 29 HOH G 631 HOH G 642 HOH G 648 HOH G 656
SITE 8 CC5 29 HOH G 721
SITE 1 CC6 29 GLU D 60 THR D 65 TRP D 66 ASN D 123
SITE 2 CC6 29 HOH D 652 HOH D 659 THR H 173 LYS H 175
SITE 3 CC6 29 LYS H 177 KCX H 201 ASP H 203 GLU H 204
SITE 4 CC6 29 HIS H 294 ARG H 295 HIS H 327 LYS H 334
SITE 5 CC6 29 LEU H 335 SER H 379 GLY H 380 GLY H 381
SITE 6 CC6 29 GLY H 403 GLY H 404 MG H 476 HOH H 624
SITE 7 CC6 29 HOH H 628 HOH H 630 HOH H 637 HOH H 682
SITE 8 CC6 29 HOH H 726
SITE 1 CC7 29 THR S 173 LYS S 175 LYS S 177 KCX S 201
SITE 2 CC7 29 ASP S 203 GLU S 204 HIS S 294 ARG S 295
SITE 3 CC7 29 HIS S 327 LYS S 334 LEU S 335 SER S 379
SITE 4 CC7 29 GLY S 380 GLY S 381 GLY S 403 GLY S 404
SITE 5 CC7 29 MG S 476 HOH S 614 HOH S 615 HOH S 623
SITE 6 CC7 29 HOH S 653 HOH S 676 HOH S 694 HOH S 758
SITE 7 CC7 29 GLU W 60 THR W 65 TRP W 66 ASN W 123
SITE 8 CC7 29 HOH W 629
SITE 1 CC8 28 THR T 173 LYS T 175 LYS T 177 KCX T 201
SITE 2 CC8 28 ASP T 203 GLU T 204 HIS T 294 ARG T 295
SITE 3 CC8 28 HIS T 327 LYS T 334 LEU T 335 SER T 379
SITE 4 CC8 28 GLY T 380 GLY T 381 GLY T 403 GLY T 404
SITE 5 CC8 28 MG T 476 HOH T 615 HOH T 662 HOH T 717
SITE 6 CC8 28 HOH T 721 HOH T 802 HOH T 886 GLU X 60
SITE 7 CC8 28 THR X 65 TRP X 66 ASN X 123 HOH X 633
SITE 1 CC9 29 THR U 173 LYS U 175 LYS U 177 KCX U 201
SITE 2 CC9 29 ASP U 203 GLU U 204 HIS U 294 ARG U 295
SITE 3 CC9 29 HIS U 327 LYS U 334 LEU U 335 SER U 379
SITE 4 CC9 29 GLY U 380 GLY U 381 GLY U 403 GLY U 404
SITE 5 CC9 29 MG U 476 HOH U 620 HOH U 625 HOH U 667
SITE 6 CC9 29 HOH U 705 HOH U 706 HOH U 779 GLU Y 60
SITE 7 CC9 29 THR Y 65 TRP Y 66 ASN Y 123 HOH Y 619
SITE 8 CC9 29 HOH Y 715
SITE 1 DC1 28 THR V 173 LYS V 175 LYS V 177 KCX V 201
SITE 2 DC1 28 ASP V 203 GLU V 204 HIS V 294 ARG V 295
SITE 3 DC1 28 HIS V 327 LYS V 334 LEU V 335 SER V 379
SITE 4 DC1 28 GLY V 380 GLY V 381 GLY V 403 GLY V 404
SITE 5 DC1 28 MG V 476 HOH V 617 HOH V 620 HOH V 623
SITE 6 DC1 28 HOH V 673 HOH V 701 HOH V 703 GLU Z 60
SITE 7 DC1 28 THR Z 65 TRP Z 66 ASN Z 123 HOH Z 657
SITE 1 DC2 30 GLU S 60 THR S 65 TRP S 66 ASN S 123
SITE 2 DC2 30 HOH S 624 THR W 173 LYS W 175 LYS W 177
SITE 3 DC2 30 KCX W 201 ASP W 203 GLU W 204 HIS W 294
SITE 4 DC2 30 ARG W 295 HIS W 327 LYS W 334 LEU W 335
SITE 5 DC2 30 SER W 379 GLY W 380 GLY W 381 GLY W 403
SITE 6 DC2 30 GLY W 404 MG W 476 HOH W 626 HOH W 632
SITE 7 DC2 30 HOH W 655 HOH W 661 HOH W 662 HOH W 665
SITE 8 DC2 30 HOH W 704 HOH W 874
SITE 1 DC3 29 GLU T 60 THR T 65 TRP T 66 ASN T 123
SITE 2 DC3 29 HOH T 664 HOH T 680 THR X 173 LYS X 175
SITE 3 DC3 29 LYS X 177 KCX X 201 ASP X 203 GLU X 204
SITE 4 DC3 29 HIS X 294 ARG X 295 HIS X 327 LYS X 334
SITE 5 DC3 29 LEU X 335 SER X 379 GLY X 380 GLY X 381
SITE 6 DC3 29 GLY X 403 GLY X 404 MG X 476 HOH X 618
SITE 7 DC3 29 HOH X 635 HOH X 637 HOH X 650 HOH X 652
SITE 8 DC3 29 HOH X 764
SITE 1 DC4 30 GLU U 60 THR U 65 TRP U 66 ASN U 123
SITE 2 DC4 30 HOH U 622 HOH U 629 THR Y 173 LYS Y 175
SITE 3 DC4 30 LYS Y 177 KCX Y 201 ASP Y 203 GLU Y 204
SITE 4 DC4 30 HIS Y 294 ARG Y 295 HIS Y 327 LYS Y 334
SITE 5 DC4 30 LEU Y 335 SER Y 379 GLY Y 380 GLY Y 381
SITE 6 DC4 30 GLY Y 403 GLY Y 404 MG Y 476 HOH Y 620
SITE 7 DC4 30 HOH Y 627 HOH Y 629 HOH Y 645 HOH Y 659
SITE 8 DC4 30 HOH Y 749 HOH Y 750
SITE 1 DC5 28 GLU V 60 THR V 65 TRP V 66 ASN V 123
SITE 2 DC5 28 HOH V 671 THR Z 173 LYS Z 175 LYS Z 177
SITE 3 DC5 28 KCX Z 201 ASP Z 203 GLU Z 204 HIS Z 294
SITE 4 DC5 28 ARG Z 295 HIS Z 327 LYS Z 334 LEU Z 335
SITE 5 DC5 28 SER Z 379 GLY Z 380 GLY Z 381 GLY Z 403
SITE 6 DC5 28 GLY Z 404 MG Z 476 HOH Z 624 HOH Z 625
SITE 7 DC5 28 HOH Z 627 HOH Z 628 HOH Z 629 HOH Z 787
SITE 1 DC6 9 VAL E 17 LYS E 18 THR E 65 TRP E 66
SITE 2 DC6 9 THR E 67 THR E 68 HOH E 656 HOH E 670
SITE 3 DC6 9 HOH E 792
SITE 1 DC7 9 VAL F 17 LYS F 18 THR F 65 TRP F 66
SITE 2 DC7 9 THR F 67 THR F 68 HOH F 659 HOH F 701
SITE 3 DC7 9 HOH F 795
SITE 1 DC8 9 VAL G 17 LYS G 18 THR G 65 TRP G 66
SITE 2 DC8 9 THR G 67 THR G 68 HOH G 676 HOH G 776
SITE 3 DC8 9 HOH G 780
SITE 1 DC9 8 LYS H 18 TYR H 24 THR H 65 TRP H 66
SITE 2 DC9 8 THR H 67 THR H 68 HOH H 732 HOH H 784
SITE 1 EC1 9 LYS A 18 THR A 65 TRP A 66 THR A 67
SITE 2 EC1 9 THR A 68 HOH A 688 HOH A 751 HOH A 795
SITE 3 EC1 9 HOH A 821
SITE 1 EC2 10 VAL B 17 LYS B 18 THR B 65 TRP B 66
SITE 2 EC2 10 THR B 67 THR B 68 HOH B 638 HOH B 652
SITE 3 EC2 10 HOH B 726 HOH B 728
SITE 1 EC3 10 VAL C 17 LYS C 18 THR C 65 TRP C 66
SITE 2 EC3 10 THR C 67 THR C 68 HOH C 627 HOH C 761
SITE 3 EC3 10 HOH C 763 HOH C 954
SITE 1 EC4 9 VAL D 17 LYS D 18 THR D 65 TRP D 66
SITE 2 EC4 9 THR D 67 THR D 68 HOH D 665 HOH D 741
SITE 3 EC4 9 HOH D 815
SITE 1 EC5 6 LEU A 270 LEU E 270 MET E 297 HOH E 717
SITE 2 EC5 6 HOH E 729 HOH E 813
SITE 1 EC6 6 LEU B 270 HOH B 769 HOH B 789 LEU F 270
SITE 2 EC6 6 MET F 297 HOH F 663
SITE 1 EC7 6 LEU C 270 HOH C 648 LEU G 270 MET G 297
SITE 2 EC7 6 HOH G 636 HOH G 816
SITE 1 EC8 6 LEU D 270 LEU H 270 MET H 297 HOH H 675
SITE 2 EC8 6 HOH H 742 HOH H 922
SITE 1 EC9 8 VAL A 149 ARG A 285 ASP A 286 HOH A 710
SITE 2 EC9 8 HOH A 769 HOH A 974 LYS B 252 HOH B 634
SITE 1 FC1 6 ILE B 282 ARG B 285 ASP B 286 HOH B 661
SITE 2 FC1 6 HOH B 747 LYS C 252
SITE 1 FC2 7 ILE C 282 ARG C 285 ASP C 286 HOH C 719
SITE 2 FC2 7 HOH C1060 LYS D 252 HOH D 642
SITE 1 FC3 8 LYS A 252 HOH A 642 ILE D 282 ARG D 285
SITE 2 FC3 8 ASP D 286 HOH D 720 HOH D 875 HOH D1059
SITE 1 FC4 6 LYS E 252 HOH E 683 ILE F 282 ARG F 285
SITE 2 FC4 6 ASP F 286 HOH F 757
SITE 1 FC5 6 LYS F 252 HOH F 722 ARG G 285 ASP G 286
SITE 2 FC5 6 HOH G 732 HOH G1026
SITE 1 FC6 7 LYS G 252 HOH G 740 ILE H 282 ASP H 286
SITE 2 FC6 7 HOH H 739 HOH H 906 HOH H1023
SITE 1 FC7 9 VAL E 149 ILE E 282 ARG E 285 ASP E 286
SITE 2 FC7 9 HOH E 701 HOH E1004 HOH E1057 LYS H 252
SITE 3 FC7 9 HOH H 671
SITE 1 FC8 9 VAL W 17 LYS W 18 THR W 65 TRP W 66
SITE 2 FC8 9 THR W 67 THR W 68 HOH W 731 HOH W 794
SITE 3 FC8 9 HOH W 910
SITE 1 FC9 10 VAL X 17 LYS X 18 THR X 65 TRP X 66
SITE 2 FC9 10 THR X 67 THR X 68 HOH X 636 HOH X 648
SITE 3 FC9 10 HOH X 738 HOH X 869
SITE 1 GC1 9 VAL Y 17 LYS Y 18 THR Y 65 TRP Y 66
SITE 2 GC1 9 THR Y 67 THR Y 68 HOH Y 634 HOH Y 842
SITE 3 GC1 9 HOH Y 957
SITE 1 GC2 10 VAL Z 17 LYS Z 18 THR Z 65 TRP Z 66
SITE 2 GC2 10 THR Z 67 THR Z 68 HOH Z 769 HOH Z 772
SITE 3 GC2 10 HOH Z 800 HOH Z 867
SITE 1 GC3 9 VAL S 17 LYS S 18 THR S 65 TRP S 66
SITE 2 GC3 9 THR S 67 THR S 68 HOH S 773 HOH S 888
SITE 3 GC3 9 HOH S 901
SITE 1 GC4 9 VAL T 17 LYS T 18 THR T 65 TRP T 66
SITE 2 GC4 9 THR T 67 THR T 68 HOH T 655 HOH T 770
SITE 3 GC4 9 HOH T 894
SITE 1 GC5 10 VAL U 17 LYS U 18 THR U 65 TRP U 66
SITE 2 GC5 10 THR U 67 THR U 68 HOH U 659 HOH U 717
SITE 3 GC5 10 HOH U 888 HOH U 945
SITE 1 GC6 9 VAL V 17 LYS V 18 THR V 65 TRP V 66
SITE 2 GC6 9 THR V 67 THR V 68 HOH V 624 HOH V 751
SITE 3 GC6 9 HOH V 806
SITE 1 GC7 8 LEU S 270 MET S 297 HOH S 638 HOH S 677
SITE 2 GC7 8 HOH S 992 HOH S1002 LEU W 270 ILE W 301
SITE 1 GC8 6 LEU T 270 HOH T 749 LEU X 270 MET X 297
SITE 2 GC8 6 HOH X 726 HOH X 812
SITE 1 GC9 6 LEU U 270 LEU Y 270 MET Y 297 HOH Y 670
SITE 2 GC9 6 HOH Y 724 HOH Y 869
SITE 1 HC1 6 LEU V 270 MET V 297 LEU Z 270 HOH Z 673
SITE 2 HC1 6 HOH Z 728 HOH Z 959
SITE 1 HC2 8 ILE S 282 ARG S 285 ASP S 286 HOH S 680
SITE 2 HC2 8 HOH S 892 HOH S1034 LYS T 252 HOH T 631
SITE 1 HC3 7 ARG T 285 ASP T 286 HOH T 726 HOH T 981
SITE 2 HC3 7 GLU U 249 LYS U 252 HOH U 639
SITE 1 HC4 8 VAL U 149 ILE U 282 ARG U 285 ASP U 286
SITE 2 HC4 8 HOH U 686 HOH U 985 LYS V 252 HOH V 714
SITE 1 HC5 9 LYS S 252 HOH S 656 VAL V 149 ILE V 282
SITE 2 HC5 9 ARG V 285 ASP V 286 HOH V 719 HOH V 808
SITE 3 HC5 9 HOH V1019
SITE 1 HC6 6 LYS W 252 ARG X 285 ASP X 286 HOH X 673
SITE 2 HC6 6 HOH X 753 HOH X 921
SITE 1 HC7 8 LYS X 252 HOH X 710 VAL Y 149 ILE Y 282
SITE 2 HC7 8 ASP Y 286 HOH Y 887 HOH Y 923 HOH Y 951
SITE 1 HC8 7 LYS Y 252 HOH Y 692 ARG Z 285 ASP Z 286
SITE 2 HC8 7 HOH Z 726 HOH Z 752 HOH Z 921
SITE 1 HC9 8 VAL W 149 ILE W 282 ARG W 285 ASP W 286
SITE 2 HC9 8 HOH W 675 HOH W 841 LYS Z 252 HOH Z 623
CRYST1 129.170 174.750 222.270 90.00 97.75 90.00 P 1 21 1 32
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 0.007742 0.000000 0.001054 0.00000
SCALE2 0.000000 0.005722 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004541 0.00000
(ATOM LINES ARE NOT SHOWN.)
END