HEADER LYASE 12-MAY-93 1RBL
TITLE STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE 1,5 BISPHOSPHATE
TITLE 2 CARBOXYLASE(SLASH)OXYGENASE FROM SYNECHOCOCCUS PCC6301
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (LARGE
COMPND 3 CHAIN);
COMPND 4 CHAIN: A, B, C, D, E, F, G, H;
COMPND 5 EC: 4.1.1.39;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (SMALL
COMPND 9 CHAIN);
COMPND 10 CHAIN: M, I, N, J, O, K, P, L;
COMPND 11 EC: 4.1.1.39;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;
SOURCE 3 ORGANISM_TAXID: 269084;
SOURCE 4 STRAIN: PCC 6301;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;
SOURCE 7 ORGANISM_TAXID: 269084;
SOURCE 8 STRAIN: PCC 6301
KEYWDS LYASE(CARBON-CARBON), LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.NEWMAN,S.GUTTERIDGE,C.-I.BRANDEN,T.A.JONES
REVDAT 4 13-JUL-11 1RBL 1 VERSN
REVDAT 3 24-FEB-09 1RBL 1 VERSN
REVDAT 2 08-MAR-95 1RBL 1 AUTHOR JRNL
REVDAT 1 22-JUN-94 1RBL 0
JRNL AUTH J.NEWMAN,C.I.BRANDEN,T.A.JONES
JRNL TITL STRUCTURE DETERMINATION AND REFINEMENT OF RIBULOSE
JRNL TITL 2 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE FROM SYNECHOCOCCUS
JRNL TITL 3 PCC6301.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 49 548 1993
JRNL REFN ISSN 0907-4449
JRNL PMID 15299492
JRNL DOI 10.1107/S090744499300530X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.NEWMAN,S.GUTTERIDGE
REMARK 1 TITL THE X-RAY STRUCTURE OF SYNECHOCOCCUS RIBULOSE BISPHOSPHATE
REMARK 1 TITL 2 CARBOXYLASE(SLASH)OXYGENASE ACTIVATED QUATERNARY COMPLEX AT
REMARK 1 TITL 3 2.2 ANGSTROMS RESOLUTION
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 36496
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 200
REMARK 3 SOLVENT ATOMS : 292
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.26
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.26
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 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:
REMARK 3 THERE ARE SEVEN NON-CRYSTALLOGRAPHIC SYMMETRY OPERATORS,
REMARK 3 AND THESE MUST BE USED TO GENERATE THE ENTIRE L8S8
REMARK 3 MOLECULE. THE FORMAT OF THE FOLLOWING TRANSFORMATIONS IS
REMARK 3 FROM X-PLOR, THUS THE SYMMETRY RELATED CHAINS ARE GENERATED
REMARK 3 BY R'=R*R + T, R=ROTATION MATRIX, T=TRANSLATION.
REMARK 4
REMARK 4 1RBL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 111.95000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 99.85000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.95000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 99.85000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 111.95000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.95000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THESE ARE THE ROTATION/TRANSLATION COMPONENTS TO MAP AN
REMARK 300 LS MONOMER (AM) ONTO THE REST OF THE MOLECULE. THESE
REMARK 300 MATRICES WERE OBTAINED FROM X-PLOR AFTER REFINEMENT OF THE
REMARK 300 WHOLE L8S8 920710.
REMARK 300
REMARK 300 MTRIX 1 TAKES AM TO BI.
REMARK 300
REMARK 300 MTRIX 2 TAKES AM TO CN.
REMARK 300
REMARK 300 MTRIX 3 TAKES AM TO DJ.
REMARK 300
REMARK 300 MTRIX 4 TAKES AM TO EO.
REMARK 300
REMARK 300 MTRIX 5 TAKES AM TO FK.
REMARK 300
REMARK 300 MTRIX 6 TAKES AM TO GP.
REMARK 300
REMARK 300 MTRIX 7 TAKES AM TO HL.
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 APPLY THE FOLLOWING TO CHAINS: A, M, B, I, C, N, D, J, E,
REMARK 350 AND CHAINS: O, F, K, G, P, H, L
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 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 SER A 9
REMARK 475 ALA A 10
REMARK 475 ALA A 11
REMARK 475 ARG M 122
REMARK 475 SER B 9
REMARK 475 ALA B 10
REMARK 475 ALA B 11
REMARK 475 ARG I 122
REMARK 475 SER C 9
REMARK 475 ALA C 10
REMARK 475 ALA C 11
REMARK 475 ARG N 122
REMARK 475 SER D 9
REMARK 475 ALA D 10
REMARK 475 ALA D 11
REMARK 475 ARG J 122
REMARK 475 SER E 9
REMARK 475 ALA E 10
REMARK 475 ALA E 11
REMARK 475 ARG O 122
REMARK 475 SER F 9
REMARK 475 ALA F 10
REMARK 475 ALA F 11
REMARK 475 ARG K 122
REMARK 475 SER G 9
REMARK 475 ALA G 10
REMARK 475 ALA G 11
REMARK 475 ARG P 122
REMARK 475 SER H 9
REMARK 475 ALA H 10
REMARK 475 ALA H 11
REMARK 475 ARG L 122
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 477 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FMT A 478 O1
REMARK 620 2 FMT A 478 O2 43.5
REMARK 620 3 CAP A 476 O2 81.4 100.6
REMARK 620 4 GLU A 204 OE1 106.7 101.5 154.6
REMARK 620 5 CAP A 476 O3 49.3 92.5 70.9 95.7
REMARK 620 6 CAP A 476 O7 137.4 166.5 68.6 90.9 91.5
REMARK 620 7 ASP A 203 OD1 131.0 89.1 100.5 92.3 171.4 85.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 477 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP B 476 O3
REMARK 620 2 CAP B 476 O7 91.5
REMARK 620 3 FMT B 478 O1 49.3 137.4
REMARK 620 4 FMT B 478 O2 92.5 166.5 43.5
REMARK 620 5 CAP B 476 O2 70.9 68.6 81.4 100.6
REMARK 620 6 GLU B 204 OE1 95.7 90.9 106.7 101.6 154.6
REMARK 620 7 ASP B 203 OD1 171.4 85.1 131.0 89.1 100.5 92.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 477 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 203 OD1
REMARK 620 2 GLU C 204 OE1 92.2
REMARK 620 3 CAP C 476 O7 85.1 90.9
REMARK 620 4 FMT C 478 O2 89.1 101.6 166.5
REMARK 620 5 CAP C 476 O3 171.4 95.7 91.5 92.5
REMARK 620 6 CAP C 476 O2 100.5 154.6 68.6 100.6 70.9
REMARK 620 7 FMT C 478 O1 131.0 106.7 137.4 43.5 49.3 81.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 477 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP D 476 O3
REMARK 620 2 FMT D 478 O1 49.3
REMARK 620 3 CAP D 476 O2 71.0 81.4
REMARK 620 4 FMT D 478 O2 92.5 43.5 100.6
REMARK 620 5 GLU D 204 OE1 95.7 106.7 154.6 101.5
REMARK 620 6 CAP D 476 O7 91.5 137.5 68.6 166.5 90.9
REMARK 620 7 ASP D 203 OD1 171.4 131.0 100.5 89.1 92.2 85.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 477 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FMT E 478 O2
REMARK 620 2 GLU E 204 OE1 101.5
REMARK 620 3 ASP E 203 OD1 89.1 92.2
REMARK 620 4 FMT E 478 O1 43.5 106.7 131.0
REMARK 620 5 CAP E 476 O2 100.6 154.6 100.5 81.4
REMARK 620 6 CAP E 476 O7 166.5 90.9 85.1 137.5 68.6
REMARK 620 7 CAP E 476 O3 92.5 95.7 171.4 49.3 71.0 91.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 477 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 FMT F 478 O2
REMARK 620 2 FMT F 478 O1 43.5
REMARK 620 3 CAP F 476 O3 92.5 49.3
REMARK 620 4 ASP F 203 OD1 89.1 130.9 171.4
REMARK 620 5 CAP F 476 O2 100.6 81.4 70.9 100.4
REMARK 620 6 CAP F 476 O7 166.5 137.5 91.5 85.1 68.6
REMARK 620 7 GLU F 204 OE1 101.5 106.7 95.7 92.3 154.6 90.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 477 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU G 204 OE1
REMARK 620 2 FMT G 478 O2 101.5
REMARK 620 3 FMT G 478 O1 106.7 43.5
REMARK 620 4 CAP G 476 O3 95.7 92.5 49.3
REMARK 620 5 CAP G 476 O2 154.6 100.6 81.4 70.9
REMARK 620 6 ASP G 203 OD1 92.3 89.1 131.0 171.4 100.5
REMARK 620 7 CAP G 476 O7 90.9 166.5 137.5 91.5 68.6 85.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 477 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAP H 476 O7
REMARK 620 2 ASP H 203 OD1 85.1
REMARK 620 3 CAP H 476 O2 68.6 100.5
REMARK 620 4 FMT H 478 O2 166.5 89.1 100.6
REMARK 620 5 FMT H 478 O1 137.5 130.9 81.4 43.5
REMARK 620 6 CAP H 476 O3 91.5 171.4 70.9 92.5 49.3
REMARK 620 7 GLU H 204 OE1 90.9 92.2 154.6 101.5 106.7 95.7
REMARK 620 N 1 2 3 4 5 6
REMARK 650
REMARK 650 HELIX
REMARK 650 HELICES A, B, BB, C, AND D PRESENTED ON THE HELIX RECORD
REMARK 650 BELOW ARE THE HELICES OF THE N-TERMINAL DOMAIN.
REMARK 700
REMARK 700 SHEET
REMARK 700 SHEET LN1 IS -2X, +1, +2X.
REMARK 700 THE DSSP RUN DID NOT INDICATE THAT STRAND 2 WAS INDEED A
REMARK 700 STRAND. HOWEVER, THE A/B BARREL IS CLEARLY THAT, SO STRAND
REMARK 700 2 IS INCLUDED AS A "REAL" STRAND.
REMARK 700 SHEET SS1 IS +1,-2X,-1.
REMARK 700 THE SHEET PRESENTED AS *LC1* ON SHEET RECORDS BELOW IS
REMARK 700 ACTUALLY AN EIGHT-STRANDED BETA-BARREL. THIS IS
REMARK 700 REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST
REMARK 700 AND LAST STRANDS ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: MG
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: THE MAGNESIUM BINDING SITE
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: THE BINDING SITE OF THE FIRST PHOSPHATE GROUP OF
REMARK 800 THE CAP
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: THE BINDING SITE OF THE 2ND PHOSPHATE OF CAP
REMARK 800
REMARK 800 SITE_IDENTIFIER: CAB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: OTHER RESIDUES INVOLVED IN BINDING THE CAP
REMARK 800
REMARK 800 SITE_IDENTIFIER: MG2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: MG3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: MG4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: MG5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: MG6
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P6
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P6
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA6
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: MG7
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P7
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P7
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA7
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: MG8
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P8
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P8
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA8
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT E 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT F 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT H 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT G 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 478
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 477
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 477
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE ADVISORY NOTICE
REMARK 999 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.
REMARK 999
REMARK 999 SWISS-PROT ENTRY NAME: RBL_SYNP6
REMARK 999
REMARK 999 SWISS-PROT RESIDUE PDB SEQRES
REMARK 999
REMARK 999 NAME NUMBER NAME CHAIN SEQ/INSERT CODE
REMARK 999 PRO 38 ARG A 41
REMARK 999 VAL 39 PHE A 42
REMARK 999 GLN 88 ALA A 91
REMARK 999 ARG 353 ALA A 356
REMARK 999 ASP 64 ALA M 76
REMARK 999 LYS 66 ALA M 78
REMARK 999 SER 67 ALA M 79
REMARK 999 GLN 97 GLU M 109
REMARK 999 VAL 101 SER M 113
DBREF 1RBL A 9 475 UNP P00880 RBL_SYNP6 6 472
DBREF 1RBL M 2 122 UNP P04716 RBS_SYNP6 1 109
DBREF 1RBL B 9 475 UNP P00880 RBL_SYNP6 6 472
DBREF 1RBL I 2 122 UNP P04716 RBS_SYNP6 1 109
DBREF 1RBL C 9 475 UNP P00880 RBL_SYNP6 6 472
DBREF 1RBL N 2 122 UNP P04716 RBS_SYNP6 1 109
DBREF 1RBL D 9 475 UNP P00880 RBL_SYNP6 6 472
DBREF 1RBL J 2 122 UNP P04716 RBS_SYNP6 1 109
DBREF 1RBL E 9 475 UNP P00880 RBL_SYNP6 6 472
DBREF 1RBL O 2 122 UNP P04716 RBS_SYNP6 1 109
DBREF 1RBL F 9 475 UNP P00880 RBL_SYNP6 6 472
DBREF 1RBL K 2 122 UNP P04716 RBS_SYNP6 1 109
DBREF 1RBL G 9 475 UNP P00880 RBL_SYNP6 6 472
DBREF 1RBL P 2 122 UNP P04716 RBS_SYNP6 1 109
DBREF 1RBL H 9 475 UNP P00880 RBL_SYNP6 6 472
DBREF 1RBL L 2 122 UNP P04716 RBS_SYNP6 1 109
SEQADV 1RBL ARG A 41 UNP P00880 PRO 38 CONFLICT
SEQADV 1RBL PHE A 42 UNP P00880 VAL 39 CONFLICT
SEQADV 1RBL ALA A 91 UNP P00880 GLN 88 CONFLICT
SEQADV 1RBL ALA A 356 UNP P00880 ARG 353 CONFLICT
SEQADV 1RBL ALA M 76 UNP P04716 ASP 63 CONFLICT
SEQADV 1RBL ALA M 78 UNP P04716 LYS 65 CONFLICT
SEQADV 1RBL ALA M 79 UNP P04716 SER 66 CONFLICT
SEQADV 1RBL GLU M 109 UNP P04716 GLN 96 CONFLICT
SEQADV 1RBL SER M 113 UNP P04716 VAL 100 CONFLICT
SEQADV 1RBL ARG B 41 UNP P00880 PRO 38 CONFLICT
SEQADV 1RBL PHE B 42 UNP P00880 VAL 39 CONFLICT
SEQADV 1RBL ALA B 91 UNP P00880 GLN 88 CONFLICT
SEQADV 1RBL ALA B 356 UNP P00880 ARG 353 CONFLICT
SEQADV 1RBL ALA I 76 UNP P04716 ASP 63 CONFLICT
SEQADV 1RBL ALA I 78 UNP P04716 LYS 65 CONFLICT
SEQADV 1RBL ALA I 79 UNP P04716 SER 66 CONFLICT
SEQADV 1RBL GLU I 109 UNP P04716 GLN 96 CONFLICT
SEQADV 1RBL SER I 113 UNP P04716 VAL 100 CONFLICT
SEQADV 1RBL ARG C 41 UNP P00880 PRO 38 CONFLICT
SEQADV 1RBL PHE C 42 UNP P00880 VAL 39 CONFLICT
SEQADV 1RBL ALA C 91 UNP P00880 GLN 88 CONFLICT
SEQADV 1RBL ALA C 356 UNP P00880 ARG 353 CONFLICT
SEQADV 1RBL ALA N 76 UNP P04716 ASP 63 CONFLICT
SEQADV 1RBL ALA N 78 UNP P04716 LYS 65 CONFLICT
SEQADV 1RBL ALA N 79 UNP P04716 SER 66 CONFLICT
SEQADV 1RBL GLU N 109 UNP P04716 GLN 96 CONFLICT
SEQADV 1RBL SER N 113 UNP P04716 VAL 100 CONFLICT
SEQADV 1RBL ARG D 41 UNP P00880 PRO 38 CONFLICT
SEQADV 1RBL PHE D 42 UNP P00880 VAL 39 CONFLICT
SEQADV 1RBL ALA D 91 UNP P00880 GLN 88 CONFLICT
SEQADV 1RBL ALA D 356 UNP P00880 ARG 353 CONFLICT
SEQADV 1RBL ALA J 76 UNP P04716 ASP 63 CONFLICT
SEQADV 1RBL ALA J 78 UNP P04716 LYS 65 CONFLICT
SEQADV 1RBL ALA J 79 UNP P04716 SER 66 CONFLICT
SEQADV 1RBL GLU J 109 UNP P04716 GLN 96 CONFLICT
SEQADV 1RBL SER J 113 UNP P04716 VAL 100 CONFLICT
SEQADV 1RBL ARG E 41 UNP P00880 PRO 38 CONFLICT
SEQADV 1RBL PHE E 42 UNP P00880 VAL 39 CONFLICT
SEQADV 1RBL ALA E 91 UNP P00880 GLN 88 CONFLICT
SEQADV 1RBL ALA E 356 UNP P00880 ARG 353 CONFLICT
SEQADV 1RBL ALA O 76 UNP P04716 ASP 63 CONFLICT
SEQADV 1RBL ALA O 78 UNP P04716 LYS 65 CONFLICT
SEQADV 1RBL ALA O 79 UNP P04716 SER 66 CONFLICT
SEQADV 1RBL GLU O 109 UNP P04716 GLN 96 CONFLICT
SEQADV 1RBL SER O 113 UNP P04716 VAL 100 CONFLICT
SEQADV 1RBL ARG F 41 UNP P00880 PRO 38 CONFLICT
SEQADV 1RBL PHE F 42 UNP P00880 VAL 39 CONFLICT
SEQADV 1RBL ALA F 91 UNP P00880 GLN 88 CONFLICT
SEQADV 1RBL ALA F 356 UNP P00880 ARG 353 CONFLICT
SEQADV 1RBL ALA K 76 UNP P04716 ASP 63 CONFLICT
SEQADV 1RBL ALA K 78 UNP P04716 LYS 65 CONFLICT
SEQADV 1RBL ALA K 79 UNP P04716 SER 66 CONFLICT
SEQADV 1RBL GLU K 109 UNP P04716 GLN 96 CONFLICT
SEQADV 1RBL SER K 113 UNP P04716 VAL 100 CONFLICT
SEQADV 1RBL ARG G 41 UNP P00880 PRO 38 CONFLICT
SEQADV 1RBL PHE G 42 UNP P00880 VAL 39 CONFLICT
SEQADV 1RBL ALA G 91 UNP P00880 GLN 88 CONFLICT
SEQADV 1RBL ALA G 356 UNP P00880 ARG 353 CONFLICT
SEQADV 1RBL ALA P 76 UNP P04716 ASP 63 CONFLICT
SEQADV 1RBL ALA P 78 UNP P04716 LYS 65 CONFLICT
SEQADV 1RBL ALA P 79 UNP P04716 SER 66 CONFLICT
SEQADV 1RBL GLU P 109 UNP P04716 GLN 96 CONFLICT
SEQADV 1RBL SER P 113 UNP P04716 VAL 100 CONFLICT
SEQADV 1RBL ARG H 41 UNP P00880 PRO 38 CONFLICT
SEQADV 1RBL PHE H 42 UNP P00880 VAL 39 CONFLICT
SEQADV 1RBL ALA H 91 UNP P00880 GLN 88 CONFLICT
SEQADV 1RBL ALA H 356 UNP P00880 ARG 353 CONFLICT
SEQADV 1RBL ALA L 76 UNP P04716 ASP 63 CONFLICT
SEQADV 1RBL ALA L 78 UNP P04716 LYS 65 CONFLICT
SEQADV 1RBL ALA L 79 UNP P04716 SER 66 CONFLICT
SEQADV 1RBL GLU L 109 UNP P04716 GLN 96 CONFLICT
SEQADV 1RBL SER L 113 UNP P04716 VAL 100 CONFLICT
SEQRES 1 A 467 SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES 2 A 467 LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES 3 A 467 ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES 4 A 467 VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES 5 A 467 SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES 6 A 467 LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES 7 A 467 ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES 8 A 467 PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES 9 A 467 VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES 10 A 467 GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES 11 A 467 ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES 12 A 467 PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES 13 A 467 TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES 14 A 467 LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES 15 A 467 GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES 16 A 467 GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES 17 A 467 ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES 18 A 467 ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES 19 A 467 THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES 20 A 467 PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES 21 A 467 PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES 22 A 467 LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES 23 A 467 ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES 24 A 467 GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES 25 A 467 SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES 26 A 467 LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES 27 A 467 ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES 28 A 467 ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES 29 A 467 GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES 30 A 467 HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES 31 A 467 VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES 32 A 467 GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES 33 A 467 GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES 34 A 467 TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES 35 A 467 TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES 36 A 467 GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES 1 M 109 SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES 2 M 109 PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES 3 M 109 ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES 4 M 109 LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES 5 M 109 TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES 6 M 109 ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES 7 M 109 SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES 8 M 109 ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES 9 M 109 HIS ARG PRO GLY ARG
SEQRES 1 B 467 SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES 2 B 467 LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES 3 B 467 ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES 4 B 467 VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES 5 B 467 SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES 6 B 467 LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES 7 B 467 ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES 8 B 467 PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES 9 B 467 VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES 10 B 467 GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES 11 B 467 ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES 12 B 467 PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES 13 B 467 TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES 14 B 467 LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES 15 B 467 GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES 16 B 467 GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES 17 B 467 ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES 18 B 467 ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES 19 B 467 THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES 20 B 467 PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES 21 B 467 PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES 22 B 467 LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES 23 B 467 ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES 24 B 467 GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES 25 B 467 SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES 26 B 467 LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES 27 B 467 ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES 28 B 467 ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES 29 B 467 GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES 30 B 467 HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES 31 B 467 VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES 32 B 467 GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES 33 B 467 GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES 34 B 467 TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES 35 B 467 TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES 36 B 467 GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES 1 I 109 SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES 2 I 109 PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES 3 I 109 ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES 4 I 109 LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES 5 I 109 TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES 6 I 109 ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES 7 I 109 SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES 8 I 109 ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES 9 I 109 HIS ARG PRO GLY ARG
SEQRES 1 C 467 SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES 2 C 467 LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES 3 C 467 ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES 4 C 467 VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES 5 C 467 SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES 6 C 467 LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES 7 C 467 ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES 8 C 467 PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES 9 C 467 VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES 10 C 467 GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES 11 C 467 ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES 12 C 467 PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES 13 C 467 TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES 14 C 467 LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES 15 C 467 GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES 16 C 467 GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES 17 C 467 ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES 18 C 467 ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES 19 C 467 THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES 20 C 467 PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES 21 C 467 PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES 22 C 467 LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES 23 C 467 ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES 24 C 467 GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES 25 C 467 SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES 26 C 467 LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES 27 C 467 ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES 28 C 467 ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES 29 C 467 GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES 30 C 467 HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES 31 C 467 VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES 32 C 467 GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES 33 C 467 GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES 34 C 467 TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES 35 C 467 TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES 36 C 467 GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES 1 N 109 SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES 2 N 109 PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES 3 N 109 ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES 4 N 109 LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES 5 N 109 TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES 6 N 109 ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES 7 N 109 SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES 8 N 109 ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES 9 N 109 HIS ARG PRO GLY ARG
SEQRES 1 D 467 SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES 2 D 467 LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES 3 D 467 ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES 4 D 467 VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES 5 D 467 SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES 6 D 467 LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES 7 D 467 ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES 8 D 467 PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES 9 D 467 VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES 10 D 467 GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES 11 D 467 ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES 12 D 467 PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES 13 D 467 TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES 14 D 467 LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES 15 D 467 GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES 16 D 467 GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES 17 D 467 ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES 18 D 467 ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES 19 D 467 THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES 20 D 467 PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES 21 D 467 PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES 22 D 467 LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES 23 D 467 ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES 24 D 467 GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES 25 D 467 SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES 26 D 467 LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES 27 D 467 ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES 28 D 467 ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES 29 D 467 GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES 30 D 467 HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES 31 D 467 VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES 32 D 467 GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES 33 D 467 GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES 34 D 467 TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES 35 D 467 TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES 36 D 467 GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES 1 J 109 SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES 2 J 109 PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES 3 J 109 ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES 4 J 109 LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES 5 J 109 TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES 6 J 109 ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES 7 J 109 SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES 8 J 109 ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES 9 J 109 HIS ARG PRO GLY ARG
SEQRES 1 E 467 SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES 2 E 467 LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES 3 E 467 ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES 4 E 467 VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES 5 E 467 SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES 6 E 467 LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES 7 E 467 ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES 8 E 467 PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES 9 E 467 VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES 10 E 467 GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES 11 E 467 ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES 12 E 467 PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES 13 E 467 TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES 14 E 467 LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES 15 E 467 GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES 16 E 467 GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES 17 E 467 ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES 18 E 467 ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES 19 E 467 THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES 20 E 467 PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES 21 E 467 PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES 22 E 467 LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES 23 E 467 ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES 24 E 467 GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES 25 E 467 SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES 26 E 467 LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES 27 E 467 ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES 28 E 467 ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES 29 E 467 GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES 30 E 467 HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES 31 E 467 VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES 32 E 467 GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES 33 E 467 GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES 34 E 467 TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES 35 E 467 TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES 36 E 467 GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES 1 O 109 SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES 2 O 109 PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES 3 O 109 ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES 4 O 109 LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES 5 O 109 TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES 6 O 109 ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES 7 O 109 SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES 8 O 109 ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES 9 O 109 HIS ARG PRO GLY ARG
SEQRES 1 F 467 SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES 2 F 467 LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES 3 F 467 ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES 4 F 467 VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES 5 F 467 SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES 6 F 467 LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES 7 F 467 ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES 8 F 467 PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES 9 F 467 VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES 10 F 467 GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES 11 F 467 ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES 12 F 467 PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES 13 F 467 TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES 14 F 467 LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES 15 F 467 GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES 16 F 467 GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES 17 F 467 ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES 18 F 467 ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES 19 F 467 THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES 20 F 467 PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES 21 F 467 PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES 22 F 467 LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES 23 F 467 ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES 24 F 467 GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES 25 F 467 SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES 26 F 467 LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES 27 F 467 ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES 28 F 467 ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES 29 F 467 GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES 30 F 467 HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES 31 F 467 VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES 32 F 467 GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES 33 F 467 GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES 34 F 467 TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES 35 F 467 TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES 36 F 467 GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES 1 K 109 SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES 2 K 109 PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES 3 K 109 ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES 4 K 109 LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES 5 K 109 TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES 6 K 109 ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES 7 K 109 SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES 8 K 109 ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES 9 K 109 HIS ARG PRO GLY ARG
SEQRES 1 G 467 SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES 2 G 467 LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES 3 G 467 ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES 4 G 467 VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES 5 G 467 SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES 6 G 467 LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES 7 G 467 ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES 8 G 467 PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES 9 G 467 VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES 10 G 467 GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES 11 G 467 ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES 12 G 467 PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES 13 G 467 TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES 14 G 467 LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES 15 G 467 GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES 16 G 467 GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES 17 G 467 ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES 18 G 467 ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES 19 G 467 THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES 20 G 467 PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES 21 G 467 PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES 22 G 467 LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES 23 G 467 ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES 24 G 467 GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES 25 G 467 SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES 26 G 467 LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES 27 G 467 ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES 28 G 467 ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES 29 G 467 GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES 30 G 467 HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES 31 G 467 VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES 32 G 467 GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES 33 G 467 GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES 34 G 467 TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES 35 G 467 TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES 36 G 467 GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES 1 P 109 SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES 2 P 109 PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES 3 P 109 ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES 4 P 109 LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES 5 P 109 TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES 6 P 109 ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES 7 P 109 SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES 8 P 109 ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES 9 P 109 HIS ARG PRO GLY ARG
SEQRES 1 H 467 SER ALA ALA GLY TYR LYS ALA GLY VAL LYS ASP TYR LYS
SEQRES 2 H 467 LEU THR TYR TYR THR PRO ASP TYR THR PRO LYS ASP THR
SEQRES 3 H 467 ASP LEU LEU ALA ALA PHE ARG PHE SER PRO GLN PRO GLY
SEQRES 4 H 467 VAL PRO ALA ASP GLU ALA GLY ALA ALA ILE ALA ALA GLU
SEQRES 5 H 467 SER SER THR GLY THR TRP THR THR VAL TRP THR ASP LEU
SEQRES 6 H 467 LEU THR ASP MET ASP ARG TYR LYS GLY LYS CYS TYR HIS
SEQRES 7 H 467 ILE GLU PRO VAL ALA GLY GLU GLU ASN SER TYR PHE ALA
SEQRES 8 H 467 PHE ILE ALA TYR PRO LEU ASP LEU PHE GLU GLU GLY SER
SEQRES 9 H 467 VAL THR ASN ILE LEU THR SER ILE VAL GLY ASN VAL PHE
SEQRES 10 H 467 GLY PHE LYS ALA ILE ARG SER LEU ARG LEU GLU ASP ILE
SEQRES 11 H 467 ARG PHE PRO VAL ALA LEU VAL LYS THR PHE GLN GLY PRO
SEQRES 12 H 467 PRO HIS GLY ILE GLN VAL GLU ARG ASP LEU LEU ASN LYS
SEQRES 13 H 467 TYR GLY ARG PRO MET LEU GLY CYS THR ILE LYS PRO LYS
SEQRES 14 H 467 LEU GLY LEU SER ALA LYS ASN TYR GLY ARG ALA VAL TYR
SEQRES 15 H 467 GLU CYS LEU ARG GLY GLY LEU ASP PHE THR LYS ASP ASP
SEQRES 16 H 467 GLU ASN ILE ASN SER GLN PRO PHE GLN ARG TRP ARG ASP
SEQRES 17 H 467 ARG PHE LEU PHE VAL ALA ASP ALA ILE HIS LYS SER GLN
SEQRES 18 H 467 ALA GLU THR GLY GLU ILE LYS GLY HIS TYR LEU ASN VAL
SEQRES 19 H 467 THR ALA PRO THR CYS GLU GLU MET MET LYS ARG ALA GLU
SEQRES 20 H 467 PHE ALA LYS GLU LEU GLY MET PRO ILE ILE MET HIS ASP
SEQRES 21 H 467 PHE LEU THR ALA GLY PHE THR ALA ASN THR THR LEU ALA
SEQRES 22 H 467 LYS TRP CYS ARG ASP ASN GLY VAL LEU LEU HIS ILE HIS
SEQRES 23 H 467 ARG ALA MET HIS ALA VAL ILE ASP ARG GLN ARG ASN HIS
SEQRES 24 H 467 GLY ILE HIS PHE ARG VAL LEU ALA LYS CYS LEU ARG LEU
SEQRES 25 H 467 SER GLY GLY ASP HIS LEU HIS SER GLY THR VAL VAL GLY
SEQRES 26 H 467 LYS LEU GLU GLY ASP LYS ALA SER THR LEU GLY PHE VAL
SEQRES 27 H 467 ASP LEU MET ARG GLU ASP HIS ILE GLU ALA ASP ARG SER
SEQRES 28 H 467 ARG GLY VAL PHE PHE THR GLN ASP TRP ALA SER MET PRO
SEQRES 29 H 467 GLY VAL LEU PRO VAL ALA SER GLY GLY ILE HIS VAL TRP
SEQRES 30 H 467 HIS MET PRO ALA LEU VAL GLU ILE PHE GLY ASP ASP SER
SEQRES 31 H 467 VAL LEU GLN PHE GLY GLY GLY THR LEU GLY HIS PRO TRP
SEQRES 32 H 467 GLY ASN ALA PRO GLY ALA THR ALA ASN ARG VAL ALA LEU
SEQRES 33 H 467 GLU ALA CYS VAL GLN ALA ARG ASN GLU GLY ARG ASP LEU
SEQRES 34 H 467 TYR ARG GLU GLY GLY ASP ILE LEU ARG GLU ALA GLY LYS
SEQRES 35 H 467 TRP SER PRO GLU LEU ALA ALA ALA LEU ASP LEU TRP LYS
SEQRES 36 H 467 GLU ILE LYS PHE GLU PHE GLU THR MET ASP LYS LEU
SEQRES 1 L 109 SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU THR
SEQRES 2 L 109 PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE ALA
SEQRES 3 L 109 ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS PRO
SEQRES 4 L 109 LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU PHE
SEQRES 5 L 109 TYR TRP THR MET TRP LYS LEU PRO LEU PHE ALA CYS ALA
SEQRES 6 L 109 ALA PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS ARG
SEQRES 7 L 109 SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY PHE
SEQRES 8 L 109 ASP ASN ILE LYS GLU CYS GLN THR SER SER PHE ILE VAL
SEQRES 9 L 109 HIS ARG PRO GLY ARG
HET MG A 477 1
HET MG B 477 1
HET MG C 477 1
HET MG D 477 1
HET MG E 477 1
HET MG F 477 1
HET MG G 477 1
HET MG H 477 1
HET CAP A 476 21
HET CAP B 476 21
HET CAP C 476 21
HET CAP D 476 21
HET CAP E 476 21
HET CAP F 476 21
HET CAP G 476 21
HET CAP H 476 21
HET FMT A 478 3
HET FMT B 478 3
HET FMT C 478 3
HET FMT D 478 3
HET FMT E 478 3
HET FMT F 478 3
HET FMT G 478 3
HET FMT H 478 3
HETNAM MG MAGNESIUM ION
HETNAM CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE
HETNAM FMT FORMIC ACID
FORMUL 17 MG 8(MG 2+)
FORMUL 25 CAP 8(C6 H14 O13 P2)
FORMUL 33 FMT 8(C H2 O2)
FORMUL 41 HOH *292(H2 O)
HELIX 1 A LYS A 21 TYR A 24 1SEE REMARK 8. 4
HELIX 2 B ALA A 50 GLU A 60 1SEE REMARK 8. 11
HELIX 3 BB MET A 77 TYR A 80 1SEE REMARK 8. 4
HELIX 4 C VAL A 113 VAL A 121 1SEE REMARK 8. 9
HELIX 5 D VAL A 142 VAL A 145 1SEE REMARK 8. 4
HELIX 6 E ILE A 155 LEU A 162 1LINKS N-TERM & C-TERM DOMAINS 8
HELIX 7 1 ALA A 182 ARG A 194 1FIRST HELIX OF A/B BARREL 13
HELIX 8 2 TRP A 214 THR A 232 12ND HELIX OF A/B BARREL 19
HELIX 9 3 CYS A 247 GLU A 259 13RD HELIX OF A/B BARREL 13
HELIX 10 4 PHE A 269 ASN A 287 14TH HELIX OF A/B BARREL 19
HELIX 11 F HIS A 298 ASP A 302 1 5
HELIX 12 5 PHE A 311 SER A 321 15TH HELIX OF A/B BARREL 11
HELIX 13 6 LYS A 339 ARG A 350 16TH HELIX OF A/B BARREL 12
HELIX 14 7 MET A 387 PHE A 394 17TH HELIX OF A/B BARREL 8
HELIX 15 P GLY A 404 LEU A 407 1P FOR PHOSPHATE BINDING HELIX 4
HELIX 16 8 ASN A 413 GLU A 433 18TH HELIX OF A/B BARREL 21
HELIX 17 G LEU A 437 TRP A 451 1 15
HELIX 18 H PRO A 453 TRP A 462 1 10
HELIX 19 B' TYR A 80 GLU A 93 12ND HELIX - SMALL SUBUNIT 14
HELIX 20 A LYS B 21 TYR B 24 1SEE REMARK 8. 4
HELIX 21 B ALA B 50 GLU B 60 1SEE REMARK 8. 11
HELIX 22 BB MET B 77 TYR B 80 1SEE REMARK 8. 4
HELIX 23 C VAL B 113 VAL B 121 1SEE REMARK 8. 9
HELIX 24 D VAL B 142 VAL B 145 1SEE REMARK 8. 4
HELIX 25 E ILE B 155 LEU B 162 1LINKS N-TERM & C-TERM DOMAINS 8
HELIX 26 1 ALA B 182 ARG B 194 1FIRST HELIX OF A/B BARREL 13
HELIX 27 2 TRP B 214 THR B 232 12ND HELIX OF A/B BARREL 19
HELIX 28 3 CYS B 247 GLU B 259 13RD HELIX OF A/B BARREL 13
HELIX 29 4 PHE B 269 ASN B 287 14TH HELIX OF A/B BARREL 19
HELIX 30 F HIS B 298 ASP B 302 1 5
HELIX 31 5 PHE B 311 SER B 321 15TH HELIX OF A/B BARREL 11
HELIX 32 6 LYS B 339 ARG B 350 16TH HELIX OF A/B BARREL 12
HELIX 33 7 MET B 387 PHE B 394 17TH HELIX OF A/B BARREL 8
HELIX 34 P GLY B 404 LEU B 407 1P FOR PHOSPHATE BINDING HELIX 4
HELIX 35 8 ASN B 413 GLU B 433 18TH HELIX OF A/B BARREL 21
HELIX 36 G LEU B 437 TRP B 451 1 15
HELIX 37 H PRO B 453 TRP B 462 1 10
HELIX 38 B' TYR B 80 GLU B 93 12ND HELIX - SMALL SUBUNIT 14
HELIX 39 A LYS C 21 TYR C 24 1SEE REMARK 8. 4
HELIX 40 B ALA C 50 GLU C 60 1SEE REMARK 8. 11
HELIX 41 BB MET C 77 TYR C 80 1SEE REMARK 8. 4
HELIX 42 C VAL C 113 VAL C 121 1SEE REMARK 8. 9
HELIX 43 D VAL C 142 VAL C 145 1SEE REMARK 8. 4
HELIX 44 E ILE C 155 LEU C 162 1LINKS N-TERM & C-TERM DOMAINS 8
HELIX 45 1 ALA C 182 ARG C 194 1FIRST HELIX OF A/B BARREL 13
HELIX 46 2 TRP C 214 THR C 232 12ND HELIX OF A/B BARREL 19
HELIX 47 3 CYS C 247 GLU C 259 13RD HELIX OF A/B BARREL 13
HELIX 48 4 PHE C 269 ASN C 287 14TH HELIX OF A/B BARREL 19
HELIX 49 F HIS C 298 ASP C 302 1 5
HELIX 50 5 PHE C 311 SER C 321 15TH HELIX OF A/B BARREL 11
HELIX 51 6 LYS C 339 ARG C 350 16TH HELIX OF A/B BARREL 12
HELIX 52 7 MET C 387 PHE C 394 17TH HELIX OF A/B BARREL 8
HELIX 53 P GLY C 404 LEU C 407 1P FOR PHOSPHATE BINDING HELIX 4
HELIX 54 8 ASN C 413 GLU C 433 18TH HELIX OF A/B BARREL 21
HELIX 55 G LEU C 437 TRP C 451 1 15
HELIX 56 H PRO C 453 TRP C 462 1 10
HELIX 57 B' TYR C 80 GLU C 93 12ND HELIX - SMALL SUBUNIT 14
HELIX 58 A LYS D 21 TYR D 24 1SEE REMARK 8. 4
HELIX 59 B ALA D 50 GLU D 60 1SEE REMARK 8. 11
HELIX 60 BB MET D 77 TYR D 80 1SEE REMARK 8. 4
HELIX 61 C VAL D 113 VAL D 121 1SEE REMARK 8. 9
HELIX 62 D VAL D 142 VAL D 145 1SEE REMARK 8. 4
HELIX 63 E ILE D 155 LEU D 162 1LINKS N-TERM & C-TERM DOMAINS 8
HELIX 64 1 ALA D 182 ARG D 194 1FIRST HELIX OF A/B BARREL 13
HELIX 65 2 TRP D 214 THR D 232 12ND HELIX OF A/B BARREL 19
HELIX 66 3 CYS D 247 GLU D 259 13RD HELIX OF A/B BARREL 13
HELIX 67 4 PHE D 269 ASN D 287 14TH HELIX OF A/B BARREL 19
HELIX 68 F HIS D 298 ASP D 302 1 5
HELIX 69 5 PHE D 311 SER D 321 15TH HELIX OF A/B BARREL 11
HELIX 70 6 LYS D 339 ARG D 350 16TH HELIX OF A/B BARREL 12
HELIX 71 7 MET D 387 PHE D 394 17TH HELIX OF A/B BARREL 8
HELIX 72 P GLY D 404 LEU D 407 1P FOR PHOSPHATE BINDING HELIX 4
HELIX 73 8 ASN D 413 GLU D 433 18TH HELIX OF A/B BARREL 21
HELIX 74 G LEU D 437 TRP D 451 1 15
HELIX 75 H PRO D 453 TRP D 462 1 10
HELIX 76 B' TYR D 80 GLU D 93 12ND HELIX - SMALL SUBUNIT 14
HELIX 77 A LYS E 21 TYR E 24 1SEE REMARK 8. 4
HELIX 78 B ALA E 50 GLU E 60 1SEE REMARK 8. 11
HELIX 79 BB MET E 77 TYR E 80 1SEE REMARK 8. 4
HELIX 80 C VAL E 113 VAL E 121 1SEE REMARK 8. 9
HELIX 81 D VAL E 142 VAL E 145 1SEE REMARK 8. 4
HELIX 82 E ILE E 155 LEU E 162 1LINKS N-TERM & C-TERM DOMAINS 8
HELIX 83 1 ALA E 182 ARG E 194 1FIRST HELIX OF A/B BARREL 13
HELIX 84 2 TRP E 214 THR E 232 12ND HELIX OF A/B BARREL 19
HELIX 85 3 CYS E 247 GLU E 259 13RD HELIX OF A/B BARREL 13
HELIX 86 4 PHE E 269 ASN E 287 14TH HELIX OF A/B BARREL 19
HELIX 87 F HIS E 298 ASP E 302 1 5
HELIX 88 5 PHE E 311 SER E 321 15TH HELIX OF A/B BARREL 11
HELIX 89 6 LYS E 339 ARG E 350 16TH HELIX OF A/B BARREL 12
HELIX 90 7 MET E 387 PHE E 394 17TH HELIX OF A/B BARREL 8
HELIX 91 P GLY E 404 LEU E 407 1P FOR PHOSPHATE BINDING HELIX 4
HELIX 92 8 ASN E 413 GLU E 433 18TH HELIX OF A/B BARREL 21
HELIX 93 G LEU E 437 TRP E 451 1 15
HELIX 94 H PRO E 453 TRP E 462 1 10
HELIX 95 B' TYR E 80 GLU E 93 12ND HELIX - SMALL SUBUNIT 14
HELIX 96 A LYS F 21 TYR F 24 1SEE REMARK 8. 4
HELIX 97 B ALA F 50 GLU F 60 1SEE REMARK 8. 11
HELIX 98 BB MET F 77 TYR F 80 1SEE REMARK 8. 4
HELIX 99 C VAL F 113 VAL F 121 1SEE REMARK 8. 9
HELIX 100 D VAL F 142 VAL F 145 1SEE REMARK 8. 4
HELIX 101 E ILE F 155 LEU F 162 1LINKS N-TERM & C-TERM DOMAINS 8
HELIX 102 1 ALA F 182 ARG F 194 1FIRST HELIX OF A/B BARREL 13
HELIX 103 2 TRP F 214 THR F 232 12ND HELIX OF A/B BARREL 19
HELIX 104 3 CYS F 247 GLU F 259 13RD HELIX OF A/B BARREL 13
HELIX 105 4 PHE F 269 ASN F 287 14TH HELIX OF A/B BARREL 19
HELIX 106 F HIS F 298 ASP F 302 1 5
HELIX 107 5 PHE F 311 SER F 321 15TH HELIX OF A/B BARREL 11
HELIX 108 6 LYS F 339 ARG F 350 16TH HELIX OF A/B BARREL 12
HELIX 109 7 MET F 387 PHE F 394 17TH HELIX OF A/B BARREL 8
HELIX 110 P GLY F 404 LEU F 407 1P FOR PHOSPHATE BINDING HELIX 4
HELIX 111 8 ASN F 413 GLU F 433 18TH HELIX OF A/B BARREL 21
HELIX 112 G LEU F 437 TRP F 451 1 15
HELIX 113 H PRO F 453 TRP F 462 1 10
HELIX 114 B' TYR F 80 GLU F 93 12ND HELIX - SMALL SUBUNIT 14
HELIX 115 A LYS G 21 TYR G 24 1SEE REMARK 8. 4
HELIX 116 B ALA G 50 GLU G 60 1SEE REMARK 8. 11
HELIX 117 BB MET G 77 TYR G 80 1SEE REMARK 8. 4
HELIX 118 C VAL G 113 VAL G 121 1SEE REMARK 8. 9
HELIX 119 D VAL G 142 VAL G 145 1SEE REMARK 8. 4
HELIX 120 E ILE G 155 LEU G 162 1LINKS N-TERM & C-TERM DOMAINS 8
HELIX 121 1 ALA G 182 ARG G 194 1FIRST HELIX OF A/B BARREL 13
HELIX 122 2 TRP G 214 THR G 232 12ND HELIX OF A/B BARREL 19
HELIX 123 3 CYS G 247 GLU G 259 13RD HELIX OF A/B BARREL 13
HELIX 124 4 PHE G 269 ASN G 287 14TH HELIX OF A/B BARREL 19
HELIX 125 F HIS G 298 ASP G 302 1 5
HELIX 126 5 PHE G 311 SER G 321 15TH HELIX OF A/B BARREL 11
HELIX 127 6 LYS G 339 ARG G 350 16TH HELIX OF A/B BARREL 12
HELIX 128 7 MET G 387 PHE G 394 17TH HELIX OF A/B BARREL 8
HELIX 129 P GLY G 404 LEU G 407 1P FOR PHOSPHATE BINDING HELIX 4
HELIX 130 8 ASN G 413 GLU G 433 18TH HELIX OF A/B BARREL 21
HELIX 131 G LEU G 437 TRP G 451 1 15
HELIX 132 H PRO G 453 TRP G 462 1 10
HELIX 133 B' TYR G 80 GLU G 93 12ND HELIX - SMALL SUBUNIT 14
HELIX 134 A LYS H 21 TYR H 24 1SEE REMARK 8. 4
HELIX 135 B ALA H 50 GLU H 60 1SEE REMARK 8. 11
HELIX 136 BB MET H 77 TYR H 80 1SEE REMARK 8. 4
HELIX 137 C VAL H 113 VAL H 121 1SEE REMARK 8. 9
HELIX 138 D VAL H 142 VAL H 145 1SEE REMARK 8. 4
HELIX 139 E ILE H 155 LEU H 162 1LINKS N-TERM & C-TERM DOMAINS 8
HELIX 140 1 ALA H 182 ARG H 194 1FIRST HELIX OF A/B BARREL 13
HELIX 141 2 TRP H 214 THR H 232 12ND HELIX OF A/B BARREL 19
HELIX 142 3 CYS H 247 GLU H 259 13RD HELIX OF A/B BARREL 13
HELIX 143 4 PHE H 269 ASN H 287 14TH HELIX OF A/B BARREL 19
HELIX 144 F HIS H 298 ASP H 302 1 5
HELIX 145 5 PHE H 311 SER H 321 15TH HELIX OF A/B BARREL 11
HELIX 146 6 LYS H 339 ARG H 350 16TH HELIX OF A/B BARREL 12
HELIX 147 7 MET H 387 PHE H 394 17TH HELIX OF A/B BARREL 8
HELIX 148 P GLY H 404 LEU H 407 1P FOR PHOSPHATE BINDING HELIX 4
HELIX 149 8 ASN H 413 GLU H 433 18TH HELIX OF A/B BARREL 21
HELIX 150 G LEU H 437 TRP H 451 1 15
HELIX 151 H PRO H 453 TRP H 462 1 10
HELIX 152 B' TYR H 80 GLU H 93 12ND HELIX - SMALL SUBUNIT 14
SHEET 1 LN1 4 LYS A 83 PRO A 89 0
SHEET 2 LN1 4 SER A 96 TYR A 103 -1
SHEET 3 LN1 4 LEU A 36 PRO A 44 -1
SHEET 4 LN1 4 ILE A 130 ARG A 139 -1
SHEET 1 LC1 9 MET A 169 GLY A 171 0
SHEET 2 LC1 9 THR A 200 ASP A 202 1
SHEET 3 LC1 9 LEU A 240 ASN A 241 1
SHEET 4 LC1 9 ILE A 264 ASP A 268 1
SHEET 5 LC1 9 LEU A 290 HIS A 294 1
SHEET 6 LC1 9 HIS A 325 HIS A 327 1
SHEET 7 LC1 9 LEU A 375 SER A 379 1
SHEET 8 LC1 9 VAL A 399 GLN A 401 1
SHEET 9 LC1 9 MET A 169 GLY A 171 1
SHEET 1 SS1 4 THR M 68 MET M 69 0
SHEET 2 SS1 4 HIS M 39 ASN M 45 -1
SHEET 3 SS1 4 TYR M 98 ASP M 105 -1
SHEET 4 SS1 4 CYS M 110 HIS M 118 -1
SHEET 1 LN2 4 LYS B 83 PRO B 89 0
SHEET 2 LN2 4 SER B 96 TYR B 103 -1
SHEET 3 LN2 4 LEU B 36 PRO B 44 -1
SHEET 4 LN2 4 ILE B 130 ARG B 139 -1
SHEET 1 LC2 9 MET B 169 GLY B 171 0
SHEET 2 LC2 9 THR B 200 ASP B 202 1
SHEET 3 LC2 9 LEU B 240 ASN B 241 1
SHEET 4 LC2 9 ILE B 264 ASP B 268 1
SHEET 5 LC2 9 LEU B 290 HIS B 294 1
SHEET 6 LC2 9 HIS B 325 HIS B 327 1
SHEET 7 LC2 9 LEU B 375 SER B 379 1
SHEET 8 LC2 9 VAL B 399 GLN B 401 1
SHEET 9 LC2 9 MET B 169 GLY B 171 1
SHEET 1 SS2 4 THR I 68 MET I 69 0
SHEET 2 SS2 4 HIS I 39 ASN I 45 -1
SHEET 3 SS2 4 TYR I 98 ASP I 105 -1
SHEET 4 SS2 4 CYS I 110 HIS I 118 -1
SHEET 1 LN3 4 LYS C 83 PRO C 89 0
SHEET 2 LN3 4 SER C 96 TYR C 103 -1
SHEET 3 LN3 4 LEU C 36 PRO C 44 -1
SHEET 4 LN3 4 ILE C 130 ARG C 139 -1
SHEET 1 LC3 9 MET C 169 GLY C 171 0
SHEET 2 LC3 9 THR C 200 ASP C 202 1
SHEET 3 LC3 9 LEU C 240 ASN C 241 1
SHEET 4 LC3 9 ILE C 264 ASP C 268 1
SHEET 5 LC3 9 LEU C 290 HIS C 294 1
SHEET 6 LC3 9 HIS C 325 HIS C 327 1
SHEET 7 LC3 9 LEU C 375 SER C 379 1
SHEET 8 LC3 9 VAL C 399 GLN C 401 1
SHEET 9 LC3 9 MET C 169 GLY C 171 1
SHEET 1 SS3 4 THR N 68 MET N 69 0
SHEET 2 SS3 4 HIS N 39 ASN N 45 -1
SHEET 3 SS3 4 TYR N 98 ASP N 105 -1
SHEET 4 SS3 4 CYS N 110 HIS N 118 -1
SHEET 1 LN4 4 LYS D 83 PRO D 89 0
SHEET 2 LN4 4 SER D 96 TYR D 103 -1
SHEET 3 LN4 4 LEU D 36 PRO D 44 -1
SHEET 4 LN4 4 ILE D 130 ARG D 139 -1
SHEET 1 LC4 9 MET D 169 GLY D 171 0
SHEET 2 LC4 9 THR D 200 ASP D 202 1
SHEET 3 LC4 9 LEU D 240 ASN D 241 1
SHEET 4 LC4 9 ILE D 264 ASP D 268 1
SHEET 5 LC4 9 LEU D 290 HIS D 294 1
SHEET 6 LC4 9 HIS D 325 HIS D 327 1
SHEET 7 LC4 9 LEU D 375 SER D 379 1
SHEET 8 LC4 9 VAL D 399 GLN D 401 1
SHEET 9 LC4 9 MET D 169 GLY D 171 1
SHEET 1 SS4 4 THR J 68 MET J 69 0
SHEET 2 SS4 4 HIS J 39 ASN J 45 -1
SHEET 3 SS4 4 TYR J 98 ASP J 105 -1
SHEET 4 SS4 4 CYS J 110 HIS J 118 -1
SHEET 1 LN5 4 LYS E 83 PRO E 89 0
SHEET 2 LN5 4 SER E 96 TYR E 103 -1
SHEET 3 LN5 4 LEU E 36 PRO E 44 -1
SHEET 4 LN5 4 ILE E 130 ARG E 139 -1
SHEET 1 LC5 9 MET E 169 GLY E 171 0
SHEET 2 LC5 9 THR E 200 ASP E 202 1
SHEET 3 LC5 9 LEU E 240 ASN E 241 1
SHEET 4 LC5 9 ILE E 264 ASP E 268 1
SHEET 5 LC5 9 LEU E 290 HIS E 294 1
SHEET 6 LC5 9 HIS E 325 HIS E 327 1
SHEET 7 LC5 9 LEU E 375 SER E 379 1
SHEET 8 LC5 9 VAL E 399 GLN E 401 1
SHEET 9 LC5 9 MET E 169 GLY E 171 1
SHEET 1 SS5 4 THR O 68 MET O 69 0
SHEET 2 SS5 4 HIS O 39 ASN O 45 -1
SHEET 3 SS5 4 TYR O 98 ASP O 105 -1
SHEET 4 SS5 4 CYS O 110 HIS O 118 -1
SHEET 1 LN6 4 LYS F 83 PRO F 89 0
SHEET 2 LN6 4 SER F 96 TYR F 103 -1
SHEET 3 LN6 4 LEU F 36 PRO F 44 -1
SHEET 4 LN6 4 ILE F 130 ARG F 139 -1
SHEET 1 LC6 9 MET F 169 GLY F 171 0
SHEET 2 LC6 9 THR F 200 ASP F 202 1
SHEET 3 LC6 9 LEU F 240 ASN F 241 1
SHEET 4 LC6 9 ILE F 264 ASP F 268 1
SHEET 5 LC6 9 LEU F 290 HIS F 294 1
SHEET 6 LC6 9 HIS F 325 HIS F 327 1
SHEET 7 LC6 9 LEU F 375 SER F 379 1
SHEET 8 LC6 9 VAL F 399 GLN F 401 1
SHEET 9 LC6 9 MET F 169 GLY F 171 1
SHEET 1 SS6 4 THR K 68 MET K 69 0
SHEET 2 SS6 4 HIS K 39 ASN K 45 -1
SHEET 3 SS6 4 TYR K 98 ASP K 105 -1
SHEET 4 SS6 4 CYS K 110 HIS K 118 -1
SHEET 1 LN7 4 LYS G 83 PRO G 89 0
SHEET 2 LN7 4 SER G 96 TYR G 103 -1
SHEET 3 LN7 4 LEU G 36 PRO G 44 -1
SHEET 4 LN7 4 ILE G 130 ARG G 139 -1
SHEET 1 LC7 9 MET G 169 GLY G 171 0
SHEET 2 LC7 9 THR G 200 ASP G 202 1
SHEET 3 LC7 9 LEU G 240 ASN G 241 1
SHEET 4 LC7 9 ILE G 264 ASP G 268 1
SHEET 5 LC7 9 LEU G 290 HIS G 294 1
SHEET 6 LC7 9 HIS G 325 HIS G 327 1
SHEET 7 LC7 9 LEU G 375 SER G 379 1
SHEET 8 LC7 9 VAL G 399 GLN G 401 1
SHEET 9 LC7 9 MET G 169 GLY G 171 1
SHEET 1 SS7 4 THR P 68 MET P 69 0
SHEET 2 SS7 4 HIS P 39 ASN P 45 -1
SHEET 3 SS7 4 TYR P 98 ASP P 105 -1
SHEET 4 SS7 4 CYS P 110 HIS P 118 -1
SHEET 1 LN8 4 LYS H 83 PRO H 89 0
SHEET 2 LN8 4 SER H 96 TYR H 103 -1
SHEET 3 LN8 4 LEU H 36 PRO H 44 -1
SHEET 4 LN8 4 ILE H 130 ARG H 139 -1
SHEET 1 LC8 9 MET H 169 GLY H 171 0
SHEET 2 LC8 9 THR H 200 ASP H 202 1
SHEET 3 LC8 9 LEU H 240 ASN H 241 1
SHEET 4 LC8 9 ILE H 264 ASP H 268 1
SHEET 5 LC8 9 LEU H 290 HIS H 294 1
SHEET 6 LC8 9 HIS H 325 HIS H 327 1
SHEET 7 LC8 9 LEU H 375 SER H 379 1
SHEET 8 LC8 9 VAL H 399 GLN H 401 1
SHEET 9 LC8 9 MET H 169 GLY H 171 1
SHEET 1 SS8 4 THR L 68 MET L 69 0
SHEET 2 SS8 4 HIS L 39 ASN L 45 -1
SHEET 3 SS8 4 TYR L 98 ASP L 105 -1
SHEET 4 SS8 4 CYS L 110 HIS L 118 -1
SSBOND 1 CYS A 247 CYS B 247 1555 1555 2.19
SSBOND 2 CYS C 247 CYS D 247 1555 1555 2.18
SSBOND 3 CYS E 247 CYS F 247 1555 1555 2.18
SSBOND 4 CYS G 247 CYS H 247 1555 1555 2.23
LINK NZ LYS A 201 C FMT A 478 1555 1555 1.45
LINK NZ LYS B 201 C FMT B 478 1555 1555 1.45
LINK NZ LYS C 201 C FMT C 478 1555 1555 1.45
LINK NZ LYS D 201 C FMT D 478 1555 1555 1.45
LINK NZ LYS E 201 C FMT E 478 1555 1555 1.45
LINK NZ LYS F 201 C FMT F 478 1555 1555 1.45
LINK NZ LYS G 201 C FMT G 478 1555 1555 1.45
LINK NZ LYS H 201 C FMT H 478 1555 1555 1.45
LINK MG MG A 477 O1 FMT A 478 1555 1555 3.13
LINK MG MG A 477 O2 FMT A 478 1555 1555 2.37
LINK MG MG A 477 O2 CAP A 476 1555 1555 2.39
LINK MG MG A 477 OE1 GLU A 204 1555 1555 2.34
LINK MG MG A 477 O3 CAP A 476 1555 1555 2.36
LINK MG MG A 477 O7 CAP A 476 1555 1555 2.41
LINK MG MG A 477 OD1 ASP A 203 1555 1555 2.33
LINK MG MG B 477 O3 CAP B 476 1555 1555 2.36
LINK MG MG B 477 O7 CAP B 476 1555 1555 2.42
LINK MG MG B 477 O1 FMT B 478 1555 1555 3.13
LINK MG MG B 477 O2 FMT B 478 1555 1555 2.37
LINK MG MG B 477 O2 CAP B 476 1555 1555 2.39
LINK MG MG B 477 OE1 GLU B 204 1555 1555 2.34
LINK MG MG B 477 OD1 ASP B 203 1555 1555 2.33
LINK MG MG C 477 OD1 ASP C 203 1555 1555 2.33
LINK MG MG C 477 OE1 GLU C 204 1555 1555 2.34
LINK MG MG C 477 O7 CAP C 476 1555 1555 2.42
LINK MG MG C 477 O2 FMT C 478 1555 1555 2.37
LINK MG MG C 477 O3 CAP C 476 1555 1555 2.36
LINK MG MG C 477 O2 CAP C 476 1555 1555 2.39
LINK MG MG C 477 O1 FMT C 478 1555 1555 3.13
LINK MG MG D 477 O3 CAP D 476 1555 1555 2.36
LINK MG MG D 477 O1 FMT D 478 1555 1555 3.13
LINK MG MG D 477 O2 CAP D 476 1555 1555 2.39
LINK MG MG D 477 O2 FMT D 478 1555 1555 2.37
LINK MG MG D 477 OE1 GLU D 204 1555 1555 2.34
LINK MG MG D 477 O7 CAP D 476 1555 1555 2.42
LINK MG MG D 477 OD1 ASP D 203 1555 1555 2.33
LINK MG MG E 477 O2 FMT E 478 1555 1555 2.37
LINK MG MG E 477 OE1 GLU E 204 1555 1555 2.34
LINK MG MG E 477 OD1 ASP E 203 1555 1555 2.33
LINK MG MG E 477 O1 FMT E 478 1555 1555 3.13
LINK MG MG E 477 O2 CAP E 476 1555 1555 2.39
LINK MG MG E 477 O7 CAP E 476 1555 1555 2.41
LINK MG MG E 477 O3 CAP E 476 1555 1555 2.36
LINK MG MG F 477 O2 FMT F 478 1555 1555 2.37
LINK MG MG F 477 O1 FMT F 478 1555 1555 3.13
LINK MG MG F 477 O3 CAP F 476 1555 1555 2.36
LINK MG MG F 477 OD1 ASP F 203 1555 1555 2.33
LINK MG MG F 477 O2 CAP F 476 1555 1555 2.39
LINK MG MG F 477 O7 CAP F 476 1555 1555 2.41
LINK MG MG F 477 OE1 GLU F 204 1555 1555 2.34
LINK MG MG G 477 OE1 GLU G 204 1555 1555 2.34
LINK MG MG G 477 O2 FMT G 478 1555 1555 2.37
LINK MG MG G 477 O1 FMT G 478 1555 1555 3.13
LINK MG MG G 477 O3 CAP G 476 1555 1555 2.36
LINK MG MG G 477 O2 CAP G 476 1555 1555 2.39
LINK MG MG G 477 OD1 ASP G 203 1555 1555 2.33
LINK MG MG G 477 O7 CAP G 476 1555 1555 2.41
LINK MG MG H 477 O7 CAP H 476 1555 1555 2.41
LINK MG MG H 477 OD1 ASP H 203 1555 1555 2.33
LINK MG MG H 477 O2 CAP H 476 1555 1555 2.39
LINK MG MG H 477 O2 FMT H 478 1555 1555 2.37
LINK MG MG H 477 O1 FMT H 478 1555 1555 3.13
LINK MG MG H 477 O3 CAP H 476 1555 1555 2.36
LINK MG MG H 477 OE1 GLU H 204 1555 1555 2.34
CISPEP 1 LYS A 175 PRO A 176 0 -4.06
CISPEP 2 LYS B 175 PRO B 176 0 -4.03
CISPEP 3 LYS C 175 PRO C 176 0 -4.16
CISPEP 4 LYS D 175 PRO D 176 0 -4.07
CISPEP 5 LYS E 175 PRO E 176 0 -4.05
CISPEP 6 LYS F 175 PRO F 176 0 -4.00
CISPEP 7 LYS G 175 PRO G 176 0 -4.05
CISPEP 8 LYS H 175 PRO H 176 0 -4.05
SITE 1 MG 3 LYS A 201 ASP A 203 GLU A 204
SITE 1 1P 4 PHE M 65 GLY A 404 GLY A 381 GLY A 403
SITE 1 2P 2 ARG A 295 HIS A 327
SITE 1 CAB 4 MG A 477 LYS A 201 HIS A 294 SER A 379
SITE 1 MG2 3 LYS B 201 ASP B 203 GLU B 204
SITE 1 1P2 4 PHE I 65 GLY B 404 GLY B 381 GLY B 403
SITE 1 2P2 2 ARG B 295 HIS B 327
SITE 1 CA2 4 MG B 477 LYS B 201 HIS B 294 SER B 379
SITE 1 MG3 3 LYS C 201 ASP C 203 GLU C 204
SITE 1 1P3 4 PHE N 65 GLY C 404 GLY C 381 GLY C 403
SITE 1 2P3 2 ARG C 295 HIS C 327
SITE 1 CA3 4 MG C 477 LYS C 201 HIS C 294 SER C 379
SITE 1 MG4 3 LYS D 201 ASP D 203 GLU D 204
SITE 1 1P4 4 PHE J 65 GLY D 404 GLY D 381 GLY D 403
SITE 1 2P4 2 ARG D 295 HIS D 327
SITE 1 CA4 4 MG D 477 LYS D 201 HIS D 294 SER D 379
SITE 1 MG5 3 LYS E 201 ASP E 203 GLU E 204
SITE 1 1P5 4 PHE O 65 GLY E 404 GLY E 381 GLY E 403
SITE 1 2P5 2 ARG E 295 HIS E 327
SITE 1 CA5 4 MG E 477 LYS E 201 HIS E 294 SER E 379
SITE 1 MG6 3 LYS F 201 ASP F 203 GLU F 204
SITE 1 1P6 4 PHE K 65 GLY F 404 GLY F 381 GLY F 403
SITE 1 2P6 2 ARG F 295 HIS F 327
SITE 1 CA6 4 MG F 477 LYS F 201 HIS F 294 SER F 379
SITE 1 MG7 3 LYS G 201 ASP G 203 GLU G 204
SITE 1 1P7 4 PHE P 65 GLY G 404 GLY G 381 GLY G 403
SITE 1 2P7 2 ARG G 295 HIS G 327
SITE 1 CA7 4 MG G 477 LYS G 201 HIS G 294 SER G 379
SITE 1 MG8 3 LYS H 201 ASP H 203 GLU H 204
SITE 1 1P8 4 PHE L 65 GLY H 404 GLY H 381 GLY H 403
SITE 1 2P8 2 ARG H 295 HIS H 327
SITE 1 CA8 4 MG H 477 LYS H 201 HIS H 294 SER H 379
SITE 1 AC1 23 THR A 173 LYS A 175 LYS A 177 HIS A 294
SITE 2 AC1 23 ARG A 295 HIS A 327 LYS A 334 LEU A 335
SITE 3 AC1 23 SER A 379 GLY A 380 GLY A 381 GLY A 403
SITE 4 AC1 23 GLY A 404 THR B 65 TRP B 66 ASN B 123
SITE 5 AC1 23 HOH A 514 HOH A 515 HOH A 520 HOH A 521
SITE 6 AC1 23 HOH A 569 HOH A 570 HOH A 571
SITE 1 AC2 18 THR A 65 TRP A 66 ASN A 123 THR B 173
SITE 2 AC2 18 LYS B 175 LYS B 177 HIS B 294 ARG B 295
SITE 3 AC2 18 HIS B 327 LYS B 334 LEU B 335 SER B 379
SITE 4 AC2 18 GLY B 380 GLY B 381 GLY B 403 GLY B 404
SITE 5 AC2 18 HOH A 502 HOH A 503
SITE 1 AC3 16 THR C 173 LYS C 175 LYS C 177 HIS C 294
SITE 2 AC3 16 ARG C 295 HIS C 327 LYS C 334 LEU C 335
SITE 3 AC3 16 SER C 379 GLY C 380 GLY C 381 GLY C 403
SITE 4 AC3 16 GLY C 404 THR D 65 TRP D 66 ASN D 123
SITE 1 AC4 16 THR C 65 TRP C 66 ASN C 123 THR D 173
SITE 2 AC4 16 LYS D 175 LYS D 177 HIS D 294 ARG D 295
SITE 3 AC4 16 HIS D 327 LYS D 334 LEU D 335 SER D 379
SITE 4 AC4 16 GLY D 380 GLY D 381 GLY D 403 GLY D 404
SITE 1 AC5 16 THR G 65 TRP G 66 ASN G 123 THR H 173
SITE 2 AC5 16 LYS H 175 LYS H 177 HIS H 294 ARG H 295
SITE 3 AC5 16 HIS H 327 LYS H 334 LEU H 335 SER H 379
SITE 4 AC5 16 GLY H 380 GLY H 381 GLY H 403 GLY H 404
SITE 1 AC6 16 THR G 173 LYS G 175 LYS G 177 HIS G 294
SITE 2 AC6 16 ARG G 295 HIS G 327 LYS G 334 LEU G 335
SITE 3 AC6 16 SER G 379 GLY G 380 GLY G 381 GLY G 403
SITE 4 AC6 16 GLY G 404 THR H 65 TRP H 66 ASN H 123
SITE 1 AC7 16 THR E 65 TRP E 66 ASN E 123 THR F 173
SITE 2 AC7 16 LYS F 175 LYS F 177 HIS F 294 ARG F 295
SITE 3 AC7 16 HIS F 327 LYS F 334 LEU F 335 SER F 379
SITE 4 AC7 16 GLY F 380 GLY F 381 GLY F 403 GLY F 404
SITE 1 AC8 16 THR E 173 LYS E 175 LYS E 177 HIS E 294
SITE 2 AC8 16 ARG E 295 HIS E 327 LYS E 334 LEU E 335
SITE 3 AC8 16 SER E 379 GLY E 380 GLY E 381 GLY E 403
SITE 4 AC8 16 GLY E 404 THR F 65 TRP F 66 ASN F 123
SITE 1 AC9 6 LYS A 201 ASP A 202 ASP A 203 GLU A 204
SITE 2 AC9 6 HIS A 294 HIS A 327
SITE 1 AD1 6 LYS D 201 ASP D 202 ASP D 203 GLU D 204
SITE 2 AD1 6 HIS D 294 HIS D 327
SITE 1 AD2 6 LYS E 201 ASP E 202 ASP E 203 GLU E 204
SITE 2 AD2 6 HIS E 294 HIS E 327
SITE 1 AD3 6 LYS F 201 ASP F 202 ASP F 203 GLU F 204
SITE 2 AD3 6 HIS F 294 HIS F 327
SITE 1 AD4 6 LYS H 201 ASP H 202 ASP H 203 GLU H 204
SITE 2 AD4 6 HIS H 294 HIS H 327
SITE 1 AD5 6 LYS G 201 ASP G 202 ASP G 203 GLU G 204
SITE 2 AD5 6 HIS G 294 HIS G 327
SITE 1 AD6 6 LYS C 201 ASP C 202 ASP C 203 GLU C 204
SITE 2 AD6 6 HIS C 294 HIS C 327
SITE 1 AD7 6 LYS B 201 ASP B 202 ASP B 203 GLU B 204
SITE 2 AD7 6 HIS B 294 HIS B 327
SITE 1 AD8 2 ASP A 203 GLU A 204
SITE 1 AD9 2 ASP B 203 GLU B 204
SITE 1 AE1 2 ASP C 203 GLU C 204
SITE 1 AE2 2 ASP D 203 GLU D 204
SITE 1 AE3 2 ASP E 203 GLU E 204
SITE 1 AE4 2 ASP F 203 GLU F 204
SITE 1 AE5 2 ASP G 203 GLU G 204
SITE 1 AE6 2 ASP H 203 GLU H 204
CRYST1 223.900 111.900 199.700 90.00 90.00 90.00 P 21 21 21 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 0.004466 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008937 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005008 0.00000
MTRIX1 1 0.055254 0.991591 0.117024 58.51700 1
MTRIX2 1 0.991747 -0.068084 0.108639 -60.77910 1
MTRIX3 1 0.115693 0.110056 -0.987169 -12.31830 1
MTRIX1 2 -0.001556 0.994481 0.104910 63.24410 1
MTRIX2 2 -0.993326 0.010562 -0.114852 104.72470 1
MTRIX3 2 -0.115326 -0.104388 0.987827 11.96200 1
MTRIX1 3 0.998390 -0.056422 0.005795 1.35870 1
MTRIX2 3 -0.056413 -0.998406 -0.001652 47.27970 1
MTRIX3 3 0.005879 0.001323 -0.999982 -0.77360 1
MTRIX1 4 -0.999944 0.000591 -0.010574 168.35741 1
MTRIX2 4 0.001717 -0.976187 -0.216926 41.89850 1
MTRIX3 4 -0.010451 -0.216932 0.976131 5.47850 1
MTRIX1 5 -0.055113 -0.992904 -0.105381 109.87600 1
MTRIX2 5 -0.993265 0.043745 0.107292 104.02560 1
MTRIX3 5 -0.101920 0.110584 -0.988627 5.96800 1
MTRIX1 6 -0.000233 -0.993280 -0.115738 105.29090 1
MTRIX2 6 0.994670 0.011703 -0.102440 -62.72860 1
MTRIX3 6 0.103106 -0.115145 0.987983 -6.23160 1
MTRIX1 7 -0.998513 0.054364 0.004006 167.12070 1
MTRIX2 7 0.053928 0.974438 0.218086 -3.88990 1
MTRIX3 7 0.007953 0.217978 -0.975921 -5.57330 1
(ATOM LINES ARE NOT SHOWN.)
END
