HEADER LYASE (CARBON-CARBON) 29-MAR-94 1RSC
TITLE STRUCTURE OF AN EFFECTOR INDUCED INACTIVATED STATE OF RIBULOSE
TITLE 2 BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE: THE BINARY COMPLEX BETWEEN
TITLE 3 ENZYME AND XYLULOSE BISPHOSPHATE
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 CELL_LINE: S2;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: SYNECHOCOCCUS ELONGATUS;
SOURCE 8 ORGANISM_TAXID: 269084;
SOURCE 9 STRAIN: PCC 6301;
SOURCE 10 CELL_LINE: S2
KEYWDS LYASE (CARBON-CARBON)
EXPDTA X-RAY DIFFRACTION
AUTHOR J.NEWMAN,S.GUTTERIDGE
REVDAT 4 13-JUL-11 1RSC 1 VERSN
REVDAT 3 24-FEB-09 1RSC 1 VERSN
REVDAT 2 01-APR-03 1RSC 1 JRNL
REVDAT 1 08-MAY-95 1RSC 0
JRNL AUTH J.NEWMAN,S.GUTTERIDGE
JRNL TITL STRUCTURE OF AN EFFECTOR-INDUCED INACTIVATED STATE OF
JRNL TITL 2 RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE: THE BINARY
JRNL TITL 3 COMPLEX BETWEEN ENZYME AND XYLULOSE 1,5-BISPHOSPHATE.
JRNL REF STRUCTURE V. 2 495 1994
JRNL REFN ISSN 0969-2126
JRNL PMID 7922027
JRNL DOI 10.1016/S0969-2126(00)00050-2
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 ACTIVATE QUATERNARY COMPLEX AT
REMARK 1 TITL 3 2.2 ANGSTROMS RESOLUTION
REMARK 1 REF J.BIOL.CHEM. V. 268 25876 1993
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.NEWMAN,C.-I.BRANDEN,T.A.JONES
REMARK 1 TITL STRUCTURE DETERMINATION AND REFINEMENT OF
REMARK 1 TITL 2 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE FROM
REMARK 1 TITL 3 SYNECHOCOCCUS PCC6301
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 49 548 1993
REMARK 1 REFN ISSN 0907-4449
REMARK 1 REFERENCE 3
REMARK 1 AUTH J.NEWMAN,S.GUTTERIDGE
REMARK 1 TITL THE PURIFICATION AND PRELIMINARY X-RAY DIFFRACTION STUDIES
REMARK 1 TITL 2 OF RECOMBINANT SYNECHOCOCCUS RIBULOSE-1,5-BISPHOSPHATE
REMARK 1 TITL 3 CARBOXYLASE(SLASH)OXYGENASE FROM E. COLI
REMARK 1 REF J.BIOL.CHEM. V. 265 15154 1990
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
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) : 0.255
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 : 144
REMARK 3 SOLVENT ATOMS : 206
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) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 0.91
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 25.62
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.79
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: NULL
REMARK 4
REMARK 4 1RSC 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 (%): 48.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
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 112.20000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 100.15000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.30000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 100.15000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 112.20000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.30000
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: THERE ARE 7 NON-CRYSTALLOGRAPHIC SYMMETRY OPERATORS, AND
REMARK 300 THESE MUST BE USED TO GENERATE THE ENTIRE L8S8 MOLECULE.
REMARK 300 THE FORMAT OF THE FOLLOWING TRANSFORMATIONS IS FROM X-PLOR,
REMARK 300 THUS THE SYMMETRY RELATED CHAINS ARE GENERATED BY: R'=R*R
REMARK 300 + T, R = ROTATION MATRIX, T = TRANSLATION. THESE ARE THE
REMARK 300 ROTATION/TRANSLATION COMPONENTS TO MAP AN LS MONOMER (AM)
REMARK 300 ONTO THE REST OF THE MOLECULE. THESE MATRICES WERE
REMARK 300 OBTAINED FROM X-PLOR AFTER REFINEMENT OF THE WHOLE L8S8
REMARK 300 920710.
REMARK 300
REMARK 300 MTRIX
REMARK 300 THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW
REMARK 300 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE
REMARK 300 VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE
REMARK 300 MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL
REMARK 300 YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED
REMARK 300 SECOND.
REMARK 300
REMARK 300 APPLIED TO TRANSFORMED TO
REMARK 300 MTRIX CHAIN RESIDUES CHAIN RESIDUES
REMARK 300 1 A 9 - 475 B 9 - 475
REMARK 300 1 M 2 - 51 I 2 - 51
REMARK 300 1 M 59 - 122 I 59 - 122
REMARK 300 2 A 9 - 475 C 9 - 475
REMARK 300 2 M 2 - 51 N 2 - 51
REMARK 300 2 M 59 - 122 N 59 - 122
REMARK 300 3 A 9 - 475 D 9 - 475
REMARK 300 3 M 2 - 51 J 2 - 51
REMARK 300 3 M 59 - 122 J 59 - 122
REMARK 300 4 A 9 - 475 E 9 - 475
REMARK 300 4 M 2 - 51 O 2 - 51
REMARK 300 4 M 59 - 122 O 59 - 122
REMARK 300 5 A 9 - 475 F 9 - 475
REMARK 300 5 M 2 - 51 F 2 - 51
REMARK 300 5 M 59 - 122 F 59 - 122
REMARK 300 6 A 9 - 475 G 9 - 475
REMARK 300 6 M 2 - 51 P 2 - 51
REMARK 300 6 M 59 - 122 P 59 - 122
REMARK 300 7 A 9 - 475 H 9 - 475
REMARK 300 7 M 2 - 51 L 2 - 51
REMARK 300 7 M 59 - 122 L 59 - 122
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 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 4
REMARK 465 PRO A 5
REMARK 465 LYS A 6
REMARK 465 THR A 7
REMARK 465 GLN A 8
REMARK 465 MET M 1
REMARK 465 TYR M 123
REMARK 465 MET B 4
REMARK 465 PRO B 5
REMARK 465 LYS B 6
REMARK 465 THR B 7
REMARK 465 GLN B 8
REMARK 465 MET I 1
REMARK 465 TYR I 123
REMARK 465 MET C 4
REMARK 465 PRO C 5
REMARK 465 LYS C 6
REMARK 465 THR C 7
REMARK 465 GLN C 8
REMARK 465 MET N 1
REMARK 465 TYR N 123
REMARK 465 MET D 4
REMARK 465 PRO D 5
REMARK 465 LYS D 6
REMARK 465 THR D 7
REMARK 465 GLN D 8
REMARK 465 MET J 1
REMARK 465 TYR J 123
REMARK 465 MET E 4
REMARK 465 PRO E 5
REMARK 465 LYS E 6
REMARK 465 THR E 7
REMARK 465 GLN E 8
REMARK 465 MET O 1
REMARK 465 TYR O 123
REMARK 465 MET F 4
REMARK 465 PRO F 5
REMARK 465 LYS F 6
REMARK 465 THR F 7
REMARK 465 GLN F 8
REMARK 465 MET K 1
REMARK 465 TYR K 123
REMARK 465 MET G 4
REMARK 465 PRO G 5
REMARK 465 LYS G 6
REMARK 465 THR G 7
REMARK 465 GLN G 8
REMARK 465 MET P 1
REMARK 465 TYR P 123
REMARK 465 MET H 4
REMARK 465 PRO H 5
REMARK 465 LYS H 6
REMARK 465 THR H 7
REMARK 465 GLN H 8
REMARK 465 MET L 1
REMARK 465 TYR L 123
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 91 CG CD OE1 NE2
REMARK 470 ASP M 76 CG OD1 OD2
REMARK 470 LYS M 78 CG CD CE NZ
REMARK 470 SER M 79 OG
REMARK 470 GLN B 91 CG CD OE1 NE2
REMARK 470 ASP I 76 CG OD1 OD2
REMARK 470 LYS I 78 CG CD CE NZ
REMARK 470 SER I 79 OG
REMARK 470 GLN C 91 CG CD OE1 NE2
REMARK 470 ASP N 76 CG OD1 OD2
REMARK 470 LYS N 78 CG CD CE NZ
REMARK 470 SER N 79 OG
REMARK 470 GLN D 91 CG CD OE1 NE2
REMARK 470 ASP J 76 CG OD1 OD2
REMARK 470 LYS J 78 CG CD CE NZ
REMARK 470 SER J 79 OG
REMARK 470 GLN E 91 CG CD OE1 NE2
REMARK 470 ASP O 76 CG OD1 OD2
REMARK 470 LYS O 78 CG CD CE NZ
REMARK 470 SER O 79 OG
REMARK 470 GLN F 91 CG CD OE1 NE2
REMARK 470 ASP K 76 CG OD1 OD2
REMARK 470 LYS K 78 CG CD CE NZ
REMARK 470 SER K 79 OG
REMARK 470 GLN G 91 CG CD OE1 NE2
REMARK 470 ASP P 76 CG OD1 OD2
REMARK 470 LYS P 78 CG CD CE NZ
REMARK 470 SER P 79 OG
REMARK 470 GLN H 91 CG CD OE1 NE2
REMARK 470 ASP L 76 CG OD1 OD2
REMARK 470 LYS L 78 CG CD CE NZ
REMARK 470 SER L 79 OG
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 ASP M 76
REMARK 475 CYS M 77
REMARK 475 LYS M 78
REMARK 475 GLY M 121
REMARK 475 ARG M 122
REMARK 475 SER B 9
REMARK 475 ALA B 10
REMARK 475 ALA B 11
REMARK 475 ASP I 76
REMARK 475 CYS I 77
REMARK 475 LYS I 78
REMARK 475 GLY I 121
REMARK 475 ARG I 122
REMARK 475 SER C 9
REMARK 475 ALA C 10
REMARK 475 ALA C 11
REMARK 475 ASP N 76
REMARK 475 CYS N 77
REMARK 475 LYS N 78
REMARK 475 GLY N 121
REMARK 475 ARG N 122
REMARK 475 SER D 9
REMARK 475 ALA D 10
REMARK 475 ALA D 11
REMARK 475 ASP J 76
REMARK 475 CYS J 77
REMARK 475 LYS J 78
REMARK 475 GLY J 121
REMARK 475 ARG J 122
REMARK 475 SER E 9
REMARK 475 ALA E 10
REMARK 475 ALA E 11
REMARK 475 ASP O 76
REMARK 475 CYS O 77
REMARK 475 LYS O 78
REMARK 475 GLY O 121
REMARK 475 ARG O 122
REMARK 475 SER F 9
REMARK 475 ALA F 10
REMARK 475 ALA F 11
REMARK 475 ASP K 76
REMARK 475 CYS K 77
REMARK 475 LYS K 78
REMARK 475 GLY K 121
REMARK 475 ARG K 122
REMARK 475 SER G 9
REMARK 475 ALA G 10
REMARK 475 ALA G 11
REMARK 475 ASP P 76
REMARK 475 CYS P 77
REMARK 475 LYS P 78
REMARK 475 GLY P 121
REMARK 475 ARG P 122
REMARK 475 SER H 9
REMARK 475 ALA H 10
REMARK 475 ALA H 11
REMARK 475 ASP L 76
REMARK 475 CYS L 77
REMARK 475 LYS L 78
REMARK 475 GLY L 121
REMARK 475 ARG L 122
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU A 93 CB CG CD OE1 OE2
REMARK 480 GLU A 94 CB CG CD OE1 OE2
REMARK 480 GLN A 429 CB CG CD OE1 NE2
REMARK 480 ARG A 431 CB CG CD NE CZ NH1 NH2
REMARK 480 TYR A 438 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR A 438 OH
REMARK 480 ARG A 439 CB CG CD NE CZ NH1 NH2
REMARK 480 ASP A 460 CB CG OD1 OD2
REMARK 480 GLU A 464 CB CG CD OE1 OE2
REMARK 480 LYS A 466 CB CG CD CE NZ
REMARK 480 LYS A 474 CB CG CD CE NZ
REMARK 480 LYS M 4 CB CG CD CE NZ
REMARK 480 ARG M 24 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU M 35 CG CD OE1 OE2
REMARK 480 GLU M 64 CG CD OE1 OE2
REMARK 480 ARG M 88 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU B 93 CB CG CD OE1 OE2
REMARK 480 GLU B 94 CB CG CD OE1 OE2
REMARK 480 GLN B 429 CB CG CD OE1 NE2
REMARK 480 ARG B 431 CB CG CD NE CZ NH1 NH2
REMARK 480 TYR B 438 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR B 438 OH
REMARK 480 ARG B 439 CB CG CD NE CZ NH1 NH2
REMARK 480 ASP B 460 CB CG OD1 OD2
REMARK 480 GLU B 464 CB CG CD OE1 OE2
REMARK 480 LYS B 466 CB CG CD CE NZ
REMARK 480 LYS B 474 CB CG CD CE NZ
REMARK 480 LYS I 4 CB CG CD CE NZ
REMARK 480 ARG I 24 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU I 35 CG CD OE1 OE2
REMARK 480 GLU I 64 CG CD OE1 OE2
REMARK 480 ARG I 88 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU C 93 CB CG CD OE1 OE2
REMARK 480 GLU C 94 CB CG CD OE1 OE2
REMARK 480 GLN C 429 CB CG CD OE1 NE2
REMARK 480 ARG C 431 CB CG CD NE CZ NH1 NH2
REMARK 480 TYR C 438 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR C 438 OH
REMARK 480 ARG C 439 CB CG CD NE CZ NH1 NH2
REMARK 480 ASP C 460 CB CG OD1 OD2
REMARK 480 GLU C 464 CB CG CD OE1 OE2
REMARK 480 LYS C 466 CB CG CD CE NZ
REMARK 480 LYS C 474 CB CG CD CE NZ
REMARK 480 LYS N 4 CB CG CD CE NZ
REMARK 480 ARG N 24 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU N 35 CG CD OE1 OE2
REMARK 480 GLU N 64 CG CD OE1 OE2
REMARK 480 ARG N 88 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU D 93 CB CG CD OE1 OE2
REMARK 480 GLU D 94 CB CG CD OE1 OE2
REMARK 480 GLN D 429 CB CG CD OE1 NE2
REMARK 480 ARG D 431 CB CG CD NE CZ NH1 NH2
REMARK 480 TYR D 438 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR D 438 OH
REMARK 480 ARG D 439 CB CG CD NE CZ NH1 NH2
REMARK 480 ASP D 460 CB CG OD1 OD2
REMARK 480 GLU D 464 CB CG CD OE1 OE2
REMARK 480 LYS D 466 CB CG CD CE NZ
REMARK 480 LYS D 474 CB CG CD CE NZ
REMARK 480 LYS J 4 CB CG CD CE NZ
REMARK 480 ARG J 24 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU J 35 CG CD OE1 OE2
REMARK 480 GLU J 64 CG CD OE1 OE2
REMARK 480 ARG J 88 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU E 93 CB CG CD OE1 OE2
REMARK 480 GLU E 94 CB CG CD OE1 OE2
REMARK 480 GLN E 429 CB CG CD OE1 NE2
REMARK 480 ARG E 431 CB CG CD NE CZ NH1 NH2
REMARK 480 TYR E 438 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR E 438 OH
REMARK 480 ARG E 439 CB CG CD NE CZ NH1 NH2
REMARK 480 ASP E 460 CB CG OD1 OD2
REMARK 480 GLU E 464 CB CG CD OE1 OE2
REMARK 480 LYS E 466 CB CG CD CE NZ
REMARK 480 LYS E 474 CB CG CD CE NZ
REMARK 480 LYS O 4 CB CG CD CE NZ
REMARK 480 ARG O 24 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU O 35 CG CD OE1 OE2
REMARK 480 GLU O 64 CG CD OE1 OE2
REMARK 480 ARG O 88 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU F 93 CB CG CD OE1 OE2
REMARK 480 GLU F 94 CB CG CD OE1 OE2
REMARK 480 GLN F 429 CB CG CD OE1 NE2
REMARK 480 ARG F 431 CB CG CD NE CZ NH1 NH2
REMARK 480 TYR F 438 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR F 438 OH
REMARK 480 ARG F 439 CB CG CD NE CZ NH1 NH2
REMARK 480 ASP F 460 CB CG OD1 OD2
REMARK 480 GLU F 464 CB CG CD OE1 OE2
REMARK 480 LYS F 466 CB CG CD CE NZ
REMARK 480 LYS F 474 CB CG CD CE NZ
REMARK 480 LYS K 4 CB CG CD CE NZ
REMARK 480 ARG K 24 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU K 35 CG CD OE1 OE2
REMARK 480 GLU K 64 CG CD OE1 OE2
REMARK 480 ARG K 88 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU G 93 CB CG CD OE1 OE2
REMARK 480 GLU G 94 CB CG CD OE1 OE2
REMARK 480 GLN G 429 CB CG CD OE1 NE2
REMARK 480 ARG G 431 CB CG CD NE CZ NH1 NH2
REMARK 480 TYR G 438 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR G 438 OH
REMARK 480 ARG G 439 CB CG CD NE CZ NH1 NH2
REMARK 480 ASP G 460 CB CG OD1 OD2
REMARK 480 GLU G 464 CB CG CD OE1 OE2
REMARK 480 LYS G 466 CB CG CD CE NZ
REMARK 480 LYS G 474 CB CG CD CE NZ
REMARK 480 LYS P 4 CB CG CD CE NZ
REMARK 480 ARG P 24 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU P 35 CG CD OE1 OE2
REMARK 480 GLU P 64 CG CD OE1 OE2
REMARK 480 ARG P 88 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU H 93 CB CG CD OE1 OE2
REMARK 480 GLU H 94 CB CG CD OE1 OE2
REMARK 480 GLN H 429 CB CG CD OE1 NE2
REMARK 480 ARG H 431 CB CG CD NE CZ NH1 NH2
REMARK 480 TYR H 438 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR H 438 OH
REMARK 480 ARG H 439 CB CG CD NE CZ NH1 NH2
REMARK 480 ASP H 460 CB CG OD1 OD2
REMARK 480 GLU H 464 CB CG CD OE1 OE2
REMARK 480 LYS H 466 CB CG CD CE NZ
REMARK 480 LYS H 474 CB CG CD CE NZ
REMARK 480 LYS L 4 CB CG CD CE NZ
REMARK 480 ARG L 24 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU L 35 CG CD OE1 OE2
REMARK 480 GLU L 64 CG CD OE1 OE2
REMARK 480 ARG L 88 CB CG CD NE CZ NH1 NH2
REMARK 700
REMARK 700 SHEET
REMARK 700 S1 IN *SHEET RECORDS BELOW IS THE L-SUBUNIT N-TERMINAL
REMARK 700 SHEET. S2 IN *SHEET* RECORDS BELOW IS THE L-SUBUNIT C-TERM
REMARK 700 DOMAIN SHEET. S3 IN *SHEET* RECORDS BELOW IS THE S-SUBUNIT
REMARK 700 SHEET. THIS SHEET IS +1, -2X, -1.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: XBP
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 1P
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: 2P
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: BP2
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: BP3
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: BP4
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: 3P5
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP5
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: BP6
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: BP7
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: 3P8
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: BP8
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 XBP A 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XBP B 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XBP C 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XBP D 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XBP E 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XBP F 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XBP G 476
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XBP H 476
DBREF 1RSC A 4 475 UNP P00880 RBL_SYNP6 1 472
DBREF 1RSC M 2 123 UNP P04716 RBS_SYNP6 1 110
DBREF 1RSC B 4 475 UNP P00880 RBL_SYNP6 1 472
DBREF 1RSC I 2 123 UNP P04716 RBS_SYNP6 1 110
DBREF 1RSC C 4 475 UNP P00880 RBL_SYNP6 1 472
DBREF 1RSC N 2 123 UNP P04716 RBS_SYNP6 1 110
DBREF 1RSC D 4 475 UNP P00880 RBL_SYNP6 1 472
DBREF 1RSC J 2 123 UNP P04716 RBS_SYNP6 1 110
DBREF 1RSC E 4 475 UNP P00880 RBL_SYNP6 1 472
DBREF 1RSC O 2 123 UNP P04716 RBS_SYNP6 1 110
DBREF 1RSC F 4 475 UNP P00880 RBL_SYNP6 1 472
DBREF 1RSC K 2 123 UNP P04716 RBS_SYNP6 1 110
DBREF 1RSC G 4 475 UNP P00880 RBL_SYNP6 1 472
DBREF 1RSC P 2 123 UNP P04716 RBS_SYNP6 1 110
DBREF 1RSC H 4 475 UNP P00880 RBL_SYNP6 1 472
DBREF 1RSC L 2 123 UNP P04716 RBS_SYNP6 1 110
SEQADV 1RSC GLU M 109 UNP P04716 GLN 96 CONFLICT
SEQADV 1RSC GLU I 109 UNP P04716 GLN 96 CONFLICT
SEQADV 1RSC GLU N 109 UNP P04716 GLN 96 CONFLICT
SEQADV 1RSC GLU J 109 UNP P04716 GLN 96 CONFLICT
SEQADV 1RSC GLU O 109 UNP P04716 GLN 96 CONFLICT
SEQADV 1RSC GLU K 109 UNP P04716 GLN 96 CONFLICT
SEQADV 1RSC GLU P 109 UNP P04716 GLN 96 CONFLICT
SEQADV 1RSC GLU L 109 UNP P04716 GLN 96 CONFLICT
SEQRES 1 A 472 MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES 2 A 472 VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES 3 A 472 THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES 4 A 472 SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES 5 A 472 ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES 6 A 472 VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES 7 A 472 GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES 8 A 472 ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES 9 A 472 PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES 10 A 472 VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES 11 A 472 ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES 12 A 472 THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES 13 A 472 ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES 14 A 472 THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES 15 A 472 GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES 16 A 472 PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES 17 A 472 GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES 18 A 472 ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES 19 A 472 HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES 20 A 472 MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES 21 A 472 ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES 22 A 472 ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES 23 A 472 LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES 24 A 472 ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES 25 A 472 LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES 26 A 472 GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES 27 A 472 THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES 28 A 472 GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES 29 A 472 TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES 30 A 472 GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES 31 A 472 PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES 32 A 472 LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES 33 A 472 ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES 34 A 472 GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES 35 A 472 ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES 36 A 472 LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES 37 A 472 MET ASP LYS LEU
SEQRES 1 M 111 MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES 2 M 111 THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES 3 M 111 ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES 4 M 111 PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES 5 M 111 PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES 6 M 111 LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES 7 M 111 ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES 8 M 111 PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES 9 M 111 VAL HIS ARG PRO GLY ARG TYR
SEQRES 1 B 472 MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES 2 B 472 VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES 3 B 472 THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES 4 B 472 SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES 5 B 472 ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES 6 B 472 VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES 7 B 472 GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES 8 B 472 ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES 9 B 472 PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES 10 B 472 VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES 11 B 472 ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES 12 B 472 THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES 13 B 472 ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES 14 B 472 THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES 15 B 472 GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES 16 B 472 PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES 17 B 472 GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES 18 B 472 ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES 19 B 472 HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES 20 B 472 MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES 21 B 472 ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES 22 B 472 ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES 23 B 472 LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES 24 B 472 ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES 25 B 472 LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES 26 B 472 GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES 27 B 472 THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES 28 B 472 GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES 29 B 472 TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES 30 B 472 GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES 31 B 472 PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES 32 B 472 LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES 33 B 472 ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES 34 B 472 GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES 35 B 472 ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES 36 B 472 LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES 37 B 472 MET ASP LYS LEU
SEQRES 1 I 111 MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES 2 I 111 THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES 3 I 111 ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES 4 I 111 PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES 5 I 111 PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES 6 I 111 LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES 7 I 111 ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES 8 I 111 PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES 9 I 111 VAL HIS ARG PRO GLY ARG TYR
SEQRES 1 C 472 MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES 2 C 472 VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES 3 C 472 THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES 4 C 472 SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES 5 C 472 ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES 6 C 472 VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES 7 C 472 GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES 8 C 472 ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES 9 C 472 PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES 10 C 472 VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES 11 C 472 ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES 12 C 472 THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES 13 C 472 ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES 14 C 472 THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES 15 C 472 GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES 16 C 472 PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES 17 C 472 GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES 18 C 472 ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES 19 C 472 HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES 20 C 472 MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES 21 C 472 ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES 22 C 472 ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES 23 C 472 LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES 24 C 472 ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES 25 C 472 LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES 26 C 472 GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES 27 C 472 THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES 28 C 472 GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES 29 C 472 TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES 30 C 472 GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES 31 C 472 PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES 32 C 472 LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES 33 C 472 ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES 34 C 472 GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES 35 C 472 ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES 36 C 472 LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES 37 C 472 MET ASP LYS LEU
SEQRES 1 N 111 MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES 2 N 111 THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES 3 N 111 ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES 4 N 111 PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES 5 N 111 PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES 6 N 111 LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES 7 N 111 ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES 8 N 111 PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES 9 N 111 VAL HIS ARG PRO GLY ARG TYR
SEQRES 1 D 472 MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES 2 D 472 VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES 3 D 472 THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES 4 D 472 SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES 5 D 472 ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES 6 D 472 VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES 7 D 472 GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES 8 D 472 ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES 9 D 472 PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES 10 D 472 VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES 11 D 472 ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES 12 D 472 THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES 13 D 472 ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES 14 D 472 THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES 15 D 472 GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES 16 D 472 PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES 17 D 472 GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES 18 D 472 ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES 19 D 472 HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES 20 D 472 MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES 21 D 472 ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES 22 D 472 ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES 23 D 472 LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES 24 D 472 ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES 25 D 472 LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES 26 D 472 GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES 27 D 472 THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES 28 D 472 GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES 29 D 472 TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES 30 D 472 GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES 31 D 472 PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES 32 D 472 LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES 33 D 472 ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES 34 D 472 GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES 35 D 472 ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES 36 D 472 LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES 37 D 472 MET ASP LYS LEU
SEQRES 1 J 111 MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES 2 J 111 THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES 3 J 111 ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES 4 J 111 PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES 5 J 111 PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES 6 J 111 LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES 7 J 111 ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES 8 J 111 PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES 9 J 111 VAL HIS ARG PRO GLY ARG TYR
SEQRES 1 E 472 MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES 2 E 472 VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES 3 E 472 THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES 4 E 472 SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES 5 E 472 ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES 6 E 472 VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES 7 E 472 GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES 8 E 472 ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES 9 E 472 PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES 10 E 472 VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES 11 E 472 ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES 12 E 472 THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES 13 E 472 ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES 14 E 472 THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES 15 E 472 GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES 16 E 472 PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES 17 E 472 GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES 18 E 472 ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES 19 E 472 HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES 20 E 472 MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES 21 E 472 ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES 22 E 472 ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES 23 E 472 LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES 24 E 472 ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES 25 E 472 LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES 26 E 472 GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES 27 E 472 THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES 28 E 472 GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES 29 E 472 TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES 30 E 472 GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES 31 E 472 PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES 32 E 472 LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES 33 E 472 ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES 34 E 472 GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES 35 E 472 ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES 36 E 472 LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES 37 E 472 MET ASP LYS LEU
SEQRES 1 O 111 MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES 2 O 111 THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES 3 O 111 ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES 4 O 111 PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES 5 O 111 PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES 6 O 111 LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES 7 O 111 ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES 8 O 111 PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES 9 O 111 VAL HIS ARG PRO GLY ARG TYR
SEQRES 1 F 472 MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES 2 F 472 VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES 3 F 472 THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES 4 F 472 SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES 5 F 472 ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES 6 F 472 VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES 7 F 472 GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES 8 F 472 ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES 9 F 472 PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES 10 F 472 VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES 11 F 472 ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES 12 F 472 THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES 13 F 472 ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES 14 F 472 THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES 15 F 472 GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES 16 F 472 PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES 17 F 472 GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES 18 F 472 ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES 19 F 472 HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES 20 F 472 MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES 21 F 472 ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES 22 F 472 ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES 23 F 472 LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES 24 F 472 ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES 25 F 472 LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES 26 F 472 GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES 27 F 472 THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES 28 F 472 GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES 29 F 472 TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES 30 F 472 GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES 31 F 472 PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES 32 F 472 LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES 33 F 472 ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES 34 F 472 GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES 35 F 472 ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES 36 F 472 LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES 37 F 472 MET ASP LYS LEU
SEQRES 1 K 111 MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES 2 K 111 THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES 3 K 111 ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES 4 K 111 PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES 5 K 111 PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES 6 K 111 LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES 7 K 111 ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES 8 K 111 PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES 9 K 111 VAL HIS ARG PRO GLY ARG TYR
SEQRES 1 G 472 MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES 2 G 472 VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES 3 G 472 THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES 4 G 472 SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES 5 G 472 ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES 6 G 472 VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES 7 G 472 GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES 8 G 472 ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES 9 G 472 PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES 10 G 472 VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES 11 G 472 ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES 12 G 472 THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES 13 G 472 ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES 14 G 472 THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES 15 G 472 GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES 16 G 472 PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES 17 G 472 GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES 18 G 472 ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES 19 G 472 HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES 20 G 472 MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES 21 G 472 ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES 22 G 472 ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES 23 G 472 LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES 24 G 472 ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES 25 G 472 LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES 26 G 472 GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES 27 G 472 THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES 28 G 472 GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES 29 G 472 TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES 30 G 472 GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES 31 G 472 PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES 32 G 472 LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES 33 G 472 ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES 34 G 472 GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES 35 G 472 ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES 36 G 472 LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES 37 G 472 MET ASP LYS LEU
SEQRES 1 P 111 MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES 2 P 111 THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES 3 P 111 ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES 4 P 111 PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES 5 P 111 PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES 6 P 111 LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES 7 P 111 ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES 8 P 111 PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES 9 P 111 VAL HIS ARG PRO GLY ARG TYR
SEQRES 1 H 472 MET PRO LYS THR GLN SER ALA ALA GLY TYR LYS ALA GLY
SEQRES 2 H 472 VAL LYS ASP TYR LYS LEU THR TYR TYR THR PRO ASP TYR
SEQRES 3 H 472 THR PRO LYS ASP THR ASP LEU LEU ALA ALA PHE ARG PHE
SEQRES 4 H 472 SER PRO GLN PRO GLY VAL PRO ALA ASP GLU ALA GLY ALA
SEQRES 5 H 472 ALA ILE ALA ALA GLU SER SER THR GLY THR TRP THR THR
SEQRES 6 H 472 VAL TRP THR ASP LEU LEU THR ASP MET ASP ARG TYR LYS
SEQRES 7 H 472 GLY LYS CYS TYR HIS ILE GLU PRO VAL GLN GLY GLU GLU
SEQRES 8 H 472 ASN SER TYR PHE ALA PHE ILE ALA TYR PRO LEU ASP LEU
SEQRES 9 H 472 PHE GLU GLU GLY SER VAL THR ASN ILE LEU THR SER ILE
SEQRES 10 H 472 VAL GLY ASN VAL PHE GLY PHE LYS ALA ILE ARG SER LEU
SEQRES 11 H 472 ARG LEU GLU ASP ILE ARG PHE PRO VAL ALA LEU VAL LYS
SEQRES 12 H 472 THR PHE GLN GLY PRO PRO HIS GLY ILE GLN VAL GLU ARG
SEQRES 13 H 472 ASP LEU LEU ASN LYS TYR GLY ARG PRO MET LEU GLY CYS
SEQRES 14 H 472 THR ILE LYS PRO LYS LEU GLY LEU SER ALA LYS ASN TYR
SEQRES 15 H 472 GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY GLY LEU ASP
SEQRES 16 H 472 PHE THR LYS ASP ASP GLU ASN ILE ASN SER GLN PRO PHE
SEQRES 17 H 472 GLN ARG TRP ARG ASP ARG PHE LEU PHE VAL ALA ASP ALA
SEQRES 18 H 472 ILE HIS LYS SER GLN ALA GLU THR GLY GLU ILE LYS GLY
SEQRES 19 H 472 HIS TYR LEU ASN VAL THR ALA PRO THR CYS GLU GLU MET
SEQRES 20 H 472 MET LYS ARG ALA GLU PHE ALA LYS GLU LEU GLY MET PRO
SEQRES 21 H 472 ILE ILE MET HIS ASP PHE LEU THR ALA GLY PHE THR ALA
SEQRES 22 H 472 ASN THR THR LEU ALA LYS TRP CYS ARG ASP ASN GLY VAL
SEQRES 23 H 472 LEU LEU HIS ILE HIS ARG ALA MET HIS ALA VAL ILE ASP
SEQRES 24 H 472 ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG VAL LEU ALA
SEQRES 25 H 472 LYS CYS LEU ARG LEU SER GLY GLY ASP HIS LEU HIS SER
SEQRES 26 H 472 GLY THR VAL VAL GLY LYS LEU GLU GLY ASP LYS ALA SER
SEQRES 27 H 472 THR LEU GLY PHE VAL ASP LEU MET ARG GLU ASP HIS ILE
SEQRES 28 H 472 GLU ALA ASP ARG SER ARG GLY VAL PHE PHE THR GLN ASP
SEQRES 29 H 472 TRP ALA SER MET PRO GLY VAL LEU PRO VAL ALA SER GLY
SEQRES 30 H 472 GLY ILE HIS VAL TRP HIS MET PRO ALA LEU VAL GLU ILE
SEQRES 31 H 472 PHE GLY ASP ASP SER VAL LEU GLN PHE GLY GLY GLY THR
SEQRES 32 H 472 LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY ALA THR ALA
SEQRES 33 H 472 ASN ARG VAL ALA LEU GLU ALA CYS VAL GLN ALA ARG ASN
SEQRES 34 H 472 GLU GLY ARG ASP LEU TYR ARG GLU GLY GLY ASP ILE LEU
SEQRES 35 H 472 ARG GLU ALA GLY LYS TRP SER PRO GLU LEU ALA ALA ALA
SEQRES 36 H 472 LEU ASP LEU TRP LYS GLU ILE LYS PHE GLU PHE GLU THR
SEQRES 37 H 472 MET ASP LYS LEU
SEQRES 1 L 111 MET SER MET LYS THR LEU PRO LYS GLU ARG ARG PHE GLU
SEQRES 2 L 111 THR PHE SER TYR LEU PRO PRO LEU SER ASP ARG GLN ILE
SEQRES 3 L 111 ALA ALA GLN ILE GLU TYR MET ILE GLU GLN GLY PHE HIS
SEQRES 4 L 111 PRO LEU ILE GLU PHE ASN GLU HIS SER ASN PRO GLU GLU
SEQRES 5 L 111 PHE TYR TRP THR MET TRP LYS LEU PRO LEU PHE ASP CYS
SEQRES 6 L 111 LYS SER PRO GLN GLN VAL LEU ASP GLU VAL ARG GLU CYS
SEQRES 7 L 111 ARG SER GLU TYR GLY ASP CYS TYR ILE ARG VAL ALA GLY
SEQRES 8 L 111 PHE ASP ASN ILE LYS GLU CYS GLN THR VAL SER PHE ILE
SEQRES 9 L 111 VAL HIS ARG PRO GLY ARG TYR
MODRES 1RSC THR E 65 THR GLYCOSYLATION SITE
MODRES 1RSC THR H 65 THR GLYCOSYLATION SITE
HET XBP A 476 18
HET XBP B 476 18
HET XBP C 476 18
HET XBP D 476 18
HET XBP E 476 18
HET XBP F 476 18
HET XBP G 476 18
HET XBP H 476 18
HETNAM XBP XYLULOSE-1,5-BISPHOSPHATE
FORMUL 17 XBP 8(C5 H12 O11 P2)
FORMUL 25 HOH *206(H2 O)
HELIX 1 A LYS A 21 TYR A 24 1 4
HELIX 2 B ALA A 50 GLU A 60 1N-TERMINAL DOMAIN HELICES 11
HELIX 3 BB MET A 77 TYR A 80 1N-TERMINAL DOMAIN HELICES 4
HELIX 4 C VAL A 113 VAL A 121 1N-TERMINAL DOMAIN HELICES 9
HELIX 5 D VAL A 142 VAL A 145 1 4
HELIX 6 E ILE A 155 LEU A 162 1N-TERM & C-TERM DOMAIN LINK 8
HELIX 7 1 ALA A 182 ARG A 194 1FIRST HELIX OF C-TERM DOMAIN 13
HELIX 8 2 TRP A 214 THR A 232 12ND HELIX OF C-TERM DOMAIN 19
HELIX 9 3 CYS A 247 GLU A 259 13RD HELIX OF C-TERM DOMAIN 13
HELIX 10 4 PHE A 269 ASN A 287 14TH HELIX OF C-TERM DOMAIN 19
HELIX 11 F HIS A 298 ASP A 302 1 5
HELIX 12 5 PHE A 311 SER A 321 15TH HELIX OF C-TERM DOMAIN 11
HELIX 13 6 LYS A 339 ARG A 350 16TH HELIX OF C-TERM DOMAIN 12
HELIX 14 7 MET A 387 PHE A 394 17TH HELIX OF C-TERM DOMAIN 8
HELIX 15 P GLY A 404 LEU A 407 1P - PHOSPHATE BINDING HELIX 4
HELIX 16 8 ASN A 413 GLU A 433 18TH HELIX OF C-TERM DOMAIN 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 MA ASP M 23 GLN M 36 11ST HELIX OF S-SUBUNIT 14
HELIX 20 MB PRO M 80 GLU M 93 12ND HELIX OF S-SUBUNIT 14
HELIX 21 A LYS B 21 TYR B 24 1 4
HELIX 22 B ALA B 50 GLU B 60 1N-TERMINAL DOMAIN HELICES 11
HELIX 23 BB MET B 77 TYR B 80 1N-TERMINAL DOMAIN HELICES 4
HELIX 24 C VAL B 113 VAL B 121 1N-TERMINAL DOMAIN HELICES 9
HELIX 25 D VAL B 142 VAL B 145 1 4
HELIX 26 E ILE B 155 LEU B 162 1N-TERM & C-TERM DOMAIN LINK 8
HELIX 27 1 ALA B 182 ARG B 194 1FIRST HELIX OF C-TERM DOMAIN 13
HELIX 28 2 TRP B 214 THR B 232 12ND HELIX OF C-TERM DOMAIN 19
HELIX 29 3 CYS B 247 GLU B 259 13RD HELIX OF C-TERM DOMAIN 13
HELIX 30 4 PHE B 269 ASN B 287 14TH HELIX OF C-TERM DOMAIN 19
HELIX 31 F HIS B 298 ASP B 302 1 5
HELIX 32 5 PHE B 311 SER B 321 15TH HELIX OF C-TERM DOMAIN 11
HELIX 33 6 LYS B 339 ARG B 350 16TH HELIX OF C-TERM DOMAIN 12
HELIX 34 7 MET B 387 PHE B 394 17TH HELIX OF C-TERM DOMAIN 8
HELIX 35 P GLY B 404 LEU B 407 1P - PHOSPHATE BINDING HELIX 4
HELIX 36 8 ASN B 413 GLU B 433 18TH HELIX OF C-TERM DOMAIN 21
HELIX 37 G LEU B 437 TRP B 451 1 15
HELIX 38 H PRO B 453 TRP B 462 1 10
HELIX 39 MA ASP I 23 GLN I 36 11ST HELIX OF S-SUBUNIT 14
HELIX 40 MB PRO I 80 GLU I 93 12ND HELIX OF S-SUBUNIT 14
HELIX 41 A LYS C 21 TYR C 24 1 4
HELIX 42 B ALA C 50 GLU C 60 1N-TERMINAL DOMAIN HELICES 11
HELIX 43 BB MET C 77 TYR C 80 1N-TERMINAL DOMAIN HELICES 4
HELIX 44 C VAL C 113 VAL C 121 1N-TERMINAL DOMAIN HELICES 9
HELIX 45 D VAL C 142 VAL C 145 1 4
HELIX 46 E ILE C 155 LEU C 162 1N-TERM & C-TERM DOMAIN LINK 8
HELIX 47 1 ALA C 182 ARG C 194 1FIRST HELIX OF C-TERM DOMAIN 13
HELIX 48 2 TRP C 214 THR C 232 12ND HELIX OF C-TERM DOMAIN 19
HELIX 49 3 CYS C 247 GLU C 259 13RD HELIX OF C-TERM DOMAIN 13
HELIX 50 4 PHE C 269 ASN C 287 14TH HELIX OF C-TERM DOMAIN 19
HELIX 51 F HIS C 298 ASP C 302 1 5
HELIX 52 5 PHE C 311 SER C 321 15TH HELIX OF C-TERM DOMAIN 11
HELIX 53 6 LYS C 339 ARG C 350 16TH HELIX OF C-TERM DOMAIN 12
HELIX 54 7 MET C 387 PHE C 394 17TH HELIX OF C-TERM DOMAIN 8
HELIX 55 P GLY C 404 LEU C 407 1P - PHOSPHATE BINDING HELIX 4
HELIX 56 8 ASN C 413 GLU C 433 18TH HELIX OF C-TERM DOMAIN 21
HELIX 57 G LEU C 437 TRP C 451 1 15
HELIX 58 H PRO C 453 TRP C 462 1 10
HELIX 59 MA ASP N 23 GLN N 36 11ST HELIX OF S-SUBUNIT 14
HELIX 60 MB PRO N 80 GLU N 93 12ND HELIX OF S-SUBUNIT 14
HELIX 61 A LYS D 21 TYR D 24 1 4
HELIX 62 B ALA D 50 GLU D 60 1N-TERMINAL DOMAIN HELICES 11
HELIX 63 BB MET D 77 TYR D 80 1N-TERMINAL DOMAIN HELICES 4
HELIX 64 C VAL D 113 VAL D 121 1N-TERMINAL DOMAIN HELICES 9
HELIX 65 D VAL D 142 VAL D 145 1 4
HELIX 66 E ILE D 155 LEU D 162 1N-TERM & C-TERM DOMAIN LINK 8
HELIX 67 1 ALA D 182 ARG D 194 1FIRST HELIX OF C-TERM DOMAIN 13
HELIX 68 2 TRP D 214 THR D 232 12ND HELIX OF C-TERM DOMAIN 19
HELIX 69 3 CYS D 247 GLU D 259 13RD HELIX OF C-TERM DOMAIN 13
HELIX 70 4 PHE D 269 ASN D 287 14TH HELIX OF C-TERM DOMAIN 19
HELIX 71 F HIS D 298 ASP D 302 1 5
HELIX 72 5 PHE D 311 SER D 321 15TH HELIX OF C-TERM DOMAIN 11
HELIX 73 6 LYS D 339 ARG D 350 16TH HELIX OF C-TERM DOMAIN 12
HELIX 74 7 MET D 387 PHE D 394 17TH HELIX OF C-TERM DOMAIN 8
HELIX 75 P GLY D 404 LEU D 407 1P - PHOSPHATE BINDING HELIX 4
HELIX 76 8 ASN D 413 GLU D 433 18TH HELIX OF C-TERM DOMAIN 21
HELIX 77 G LEU D 437 TRP D 451 1 15
HELIX 78 H PRO D 453 TRP D 462 1 10
HELIX 79 MA ASP J 23 GLN J 36 11ST HELIX OF S-SUBUNIT 14
HELIX 80 MB PRO J 80 GLU J 93 12ND HELIX OF S-SUBUNIT 14
HELIX 81 A LYS E 21 TYR E 24 1 4
HELIX 82 B ALA E 50 GLU E 60 1N-TERMINAL DOMAIN HELICES 11
HELIX 83 BB MET E 77 TYR E 80 1N-TERMINAL DOMAIN HELICES 4
HELIX 84 C VAL E 113 VAL E 121 1N-TERMINAL DOMAIN HELICES 9
HELIX 85 D VAL E 142 VAL E 145 1 4
HELIX 86 E ILE E 155 LEU E 162 1N-TERM & C-TERM DOMAIN LINK 8
HELIX 87 1 ALA E 182 ARG E 194 1FIRST HELIX OF C-TERM DOMAIN 13
HELIX 88 2 TRP E 214 THR E 232 12ND HELIX OF C-TERM DOMAIN 19
HELIX 89 3 CYS E 247 GLU E 259 13RD HELIX OF C-TERM DOMAIN 13
HELIX 90 4 PHE E 269 ASN E 287 14TH HELIX OF C-TERM DOMAIN 19
HELIX 91 F HIS E 298 ASP E 302 1 5
HELIX 92 5 PHE E 311 SER E 321 15TH HELIX OF C-TERM DOMAIN 11
HELIX 93 6 LYS E 339 ARG E 350 16TH HELIX OF C-TERM DOMAIN 12
HELIX 94 7 MET E 387 PHE E 394 17TH HELIX OF C-TERM DOMAIN 8
HELIX 95 P GLY E 404 LEU E 407 1P - PHOSPHATE BINDING HELIX 4
HELIX 96 8 ASN E 413 GLU E 433 18TH HELIX OF C-TERM DOMAIN 21
HELIX 97 G LEU E 437 TRP E 451 1 15
HELIX 98 H PRO E 453 TRP E 462 1 10
HELIX 99 MA ASP O 23 GLN O 36 11ST HELIX OF S-SUBUNIT 14
HELIX 100 MB PRO O 80 GLU O 93 12ND HELIX OF S-SUBUNIT 14
HELIX 101 A LYS F 21 TYR F 24 1 4
HELIX 102 B ALA F 50 GLU F 60 1N-TERMINAL DOMAIN HELICES 11
HELIX 103 BB MET F 77 TYR F 80 1N-TERMINAL DOMAIN HELICES 4
HELIX 104 C VAL F 113 VAL F 121 1N-TERMINAL DOMAIN HELICES 9
HELIX 105 D VAL F 142 VAL F 145 1 4
HELIX 106 E ILE F 155 LEU F 162 1N-TERM & C-TERM DOMAIN LINK 8
HELIX 107 1 ALA F 182 ARG F 194 1FIRST HELIX OF C-TERM DOMAIN 13
HELIX 108 2 TRP F 214 THR F 232 12ND HELIX OF C-TERM DOMAIN 19
HELIX 109 3 CYS F 247 GLU F 259 13RD HELIX OF C-TERM DOMAIN 13
HELIX 110 4 PHE F 269 ASN F 287 14TH HELIX OF C-TERM DOMAIN 19
HELIX 111 F HIS F 298 ASP F 302 1 5
HELIX 112 5 PHE F 311 SER F 321 15TH HELIX OF C-TERM DOMAIN 11
HELIX 113 6 LYS F 339 ARG F 350 16TH HELIX OF C-TERM DOMAIN 12
HELIX 114 7 MET F 387 PHE F 394 17TH HELIX OF C-TERM DOMAIN 8
HELIX 115 P GLY F 404 LEU F 407 1P - PHOSPHATE BINDING HELIX 4
HELIX 116 8 ASN F 413 GLU F 433 18TH HELIX OF C-TERM DOMAIN 21
HELIX 117 G LEU F 437 TRP F 451 1 15
HELIX 118 H PRO F 453 TRP F 462 1 10
HELIX 119 MA ASP K 23 GLN K 36 11ST HELIX OF S-SUBUNIT 14
HELIX 120 MB PRO K 80 GLU K 93 12ND HELIX OF S-SUBUNIT 14
HELIX 121 A LYS G 21 TYR G 24 1 4
HELIX 122 B ALA G 50 GLU G 60 1N-TERMINAL DOMAIN HELICES 11
HELIX 123 BB MET G 77 TYR G 80 1N-TERMINAL DOMAIN HELICES 4
HELIX 124 C VAL G 113 VAL G 121 1N-TERMINAL DOMAIN HELICES 9
HELIX 125 D VAL G 142 VAL G 145 1 4
HELIX 126 E ILE G 155 LEU G 162 1N-TERM & C-TERM DOMAIN LINK 8
HELIX 127 1 ALA G 182 ARG G 194 1FIRST HELIX OF C-TERM DOMAIN 13
HELIX 128 2 TRP G 214 THR G 232 12ND HELIX OF C-TERM DOMAIN 19
HELIX 129 3 CYS G 247 GLU G 259 13RD HELIX OF C-TERM DOMAIN 13
HELIX 130 4 PHE G 269 ASN G 287 14TH HELIX OF C-TERM DOMAIN 19
HELIX 131 F HIS G 298 ASP G 302 1 5
HELIX 132 5 PHE G 311 SER G 321 15TH HELIX OF C-TERM DOMAIN 11
HELIX 133 6 LYS G 339 ARG G 350 16TH HELIX OF C-TERM DOMAIN 12
HELIX 134 7 MET G 387 PHE G 394 17TH HELIX OF C-TERM DOMAIN 8
HELIX 135 P GLY G 404 LEU G 407 1P - PHOSPHATE BINDING HELIX 4
HELIX 136 8 ASN G 413 GLU G 433 18TH HELIX OF C-TERM DOMAIN 21
HELIX 137 G LEU G 437 TRP G 451 1 15
HELIX 138 H PRO G 453 TRP G 462 1 10
HELIX 139 MA ASP P 23 GLN P 36 11ST HELIX OF S-SUBUNIT 14
HELIX 140 MB PRO P 80 GLU P 93 12ND HELIX OF S-SUBUNIT 14
HELIX 141 A LYS H 21 TYR H 24 1 4
HELIX 142 B ALA H 50 GLU H 60 1N-TERMINAL DOMAIN HELICES 11
HELIX 143 BB MET H 77 TYR H 80 1N-TERMINAL DOMAIN HELICES 4
HELIX 144 C VAL H 113 VAL H 121 1N-TERMINAL DOMAIN HELICES 9
HELIX 145 D VAL H 142 VAL H 145 1 4
HELIX 146 E ILE H 155 LEU H 162 1N-TERM & C-TERM DOMAIN LINK 8
HELIX 147 1 ALA H 182 ARG H 194 1FIRST HELIX OF C-TERM DOMAIN 13
HELIX 148 2 TRP H 214 THR H 232 12ND HELIX OF C-TERM DOMAIN 19
HELIX 149 3 CYS H 247 GLU H 259 13RD HELIX OF C-TERM DOMAIN 13
HELIX 150 4 PHE H 269 ASN H 287 14TH HELIX OF C-TERM DOMAIN 19
HELIX 151 F HIS H 298 ASP H 302 1 5
HELIX 152 5 PHE H 311 SER H 321 15TH HELIX OF C-TERM DOMAIN 11
HELIX 153 6 LYS H 339 ARG H 350 16TH HELIX OF C-TERM DOMAIN 12
HELIX 154 7 MET H 387 PHE H 394 17TH HELIX OF C-TERM DOMAIN 8
HELIX 155 P GLY H 404 LEU H 407 1P - PHOSPHATE BINDING HELIX 4
HELIX 156 8 ASN H 413 GLU H 433 18TH HELIX OF C-TERM DOMAIN 21
HELIX 157 G LEU H 437 TRP H 451 1 15
HELIX 158 H PRO H 453 TRP H 462 1 10
HELIX 159 MA ASP L 23 GLN L 36 11ST HELIX OF S-SUBUNIT 14
HELIX 160 MB PRO L 80 GLU L 93 12ND HELIX OF S-SUBUNIT 14
SHEET 1 S1 4 LYS A 83 PRO A 89 0
SHEET 2 S1 4 SER A 96 TYR A 103 -1
SHEET 3 S1 4 LEU A 36 PRO A 44 -1
SHEET 4 S1 4 ILE A 130 ARG A 139 -1
SHEET 1 S2 8 MET A 169 GLY A 171 0
SHEET 2 S2 8 THR A 200 ASP A 202 1
SHEET 3 S2 8 LEU A 240 ASN A 241 1
SHEET 4 S2 8 ILE A 264 ASP A 268 1
SHEET 5 S2 8 LEU A 290 HIS A 294 1
SHEET 6 S2 8 HIS A 325 HIS A 327 1
SHEET 7 S2 8 LEU A 375 SER A 379 1
SHEET 8 S2 8 VAL A 399 GLN A 401 1
SHEET 1 S3 4 THR M 68 MET M 69 0
SHEET 2 S3 4 HIS M 39 ASN M 45 -1
SHEET 3 S3 4 TYR M 98 ASP M 105 -1
SHEET 4 S3 4 CYS M 110 HIS M 118 -1
SHEET 1 S4 4 LYS B 83 PRO B 89 0
SHEET 2 S4 4 SER B 96 TYR B 103 -1
SHEET 3 S4 4 LEU B 36 PRO B 44 -1
SHEET 4 S4 4 ILE B 130 ARG B 139 -1
SHEET 1 S5 8 MET B 169 GLY B 171 0
SHEET 2 S5 8 THR B 200 ASP B 202 1
SHEET 3 S5 8 LEU B 240 ASN B 241 1
SHEET 4 S5 8 ILE B 264 ASP B 268 1
SHEET 5 S5 8 LEU B 290 HIS B 294 1
SHEET 6 S5 8 HIS B 325 HIS B 327 1
SHEET 7 S5 8 LEU B 375 SER B 379 1
SHEET 8 S5 8 VAL B 399 GLN B 401 1
SHEET 1 S6 4 THR I 68 MET I 69 0
SHEET 2 S6 4 HIS I 39 ASN I 45 -1
SHEET 3 S6 4 TYR I 98 ASP I 105 -1
SHEET 4 S6 4 CYS I 110 HIS I 118 -1
SHEET 1 S7 4 LYS C 83 PRO C 89 0
SHEET 2 S7 4 SER C 96 TYR C 103 -1
SHEET 3 S7 4 LEU C 36 PRO C 44 -1
SHEET 4 S7 4 ILE C 130 ARG C 139 -1
SHEET 1 S8 8 MET C 169 GLY C 171 0
SHEET 2 S8 8 THR C 200 ASP C 202 1
SHEET 3 S8 8 LEU C 240 ASN C 241 1
SHEET 4 S8 8 ILE C 264 ASP C 268 1
SHEET 5 S8 8 LEU C 290 HIS C 294 1
SHEET 6 S8 8 HIS C 325 HIS C 327 1
SHEET 7 S8 8 LEU C 375 SER C 379 1
SHEET 8 S8 8 VAL C 399 GLN C 401 1
SHEET 1 S9 4 THR N 68 MET N 69 0
SHEET 2 S9 4 HIS N 39 ASN N 45 -1
SHEET 3 S9 4 TYR N 98 ASP N 105 -1
SHEET 4 S9 4 CYS N 110 HIS N 118 -1
SHEET 1 S10 4 LYS D 83 PRO D 89 0
SHEET 2 S10 4 SER D 96 TYR D 103 -1
SHEET 3 S10 4 LEU D 36 PRO D 44 -1
SHEET 4 S10 4 ILE D 130 ARG D 139 -1
SHEET 1 S11 8 MET D 169 GLY D 171 0
SHEET 2 S11 8 THR D 200 ASP D 202 1
SHEET 3 S11 8 LEU D 240 ASN D 241 1
SHEET 4 S11 8 ILE D 264 ASP D 268 1
SHEET 5 S11 8 LEU D 290 HIS D 294 1
SHEET 6 S11 8 HIS D 325 HIS D 327 1
SHEET 7 S11 8 LEU D 375 SER D 379 1
SHEET 8 S11 8 VAL D 399 GLN D 401 1
SHEET 1 S12 4 THR J 68 MET J 69 0
SHEET 2 S12 4 HIS J 39 ASN J 45 -1
SHEET 3 S12 4 TYR J 98 ASP J 105 -1
SHEET 4 S12 4 CYS J 110 HIS J 118 -1
SHEET 1 S13 4 LYS E 83 PRO E 89 0
SHEET 2 S13 4 SER E 96 TYR E 103 -1
SHEET 3 S13 4 LEU E 36 PRO E 44 -1
SHEET 4 S13 4 ILE E 130 ARG E 139 -1
SHEET 1 S14 8 MET E 169 GLY E 171 0
SHEET 2 S14 8 THR E 200 ASP E 202 1
SHEET 3 S14 8 LEU E 240 ASN E 241 1
SHEET 4 S14 8 ILE E 264 ASP E 268 1
SHEET 5 S14 8 LEU E 290 HIS E 294 1
SHEET 6 S14 8 HIS E 325 HIS E 327 1
SHEET 7 S14 8 LEU E 375 SER E 379 1
SHEET 8 S14 8 VAL E 399 GLN E 401 1
SHEET 1 S15 4 THR O 68 MET O 69 0
SHEET 2 S15 4 HIS O 39 ASN O 45 -1
SHEET 3 S15 4 TYR O 98 ASP O 105 -1
SHEET 4 S15 4 CYS O 110 HIS O 118 -1
SHEET 1 S16 4 LYS F 83 PRO F 89 0
SHEET 2 S16 4 SER F 96 TYR F 103 -1
SHEET 3 S16 4 LEU F 36 PRO F 44 -1
SHEET 4 S16 4 ILE F 130 ARG F 139 -1
SHEET 1 S17 8 MET F 169 GLY F 171 0
SHEET 2 S17 8 THR F 200 ASP F 202 1
SHEET 3 S17 8 LEU F 240 ASN F 241 1
SHEET 4 S17 8 ILE F 264 ASP F 268 1
SHEET 5 S17 8 LEU F 290 HIS F 294 1
SHEET 6 S17 8 HIS F 325 HIS F 327 1
SHEET 7 S17 8 LEU F 375 SER F 379 1
SHEET 8 S17 8 VAL F 399 GLN F 401 1
SHEET 1 S18 4 THR K 68 MET K 69 0
SHEET 2 S18 4 HIS K 39 ASN K 45 -1
SHEET 3 S18 4 TYR K 98 ASP K 105 -1
SHEET 4 S18 4 CYS K 110 HIS K 118 -1
SHEET 1 S19 4 LYS G 83 PRO G 89 0
SHEET 2 S19 4 SER G 96 TYR G 103 -1
SHEET 3 S19 4 LEU G 36 PRO G 44 -1
SHEET 4 S19 4 ILE G 130 ARG G 139 -1
SHEET 1 S20 8 MET G 169 GLY G 171 0
SHEET 2 S20 8 THR G 200 ASP G 202 1
SHEET 3 S20 8 LEU G 240 ASN G 241 1
SHEET 4 S20 8 ILE G 264 ASP G 268 1
SHEET 5 S20 8 LEU G 290 HIS G 294 1
SHEET 6 S20 8 HIS G 325 HIS G 327 1
SHEET 7 S20 8 LEU G 375 SER G 379 1
SHEET 8 S20 8 VAL G 399 GLN G 401 1
SHEET 1 S21 4 THR P 68 MET P 69 0
SHEET 2 S21 4 HIS P 39 ASN P 45 -1
SHEET 3 S21 4 TYR P 98 ASP P 105 -1
SHEET 4 S21 4 CYS P 110 HIS P 118 -1
SHEET 1 S22 4 LYS H 83 PRO H 89 0
SHEET 2 S22 4 SER H 96 TYR H 103 -1
SHEET 3 S22 4 LEU H 36 PRO H 44 -1
SHEET 4 S22 4 ILE H 130 ARG H 139 -1
SHEET 1 S23 8 MET H 169 GLY H 171 0
SHEET 2 S23 8 THR H 200 ASP H 202 1
SHEET 3 S23 8 LEU H 240 ASN H 241 1
SHEET 4 S23 8 ILE H 264 ASP H 268 1
SHEET 5 S23 8 LEU H 290 HIS H 294 1
SHEET 6 S23 8 HIS H 325 HIS H 327 1
SHEET 7 S23 8 LEU H 375 SER H 379 1
SHEET 8 S23 8 VAL H 399 GLN H 401 1
SHEET 1 S24 4 THR L 68 MET L 69 0
SHEET 2 S24 4 HIS L 39 ASN L 45 -1
SHEET 3 S24 4 TYR L 98 ASP L 105 -1
SHEET 4 S24 4 CYS L 110 HIS L 118 -1
SSBOND 1 CYS A 247 CYS B 247 1555 1555 2.53
SSBOND 2 CYS C 247 CYS D 247 1555 1555 2.57
SSBOND 3 CYS E 247 CYS F 247 1555 1555 2.59
SSBOND 4 CYS G 247 CYS H 247 1555 1555 2.75
LINK O2P XBP F 476 OG1 THR E 65 1555 1555 2.04
LINK OG1 THR H 65 O2P XBP G 476 1555 1555 2.00
CISPEP 1 LYS A 175 PRO A 176 0 -5.26
CISPEP 2 LYS B 175 PRO B 176 0 -5.26
CISPEP 3 LYS C 175 PRO C 176 0 -5.29
CISPEP 4 LYS D 175 PRO D 176 0 -5.25
CISPEP 5 LYS E 175 PRO E 176 0 -5.34
CISPEP 6 LYS F 175 PRO F 176 0 -5.27
CISPEP 7 LYS G 175 PRO G 176 0 -5.24
CISPEP 8 LYS H 175 PRO H 176 0 -5.19
SITE 1 1P 4 LYS A 334 GLY A 381 GLY A 403 GLY A 404
SITE 1 2P 3 HIS A 327 ARG A 295 SER A 379
SITE 1 XBP 6 LYS A 175 ASP A 203 GLU A 204 HIS A 294
SITE 2 XBP 6 LYS A 334 SER A 379
SITE 1 1P2 4 LYS B 334 GLY B 381 GLY B 403 GLY B 404
SITE 1 2P2 3 HIS B 327 ARG B 295 SER B 379
SITE 1 BP2 6 LYS B 175 ASP B 203 GLU B 204 HIS B 294
SITE 2 BP2 6 LYS B 334 SER B 379
SITE 1 1P3 4 LYS C 334 GLY C 381 GLY C 403 GLY C 404
SITE 1 2P3 3 HIS C 327 ARG C 295 SER C 379
SITE 1 BP3 6 LYS C 175 ASP C 203 GLU C 204 HIS C 294
SITE 2 BP3 6 LYS C 334 SER C 379
SITE 1 1P4 4 LYS D 334 GLY D 381 GLY D 403 GLY D 404
SITE 1 2P4 3 HIS D 327 ARG D 295 SER D 379
SITE 1 BP4 6 LYS D 175 ASP D 203 GLU D 204 HIS D 294
SITE 2 BP4 6 LYS D 334 SER D 379
SITE 1 1P5 4 LYS E 334 GLY E 381 GLY E 403 GLY E 404
SITE 1 3P5 3 HIS E 327 ARG E 295 SER E 379
SITE 1 BP5 6 LYS E 175 ASP E 203 GLU E 204 HIS E 294
SITE 2 BP5 6 LYS E 334 SER E 379
SITE 1 1P6 4 LYS F 334 GLY F 381 GLY F 403 GLY F 404
SITE 1 2P6 3 HIS F 327 ARG F 295 SER F 379
SITE 1 BP6 6 LYS F 175 ASP F 203 GLU F 204 HIS F 294
SITE 2 BP6 6 LYS F 334 SER F 379
SITE 1 1P7 4 LYS G 334 GLY G 381 GLY G 403 GLY G 404
SITE 1 2P7 3 HIS G 327 ARG G 295 SER G 379
SITE 1 BP7 6 LYS G 175 ASP G 203 GLU G 204 HIS G 294
SITE 2 BP7 6 LYS G 334 SER G 379
SITE 1 1P8 4 LYS H 334 GLY H 381 GLY H 403 GLY H 404
SITE 1 3P8 3 HIS H 327 ARG H 295 SER H 379
SITE 1 BP8 6 LYS H 175 ASP H 203 GLU H 204 HIS H 294
SITE 2 BP8 6 LYS H 334 SER H 379
SITE 1 AC1 25 LYS A 175 LYS A 177 ASP A 203 GLU A 204
SITE 2 AC1 25 HIS A 294 ARG A 295 HIS A 327 LYS A 334
SITE 3 AC1 25 LEU A 335 SER A 379 GLY A 380 GLY A 381
SITE 4 AC1 25 GLY A 403 GLY A 404 HOH A 496 HOH A 588
SITE 5 AC1 25 HOH A 589 HOH A 590 HOH A 598 HOH A 599
SITE 6 AC1 25 GLU B 60 THR B 65 TRP B 66 ASN B 123
SITE 7 AC1 25 HOH B 477
SITE 1 AC2 20 GLU A 60 THR A 65 TRP A 66 ASN A 123
SITE 2 AC2 20 HOH A 615 LYS B 175 LYS B 177 ASP B 203
SITE 3 AC2 20 GLU B 204 HIS B 294 ARG B 295 HIS B 327
SITE 4 AC2 20 LYS B 334 LEU B 335 SER B 379 GLY B 380
SITE 5 AC2 20 GLY B 381 GLY B 403 GLY B 404 HOH B 479
SITE 1 AC3 18 LYS C 175 LYS C 177 ASP C 203 GLU C 204
SITE 2 AC3 18 HIS C 294 ARG C 295 HIS C 327 LYS C 334
SITE 3 AC3 18 LEU C 335 SER C 379 GLY C 380 GLY C 381
SITE 4 AC3 18 GLY C 403 GLY C 404 GLU D 60 THR D 65
SITE 5 AC3 18 TRP D 66 ASN D 123
SITE 1 AC4 18 GLU C 60 THR C 65 TRP C 66 ASN C 123
SITE 2 AC4 18 LYS D 175 LYS D 177 ASP D 203 GLU D 204
SITE 3 AC4 18 HIS D 294 ARG D 295 HIS D 327 LYS D 334
SITE 4 AC4 18 LEU D 335 SER D 379 GLY D 380 GLY D 381
SITE 5 AC4 18 GLY D 403 GLY D 404
SITE 1 AC5 18 LYS E 175 LYS E 177 ASP E 203 GLU E 204
SITE 2 AC5 18 HIS E 294 ARG E 295 HIS E 327 LYS E 334
SITE 3 AC5 18 LEU E 335 SER E 379 GLY E 380 GLY E 381
SITE 4 AC5 18 GLY E 403 GLY E 404 GLU F 60 THR F 65
SITE 5 AC5 18 TRP F 66 ASN F 123
SITE 1 AC6 18 GLU E 60 THR E 65 TRP E 66 ASN E 123
SITE 2 AC6 18 LYS F 175 LYS F 177 ASP F 203 GLU F 204
SITE 3 AC6 18 HIS F 294 ARG F 295 HIS F 327 LYS F 334
SITE 4 AC6 18 LEU F 335 SER F 379 GLY F 380 GLY F 381
SITE 5 AC6 18 GLY F 403 GLY F 404
SITE 1 AC7 18 LYS G 175 LYS G 177 ASP G 203 GLU G 204
SITE 2 AC7 18 HIS G 294 ARG G 295 HIS G 327 LYS G 334
SITE 3 AC7 18 LEU G 335 SER G 379 GLY G 380 GLY G 381
SITE 4 AC7 18 GLY G 403 GLY G 404 GLU H 60 THR H 65
SITE 5 AC7 18 TRP H 66 ASN H 123
SITE 1 AC8 18 GLU G 60 THR G 65 TRP G 66 ASN G 123
SITE 2 AC8 18 LYS H 175 LYS H 177 ASP H 203 GLU H 204
SITE 3 AC8 18 HIS H 294 ARG H 295 HIS H 327 LYS H 334
SITE 4 AC8 18 LEU H 335 SER H 379 GLY H 380 GLY H 381
SITE 5 AC8 18 GLY H 403 GLY H 404
CRYST1 224.400 112.600 200.300 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 0.004456 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008881 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004993 0.00000
MTRIX1 1 0.054944 0.991599 0.117102 58.71750 1
MTRIX2 1 0.991904 -0.067652 0.107466 -60.96300 1
MTRIX3 1 0.114485 0.110249 -0.987288 -12.23330 1
MTRIX1 2 -0.003182 0.994466 0.105014 63.56160 1
MTRIX2 2 -0.993371 0.008924 -0.114609 104.72820 1
MTRIX3 2 -0.114912 -0.104682 0.987845 11.92890 1
MTRIX1 3 0.998457 -0.055196 0.006022 1.26820 1
MTRIX2 3 -0.055177 -0.998471 -0.003268 46.89430 1
MTRIX3 3 0.006193 0.002931 -0.999977 -0.86640 1
MTRIX1 4 -0.999944 0.001258 -0.010490 168.47231 1
MTRIX2 4 0.003491 -0.976470 -0.215626 41.55370 1
MTRIX3 4 -0.009972 -0.215651 0.976420 5.38740 1
MTRIX1 5 -0.056378 -0.992918 -0.104574 109.90480 1
MTRIX2 5 -0.993220 0.045110 0.107144 103.99110 1
MTRIX3 5 -0.101667 0.109906 -0.988729 5.96560 1
MTRIX1 6 -0.001047 -0.993269 -0.115824 105.05120 1
MTRIX2 6 0.994820 0.012807 -0.100839 -62.86620 1
MTRIX3 6 0.101644 -0.115118 0.988138 -6.11100 1
MTRIX1 7 -0.998542 0.053826 0.004015 167.20731 1
MTRIX2 7 0.053403 0.974410 0.218344 -3.71750 1
MTRIX3 7 0.007841 0.218240 -0.975864 -5.55990 1
(ATOM LINES ARE NOT SHOWN.)
END
