HEADER HYDROLASE 09-OCT-00 1G0U
TITLE A GATED CHANNEL INTO THE PROTEASOME CORE PARTICLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEASOME COMPONENT Y7;
COMPND 3 CHAIN: A, O;
COMPND 4 SYNONYM: MACROPAIN SUBUNIT Y7, PROTEINASE YSCE SUBUNIT 7,
COMPND 5 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT Y7;
COMPND 6 EC: 3.4.99.46;
COMPND 7 OTHER_DETAILS: PART OF 20S SUBUNIT;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROTEASOME COMPONENT Y13;
COMPND 10 CHAIN: B, P;
COMPND 11 SYNONYM: MACROPAIN SUBUNIT Y13, PROTEINASE YSCE SUBUNIT 13,
COMPND 12 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT Y13;
COMPND 13 EC: 3.4.99.46;
COMPND 14 OTHER_DETAILS: PART OF 20S SUBUNIT;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: PROTEASOME COMPONENT PRE6;
COMPND 17 CHAIN: C, Q;
COMPND 18 SYNONYM: MACROPAIN SUBUNIT PRE6, PROTEINASE YSCE SUBUNIT PRE6,
COMPND 19 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PRE6;
COMPND 20 EC: 3.4.99.46;
COMPND 21 OTHER_DETAILS: PART OF 20S SUBUNIT;
COMPND 22 MOL_ID: 4;
COMPND 23 MOLECULE: PROTEASOME COMPONENT PUP2;
COMPND 24 CHAIN: D, R;
COMPND 25 SYNONYM: MACROPAIN SUBUNIT PUP2, PROTEINASE YSCE SUBUNIT PUP2,
COMPND 26 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PUP2;
COMPND 27 EC: 3.4.99.46;
COMPND 28 OTHER_DETAILS: PART OF 20S SUBUNIT;
COMPND 29 MOL_ID: 5;
COMPND 30 MOLECULE: PROTEASOME COMPONENT PRE5;
COMPND 31 CHAIN: E, S;
COMPND 32 SYNONYM: MACROPAIN SUBUNIT PRE5, PROTEINASE YSCE SUBUNIT PRE5,
COMPND 33 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PRE5;
COMPND 34 EC: 3.4.99.46;
COMPND 35 OTHER_DETAILS: PART OF 20S SUBUNIT;
COMPND 36 MOL_ID: 6;
COMPND 37 MOLECULE: PROTEASOME COMPONENT C1;
COMPND 38 CHAIN: F, T;
COMPND 39 SYNONYM: MACROPAIN SUBUNIT C1, PROTEINASE YSCE SUBUNIT 1,
COMPND 40 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C1;
COMPND 41 EC: 3.4.99.46;
COMPND 42 OTHER_DETAILS: PART OF 20S SUBUNIT;
COMPND 43 MOL_ID: 7;
COMPND 44 MOLECULE: PROTEASOME COMPONENT C7-ALPHA;
COMPND 45 CHAIN: G, U;
COMPND 46 SYNONYM: MACROPAIN SUBUNIT C7-ALPHA, PROTEINASE YSCE SUBUNIT 7,
COMPND 47 MULTICATALYTIC ENDOPEPTIDASE COMPLEX C7, COMPONENT Y8, SCL1
COMPND 48 SUPPRESSOR PROTEIN;
COMPND 49 EC: 3.4.99.46;
COMPND 50 OTHER_DETAILS: PART OF 20S SUBUNIT;
COMPND 51 MOL_ID: 8;
COMPND 52 MOLECULE: PROTEASOME COMPONENT PUP1;
COMPND 53 CHAIN: H, V;
COMPND 54 SYNONYM: MACROPAIN SUBUNIT PUP1, PROTEINASE YSCE SUBUNIT PUP1,
COMPND 55 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PUP1;
COMPND 56 EC: 3.4.99.46;
COMPND 57 OTHER_DETAILS: PART OF 20S SUBUNIT;
COMPND 58 MOL_ID: 9;
COMPND 59 MOLECULE: PROTEASOME COMPONENT PUP3;
COMPND 60 CHAIN: I, W;
COMPND 61 SYNONYM: MACROPAIN SUBUNIT PUP3, MULTICATALYTIC ENDOPEPTIDASE COMPLEX
COMPND 62 SUBUNIT PUP3;
COMPND 63 EC: 3.4.99.46;
COMPND 64 OTHER_DETAILS: PART OF 20S SUBUNIT;
COMPND 65 MOL_ID: 10;
COMPND 66 MOLECULE: PROTEASOME COMPONENT C11;
COMPND 67 CHAIN: J, X;
COMPND 68 SYNONYM: MACROPAIN SUBUNIT C11, PROTEINASE YSCE SUBUNIT 11,
COMPND 69 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C11;
COMPND 70 EC: 3.4.99.46;
COMPND 71 OTHER_DETAILS: PART OF 20S SUBUNIT;
COMPND 72 MOL_ID: 11;
COMPND 73 MOLECULE: PROTEASOME COMPONENT PRE2;
COMPND 74 CHAIN: K, Y;
COMPND 75 SYNONYM: MACROPAIN SUBUNIT PRE2, PROTEINASE YSCE SUBUNIT PRE2,
COMPND 76 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PRE2;
COMPND 77 EC: 3.4.99.46;
COMPND 78 OTHER_DETAILS: PART OF 20S SUBUNIT;
COMPND 79 MOL_ID: 12;
COMPND 80 MOLECULE: PROTEASOME COMPONENT C5;
COMPND 81 CHAIN: L, Z;
COMPND 82 SYNONYM: MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT C5;
COMPND 83 EC: 3.4.99.46;
COMPND 84 OTHER_DETAILS: PART OF 20S SUBUNIT;
COMPND 85 MOL_ID: 13;
COMPND 86 MOLECULE: PROTEASOME COMPONENT PRE4;
COMPND 87 CHAIN: M, 1;
COMPND 88 SYNONYM: MACROPAIN SUBUNIT PRE4, PROTEINASE YSCE SUBUNIT PRE4,
COMPND 89 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PRE4;
COMPND 90 EC: 3.4.99.46;
COMPND 91 OTHER_DETAILS: PART OF 20S SUBUNIT;
COMPND 92 MOL_ID: 14;
COMPND 93 MOLECULE: PROTEASOME COMPONENT PRE3;
COMPND 94 CHAIN: N, 2;
COMPND 95 SYNONYM: MACROPAIN SUBUNIT PRE3, PROTEINASE YSCE SUBUNIT PRE3,
COMPND 96 MULTICATALYTIC ENDOPEPTIDASE COMPLEX SUBUNIT PRE3;
COMPND 97 EC: 3.4.99.46;
COMPND 98 OTHER_DETAILS: PART OF 20S SUBUNIT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 VARIANT: SUB61;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 8 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 9 ORGANISM_TAXID: 4932;
SOURCE 10 VARIANT: SUB61;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 4932;
SOURCE 15 VARIANT: SUB61;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 18 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 19 ORGANISM_TAXID: 4932;
SOURCE 20 VARIANT: SUB61;
SOURCE 21 MOL_ID: 5;
SOURCE 22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 23 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 24 ORGANISM_TAXID: 4932;
SOURCE 25 VARIANT: SUB61;
SOURCE 26 MOL_ID: 6;
SOURCE 27 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 28 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 29 ORGANISM_TAXID: 4932;
SOURCE 30 VARIANT: SUB61;
SOURCE 31 MOL_ID: 7;
SOURCE 32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 33 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 34 ORGANISM_TAXID: 4932;
SOURCE 35 VARIANT: SUB61;
SOURCE 36 MOL_ID: 8;
SOURCE 37 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 38 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 39 ORGANISM_TAXID: 4932;
SOURCE 40 VARIANT: SUB61;
SOURCE 41 MOL_ID: 9;
SOURCE 42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 43 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 44 ORGANISM_TAXID: 4932;
SOURCE 45 VARIANT: SUB61;
SOURCE 46 MOL_ID: 10;
SOURCE 47 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 48 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 49 ORGANISM_TAXID: 4932;
SOURCE 50 VARIANT: SUB61;
SOURCE 51 MOL_ID: 11;
SOURCE 52 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 53 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 54 ORGANISM_TAXID: 4932;
SOURCE 55 VARIANT: SUB61;
SOURCE 56 MOL_ID: 12;
SOURCE 57 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 58 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 59 ORGANISM_TAXID: 4932;
SOURCE 60 VARIANT: SUB61;
SOURCE 61 MOL_ID: 13;
SOURCE 62 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 63 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 64 ORGANISM_TAXID: 4932;
SOURCE 65 VARIANT: SUB61;
SOURCE 66 MOL_ID: 14;
SOURCE 67 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 68 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 69 ORGANISM_TAXID: 4932;
SOURCE 70 VARIANT: SUB61
KEYWDS PROTEASOME, UBIQUITIN, DEGRADATION, PROTEASE, NTN-HYDROLASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.GROLL,M.BAJOREK,A.KOHLER,L.MORODER,D.M.RUBIN,R.HUBER,M.H.GLICKMAN,
AUTHOR 2 D.FINLEY
REVDAT 4 07-FEB-24 1G0U 1 REMARK LINK
REVDAT 3 24-FEB-09 1G0U 1 VERSN
REVDAT 2 06-JAN-04 1G0U 1 ATOM REMARK
REVDAT 1 06-NOV-00 1G0U 0
JRNL AUTH M.GROLL,M.BAJOREK,A.KOHLER,L.MORODER,D.M.RUBIN,R.HUBER,
JRNL AUTH 2 M.H.GLICKMAN,D.FINLEY
JRNL TITL A GATED CHANNEL INTO THE PROTEASOME CORE PARTICLE.
JRNL REF NAT.STRUCT.BIOL. V. 7 1062 2000
JRNL REFN ISSN 1072-8368
JRNL PMID 11062564
JRNL DOI 10.1038/80992
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
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 : 378678
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.250
REMARK 3 FREE R VALUE : 0.303
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 18933
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 : 48906
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 2908
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.40
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) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.878
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 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 1G0U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012092.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-SEP-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.050
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 378678
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.16100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.4
REMARK 200 DATA REDUNDANCY IN SHELL : 0.20
REMARK 200 R MERGE FOR SHELL (I) : 0.39600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: 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 (%): 67.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22MM MAGNESIUM ACETATE, 4%
REMARK 280 DIMETHYLSULFOXIDE, 100MM MORPHOLINOETHANESULFONIC ACID, 11%
REMARK 280 METHYLPENTANEDIOL, PH 6.7, HANGING DROP VAPOUR-DIFFUSION,
REMARK 280 TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 150.55000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MULTISUBUNIT COMPLEX COMPOSED
REMARK 300 OF 28 SUBUNITS, WHEREAS 14 SUBUNITS ARE DIFFERENT.
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: 28-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 28-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 112920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 217200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -510.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S,
REMARK 350 AND CHAINS: T, U, V, W, X, Y, Z, 1, 2
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 THR A 5
REMARK 465 ASP A 6
REMARK 465 ARG A 7
REMARK 465 MET B 3
REMARK 465 GLY B 4
REMARK 465 SER B 5
REMARK 465 ARG B 6
REMARK 465 ARG B 7
REMARK 465 TYR B 8
REMARK 465 ASP B 9
REMARK 465 SER B 10
REMARK 465 ARG B 11
REMARK 465 THR B 12
REMARK 465 MET C 5
REMARK 465 SER C 6
REMARK 465 GLY C 7
REMARK 465 TYR C 8
REMARK 465 ASP C 9
REMARK 465 MET D 1
REMARK 465 PHE D 2
REMARK 465 LEU D 3
REMARK 465 THR D 4
REMARK 465 ARG D 5
REMARK 465 SER D 6
REMARK 465 GLU D 7
REMARK 465 TYR D 8
REMARK 465 ASP D 9
REMARK 465 ARG D 10
REMARK 465 GLY D 11
REMARK 465 MET E 3
REMARK 465 PHE E 4
REMARK 465 ARG E 5
REMARK 465 ASN E 6
REMARK 465 MET F 1
REMARK 465 THR F 2
REMARK 465 SER F 3
REMARK 465 ILE F 4
REMARK 465 GLY F 5
REMARK 465 THR F 6
REMARK 465 MET G -3
REMARK 465 SER G -2
REMARK 465 GLY G -1
REMARK 465 ALA G 0
REMARK 465 ALA G 1
REMARK 465 ALA G 2
REMARK 465 ALA G 3
REMARK 465 SER G 4
REMARK 465 ALA G 5
REMARK 465 ALA G 6
REMARK 465 GLY G 7
REMARK 465 TYR G 8
REMARK 465 MET I -9
REMARK 465 MET L -28
REMARK 465 ALA L -27
REMARK 465 THR L -26
REMARK 465 ILE L -25
REMARK 465 ALA L -24
REMARK 465 SER L -23
REMARK 465 GLU L -22
REMARK 465 TYR L -21
REMARK 465 SER L -20
REMARK 465 SER L -19
REMARK 465 GLU L -18
REMARK 465 ALA L -17
REMARK 465 SER L -16
REMARK 465 ASN L -15
REMARK 465 THR L -14
REMARK 465 PRO L -13
REMARK 465 ILE L -12
REMARK 465 GLU L -11
REMARK 465 HIS L -10
REMARK 465 MET M -41
REMARK 465 ASN M -40
REMARK 465 HIS M -39
REMARK 465 ASP M -38
REMARK 465 PRO M -37
REMARK 465 PHE M -36
REMARK 465 SER M -35
REMARK 465 TRP M -34
REMARK 465 GLY M -33
REMARK 465 ARG M -32
REMARK 465 PRO M -31
REMARK 465 ALA M -30
REMARK 465 ASP M -29
REMARK 465 SER M -28
REMARK 465 THR M -27
REMARK 465 TYR M -26
REMARK 465 GLY M -25
REMARK 465 ALA M -24
REMARK 465 TYR M -23
REMARK 465 ASN M -22
REMARK 465 THR M -21
REMARK 465 GLN M -20
REMARK 465 ILE M -19
REMARK 465 ALA M -18
REMARK 465 ASN M -17
REMARK 465 ALA M -16
REMARK 465 GLY M -15
REMARK 465 ALA M -14
REMARK 465 SER M -13
REMARK 465 PRO M -12
REMARK 465 MET M -11
REMARK 465 VAL M -10
REMARK 465 ASN M -9
REMARK 465 MET O 4
REMARK 465 THR O 5
REMARK 465 ASP O 6
REMARK 465 ARG O 7
REMARK 465 MET P 3
REMARK 465 GLY P 4
REMARK 465 SER P 5
REMARK 465 ARG P 6
REMARK 465 ARG P 7
REMARK 465 TYR P 8
REMARK 465 ASP P 9
REMARK 465 SER P 10
REMARK 465 ARG P 11
REMARK 465 THR P 12
REMARK 465 MET Q 5
REMARK 465 SER Q 6
REMARK 465 GLY Q 7
REMARK 465 TYR Q 8
REMARK 465 ASP Q 9
REMARK 465 MET R 1
REMARK 465 PHE R 2
REMARK 465 LEU R 3
REMARK 465 THR R 4
REMARK 465 ARG R 5
REMARK 465 SER R 6
REMARK 465 GLU R 7
REMARK 465 TYR R 8
REMARK 465 ASP R 9
REMARK 465 ARG R 10
REMARK 465 GLY R 11
REMARK 465 MET S 3
REMARK 465 PHE S 4
REMARK 465 ARG S 5
REMARK 465 ASN S 6
REMARK 465 MET T 1
REMARK 465 THR T 2
REMARK 465 SER T 3
REMARK 465 ILE T 4
REMARK 465 GLY T 5
REMARK 465 THR T 6
REMARK 465 MET U -3
REMARK 465 SER U -2
REMARK 465 GLY U -1
REMARK 465 ALA U 0
REMARK 465 ALA U 1
REMARK 465 ALA U 2
REMARK 465 ALA U 3
REMARK 465 SER U 4
REMARK 465 ALA U 5
REMARK 465 ALA U 6
REMARK 465 GLY U 7
REMARK 465 TYR U 8
REMARK 465 MET W -9
REMARK 465 MET Z -28
REMARK 465 ALA Z -27
REMARK 465 THR Z -26
REMARK 465 ILE Z -25
REMARK 465 ALA Z -24
REMARK 465 SER Z -23
REMARK 465 GLU Z -22
REMARK 465 TYR Z -21
REMARK 465 SER Z -20
REMARK 465 SER Z -19
REMARK 465 GLU Z -18
REMARK 465 ALA Z -17
REMARK 465 SER Z -16
REMARK 465 ASN Z -15
REMARK 465 THR Z -14
REMARK 465 PRO Z -13
REMARK 465 ILE Z -12
REMARK 465 GLU Z -11
REMARK 465 HIS Z -10
REMARK 465 MET 1 -41
REMARK 465 ASN 1 -40
REMARK 465 HIS 1 -39
REMARK 465 ASP 1 -38
REMARK 465 PRO 1 -37
REMARK 465 PHE 1 -36
REMARK 465 SER 1 -35
REMARK 465 TRP 1 -34
REMARK 465 GLY 1 -33
REMARK 465 ARG 1 -32
REMARK 465 PRO 1 -31
REMARK 465 ALA 1 -30
REMARK 465 ASP 1 -29
REMARK 465 SER 1 -28
REMARK 465 THR 1 -27
REMARK 465 TYR 1 -26
REMARK 465 GLY 1 -25
REMARK 465 ALA 1 -24
REMARK 465 TYR 1 -23
REMARK 465 ASN 1 -22
REMARK 465 THR 1 -21
REMARK 465 GLN 1 -20
REMARK 465 ILE 1 -19
REMARK 465 ALA 1 -18
REMARK 465 ASN 1 -17
REMARK 465 ALA 1 -16
REMARK 465 GLY 1 -15
REMARK 465 ALA 1 -14
REMARK 465 SER 1 -13
REMARK 465 PRO 1 -12
REMARK 465 MET 1 -11
REMARK 465 VAL 1 -10
REMARK 465 ASN 1 -9
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 THR B 13 OG1 CG2
REMARK 470 ARG C 10 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 12 CG1 CG2
REMARK 470 ASN E 7 CG OD1 ND2
REMARK 470 ASP G 9 CG OD1 OD2
REMARK 470 THR P 13 OG1 CG2
REMARK 470 ARG Q 10 CG CD NE CZ NH1 NH2
REMARK 470 VAL R 12 CG1 CG2
REMARK 470 ASN S 7 CG OD1 ND2
REMARK 470 ASP U 9 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 MET D 128 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 MET R 128 N - CA - C ANGL. DEV. = -18.5 DEGREES
REMARK 500 LEU Y 4 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 17 -28.70 -39.43
REMARK 500 SER A 56 147.41 178.89
REMARK 500 THR A 63 23.48 -66.72
REMARK 500 PRO A 72 -2.15 -55.28
REMARK 500 TYR A 100 -72.69 -151.14
REMARK 500 ILE A 102A -36.93 -130.09
REMARK 500 GLN A 125 -32.37 -143.46
REMARK 500 LYS A 167 -92.16 -20.11
REMARK 500 ASP A 182 32.58 -76.08
REMARK 500 ALA A 235 51.28 -102.89
REMARK 500 TYR B 22 -73.04 -42.69
REMARK 500 VAL B 54 107.05 38.69
REMARK 500 THR B 63 43.05 -84.44
REMARK 500 THR B 64 88.37 -160.66
REMARK 500 PRO B 131 -178.86 -63.95
REMARK 500 ASP B 182 -39.61 -32.29
REMARK 500 MET B 184 173.69 -52.42
REMARK 500 SER B 204A -74.38 -35.77
REMARK 500 ASP B 208 -2.11 -59.44
REMARK 500 ASP B 218C -142.38 174.51
REMARK 500 ASN C 44 43.75 -149.32
REMARK 500 CYS C 45 170.29 178.81
REMARK 500 LEU C 58 31.04 160.62
REMARK 500 ASP C 60 77.74 -100.30
REMARK 500 THR C 63 130.13 -37.45
REMARK 500 SER C 72 -15.83 -44.72
REMARK 500 ARG C 180B 7.19 -68.29
REMARK 500 PRO C 183 88.02 -40.13
REMARK 500 ALA C 184 28.43 -66.99
REMARK 500 GLN C 202 85.19 79.30
REMARK 500 THR C 203 88.08 24.63
REMARK 500 ALA C 207 -82.28 -78.55
REMARK 500 LYS C 208 -9.64 -55.37
REMARK 500 GLU C 239 21.12 -70.10
REMARK 500 GLU C 242 24.88 -76.33
REMARK 500 ARG D 53 66.42 67.82
REMARK 500 THR D 55 21.72 -76.89
REMARK 500 SER D 56 166.42 170.40
REMARK 500 ALA D 122 77.60 -65.08
REMARK 500 ALA D 127 50.93 -119.84
REMARK 500 SER D 180D 56.22 -66.21
REMARK 500 SER D 180E 35.57 178.45
REMARK 500 SER E 42 -153.42 -119.35
REMARK 500 SER E 59 -166.86 -104.52
REMARK 500 GLN E 64 122.76 -28.64
REMARK 500 ASP E 142 -157.18 -139.83
REMARK 500 PRO E 153 -19.90 -46.24
REMARK 500 THR E 163 -173.98 169.35
REMARK 500 ARG E 202 -50.96 -174.95
REMARK 500 LYS E 217 -66.78 -22.63
REMARK 500
REMARK 500 THIS ENTRY HAS 258 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR L 145 0.07 SIDE CHAIN
REMARK 500 TYR O 85 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG L9002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 105 OE2
REMARK 620 2 HOH D 254 O 89.4
REMARK 620 3 SER L 75 OG 157.1 93.8
REMARK 620 4 SER L 78 OG 89.2 85.2 68.6
REMARK 620 5 HOH L9010 O 104.7 88.6 98.1 164.8
REMARK 620 6 HOH L9015 O 83.9 158.9 100.2 114.5 73.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G9001 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 13 OG1
REMARK 620 2 TYR G 123 O 78.3
REMARK 620 3 ARG G 126 O 89.1 105.2
REMARK 620 4 MET G 129 O 153.6 104.9 114.5
REMARK 620 5 HOH G9019 O 67.2 125.4 114.8 91.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G9010 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA G 127 O
REMARK 620 2 TYR G 128 N 71.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H9007 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE H 163 O
REMARK 620 2 ASP H 166 O 121.0
REMARK 620 3 SER H 169 O 104.2 85.7
REMARK 620 4 HOH H1721 O 91.0 99.9 158.2
REMARK 620 5 ASP Z 194 OXT 104.2 134.7 85.1 76.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I9003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH H 814 O
REMARK 620 2 HOH I9030 O 105.1
REMARK 620 3 HOH I9067 O 142.4 65.7
REMARK 620 4 HOH I9093 O 125.9 126.1 81.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG I9005 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA I 163 O
REMARK 620 2 ASP I 166 O 93.3
REMARK 620 3 SER I 169 O 125.7 90.6
REMARK 620 4 HOH I9011 O 108.7 156.7 82.7
REMARK 620 5 HOH I9013 O 161.2 73.4 68.9 83.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Y9018 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 194 O
REMARK 620 2 ALA Y 163 O 101.4
REMARK 620 3 ASP Y 166 O 145.2 106.1
REMARK 620 4 SER Y 169 O 106.5 98.5 90.2
REMARK 620 5 HOH Y9024 O 84.5 89.1 75.2 165.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG K9008 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA K 163 O
REMARK 620 2 ASP K 166 O 82.3
REMARK 620 3 SER K 169 O 96.9 85.6
REMARK 620 4 HOH K9080 O 81.5 72.1 157.7
REMARK 620 5 ASP W 194 O 112.1 147.8 119.1 81.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG L9004 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR L 163 O
REMARK 620 2 HIS L 166 O 89.8
REMARK 620 3 VAL L 169 O 114.9 99.1
REMARK 620 4 HOH L9031 O 96.3 172.0 73.8
REMARK 620 5 HOH L9104 O 76.3 107.5 151.4 79.1
REMARK 620 6 HOH L9106 O 135.4 108.8 102.1 70.1 59.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG V9017 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP L 194 OXT
REMARK 620 2 HOH L9038 O 66.6
REMARK 620 3 ILE V 163 O 109.8 88.1
REMARK 620 4 ASP V 166 O 121.7 88.9 121.8
REMARK 620 5 SER V 169 O 92.7 152.3 117.1 86.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG N9006 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE N 163 O
REMARK 620 2 ASP N 166 O 68.9
REMARK 620 3 SER N 169 O 93.1 70.0
REMARK 620 4 HOH N 556 O 148.3 126.8 117.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Z9012 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU R 105 OE2
REMARK 620 2 HOH R1666 O 87.9
REMARK 620 3 SER Z 75 OG 145.3 99.7
REMARK 620 4 SER Z 78 OG 85.6 89.2 60.9
REMARK 620 5 HOH Z1650 O 110.8 87.1 103.4 163.0
REMARK 620 6 HOH Z1667 O 79.5 158.3 100.7 107.2 81.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG U9011 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR U 13 OG1
REMARK 620 2 TYR U 123 O 77.1
REMARK 620 3 ARG U 126 O 87.8 92.7
REMARK 620 4 MET U 129 O 155.8 92.3 114.7
REMARK 620 5 HOH U1558 O 70.8 124.9 128.5 99.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG U9020 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA U 127 O
REMARK 620 2 TYR U 128 O 97.5
REMARK 620 3 TYR U 128 N 66.4 83.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG W9013 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH V2268 O
REMARK 620 2 HOH W9026 O 122.6
REMARK 620 3 HOH W9075 O 104.6 132.8
REMARK 620 4 HOH W9113 O 134.0 75.3 70.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG W9015 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA W 163 O
REMARK 620 2 ASP W 166 O 82.8
REMARK 620 3 SER W 169 O 127.5 92.2
REMARK 620 4 HOH W9055 O 109.9 158.5 93.1
REMARK 620 5 HOH W9057 O 153.3 81.8 74.8 79.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Z9014 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR Z 163 O
REMARK 620 2 HIS Z 166 O 100.3
REMARK 620 3 VAL Z 169 O 124.6 94.2
REMARK 620 4 HOH Z 849 O 76.0 105.6 148.7
REMARK 620 5 HOH Z 975 O 131.4 102.0 96.1 56.6
REMARK 620 6 HOH Z1710 O 95.9 162.9 81.1 72.8 62.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 29016 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE 2 163 O
REMARK 620 2 ASP 2 166 O 78.9
REMARK 620 3 SER 2 169 O 104.8 84.8
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 9001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 9002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 9003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 9004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 9005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 9006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 9007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 9008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 9009
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 9010
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG U 9011
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Z 9012
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG W 9013
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Z 9014
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG W 9015
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 9016
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG V 9017
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Y 9018
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG T 9019
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG U 9020
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RYP RELATED DB: PDB
REMARK 900 20S WT-PROTEASOME FROM YEAST
DBREF 1G0U A 4 236 UNP P23639 PSA2_YEAST 1 250
DBREF 1G0U B 3 239 UNP P23638 PSA4_YEAST 1 245
DBREF 1G0U C 5 243 UNP P40303 PSA7_YEAST 1 243
DBREF 1G0U D 1 244 UNP P32379 PSA5_YEAST 1 250
DBREF 1G0U E 3 233 UNP P40302 PSA1_YEAST 1 234
DBREF 1G0U F 1 241 UNP P21242 PSA3_YEAST 1 247
DBREF 1G0U G -3 240 UNP P21243 PSA6_YEAST 1 252
DBREF 1G0U H 1 223 UNP P25043 PSB7_YEAST 30 251
DBREF 1G0U I -9 194 UNP P25451 PSB3_YEAST 1 205
DBREF 1G0U J -1 193 UNP P22141 PSB2_YEAST 1 198
DBREF 1G0U K 1 211 UNP P30656 PSB5_YEAST 76 287
DBREF 1G0U L -28 194 UNP P23724 PSB1_YEAST 1 241
DBREF 1G0U M -41 211 UNP P30657 PSB4_YEAST 1 266
DBREF 1G0U N 1 187J UNP P38624 PSB6_YEAST 20 215
DBREF 1G0U O 4 236 UNP P23639 PSA2_YEAST 1 250
DBREF 1G0U P 3 239 UNP P23638 PSA4_YEAST 1 245
DBREF 1G0U Q 5 243 UNP P40303 PSA7_YEAST 1 243
DBREF 1G0U R 1 244 UNP P32379 PSA5_YEAST 1 250
DBREF 1G0U S 3 233 UNP P40302 PSA1_YEAST 1 234
DBREF 1G0U T 1 241 UNP P21242 PSA3_YEAST 1 247
DBREF 1G0U U -3 240 UNP P21243 PSA6_YEAST 1 252
DBREF 1G0U V 1 223 UNP P25043 PSB7_YEAST 30 251
DBREF 1G0U W -9 194 UNP P25451 PSB3_YEAST 1 205
DBREF 1G0U X -1 193 UNP P22141 PSB2_YEAST 1 198
DBREF 1G0U Y 1 211 UNP P30656 PSB5_YEAST 76 287
DBREF 1G0U Z -28 194 UNP P23724 PSB1_YEAST 1 241
DBREF 1G0U 1 -41 211 UNP P30657 PSB4_YEAST 1 266
DBREF 1G0U 2 1 187J UNP P38624 PSB6_YEAST 20 215
SEQRES 1 A 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 A 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 A 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 A 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 A 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 A 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 A 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 A 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 A 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 A 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 A 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 A 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 A 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 A 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 A 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 A 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 A 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 A 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 A 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 A 250 GLU ALA LEU
SEQRES 1 B 245 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 B 245 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 B 245 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 B 245 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 B 245 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 B 245 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 B 245 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 B 245 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 B 245 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 B 245 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 B 245 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 B 245 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 B 245 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 B 245 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 B 245 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 B 245 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 B 245 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 B 245 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 B 245 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR
SEQRES 1 C 243 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 C 243 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 C 243 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 C 243 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 C 243 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 C 243 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 C 243 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 C 243 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 C 243 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 C 243 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 C 243 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 C 243 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 C 243 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 C 243 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 C 243 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 C 243 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 C 243 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 C 243 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 C 243 GLN ILE GLU GLN GLU LYS GLN GLU GLN
SEQRES 1 D 241 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 D 241 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 D 241 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 D 241 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 D 241 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 D 241 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 D 241 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 D 241 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 D 241 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 D 241 ASP LEU ALA ALA ALA ALA ALA MET SER ARG PRO PHE GLY
SEQRES 11 D 241 VAL ALA LEU LEU ILE ALA GLY HIS ASP ALA ASP ASP GLY
SEQRES 12 D 241 TYR GLN LEU PHE HIS ALA GLU PRO SER GLY THR PHE TYR
SEQRES 13 D 241 ARG TYR ASN ALA LYS ALA ILE GLY SER GLY SER GLU GLY
SEQRES 14 D 241 ALA GLN ALA GLU LEU LEU ASN GLU TRP HIS SER SER LEU
SEQRES 15 D 241 THR LEU LYS GLU ALA GLU LEU LEU VAL LEU LYS ILE LEU
SEQRES 16 D 241 LYS GLN VAL MET GLU GLU LYS LEU ASP GLU ASN ASN ALA
SEQRES 17 D 241 GLN LEU SER CYS ILE THR LYS GLN ASP GLY PHE LYS ILE
SEQRES 18 D 241 TYR ASP ASN GLU LYS THR ALA GLU LEU ILE LYS GLU LEU
SEQRES 19 D 241 LYS GLU LYS GLU ALA ALA GLU
SEQRES 1 E 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 E 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 E 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 E 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 E 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 E 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 E 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 E 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 E 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 E 234 LYS ASN THR GLN SER ALA GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 E 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 E 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 E 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 E 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 E 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 E 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 E 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 E 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 F 248 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 F 248 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 F 248 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 F 248 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 F 248 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 F 248 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 F 248 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 F 248 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 F 248 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 F 248 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 F 248 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 F 248 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 F 248 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 F 248 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 F 248 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 F 248 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 F 248 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 F 248 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 F 248 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 F 248 ASN
SEQRES 1 G 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 G 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 G 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 G 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 G 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 G 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 G 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 G 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 G 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 G 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 G 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 G 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 G 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 G 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 G 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 G 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 G 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 G 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 G 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 G 252 ILE ALA GLU GLN ASP
SEQRES 1 H 222 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 H 222 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 H 222 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 H 222 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 H 222 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 H 222 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 H 222 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 H 222 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 H 222 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 H 222 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 H 222 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 H 222 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 H 222 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 H 222 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 H 222 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 H 222 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 H 222 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 H 222 ASP
SEQRES 1 I 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 I 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 I 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 I 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 I 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 I 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 I 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 I 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 I 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 I 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 I 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 I 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 I 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 I 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 I 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 I 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 J 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 J 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 J 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 J 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 J 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 J 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 J 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 J 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 J 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 J 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 J 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 J 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 J 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 J 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 J 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 J 198 GLN ALA GLN
SEQRES 1 K 212 THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE
SEQRES 2 K 212 VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL
SEQRES 3 K 212 ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 K 212 PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS
SEQRES 5 K 212 GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU
SEQRES 6 K 212 HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 K 212 ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS
SEQRES 8 K 212 GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR
SEQRES 9 K 212 THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER
SEQRES 10 K 212 ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY
SEQRES 11 K 212 SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN
SEQRES 12 K 212 TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU
SEQRES 13 K 212 GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA
SEQRES 14 K 212 TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU
SEQRES 15 K 212 ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU
SEQRES 16 K 212 LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN
SEQRES 17 K 212 ASN VAL ILE GLY
SEQRES 1 L 241 MET ALA THR ILE ALA SER GLU TYR SER SER GLU ALA SER
SEQRES 2 L 241 ASN THR PRO ILE GLU HIS GLN PHE ASN PRO TYR GLY ASP
SEQRES 3 L 241 ASN GLY GLY THR ILE LEU GLY ILE ALA GLY GLU ASP PHE
SEQRES 4 L 241 ALA VAL LEU ALA GLY ASP THR ARG ASN ILE THR ASP TYR
SEQRES 5 L 241 SER ILE ASN SER ARG TYR GLU PRO LYS VAL PHE ASP CYS
SEQRES 6 L 241 GLY ASP ASN ILE VAL MET SER ALA ASN GLY PHE ALA ALA
SEQRES 7 L 241 ASP GLY ASP ALA LEU VAL LYS ARG PHE LYS ASN SER VAL
SEQRES 8 L 241 LYS TRP TYR HIS PHE ASP HIS ASN ASP LYS LYS LEU SER
SEQRES 9 L 241 ILE ASN SER ALA ALA ARG ASN ILE GLN HIS LEU LEU TYR
SEQRES 10 L 241 GLY LYS ARG PHE PHE PRO TYR TYR VAL HIS THR ILE ILE
SEQRES 11 L 241 ALA GLY LEU ASP GLU ASP GLY LYS GLY ALA VAL TYR SER
SEQRES 12 L 241 PHE ASP PRO VAL GLY SER TYR GLU ARG GLU GLN CYS ARG
SEQRES 13 L 241 ALA GLY GLY ALA ALA ALA SER LEU ILE MET PRO PHE LEU
SEQRES 14 L 241 ASP ASN GLN VAL ASN PHE LYS ASN GLN TYR GLU PRO GLY
SEQRES 15 L 241 THR ASN GLY LYS VAL LYS LYS PRO LEU LYS TYR LEU SER
SEQRES 16 L 241 VAL GLU GLU VAL ILE LYS LEU VAL ARG ASP SER PHE THR
SEQRES 17 L 241 SER ALA THR GLU ARG HIS ILE GLN VAL GLY ASP GLY LEU
SEQRES 18 L 241 GLU ILE LEU ILE VAL THR LYS ASP GLY VAL ARG LYS GLU
SEQRES 19 L 241 PHE TYR GLU LEU LYS ARG ASP
SEQRES 1 M 266 MET ASN HIS ASP PRO PHE SER TRP GLY ARG PRO ALA ASP
SEQRES 2 M 266 SER THR TYR GLY ALA TYR ASN THR GLN ILE ALA ASN ALA
SEQRES 3 M 266 GLY ALA SER PRO MET VAL ASN THR GLN GLN PRO ILE VAL
SEQRES 4 M 266 THR GLY THR SER VAL ILE SER MET LYS TYR ASP ASN GLY
SEQRES 5 M 266 VAL ILE ILE ALA ALA ASP ASN LEU GLY SER TYR GLY SER
SEQRES 6 M 266 LEU LEU ARG PHE ASN GLY VAL GLU ARG LEU ILE PRO VAL
SEQRES 7 M 266 GLY ASP ASN THR VAL VAL GLY ILE SER GLY ASP ILE SER
SEQRES 8 M 266 ASP MET GLN HIS ILE GLU ARG LEU LEU LYS ASP LEU VAL
SEQRES 9 M 266 THR GLU ASN ALA TYR ASP ASN PRO LEU ALA ASP ALA GLU
SEQRES 10 M 266 GLU ALA LEU GLU PRO SER TYR ILE PHE GLU TYR LEU ALA
SEQRES 11 M 266 THR VAL MET TYR GLN ARG ARG SER LYS MET ASN PRO LEU
SEQRES 12 M 266 TRP ASN ALA ILE ILE VAL ALA GLY VAL GLN SER ASN GLY
SEQRES 13 M 266 ASP GLN PHE LEU ARG TYR VAL ASN LEU LEU GLY VAL THR
SEQRES 14 M 266 TYR SER SER PRO THR LEU ALA THR GLY PHE GLY ALA HIS
SEQRES 15 M 266 MET ALA ASN PRO LEU LEU ARG LYS VAL VAL ASP ARG GLU
SEQRES 16 M 266 SER ASP ILE PRO LYS THR THR VAL GLN VAL ALA GLU GLU
SEQRES 17 M 266 ALA ILE VAL ASN ALA MET ARG VAL LEU TYR TYR ARG ASP
SEQRES 18 M 266 ALA ARG SER SER ARG ASN PHE SER LEU ALA ILE ILE ASP
SEQRES 19 M 266 LYS ASN THR GLY LEU THR PHE LYS LYS ASN LEU GLN VAL
SEQRES 20 M 266 GLU ASN MET LYS TRP ASP PHE ALA LYS ASP ILE LYS GLY
SEQRES 21 M 266 TYR GLY THR GLN LYS ILE
SEQRES 1 N 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 N 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 N 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 N 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 N 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 N 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 N 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 N 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 N 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 N 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 N 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 N 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 N 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 N 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 N 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 N 196 LEU
SEQRES 1 O 250 MET THR ASP ARG TYR SER PHE SER LEU THR THR PHE SER
SEQRES 2 O 250 PRO SER GLY LYS LEU GLY GLN ILE ASP TYR ALA LEU THR
SEQRES 3 O 250 ALA VAL LYS GLN GLY VAL THR SER LEU GLY ILE LYS ALA
SEQRES 4 O 250 THR ASN GLY VAL VAL ILE ALA THR GLU LYS LYS SER SER
SEQRES 5 O 250 SER PRO LEU ALA MET SER GLU THR LEU SER LYS VAL SER
SEQRES 6 O 250 LEU LEU THR PRO ASP ILE GLY ALA VAL TYR SER GLY MET
SEQRES 7 O 250 GLY PRO ASP TYR ARG VAL LEU VAL ASP LYS SER ARG LYS
SEQRES 8 O 250 VAL ALA HIS THR SER TYR LYS ARG ILE TYR GLY GLU TYR
SEQRES 9 O 250 PRO PRO THR LYS LEU LEU VAL SER GLU VAL ALA LYS ILE
SEQRES 10 O 250 MET GLN GLU ALA THR GLN SER GLY GLY VAL ARG PRO PHE
SEQRES 11 O 250 GLY VAL SER LEU LEU ILE ALA GLY HIS ASP GLU PHE ASN
SEQRES 12 O 250 GLY PHE SER LEU TYR GLN VAL ASP PRO SER GLY SER TYR
SEQRES 13 O 250 PHE PRO TRP LYS ALA THR ALA ILE GLY LYS GLY SER VAL
SEQRES 14 O 250 ALA ALA LYS THR PHE LEU GLU LYS ARG TRP ASN ASP GLU
SEQRES 15 O 250 LEU GLU LEU GLU ASP ALA ILE HIS ILE ALA LEU LEU THR
SEQRES 16 O 250 LEU LYS GLU SER VAL GLU GLY GLU PHE ASN GLY ASP THR
SEQRES 17 O 250 ILE GLU LEU ALA ILE ILE GLY ASP GLU ASN PRO ASP LEU
SEQRES 18 O 250 LEU GLY TYR THR GLY ILE PRO THR ASP LYS GLY PRO ARG
SEQRES 19 O 250 PHE ARG LYS LEU THR SER GLN GLU ILE ASN ASP ARG LEU
SEQRES 20 O 250 GLU ALA LEU
SEQRES 1 P 245 MET GLY SER ARG ARG TYR ASP SER ARG THR THR ILE PHE
SEQRES 2 P 245 SER PRO GLU GLY ARG LEU TYR GLN VAL GLU TYR ALA LEU
SEQRES 3 P 245 GLU SER ILE SER HIS ALA GLY THR ALA ILE GLY ILE MET
SEQRES 4 P 245 ALA SER ASP GLY ILE VAL LEU ALA ALA GLU ARG LYS VAL
SEQRES 5 P 245 THR SER THR LEU LEU GLU GLN ASP THR SER THR GLU LYS
SEQRES 6 P 245 LEU TYR LYS LEU ASN ASP LYS ILE ALA VAL ALA VAL ALA
SEQRES 7 P 245 GLY LEU THR ALA ASP ALA GLU ILE LEU ILE ASN THR ALA
SEQRES 8 P 245 ARG ILE HIS ALA GLN ASN TYR LEU LYS THR TYR ASN GLU
SEQRES 9 P 245 ASP ILE PRO VAL GLU ILE LEU VAL ARG ARG LEU SER ASP
SEQRES 10 P 245 ILE LYS GLN GLY TYR THR GLN HIS GLY GLY LEU ARG PRO
SEQRES 11 P 245 PHE GLY VAL SER PHE ILE TYR ALA GLY TYR ASP ASP ARG
SEQRES 12 P 245 TYR GLY TYR GLN LEU TYR THR SER ASN PRO SER GLY ASN
SEQRES 13 P 245 TYR THR GLY TRP LYS ALA ILE SER VAL GLY ALA ASN THR
SEQRES 14 P 245 SER ALA ALA GLN THR LEU LEU GLN MET ASP TYR LYS ASP
SEQRES 15 P 245 ASP MET LYS VAL ASP ASP ALA ILE GLU LEU ALA LEU LYS
SEQRES 16 P 245 THR LEU SER LYS THR THR ASP SER SER ALA LEU THR TYR
SEQRES 17 P 245 ASP ARG LEU GLU PHE ALA THR ILE ARG LYS GLY ALA ASN
SEQRES 18 P 245 ASP GLY GLU VAL TYR GLN LYS ILE PHE LYS PRO GLN GLU
SEQRES 19 P 245 ILE LYS ASP ILE LEU VAL LYS THR GLY ILE THR
SEQRES 1 Q 243 MET SER GLY TYR ASP ARG ALA LEU SER ILE PHE SER PRO
SEQRES 2 Q 243 ASP GLY HIS ILE PHE GLN VAL GLU TYR ALA LEU GLU ALA
SEQRES 3 Q 243 VAL LYS ARG GLY THR CYS ALA VAL GLY VAL LYS GLY LYS
SEQRES 4 Q 243 ASN CYS VAL VAL LEU GLY CYS GLU ARG ARG SER THR LEU
SEQRES 5 Q 243 LYS LEU GLN ASP THR ARG ILE THR PRO SER LYS VAL SER
SEQRES 6 Q 243 LYS ILE ASP SER HIS VAL VAL LEU SER PHE SER GLY LEU
SEQRES 7 Q 243 ASN ALA ASP SER ARG ILE LEU ILE GLU LYS ALA ARG VAL
SEQRES 8 Q 243 GLU ALA GLN SER HIS ARG LEU THR LEU GLU ASP PRO VAL
SEQRES 9 Q 243 THR VAL GLU TYR LEU THR ARG TYR VAL ALA GLY VAL GLN
SEQRES 10 Q 243 GLN ARG TYR THR GLN SER GLY GLY VAL ARG PRO PHE GLY
SEQRES 11 Q 243 VAL SER THR LEU ILE ALA GLY PHE ASP PRO ARG ASP ASP
SEQRES 12 Q 243 GLU PRO LYS LEU TYR GLN THR GLU PRO SER GLY ILE TYR
SEQRES 13 Q 243 SER SER TRP SER ALA GLN THR ILE GLY ARG ASN SER LYS
SEQRES 14 Q 243 THR VAL ARG GLU PHE LEU GLU LYS ASN TYR ASP ARG LYS
SEQRES 15 Q 243 GLU PRO PRO ALA THR VAL GLU GLU CYS VAL LYS LEU THR
SEQRES 16 Q 243 VAL ARG SER LEU LEU GLU VAL VAL GLN THR GLY ALA LYS
SEQRES 17 Q 243 ASN ILE GLU ILE THR VAL VAL LYS PRO ASP SER ASP ILE
SEQRES 18 Q 243 VAL ALA LEU SER SER GLU GLU ILE ASN GLN TYR VAL THR
SEQRES 19 Q 243 GLN ILE GLU GLN GLU LYS GLN GLU GLN
SEQRES 1 R 241 MET PHE LEU THR ARG SER GLU TYR ASP ARG GLY VAL SER
SEQRES 2 R 241 THR PHE SER PRO GLU GLY ARG LEU PHE GLN VAL GLU TYR
SEQRES 3 R 241 SER LEU GLU ALA ILE LYS LEU GLY SER THR ALA ILE GLY
SEQRES 4 R 241 ILE ALA THR LYS GLU GLY VAL VAL LEU GLY VAL GLU LYS
SEQRES 5 R 241 ARG ALA THR SER PRO LEU LEU GLU SER ASP SER ILE GLU
SEQRES 6 R 241 LYS ILE VAL GLU ILE ASP ARG HIS ILE GLY CYS ALA MET
SEQRES 7 R 241 SER GLY LEU THR ALA ASP ALA ARG SER MET ILE GLU HIS
SEQRES 8 R 241 ALA ARG THR ALA ALA VAL THR HIS ASN LEU TYR TYR ASP
SEQRES 9 R 241 GLU ASP ILE ASN VAL GLU SER LEU THR GLN SER VAL CYS
SEQRES 10 R 241 ASP LEU ALA ALA ALA ALA ALA MET SER ARG PRO PHE GLY
SEQRES 11 R 241 VAL ALA LEU LEU ILE ALA GLY HIS ASP ALA ASP ASP GLY
SEQRES 12 R 241 TYR GLN LEU PHE HIS ALA GLU PRO SER GLY THR PHE TYR
SEQRES 13 R 241 ARG TYR ASN ALA LYS ALA ILE GLY SER GLY SER GLU GLY
SEQRES 14 R 241 ALA GLN ALA GLU LEU LEU ASN GLU TRP HIS SER SER LEU
SEQRES 15 R 241 THR LEU LYS GLU ALA GLU LEU LEU VAL LEU LYS ILE LEU
SEQRES 16 R 241 LYS GLN VAL MET GLU GLU LYS LEU ASP GLU ASN ASN ALA
SEQRES 17 R 241 GLN LEU SER CYS ILE THR LYS GLN ASP GLY PHE LYS ILE
SEQRES 18 R 241 TYR ASP ASN GLU LYS THR ALA GLU LEU ILE LYS GLU LEU
SEQRES 19 R 241 LYS GLU LYS GLU ALA ALA GLU
SEQRES 1 S 234 MET PHE ARG ASN ASN TYR ASP GLY ASP THR VAL THR PHE
SEQRES 2 S 234 SER PRO THR GLY ARG LEU PHE GLN VAL GLU TYR ALA LEU
SEQRES 3 S 234 GLU ALA ILE LYS GLN GLY SER VAL THR VAL GLY LEU ARG
SEQRES 4 S 234 SER ASN THR HIS ALA VAL LEU VAL ALA LEU LYS ARG ASN
SEQRES 5 S 234 ALA ASP GLU LEU SER SER TYR GLN LYS LYS ILE ILE LYS
SEQRES 6 S 234 CYS ASP GLU HIS MET GLY LEU SER LEU ALA GLY LEU ALA
SEQRES 7 S 234 PRO ASP ALA ARG VAL LEU SER ASN TYR LEU ARG GLN GLN
SEQRES 8 S 234 CYS ASN TYR SER SER LEU VAL PHE ASN ARG LYS LEU ALA
SEQRES 9 S 234 VAL GLU ARG ALA GLY HIS LEU LEU CYS ASP LYS ALA GLN
SEQRES 10 S 234 LYS ASN THR GLN SER ALA GLY GLY ARG PRO TYR GLY VAL
SEQRES 11 S 234 GLY LEU LEU ILE ILE GLY TYR ASP LYS SER GLY ALA HIS
SEQRES 12 S 234 LEU LEU GLU PHE GLN PRO SER GLY ASN VAL THR GLU LEU
SEQRES 13 S 234 TYR GLY THR ALA ILE GLY ALA ARG SER GLN GLY ALA LYS
SEQRES 14 S 234 THR TYR LEU GLU ARG THR LEU ASP THR PHE ILE LYS ILE
SEQRES 15 S 234 ASP GLY ASN PRO ASP GLU LEU ILE LYS ALA GLY VAL GLU
SEQRES 16 S 234 ALA ILE SER GLN SER LEU ARG ASP GLU SER LEU THR VAL
SEQRES 17 S 234 ASP ASN LEU SER ILE ALA ILE VAL GLY LYS ASP THR PRO
SEQRES 18 S 234 PHE THR ILE TYR ASP GLY GLU ALA VAL ALA LYS TYR ILE
SEQRES 1 T 248 MET THR SER ILE GLY THR GLY TYR ASP LEU SER ASN SER
SEQRES 2 T 248 VAL PHE SER PRO ASP GLY ARG ASN PHE GLN VAL GLU TYR
SEQRES 3 T 248 ALA VAL LYS ALA VAL GLU ASN GLY THR THR SER ILE GLY
SEQRES 4 T 248 ILE LYS CYS ASN ASP GLY VAL VAL PHE ALA VAL GLU LYS
SEQRES 5 T 248 LEU ILE THR SER LYS LEU LEU VAL PRO GLN LYS ASN VAL
SEQRES 6 T 248 LYS ILE GLN VAL VAL ASP ARG HIS ILE GLY CYS VAL TYR
SEQRES 7 T 248 SER GLY LEU ILE PRO ASP GLY ARG HIS LEU VAL ASN ARG
SEQRES 8 T 248 GLY ARG GLU GLU ALA ALA SER PHE LYS LYS LEU TYR LYS
SEQRES 9 T 248 THR PRO ILE PRO ILE PRO ALA PHE ALA ASP ARG LEU GLY
SEQRES 10 T 248 GLN TYR VAL GLN ALA HIS THR LEU TYR ASN SER VAL ARG
SEQRES 11 T 248 PRO PHE GLY VAL SER THR ILE PHE GLY GLY VAL ASP LYS
SEQRES 12 T 248 ASN GLY ALA HIS LEU TYR MET LEU GLU PRO SER GLY SER
SEQRES 13 T 248 TYR TRP GLY TYR LYS GLY ALA ALA THR GLY LYS GLY ARG
SEQRES 14 T 248 GLN SER ALA LYS ALA GLU LEU GLU LYS LEU VAL ASP HIS
SEQRES 15 T 248 HIS PRO GLU GLY LEU SER ALA ARG GLU ALA VAL LYS GLN
SEQRES 16 T 248 ALA ALA LYS ILE ILE TYR LEU ALA HIS GLU ASP ASN LYS
SEQRES 17 T 248 GLU LYS ASP PHE GLU LEU GLU ILE SER TRP CYS SER LEU
SEQRES 18 T 248 SER GLU THR ASN GLY LEU HIS LYS PHE VAL LYS GLY ASP
SEQRES 19 T 248 LEU LEU GLN GLU ALA ILE ASP PHE ALA GLN LYS GLU ILE
SEQRES 20 T 248 ASN
SEQRES 1 U 252 MET SER GLY ALA ALA ALA ALA SER ALA ALA GLY TYR ASP
SEQRES 2 U 252 ARG HIS ILE THR ILE PHE SER PRO GLU GLY ARG LEU TYR
SEQRES 3 U 252 GLN VAL GLU TYR ALA PHE LYS ALA THR ASN GLN THR ASN
SEQRES 4 U 252 ILE ASN SER LEU ALA VAL ARG GLY LYS ASP CYS THR VAL
SEQRES 5 U 252 VAL ILE SER GLN LYS LYS VAL PRO ASP LYS LEU LEU ASP
SEQRES 6 U 252 PRO THR THR VAL SER TYR ILE PHE CYS ILE SER ARG THR
SEQRES 7 U 252 ILE GLY MET VAL VAL ASN GLY PRO ILE PRO ASP ALA ARG
SEQRES 8 U 252 ASN ALA ALA LEU ARG ALA LYS ALA GLU ALA ALA GLU PHE
SEQRES 9 U 252 ARG TYR LYS TYR GLY TYR ASP MET PRO CYS ASP VAL LEU
SEQRES 10 U 252 ALA LYS ARG MET ALA ASN LEU SER GLN ILE TYR THR GLN
SEQRES 11 U 252 ARG ALA TYR MET ARG PRO LEU GLY VAL ILE LEU THR PHE
SEQRES 12 U 252 VAL SER VAL ASP GLU GLU LEU GLY PRO SER ILE TYR LYS
SEQRES 13 U 252 THR ASP PRO ALA GLY TYR TYR VAL GLY TYR LYS ALA THR
SEQRES 14 U 252 ALA THR GLY PRO LYS GLN GLN GLU ILE THR THR ASN LEU
SEQRES 15 U 252 GLU ASN HIS PHE LYS LYS SER LYS ILE ASP HIS ILE ASN
SEQRES 16 U 252 GLU GLU SER TRP GLU LYS VAL VAL GLU PHE ALA ILE THR
SEQRES 17 U 252 HIS MET ILE ASP ALA LEU GLY THR GLU PHE SER LYS ASN
SEQRES 18 U 252 ASP LEU GLU VAL GLY VAL ALA THR LYS ASP LYS PHE PHE
SEQRES 19 U 252 THR LEU SER ALA GLU ASN ILE GLU GLU ARG LEU VAL ALA
SEQRES 20 U 252 ILE ALA GLU GLN ASP
SEQRES 1 V 222 THR THR ILE VAL GLY VAL LYS PHE ASN ASN GLY VAL VAL
SEQRES 2 V 222 ILE ALA ALA ASP THR ARG SER THR GLN GLY PRO ILE VAL
SEQRES 3 V 222 ALA ASP LYS ASN CYS ALA LYS LEU HIS ARG ILE SER PRO
SEQRES 4 V 222 LYS ILE TRP CYS ALA GLY ALA GLY THR ALA ALA ASP THR
SEQRES 5 V 222 GLU ALA VAL THR GLN LEU ILE GLY SER ASN ILE GLU LEU
SEQRES 6 V 222 HIS SER LEU TYR THR SER ARG GLU PRO ARG VAL VAL SER
SEQRES 7 V 222 ALA LEU GLN MET LEU LYS GLN HIS LEU PHE LYS TYR GLN
SEQRES 8 V 222 GLY HIS ILE GLY ALA TYR LEU ILE VAL ALA GLY VAL ASP
SEQRES 9 V 222 PRO THR GLY SER HIS LEU PHE SER ILE HIS ALA HIS GLY
SEQRES 10 V 222 SER THR ASP VAL GLY TYR TYR LEU SER LEU GLY SER GLY
SEQRES 11 V 222 SER LEU ALA ALA MET ALA VAL LEU GLU SER HIS TRP LYS
SEQRES 12 V 222 GLN ASP LEU THR LYS GLU GLU ALA ILE LYS LEU ALA SER
SEQRES 13 V 222 ASP ALA ILE GLN ALA GLY ILE TRP ASN ASP LEU GLY SER
SEQRES 14 V 222 GLY SER ASN VAL ASP VAL CYS VAL MET GLU ILE GLY LYS
SEQRES 15 V 222 ASP ALA GLU TYR LEU ARG ASN TYR LEU THR PRO ASN VAL
SEQRES 16 V 222 ARG GLU GLU LYS GLN LYS SER TYR LYS PHE PRO ARG GLY
SEQRES 17 V 222 THR THR ALA VAL LEU LYS GLU SER ILE VAL ASN ILE CYS
SEQRES 18 V 222 ASP
SEQRES 1 W 205 MET SER ASP PRO SER SER ILE ASN GLY GLY ILE VAL VAL
SEQRES 2 W 205 ALA MET THR GLY LYS ASP CYS VAL ALA ILE ALA CYS ASP
SEQRES 3 W 205 LEU ARG LEU GLY SER GLN SER LEU GLY VAL SER ASN LYS
SEQRES 4 W 205 PHE GLU LYS ILE PHE HIS TYR GLY HIS VAL PHE LEU GLY
SEQRES 5 W 205 ILE THR GLY LEU ALA THR ASP VAL THR THR LEU ASN GLU
SEQRES 6 W 205 MET PHE ARG TYR LYS THR ASN LEU TYR LYS LEU LYS GLU
SEQRES 7 W 205 GLU ARG ALA ILE GLU PRO GLU THR PHE THR GLN LEU VAL
SEQRES 8 W 205 SER SER SER LEU TYR GLU ARG ARG PHE GLY PRO TYR PHE
SEQRES 9 W 205 VAL GLY PRO VAL VAL ALA GLY ILE ASN SER LYS SER GLY
SEQRES 10 W 205 LYS PRO PHE ILE ALA GLY PHE ASP LEU ILE GLY CYS ILE
SEQRES 11 W 205 ASP GLU ALA LYS ASP PHE ILE VAL SER GLY THR ALA SER
SEQRES 12 W 205 ASP GLN LEU PHE GLY MET CYS GLU SER LEU TYR GLU PRO
SEQRES 13 W 205 ASN LEU GLU PRO GLU ASP LEU PHE GLU THR ILE SER GLN
SEQRES 14 W 205 ALA LEU LEU ASN ALA ALA ASP ARG ASP ALA LEU SER GLY
SEQRES 15 W 205 TRP GLY ALA VAL VAL TYR ILE ILE LYS LYS ASP GLU VAL
SEQRES 16 W 205 VAL LYS ARG TYR LEU LYS MET ARG GLN ASP
SEQRES 1 X 198 MET ASP ILE ILE LEU GLY ILE ARG VAL GLN ASP SER VAL
SEQRES 2 X 198 ILE LEU ALA SER SER LYS ALA VAL THR ARG GLY ILE SER
SEQRES 3 X 198 VAL LEU LYS ASP SER ASP ASP LYS THR ARG GLN LEU SER
SEQRES 4 X 198 PRO HIS THR LEU MET SER PHE ALA GLY GLU ALA GLY ASP
SEQRES 5 X 198 THR VAL GLN PHE ALA GLU TYR ILE GLN ALA ASN ILE GLN
SEQRES 6 X 198 LEU TYR SER ILE ARG GLU ASP TYR GLU LEU SER PRO GLN
SEQRES 7 X 198 ALA VAL SER SER PHE VAL ARG GLN GLU LEU ALA LYS SER
SEQRES 8 X 198 ILE ARG SER ARG ARG PRO TYR GLN VAL ASN VAL LEU ILE
SEQRES 9 X 198 GLY GLY TYR ASP LYS LYS LYS ASN LYS PRO GLU LEU TYR
SEQRES 10 X 198 GLN ILE ASP TYR LEU GLY THR LYS VAL GLU LEU PRO TYR
SEQRES 11 X 198 GLY ALA HIS GLY TYR SER GLY PHE TYR THR PHE SER LEU
SEQRES 12 X 198 LEU ASP HIS HIS TYR ARG PRO ASP MET THR THR GLU GLU
SEQRES 13 X 198 GLY LEU ASP LEU LEU LYS LEU CYS VAL GLN GLU LEU GLU
SEQRES 14 X 198 LYS ARG MET PRO MET ASP PHE LYS GLY VAL ILE VAL LYS
SEQRES 15 X 198 ILE VAL ASP LYS ASP GLY ILE ARG GLN VAL ASP ASP PHE
SEQRES 16 X 198 GLN ALA GLN
SEQRES 1 Y 212 THR THR THR LEU ALA PHE ARG PHE GLN GLY GLY ILE ILE
SEQRES 2 Y 212 VAL ALA VAL ASP SER ARG ALA THR ALA GLY ASN TRP VAL
SEQRES 3 Y 212 ALA SER GLN THR VAL LYS LYS VAL ILE GLU ILE ASN PRO
SEQRES 4 Y 212 PHE LEU LEU GLY THR MET ALA GLY GLY ALA ALA ASP CYS
SEQRES 5 Y 212 GLN PHE TRP GLU THR TRP LEU GLY SER GLN CYS ARG LEU
SEQRES 6 Y 212 HIS GLU LEU ARG GLU LYS GLU ARG ILE SER VAL ALA ALA
SEQRES 7 Y 212 ALA SER LYS ILE LEU SER ASN LEU VAL TYR GLN TYR LYS
SEQRES 8 Y 212 GLY ALA GLY LEU SER MET GLY THR MET ILE CYS GLY TYR
SEQRES 9 Y 212 THR ARG LYS GLU GLY PRO THR ILE TYR TYR VAL ASP SER
SEQRES 10 Y 212 ASP GLY THR ARG LEU LYS GLY ASP ILE PHE CYS VAL GLY
SEQRES 11 Y 212 SER GLY GLN THR PHE ALA TYR GLY VAL LEU ASP SER ASN
SEQRES 12 Y 212 TYR LYS TRP ASP LEU SER VAL GLU ASP ALA LEU TYR LEU
SEQRES 13 Y 212 GLY LYS ARG SER ILE LEU ALA ALA ALA HIS ARG ASP ALA
SEQRES 14 Y 212 TYR SER GLY GLY SER VAL ASN LEU TYR HIS VAL THR GLU
SEQRES 15 Y 212 ASP GLY TRP ILE TYR HIS GLY ASN HIS ASP VAL GLY GLU
SEQRES 16 Y 212 LEU PHE TRP LYS VAL LYS GLU GLU GLU GLY SER PHE ASN
SEQRES 17 Y 212 ASN VAL ILE GLY
SEQRES 1 Z 241 MET ALA THR ILE ALA SER GLU TYR SER SER GLU ALA SER
SEQRES 2 Z 241 ASN THR PRO ILE GLU HIS GLN PHE ASN PRO TYR GLY ASP
SEQRES 3 Z 241 ASN GLY GLY THR ILE LEU GLY ILE ALA GLY GLU ASP PHE
SEQRES 4 Z 241 ALA VAL LEU ALA GLY ASP THR ARG ASN ILE THR ASP TYR
SEQRES 5 Z 241 SER ILE ASN SER ARG TYR GLU PRO LYS VAL PHE ASP CYS
SEQRES 6 Z 241 GLY ASP ASN ILE VAL MET SER ALA ASN GLY PHE ALA ALA
SEQRES 7 Z 241 ASP GLY ASP ALA LEU VAL LYS ARG PHE LYS ASN SER VAL
SEQRES 8 Z 241 LYS TRP TYR HIS PHE ASP HIS ASN ASP LYS LYS LEU SER
SEQRES 9 Z 241 ILE ASN SER ALA ALA ARG ASN ILE GLN HIS LEU LEU TYR
SEQRES 10 Z 241 GLY LYS ARG PHE PHE PRO TYR TYR VAL HIS THR ILE ILE
SEQRES 11 Z 241 ALA GLY LEU ASP GLU ASP GLY LYS GLY ALA VAL TYR SER
SEQRES 12 Z 241 PHE ASP PRO VAL GLY SER TYR GLU ARG GLU GLN CYS ARG
SEQRES 13 Z 241 ALA GLY GLY ALA ALA ALA SER LEU ILE MET PRO PHE LEU
SEQRES 14 Z 241 ASP ASN GLN VAL ASN PHE LYS ASN GLN TYR GLU PRO GLY
SEQRES 15 Z 241 THR ASN GLY LYS VAL LYS LYS PRO LEU LYS TYR LEU SER
SEQRES 16 Z 241 VAL GLU GLU VAL ILE LYS LEU VAL ARG ASP SER PHE THR
SEQRES 17 Z 241 SER ALA THR GLU ARG HIS ILE GLN VAL GLY ASP GLY LEU
SEQRES 18 Z 241 GLU ILE LEU ILE VAL THR LYS ASP GLY VAL ARG LYS GLU
SEQRES 19 Z 241 PHE TYR GLU LEU LYS ARG ASP
SEQRES 1 1 266 MET ASN HIS ASP PRO PHE SER TRP GLY ARG PRO ALA ASP
SEQRES 2 1 266 SER THR TYR GLY ALA TYR ASN THR GLN ILE ALA ASN ALA
SEQRES 3 1 266 GLY ALA SER PRO MET VAL ASN THR GLN GLN PRO ILE VAL
SEQRES 4 1 266 THR GLY THR SER VAL ILE SER MET LYS TYR ASP ASN GLY
SEQRES 5 1 266 VAL ILE ILE ALA ALA ASP ASN LEU GLY SER TYR GLY SER
SEQRES 6 1 266 LEU LEU ARG PHE ASN GLY VAL GLU ARG LEU ILE PRO VAL
SEQRES 7 1 266 GLY ASP ASN THR VAL VAL GLY ILE SER GLY ASP ILE SER
SEQRES 8 1 266 ASP MET GLN HIS ILE GLU ARG LEU LEU LYS ASP LEU VAL
SEQRES 9 1 266 THR GLU ASN ALA TYR ASP ASN PRO LEU ALA ASP ALA GLU
SEQRES 10 1 266 GLU ALA LEU GLU PRO SER TYR ILE PHE GLU TYR LEU ALA
SEQRES 11 1 266 THR VAL MET TYR GLN ARG ARG SER LYS MET ASN PRO LEU
SEQRES 12 1 266 TRP ASN ALA ILE ILE VAL ALA GLY VAL GLN SER ASN GLY
SEQRES 13 1 266 ASP GLN PHE LEU ARG TYR VAL ASN LEU LEU GLY VAL THR
SEQRES 14 1 266 TYR SER SER PRO THR LEU ALA THR GLY PHE GLY ALA HIS
SEQRES 15 1 266 MET ALA ASN PRO LEU LEU ARG LYS VAL VAL ASP ARG GLU
SEQRES 16 1 266 SER ASP ILE PRO LYS THR THR VAL GLN VAL ALA GLU GLU
SEQRES 17 1 266 ALA ILE VAL ASN ALA MET ARG VAL LEU TYR TYR ARG ASP
SEQRES 18 1 266 ALA ARG SER SER ARG ASN PHE SER LEU ALA ILE ILE ASP
SEQRES 19 1 266 LYS ASN THR GLY LEU THR PHE LYS LYS ASN LEU GLN VAL
SEQRES 20 1 266 GLU ASN MET LYS TRP ASP PHE ALA LYS ASP ILE LYS GLY
SEQRES 21 1 266 TYR GLY THR GLN LYS ILE
SEQRES 1 2 196 THR SER ILE MET ALA VAL THR PHE LYS ASP GLY VAL ILE
SEQRES 2 2 196 LEU GLY ALA ASP SER ARG THR THR THR GLY ALA TYR ILE
SEQRES 3 2 196 ALA ASN ARG VAL THR ASP LYS LEU THR ARG VAL HIS ASP
SEQRES 4 2 196 LYS ILE TRP CYS CYS ARG SER GLY SER ALA ALA ASP THR
SEQRES 5 2 196 GLN ALA ILE ALA ASP ILE VAL GLN TYR HIS LEU GLU LEU
SEQRES 6 2 196 TYR THR SER GLN TYR GLY THR PRO SER THR GLU THR ALA
SEQRES 7 2 196 ALA SER VAL PHE LYS GLU LEU CYS TYR GLU ASN LYS ASP
SEQRES 8 2 196 ASN LEU THR ALA GLY ILE ILE VAL ALA GLY TYR ASP ASP
SEQRES 9 2 196 LYS ASN LYS GLY GLU VAL TYR THR ILE PRO LEU GLY GLY
SEQRES 10 2 196 SER VAL HIS LYS LEU PRO TYR ALA ILE ALA GLY SER GLY
SEQRES 11 2 196 SER THR PHE ILE TYR GLY TYR CYS ASP LYS ASN PHE ARG
SEQRES 12 2 196 GLU ASN MET SER LYS GLU GLU THR VAL ASP PHE ILE LYS
SEQRES 13 2 196 HIS SER LEU SER GLN ALA ILE LYS TRP ASP GLY SER SER
SEQRES 14 2 196 GLY GLY VAL ILE ARG MET VAL VAL LEU THR ALA ALA GLY
SEQRES 15 2 196 VAL GLU ARG LEU ILE PHE TYR PRO ASP GLU TYR GLU GLN
SEQRES 16 2 196 LEU
HET MG F9009 1
HET MG G9001 1
HET MG G9010 1
HET MG H9007 1
HET MG I9003 1
HET MG I9005 1
HET MG K9008 1
HET MG L9002 1
HET MG L9004 1
HET MG N9006 1
HET MG T9019 1
HET MG U9011 1
HET MG U9020 1
HET MG V9017 1
HET MG W9013 1
HET MG W9015 1
HET MG Y9018 1
HET MG Z9012 1
HET MG Z9014 1
HET MG 29016 1
HETNAM MG MAGNESIUM ION
FORMUL 29 MG 20(MG 2+)
FORMUL 49 HOH *2908(H2 O)
HELIX 1 1 GLY A 22 GLN A 33 1 12
HELIX 2 2 MET A 60 LEU A 64 5 5
HELIX 3 3 MET A 81 SER A 99 1 19
HELIX 4 4 TYR A 100 GLY A 104 1 6
HELIX 5 5 PRO A 108 THR A 124 1 17
HELIX 6 6 GLY A 168 TRP A 180 1 13
HELIX 7 7 GLU A 185 VAL A 202 1 17
HELIX 8 8 ASN A 217B LEU A 217G 5 5
HELIX 9 9 THR A 225 GLU A 234 1 10
HELIX 10 10 LEU B 21 HIS B 33 1 13
HELIX 11 11 LEU B 81 ASN B 104 1 24
HELIX 12 12 PRO B 108 HIS B 126 1 19
HELIX 13 13 ASN B 168 TYR B 180 1 13
HELIX 14 14 LYS B 185 THR B 202 1 17
HELIX 15 15 THR B 206 ASP B 208 5 3
HELIX 16 16 LYS B 225 THR B 236 1 12
HELIX 17 17 ILE C 21 GLY C 34 1 14
HELIX 18 18 LEU C 81 GLU C 104 1 24
HELIX 19 19 THR C 108 TYR C 123 1 16
HELIX 20 20 ASN C 168 TYR C 180 1 13
HELIX 21 21 THR C 185 GLN C 202 1 18
HELIX 22 22 SER C 225 GLU C 242 1 18
HELIX 23 23 LEU D 21 LEU D 33 1 13
HELIX 24 24 GLU D 60 ILE D 64 5 5
HELIX 25 25 ASP D 84 ASP D 104 1 21
HELIX 26 26 ASN D 108 ALA D 121 1 14
HELIX 27 27 GLY D 168 TRP D 180 1 13
HELIX 28 28 THR D 185 MET D 201 1 17
HELIX 29 29 ASP D 225 ALA D 242 1 17
HELIX 30 30 LEU E 21 GLN E 33 1 13
HELIX 31 31 LEU E 81 ASN E 104 1 24
HELIX 32 32 ALA E 108 ASN E 123 1 16
HELIX 33 33 SER E 169 ILE E 180D 1 16
HELIX 34 34 ASN E 185 SER E 198 1 14
HELIX 35 35 GLN E 199 LEU E 201 5 3
HELIX 36 36 GLU E 227 ILE E 233 5 7
HELIX 37 37 ASN F 21 ASN F 33 1 13
HELIX 38 38 LEU F 81 LYS F 104 1 24
HELIX 39 39 PRO F 108 HIS F 123 1 16
HELIX 40 40 GLY F 168 HIS F 180C 1 16
HELIX 41 41 SER F 185 HIS F 202 1 17
HELIX 42 42 GLU F 203 LYS F 206 5 4
HELIX 43 43 GLY F 226 ILE F 240 1 15
HELIX 44 44 LEU G 21 THR G 31 1 11
HELIX 45 45 ASP G 60 VAL G 64 5 5
HELIX 46 46 PRO G 81 GLY G 104 1 24
HELIX 47 47 PRO G 108 ARG G 126 1 19
HELIX 48 48 LYS G 168 LYS G 179E 1 17
HELIX 49 49 SER G 184M GLY G 202 1 18
HELIX 50 50 SER G 206 ASN G 208 5 3
HELIX 51 51 SER G 225 ALA G 237 1 13
HELIX 52 52 THR H 48 SER H 71 1 24
HELIX 53 53 ARG H 75 TYR H 90 1 16
HELIX 54 54 GLY H 130 TRP H 142 1 13
HELIX 55 55 THR H 147 ASP H 166 1 20
HELIX 56 56 ASP I -7 ILE I -3 5 5
HELIX 57 57 LEU I 48 GLU I 71 1 24
HELIX 58 58 GLU I 75 GLU I 89 1 15
HELIX 59 59 ALA I 130 TYR I 142 1 13
HELIX 60 60 GLU I 147 ARG I 165 1 19
HELIX 61 61 GLU J 48 ASP J 71 1 24
HELIX 62 62 SER J 75 ILE J 90A 1 17
HELIX 63 63 TYR J 129 TYR J 142 1 14
HELIX 64 64 THR J 147 MET J 166 1 20
HELIX 65 65 GLY K 48 LYS K 71 1 24
HELIX 66 66 SER K 75 TYR K 90 1 16
HELIX 67 67 GLY K 130 TYR K 142 1 13
HELIX 68 68 SER K 147 ASP K 166 1 20
HELIX 69 69 VAL K 192 GLY K 204 1 13
HELIX 70 70 PHE L 48 HIS L 70 1 23
HELIX 71 71 SER L 75 LYS L 90 1 16
HELIX 72 72 ALA L 130 VAL L 142 1 13
HELIX 73 73 SER L 147 HIS L 166 1 20
HELIX 74 74 ILE M 49 TYR M 68 1 20
HELIX 75 75 GLU M 75 LYS M 92A 1 19
HELIX 76 76 GLY M 128 MET M 133 1 6
HELIX 77 77 MET M 133 ARG M 139 1 7
HELIX 78 78 ARG M 141C THR M 146 5 8
HELIX 79 79 THR M 147 ASP M 166 1 20
HELIX 80 80 TRP M 197 ILE M 203 5 7
HELIX 81 81 SER N 48 GLY N 72 1 24
HELIX 82 82 SER N 75 ASN N 90 1 16
HELIX 83 83 LYS N 91 LEU N 95 5 4
HELIX 84 84 GLY N 128 PHE N 133 5 6
HELIX 85 85 ILE N 134 PHE N 142 1 9
HELIX 86 86 SER N 147 ASP N 166 1 20
HELIX 87 87 TYR N 187C GLU N 187H 1 6
HELIX 88 88 GLY O 22 GLY O 34 1 13
HELIX 89 89 MET O 81 SER O 99 1 19
HELIX 90 90 TYR O 100 GLY O 104 1 6
HELIX 91 91 PRO O 108 SER O 126 1 19
HELIX 92 92 GLY O 168 TRP O 180 1 13
HELIX 93 93 GLU O 185 VAL O 202 1 17
HELIX 94 94 ASN O 217B LEU O 217G 5 5
HELIX 95 95 THR O 225 GLU O 234 1 10
HELIX 96 96 LEU P 21 HIS P 33 1 13
HELIX 97 97 LEU P 81 ASN P 104 1 24
HELIX 98 98 PRO P 108 HIS P 126 1 19
HELIX 99 99 ASN P 168 TYR P 180 1 13
HELIX 100 100 LYS P 185 THR P 202 1 17
HELIX 101 101 THR P 206 ASP P 208 5 3
HELIX 102 102 LYS P 225 THR P 236 1 12
HELIX 103 103 ILE Q 21 GLY Q 34 1 14
HELIX 104 104 LEU Q 81 GLU Q 104 1 24
HELIX 105 105 THR Q 108 THR Q 124 1 17
HELIX 106 106 ASN Q 168 TYR Q 180 1 13
HELIX 107 107 THR Q 185 GLN Q 202 1 18
HELIX 108 108 SER Q 225 GLU Q 242 1 18
HELIX 109 109 LEU R 21 LEU R 33 1 13
HELIX 110 110 GLU R 60 ILE R 64 5 5
HELIX 111 111 ASP R 84 ASP R 104 1 21
HELIX 112 112 ASN R 108 ALA R 121 1 14
HELIX 113 113 GLY R 168 TRP R 180 1 13
HELIX 114 114 THR R 185 MET R 201 1 17
HELIX 115 115 ASP R 225 ALA R 242 1 17
HELIX 116 116 LEU S 21 GLN S 33 1 13
HELIX 117 117 LEU S 81 ASN S 104 1 24
HELIX 118 118 ALA S 108 ASN S 123 1 16
HELIX 119 119 SER S 169 ILE S 180D 1 16
HELIX 120 120 ASN S 185 GLN S 199 1 15
HELIX 121 121 GLU S 227 ILE S 233 5 7
HELIX 122 122 ASN T 21 ASN T 33 1 13
HELIX 123 123 LEU T 81 LYS T 104 1 24
HELIX 124 124 PRO T 108 HIS T 123 1 16
HELIX 125 125 GLY T 168 HIS T 180C 1 16
HELIX 126 126 SER T 185 HIS T 202 1 17
HELIX 127 127 GLU T 203 LYS T 206 5 4
HELIX 128 128 GLY T 226 ILE T 240 1 15
HELIX 129 129 LEU U 21 THR U 31 1 11
HELIX 130 130 ASP U 60 VAL U 64 5 5
HELIX 131 131 PRO U 81 GLY U 104 1 24
HELIX 132 132 PRO U 108 ARG U 126 1 19
HELIX 133 133 LYS U 168 LYS U 179E 1 17
HELIX 134 134 SER U 184M GLY U 202 1 18
HELIX 135 135 SER U 206 ASN U 208 5 3
HELIX 136 136 SER U 225 ALA U 237 1 13
HELIX 137 137 THR V 48 SER V 71 1 24
HELIX 138 138 ARG V 75 TYR V 90 1 16
HELIX 139 139 GLY V 130 TRP V 142 1 13
HELIX 140 140 THR V 147 ASP V 166 1 20
HELIX 141 141 ASP W -7 ILE W -3 5 5
HELIX 142 142 LEU W 48 GLU W 71 1 24
HELIX 143 143 GLU W 75 GLU W 89 1 15
HELIX 144 144 ALA W 130 TYR W 142 1 13
HELIX 145 145 GLU W 147 ARG W 165 1 19
HELIX 146 146 GLU X 48 ASP X 71 1 24
HELIX 147 147 SER X 75 ILE X 90A 1 17
HELIX 148 148 TYR X 129 TYR X 142 1 14
HELIX 149 149 THR X 147 MET X 166 1 20
HELIX 150 150 GLY Y 48 GLU Y 70 1 23
HELIX 151 151 SER Y 75 TYR Y 90 1 16
HELIX 152 152 GLY Y 130 TYR Y 142 1 13
HELIX 153 153 SER Y 147 ASP Y 166 1 20
HELIX 154 154 VAL Y 192 GLY Y 204 1 13
HELIX 155 155 PHE Z 48 HIS Z 70 1 23
HELIX 156 156 SER Z 75 LYS Z 90 1 16
HELIX 157 157 ALA Z 130 VAL Z 142 1 13
HELIX 158 158 SER Z 147 HIS Z 166 1 20
HELIX 159 159 ILE 1 49 TYR 1 68 1 20
HELIX 160 160 GLU 1 75 LYS 1 92A 1 19
HELIX 161 161 GLY 1 128 MET 1 133 1 6
HELIX 162 162 MET 1 133 ARG 1 139 1 7
HELIX 163 163 ARG 1 141C THR 1 146 5 8
HELIX 164 164 THR 1 147 ASP 1 166 1 20
HELIX 165 165 TRP 1 197 ILE 1 203 5 7
HELIX 166 166 SER 2 48 GLY 2 72 1 24
HELIX 167 167 SER 2 75 ASN 2 90 1 16
HELIX 168 168 LYS 2 91 LEU 2 95 5 4
HELIX 169 169 GLY 2 130 PHE 2 142 1 13
HELIX 170 170 SER 2 147 ASP 2 166 1 20
HELIX 171 171 TYR 2 187C GLU 2 187H 1 6
SHEET 1 A 2 PHE A 15 SER A 16 0
SHEET 2 A 2 LYS A 20 LEU A 21 -1 O LYS A 20 N SER A 16
SHEET 1 B 5 ALA A 162 ILE A 165 0
SHEET 2 B 5 SER A 37 LYS A 41 -1 N SER A 37 O ILE A 165
SHEET 3 B 5 VAL A 46 GLU A 51 -1 O ALA A 49 N LEU A 38
SHEET 4 B 5 ILE A 210 ILE A 215 -1 O ALA A 213 N ILE A 48
SHEET 5 B 5 PHE A 221 LYS A 223 -1 O ARG A 222 N ILE A 214
SHEET 1 C 5 VAL A 67 THR A 71 0
SHEET 2 C 5 ILE A 74 GLY A 80 -1 O ILE A 74 N THR A 71
SHEET 3 C 5 VAL A 134 ASP A 142 -1 O ALA A 139 N GLY A 75
SHEET 4 C 5 GLY A 146 VAL A 151 -1 O TYR A 149 N ILE A 138
SHEET 5 C 5 TYR A 157 PRO A 159 -1 O PHE A 158 N GLN A 150
SHEET 1 D 6 TYR A 217I THR A 217J 0
SHEET 2 D 6 ALA H 184 LEU H 192 1 O ALA H 184 N THR A 217J
SHEET 3 D 6 VAL H 173 GLU H 179 -1 N VAL H 175 O LEU H 187
SHEET 4 D 6 GLY H 11 ALA H 16 -1 N ALA H 16 O ASP H 174
SHEET 5 D 6 ILE H 3 PHE H 8 -1 N VAL H 6 O VAL H 13
SHEET 6 D 6 TYR H 124 LEU H 127 -1 O LEU H 125 N GLY H 5
SHEET 1 E 5 ALA B 162 VAL B 165 0
SHEET 2 E 5 ALA B 37 MET B 41 -1 N GLY B 39 O ILE B 163
SHEET 3 E 5 GLY B 45 GLU B 51 -1 O ALA B 49 N ILE B 38
SHEET 4 E 5 LEU B 210 ARG B 216 -1 O ALA B 213 N LEU B 48
SHEET 5 E 5 TYR B 220 ILE B 223 -1 O TYR B 220 N ARG B 216
SHEET 1 F 5 LEU B 67 ASN B 71 0
SHEET 2 F 5 ILE B 74 GLY B 80 -1 O VAL B 76 N TYR B 68
SHEET 3 F 5 VAL B 134 ASP B 142 -1 O ILE B 137 N ALA B 77
SHEET 4 F 5 GLY B 145 SER B 151 -1 O GLN B 147 N GLY B 140
SHEET 5 F 5 TYR B 157 GLY B 159 -1 O THR B 158 N THR B 150
SHEET 1 G 5 ALA C 162 ILE C 165 0
SHEET 2 G 5 ALA C 37 LYS C 41 -1 N ALA C 37 O ILE C 165
SHEET 3 G 5 VAL C 46 GLU C 51 -1 O GLY C 49 N VAL C 38
SHEET 4 G 5 ILE C 210 LYS C 216 -1 O THR C 213 N LEU C 48
SHEET 5 G 5 ASP C 220 ALA C 223 -1 O VAL C 222 N VAL C 214
SHEET 1 H 5 VAL C 67 ASP C 71 0
SHEET 2 H 5 VAL C 74 GLY C 80 -1 O LEU C 76 N SER C 68
SHEET 3 H 5 VAL C 134 PHE C 141 -1 O LEU C 137 N SER C 77
SHEET 4 H 5 PRO C 146 THR C 151 -1 O TYR C 149 N ILE C 138
SHEET 5 H 5 TYR C 157 SER C 159 -1 O SER C 158 N GLN C 150
SHEET 1 I 5 ALA D 162 ILE D 165 0
SHEET 2 I 5 ALA D 37 ALA D 41 -1 N GLY D 39 O LYS D 163
SHEET 3 I 5 VAL D 46 GLU D 51 -1 O GLY D 49 N ILE D 38
SHEET 4 I 5 ALA D 210 THR D 216 -1 O GLN D 211 N VAL D 50
SHEET 5 I 5 GLY D 220 ILE D 223 -1 O GLY D 220 N THR D 216
SHEET 1 J 5 ILE D 67 ASP D 71 0
SHEET 2 J 5 ILE D 74 GLY D 80 -1 O ILE D 74 N ASP D 71
SHEET 3 J 5 VAL D 134 ASP D 142 -1 O ALA D 139 N GLY D 75
SHEET 4 J 5 GLY D 145 ALA D 151 -1 O PHE D 149 N ILE D 138
SHEET 5 J 5 PHE D 157 TYR D 160 -1 O TYR D 158 N HIS D 150
SHEET 1 K 5 GLY E 162 ILE E 165 0
SHEET 2 K 5 THR E 37 ARG E 41 -1 N GLY E 39 O THR E 163
SHEET 3 K 5 HIS E 45 LEU E 51 -1 O VAL E 49 N VAL E 38
SHEET 4 K 5 LEU E 210 GLY E 216 -1 O SER E 211 N ALA E 50
SHEET 5 K 5 THR E 219 ASP E 225 -1 O TYR E 224 N ILE E 212
SHEET 1 L 5 ILE E 67 ASP E 71 0
SHEET 2 L 5 MET E 74 GLY E 80 -1 O LEU E 76 N ILE E 68
SHEET 3 L 5 VAL E 134 ASP E 142 -1 O ILE E 139 N GLY E 75
SHEET 4 L 5 GLY E 145 GLN E 152 -1 O LEU E 149 N ILE E 138
SHEET 5 L 5 ASN E 156 LEU E 160 -1 O ASN E 156 N GLN E 152
SHEET 1 M 5 GLY F 162 THR F 165 0
SHEET 2 M 5 SER F 37 LYS F 41 -1 N GLY F 39 O ALA F 163
SHEET 3 M 5 GLY F 45 LEU F 53 -1 O ALA F 49 N ILE F 38
SHEET 4 M 5 PHE F 208 SER F 216 -1 O SER F 213 N PHE F 48
SHEET 5 M 5 HIS F 221 PHE F 223 -1 O LYS F 222 N TRP F 214
SHEET 1 N 5 GLN F 68 VAL F 70 0
SHEET 2 N 5 ILE F 74 GLY F 80 -1 O CYS F 76 N GLN F 68
SHEET 3 N 5 VAL F 134 ASP F 142 -1 O ILE F 137 N VAL F 77
SHEET 4 N 5 GLY F 145 LEU F 151 -1 O LEU F 151 N THR F 136
SHEET 5 N 5 TYR F 157 GLY F 159 -1 O TRP F 158 N MET F 150
SHEET 1 O 5 ALA G 162 THR G 165 0
SHEET 2 O 5 SER G 37 ARG G 41 -1 N ALA G 39 O THR G 163
SHEET 3 O 5 THR G 46 GLN G 51 -1 O VAL G 47 N VAL G 40
SHEET 4 O 5 LEU G 210 THR G 216 -1 O GLY G 213 N VAL G 48
SHEET 5 O 5 LYS G 220 THR G 223 -1 O PHE G 222 N VAL G 214
SHEET 1 P 5 ILE G 67 CYS G 69 0
SHEET 2 P 5 GLY G 75 ASN G 79 -1 O MET G 76 N PHE G 68
SHEET 3 P 5 ILE G 135 ASP G 142 -1 O VAL G 139 N GLY G 75
SHEET 4 P 5 GLY G 145 ASP G 152 -1 O TYR G 149 N PHE G 138
SHEET 5 P 5 TYR G 156 GLY G 159 -1 O VAL G 158 N LYS G 150
SHEET 1 Q 2 SER H 20 GLN H 22 0
SHEET 2 Q 2 ILE H 25 ASP H 28 -1 O ASP H 28 N SER H 20
SHEET 1 R 5 LEU H 34 SER H 38 0
SHEET 2 R 5 ILE H 41 GLY H 47 -1 O CYS H 43 N HIS H 35
SHEET 3 R 5 ALA H 97 ASP H 105 -1 O ALA H 102 N TRP H 42
SHEET 4 R 5 GLY H 107 HIS H 114 -1 O ILE H 113 N LEU H 99
SHEET 5 R 5 SER H 118 VAL H 121 -1 O SER H 118 N HIS H 114
SHEET 1 S 6 VAL H 213 ILE H 218 0
SHEET 2 S 6 VAL I 184 LEU I 189 -1 O LYS I 186 N SER H 217
SHEET 3 S 6 ALA I 173 LYS I 179 -1 N ILE I 177 O VAL I 185
SHEET 4 S 6 CYS I 11 ASP I 17 -1 N VAL I 12 O ILE I 178
SHEET 5 S 6 ILE I 2 GLY I 8 -1 N MET I 6 O ALA I 13
SHEET 6 S 6 PHE I 124 GLY I 128 -1 O ILE I 125 N ALA I 5
SHEET 1 T 2 LEU I 20 SER I 22 0
SHEET 2 T 2 LEU I 25 SER I 28 -1 O VAL I 27 N LEU I 20
SHEET 1 U 5 ILE I 34 HIS I 36 0
SHEET 2 U 5 VAL I 41 GLY I 47 -1 O LEU I 43 N PHE I 35
SHEET 3 U 5 VAL I 97 ILE I 104 -1 O ALA I 102 N PHE I 42
SHEET 4 U 5 PRO I 108 PHE I 113 -1 O PHE I 109 N GLY I 103
SHEET 5 U 5 ILE I 119 ASP I 120 -1 O ASP I 120 N GLY I 112
SHEET 1 V 5 TYR J 124 ALA J 126 0
SHEET 2 V 5 ILE J 3 ARG J 7 -1 N GLY J 5 O GLY J 125
SHEET 3 V 5 SER J 11 SER J 17 -1 O ILE J 13 N ILE J 6
SHEET 4 V 5 VAL J 173 ASP J 179 -1 O LYS J 176 N LEU J 14
SHEET 5 V 5 GLY J 183 GLN J 186 -1 O ARG J 185 N ILE J 177
SHEET 1 W 2 VAL J 20 ARG J 22 0
SHEET 2 W 2 SER J 25 LYS J 28 -1 O LYS J 28 N VAL J 20
SHEET 1 X 5 THR J 34 SER J 38 0
SHEET 2 X 5 THR J 41 GLY J 47 -1 O MET J 43 N ARG J 35
SHEET 3 X 5 VAL J 97 ASP J 105 -1 O GLY J 102 N LEU J 42
SHEET 4 X 5 LYS J 107 ILE J 113 -1 O GLU J 109 N GLY J 103
SHEET 5 X 5 LYS J 119 GLU J 121 -1 O VAL J 120 N GLN J 112
SHEET 1 Y 5 ILE K 124 VAL K 127 0
SHEET 2 Y 5 THR K 3 PHE K 8 -1 N THR K 3 O VAL K 127
SHEET 3 Y 5 GLY K 11 VAL K 16 -1 O ILE K 13 N PHE K 6
SHEET 4 Y 5 SER K 172 THR K 179 -1 O VAL K 178 N ILE K 12
SHEET 5 Y 5 GLY K 183 ASP K 191 -1 O ILE K 185 N HIS K 177
SHEET 1 Z 2 ALA K 20 ALA K 22 0
SHEET 2 Z 2 TRP K 25 SER K 28 -1 O SER K 28 N ALA K 20
SHEET 1 AA 5 VAL K 34 ASN K 38 0
SHEET 2 AA 5 LEU K 41 THR K 44 -1 O GLY K 43 N ILE K 35
SHEET 3 AA 5 GLY K 98 THR K 105 -1 O CYS K 102 N LEU K 42
SHEET 4 AA 5 GLY K 107 ASP K 114 -1 O THR K 109 N GLY K 103
SHEET 5 AA 5 THR K 118 GLY K 122 -1 O LEU K 120 N TYR K 112
SHEET 1 AB 5 CYS L 124 GLY L 128 0
SHEET 2 AB 5 THR L 2 ALA L 7 -1 N ILE L 3 O GLY L 127
SHEET 3 AB 5 ALA L 12 ASP L 17 -1 O ALA L 15 N LEU L 4
SHEET 4 AB 5 GLY L 172 THR L 179 -1 O VAL L 178 N ALA L 12
SHEET 5 AB 5 GLY L 183 GLU L 190 -1 O ARG L 185 N ILE L 177
SHEET 1 AC 2 ASN L 20 THR L 22 0
SHEET 2 AC 2 SER L 25 SER L 28 -1 O SER L 28 N ASN L 20
SHEET 1 AD 5 PHE L 35 ASP L 36 0
SHEET 2 AD 5 ILE L 41 GLY L 47 -1 O MET L 43 N PHE L 35
SHEET 3 AD 5 VAL L 97 LEU L 104 -1 O ALA L 102 N VAL L 42
SHEET 4 AD 5 GLY L 108 PHE L 113 -1 O PHE L 113 N THR L 99
SHEET 5 AD 5 TYR L 119 ARG L 121 -1 O GLU L 120 N SER L 112
SHEET 1 AE 5 LEU M 25 PHE M 28 0
SHEET 2 AE 5 GLY M 20 TYR M 22 -1 N GLY M 20 O PHE M 28
SHEET 3 AE 5 VAL M -3 GLY M -1 -1 N THR M -2 O SER M 21
SHEET 4 AE 5 THR M 41 ASP M 48 -1 O GLY M 47 N GLY M -1
SHEET 5 AE 5 LEU M 34 PRO M 36 -1 N ILE M 35 O VAL M 43
SHEET 1 AF 7 LEU M 25 PHE M 28 0
SHEET 2 AF 7 GLY M 20 TYR M 22 -1 N GLY M 20 O PHE M 28
SHEET 3 AF 7 VAL M -3 GLY M -1 -1 N THR M -2 O SER M 21
SHEET 4 AF 7 THR M 41 ASP M 48 -1 O GLY M 47 N GLY M -1
SHEET 5 AF 7 ASN M 97 VAL M 104 -1 O ALA M 98 N SER M 46
SHEET 6 AF 7 GLN M 108 ASN M 114 -1 O PHE M 109 N GLY M 103
SHEET 7 AF 7 THR M 119 TYR M 120 -1 O TYR M 120 N TYR M 112
SHEET 1 AG 5 THR M 124 ALA M 126 0
SHEET 2 AG 5 VAL M 3 TYR M 8 -1 N SER M 5 O LEU M 125
SHEET 3 AG 5 GLY M 11 ASP M 17 -1 O GLY M 11 N TYR M 8
SHEET 4 AG 5 ASN M 172 ASP M 179 -1 O ALA M 176 N ILE M 14
SHEET 5 AG 5 GLY M 183 GLN M 191 -1 O GLY M 183 N ASP M 179
SHEET 1 AH 5 TYR N 124 ALA N 127 0
SHEET 2 AH 5 ILE N 3 THR N 7 -1 N ILE N 3 O ALA N 127
SHEET 3 AH 5 GLY N 11 ALA N 16 -1 O ILE N 13 N VAL N 6
SHEET 4 AH 5 ILE N 173 THR N 179 -1 O LEU N 178 N VAL N 12
SHEET 5 AH 5 GLY N 183 PHE N 187B-1 O LEU N 187 N MET N 175
SHEET 1 AI 2 THR N 20 THR N 22 0
SHEET 2 AI 2 TYR N 25 ASN N 28 -1 O ASN N 28 N THR N 20
SHEET 1 AJ 5 LEU N 34 HIS N 38 0
SHEET 2 AJ 5 ILE N 41 GLY N 47 -1 O CYS N 43 N THR N 35
SHEET 3 AJ 5 ALA N 97 ASP N 105 -1 O ALA N 102 N TRP N 42
SHEET 4 AJ 5 LYS N 107 ILE N 113 -1 O ILE N 113 N ILE N 99
SHEET 5 AJ 5 HIS N 120 LEU N 122 -1 O HIS N 120 N THR N 112
SHEET 1 AK 2 PHE O 15 SER O 16 0
SHEET 2 AK 2 LYS O 20 LEU O 21 -1 O LYS O 20 N SER O 16
SHEET 1 AL 5 ALA O 162 ILE O 165 0
SHEET 2 AL 5 SER O 37 LYS O 41 -1 N GLY O 39 O THR O 163
SHEET 3 AL 5 VAL O 46 GLU O 51 -1 O VAL O 47 N ILE O 40
SHEET 4 AL 5 ILE O 210 ILE O 215 -1 O ALA O 213 N ILE O 48
SHEET 5 AL 5 PHE O 221 LYS O 223 -1 O ARG O 222 N ILE O 214
SHEET 1 AM 5 VAL O 67 THR O 71 0
SHEET 2 AM 5 ILE O 74 GLY O 80 -1 O ALA O 76 N SER O 68
SHEET 3 AM 5 VAL O 134 ASP O 142 -1 O ALA O 139 N GLY O 75
SHEET 4 AM 5 GLY O 146 VAL O 151 -1 O VAL O 151 N LEU O 136
SHEET 5 AM 5 TYR O 157 PRO O 159 -1 O PHE O 158 N GLN O 150
SHEET 1 AN 6 TYR O 217I THR O 217J 0
SHEET 2 AN 6 ALA V 184 LEU V 192 1 O TYR V 186 N THR O 217J
SHEET 3 AN 6 VAL V 173 GLU V 179 -1 N VAL V 177 O GLU V 185
SHEET 4 AN 6 GLY V 11 ASP V 17 -1 N VAL V 12 O MET V 178
SHEET 5 AN 6 ILE V 3 PHE V 8 -1 N VAL V 6 O VAL V 13
SHEET 6 AN 6 TYR V 124 LEU V 127 -1 O LEU V 127 N ILE V 3
SHEET 1 AO 5 ALA P 162 VAL P 165 0
SHEET 2 AO 5 ALA P 37 MET P 41 -1 N GLY P 39 O ILE P 163
SHEET 3 AO 5 GLY P 45 GLU P 51 -1 O ALA P 49 N ILE P 38
SHEET 4 AO 5 LEU P 210 ARG P 216 -1 O ALA P 213 N LEU P 48
SHEET 5 AO 5 TYR P 220 ILE P 223 -1 O TYR P 220 N ARG P 216
SHEET 1 AP 5 LEU P 67 ASN P 71 0
SHEET 2 AP 5 ILE P 74 GLY P 80 -1 O VAL P 76 N TYR P 68
SHEET 3 AP 5 VAL P 134 ASP P 142 -1 O ALA P 139 N ALA P 75
SHEET 4 AP 5 GLY P 145 SER P 151 -1 O TYR P 149 N TYR P 138
SHEET 5 AP 5 TYR P 157 GLY P 159 -1 O THR P 158 N THR P 150
SHEET 1 AQ 5 ALA Q 162 ILE Q 165 0
SHEET 2 AQ 5 ALA Q 37 LYS Q 41 -1 N ALA Q 37 O ILE Q 165
SHEET 3 AQ 5 VAL Q 46 GLU Q 51 -1 O GLY Q 49 N VAL Q 38
SHEET 4 AQ 5 ILE Q 210 LYS Q 216 -1 O VAL Q 215 N VAL Q 46
SHEET 5 AQ 5 ASP Q 220 ALA Q 223 -1 O ASP Q 220 N LYS Q 216
SHEET 1 AR 5 VAL Q 67 ASP Q 71 0
SHEET 2 AR 5 VAL Q 74 GLY Q 80 -1 O LEU Q 76 N SER Q 68
SHEET 3 AR 5 VAL Q 134 PHE Q 141 -1 O ALA Q 139 N VAL Q 75
SHEET 4 AR 5 PRO Q 146 THR Q 151 -1 O TYR Q 149 N ILE Q 138
SHEET 5 AR 5 TYR Q 157 SER Q 159 -1 O SER Q 158 N GLN Q 150
SHEET 1 AS 5 ALA R 162 ILE R 165 0
SHEET 2 AS 5 ALA R 37 ALA R 41 -1 N GLY R 39 O LYS R 163
SHEET 3 AS 5 VAL R 46 GLU R 51 -1 O GLY R 49 N ILE R 38
SHEET 4 AS 5 ALA R 210 THR R 216 -1 O SER R 213 N LEU R 48
SHEET 5 AS 5 GLY R 220 ILE R 223 -1 O GLY R 220 N THR R 216
SHEET 1 AT 5 ILE R 67 ASP R 71 0
SHEET 2 AT 5 ILE R 74 GLY R 80 -1 O CYS R 76 N VAL R 68
SHEET 3 AT 5 VAL R 134 ASP R 142 -1 O LEU R 137 N ALA R 77
SHEET 4 AT 5 GLY R 145 ALA R 151 -1 O GLN R 147 N GLY R 140
SHEET 5 AT 5 PHE R 157 TYR R 160 -1 O TYR R 158 N HIS R 150
SHEET 1 AU 5 GLY S 162 ILE S 165 0
SHEET 2 AU 5 THR S 37 ARG S 41 -1 N GLY S 39 O THR S 163
SHEET 3 AU 5 HIS S 45 ALA S 50 -1 O VAL S 49 N VAL S 38
SHEET 4 AU 5 SER S 211 GLY S 216 -1 O ALA S 213 N LEU S 48
SHEET 5 AU 5 THR S 219 ASP S 225 -1 O TYR S 224 N ILE S 212
SHEET 1 AV 5 ILE S 67 ASP S 71 0
SHEET 2 AV 5 MET S 74 GLY S 80 -1 O LEU S 76 N ILE S 68
SHEET 3 AV 5 VAL S 134 ASP S 142 -1 O GLY S 135 N ALA S 79
SHEET 4 AV 5 GLY S 145 GLN S 152 -1 O PHE S 151 N LEU S 136
SHEET 5 AV 5 ASN S 156 GLU S 159 -1 O ASN S 156 N GLN S 152
SHEET 1 AW 5 GLY T 162 THR T 165 0
SHEET 2 AW 5 SER T 37 LYS T 41 -1 N GLY T 39 O ALA T 163
SHEET 3 AW 5 GLY T 45 LEU T 53 -1 O ALA T 49 N ILE T 38
SHEET 4 AW 5 PHE T 208 SER T 216 -1 O SER T 213 N PHE T 48
SHEET 5 AW 5 HIS T 221 PHE T 223 -1 O LYS T 222 N TRP T 214
SHEET 1 AX 5 GLN T 68 VAL T 70 0
SHEET 2 AX 5 ILE T 74 GLY T 80 -1 O CYS T 76 N GLN T 68
SHEET 3 AX 5 VAL T 134 ASP T 142 -1 O ILE T 137 N VAL T 77
SHEET 4 AX 5 GLY T 145 LEU T 151 -1 O TYR T 149 N PHE T 138
SHEET 5 AX 5 TYR T 157 GLY T 159 -1 O TRP T 158 N MET T 150
SHEET 1 AY 5 ALA U 162 THR U 165 0
SHEET 2 AY 5 SER U 37 ARG U 41 -1 N SER U 37 O THR U 165
SHEET 3 AY 5 THR U 46 GLN U 51 -1 O VAL U 47 N VAL U 40
SHEET 4 AY 5 LEU U 210 THR U 216 -1 O ALA U 215 N THR U 46
SHEET 5 AY 5 LYS U 220 THR U 223 -1 O PHE U 222 N VAL U 214
SHEET 1 AZ 5 ILE U 67 CYS U 69 0
SHEET 2 AZ 5 GLY U 75 ASN U 79 -1 O MET U 76 N PHE U 68
SHEET 3 AZ 5 ILE U 135 ASP U 142 -1 O VAL U 139 N GLY U 75
SHEET 4 AZ 5 GLY U 145 THR U 151 -1 O TYR U 149 N PHE U 138
SHEET 5 AZ 5 TYR U 157 GLY U 159 -1 O VAL U 158 N LYS U 150
SHEET 1 BA 2 SER V 20 GLN V 22 0
SHEET 2 BA 2 ILE V 25 ASP V 28 -1 O ALA V 27 N SER V 20
SHEET 1 BB 5 LEU V 34 SER V 38 0
SHEET 2 BB 5 ILE V 41 GLY V 47 -1 O CYS V 43 N HIS V 35
SHEET 3 BB 5 ALA V 97 ASP V 105 -1 O ALA V 102 N TRP V 42
SHEET 4 BB 5 GLY V 107 HIS V 114 -1 O ILE V 113 N LEU V 99
SHEET 5 BB 5 SER V 118 VAL V 121 -1 O SER V 118 N HIS V 114
SHEET 1 BC 6 VAL V 213 VAL V 219 0
SHEET 2 BC 6 VAL W 184 LEU W 189 -1 O VAL W 184 N VAL V 219
SHEET 3 BC 6 ALA W 173 LYS W 179 -1 N ALA W 173 O LEU W 189
SHEET 4 BC 6 CYS W 11 ASP W 17 -1 N VAL W 12 O ILE W 178
SHEET 5 BC 6 ILE W 2 GLY W 8 -1 N MET W 6 O ALA W 13
SHEET 6 BC 6 PHE W 124 GLY W 128 -1 O SER W 127 N VAL W 3
SHEET 1 BD 2 LEU W 20 SER W 22 0
SHEET 2 BD 2 LEU W 25 SER W 28 -1 O VAL W 27 N LEU W 20
SHEET 1 BE 5 ILE W 34 TYR W 38 0
SHEET 2 BE 5 VAL W 41 GLY W 47 -1 O LEU W 43 N PHE W 35
SHEET 3 BE 5 VAL W 97 ILE W 104 -1 O ALA W 102 N PHE W 42
SHEET 4 BE 5 PRO W 108 PHE W 113 -1 O ALA W 111 N VAL W 101
SHEET 5 BE 5 ILE W 119 ASP W 120 -1 O ASP W 120 N GLY W 112
SHEET 1 BF 5 TYR X 124 ALA X 126 0
SHEET 2 BF 5 ILE X 3 ARG X 7 -1 N GLY X 5 O GLY X 125
SHEET 3 BF 5 SER X 11 SER X 17 -1 O ILE X 13 N ILE X 6
SHEET 4 BF 5 VAL X 173 ASP X 179 -1 O LYS X 176 N LEU X 14
SHEET 5 BF 5 GLY X 183 GLN X 186 -1 O ARG X 185 N ILE X 177
SHEET 1 BG 2 VAL X 20 ARG X 22 0
SHEET 2 BG 2 SER X 25 LYS X 28 -1 O LYS X 28 N VAL X 20
SHEET 1 BH 5 THR X 34 SER X 38 0
SHEET 2 BH 5 THR X 41 GLY X 47 -1 O MET X 43 N ARG X 35
SHEET 3 BH 5 VAL X 97 ASP X 105 -1 O GLY X 102 N LEU X 42
SHEET 4 BH 5 LYS X 107 ILE X 113 -1 O GLU X 109 N GLY X 103
SHEET 5 BH 5 LYS X 119 GLU X 121 -1 O VAL X 120 N GLN X 112
SHEET 1 BI 5 ILE Y 124 VAL Y 127 0
SHEET 2 BI 5 THR Y 3 PHE Y 8 -1 N THR Y 3 O VAL Y 127
SHEET 3 BI 5 GLY Y 11 VAL Y 16 -1 O ALA Y 15 N LEU Y 4
SHEET 4 BI 5 SER Y 172 THR Y 179 -1 O VAL Y 178 N ILE Y 12
SHEET 5 BI 5 GLY Y 183 ASP Y 191 -1 O ILE Y 185 N HIS Y 177
SHEET 1 BJ 2 ALA Y 20 ALA Y 22 0
SHEET 2 BJ 2 TRP Y 25 SER Y 28 -1 O TRP Y 25 N ALA Y 22
SHEET 1 BK 5 VAL Y 34 ASN Y 38 0
SHEET 2 BK 5 LEU Y 41 THR Y 44 -1 O GLY Y 43 N ILE Y 35
SHEET 3 BK 5 GLY Y 98 THR Y 105 -1 O CYS Y 102 N LEU Y 42
SHEET 4 BK 5 GLY Y 107 ASP Y 114 -1 O VAL Y 113 N THR Y 99
SHEET 5 BK 5 ARG Y 119 GLY Y 122 -1 O LEU Y 120 N TYR Y 112
SHEET 1 BL 5 CYS Z 124 GLY Z 128 0
SHEET 2 BL 5 THR Z 2 GLY Z 8 -1 N ILE Z 3 O GLY Z 127
SHEET 3 BL 5 PHE Z 11 ASP Z 17 -1 O ALA Z 15 N LEU Z 4
SHEET 4 BL 5 GLY Z 172 THR Z 179 -1 O VAL Z 178 N ALA Z 12
SHEET 5 BL 5 GLY Z 183 GLU Z 190 -1 O ARG Z 185 N ILE Z 177
SHEET 1 BM 2 ASN Z 20 THR Z 22 0
SHEET 2 BM 2 SER Z 25 SER Z 28 -1 O ASN Z 27 N ASN Z 20
SHEET 1 BN 5 VAL Z 34 ASP Z 36 0
SHEET 2 BN 5 ILE Z 41 GLY Z 47 -1 O MET Z 43 N PHE Z 35
SHEET 3 BN 5 VAL Z 97 LEU Z 104 -1 O ALA Z 102 N VAL Z 42
SHEET 4 BN 5 GLY Z 108 PHE Z 113 -1 O PHE Z 113 N THR Z 99
SHEET 5 BN 5 TYR Z 119 GLU Z 122 -1 O GLU Z 122 N VAL Z 110
SHEET 1 BO 5 LEU 1 25 PHE 1 28 0
SHEET 2 BO 5 GLY 1 20 TYR 1 22 -1 N GLY 1 20 O PHE 1 28
SHEET 3 BO 5 VAL 1 -3 GLY 1 -1 -1 N THR 1 -2 O SER 1 21
SHEET 4 BO 5 THR 1 41 ASP 1 48 -1 O GLY 1 47 N GLY 1 -1
SHEET 5 BO 5 LEU 1 34 PRO 1 36 -1 N ILE 1 35 O VAL 1 43
SHEET 1 BP 7 LEU 1 25 PHE 1 28 0
SHEET 2 BP 7 GLY 1 20 TYR 1 22 -1 N GLY 1 20 O PHE 1 28
SHEET 3 BP 7 VAL 1 -3 GLY 1 -1 -1 N THR 1 -2 O SER 1 21
SHEET 4 BP 7 THR 1 41 ASP 1 48 -1 O GLY 1 47 N GLY 1 -1
SHEET 5 BP 7 ASN 1 97 VAL 1 104 -1 O ILE 1 100 N GLY 1 44
SHEET 6 BP 7 GLN 1 108 ASN 1 114 -1 O PHE 1 109 N GLY 1 103
SHEET 7 BP 7 THR 1 119 TYR 1 120 -1 O TYR 1 120 N TYR 1 112
SHEET 1 BQ 5 THR 1 124 ALA 1 126 0
SHEET 2 BQ 5 VAL 1 3 TYR 1 8 -1 N SER 1 5 O LEU 1 125
SHEET 3 BQ 5 GLY 1 11 ASP 1 17 -1 O GLY 1 11 N TYR 1 8
SHEET 4 BQ 5 ASN 1 172 ASP 1 179 -1 O ILE 1 178 N VAL 1 12
SHEET 5 BQ 5 GLY 1 183 GLN 1 191 -1 O GLY 1 183 N ASP 1 179
SHEET 1 BR 5 TYR 2 124 ALA 2 127 0
SHEET 2 BR 5 ILE 2 3 THR 2 7 -1 N ILE 2 3 O ALA 2 127
SHEET 3 BR 5 GLY 2 11 ALA 2 16 -1 O GLY 2 15 N MET 2 4
SHEET 4 BR 5 ILE 2 173 THR 2 179 -1 O ARG 2 174 N ALA 2 16
SHEET 5 BR 5 GLY 2 183 PHE 2 187B-1 O GLU 2 185 N VAL 2 177
SHEET 1 BS 2 THR 2 20 THR 2 22 0
SHEET 2 BS 2 TYR 2 25 ASN 2 28 -1 O ASN 2 28 N THR 2 20
SHEET 1 BT 5 LEU 2 34 HIS 2 38 0
SHEET 2 BT 5 ILE 2 41 GLY 2 47 -1 O CYS 2 43 N THR 2 35
SHEET 3 BT 5 ALA 2 97 ASP 2 105 -1 O ILE 2 100 N CYS 2 44
SHEET 4 BT 5 LYS 2 107 ILE 2 113 -1 O ILE 2 113 N ILE 2 99
SHEET 5 BT 5 HIS 2 120 LEU 2 122 -1 O HIS 2 120 N THR 2 112
LINK OE2 GLU D 105 MG MG L9002 1555 1555 2.40
LINK O HOH D 254 MG MG L9002 1555 1555 2.16
LINK OG1 THR G 13 MG MG G9001 1555 1555 2.75
LINK O TYR G 123 MG MG G9001 1555 1555 1.99
LINK O ARG G 126 MG MG G9001 1555 1555 2.00
LINK O ALA G 127 MG MG G9010 1555 1555 1.61
LINK N TYR G 128 MG MG G9010 1555 1555 2.15
LINK O MET G 129 MG MG G9001 1555 1555 1.96
LINK MG MG G9001 O HOH G9019 1555 1555 2.49
LINK O ILE H 163 MG MG H9007 1555 1555 2.17
LINK O ASP H 166 MG MG H9007 1555 1555 2.08
LINK O SER H 169 MG MG H9007 1555 1555 2.55
LINK O HOH H 814 MG MG I9003 1555 1555 3.05
LINK O HOH H1721 MG MG H9007 1555 1555 2.35
LINK MG MG H9007 OXT ASP Z 194 1555 1555 2.33
LINK O ALA I 163 MG MG I9005 1555 1555 2.01
LINK O ASP I 166 MG MG I9005 1555 1555 2.23
LINK O SER I 169 MG MG I9005 1555 1555 2.48
LINK O ASP I 194 MG MG Y9018 1555 1555 2.28
LINK MG MG I9003 O HOH I9030 1555 1555 2.56
LINK MG MG I9003 O HOH I9067 1555 1555 2.80
LINK MG MG I9003 O HOH I9093 1555 1555 2.37
LINK MG MG I9005 O HOH I9011 1555 1555 2.60
LINK MG MG I9005 O HOH I9013 1555 1555 2.61
LINK O ALA K 163 MG MG K9008 1555 1555 2.43
LINK O ASP K 166 MG MG K9008 1555 1555 2.50
LINK O SER K 169 MG MG K9008 1555 1555 2.56
LINK MG MG K9008 O HOH K9080 1555 1555 2.93
LINK MG MG K9008 O ASP W 194 1555 1555 2.01
LINK OG SER L 75 MG MG L9002 1555 1555 2.40
LINK OG SER L 78 MG MG L9002 1555 1555 2.58
LINK O THR L 163 MG MG L9004 1555 1555 2.41
LINK O HIS L 166 MG MG L9004 1555 1555 2.14
LINK O VAL L 169 MG MG L9004 1555 1555 2.41
LINK OXT ASP L 194 MG MG V9017 1555 1555 2.36
LINK MG MG L9002 O HOH L9010 1555 1555 2.26
LINK MG MG L9002 O HOH L9015 1555 1555 2.24
LINK MG MG L9004 O HOH L9031 1555 1555 2.31
LINK MG MG L9004 O HOH L9104 1555 1555 1.67
LINK MG MG L9004 O HOH L9106 1555 1555 3.02
LINK O HOH L9038 MG MG V9017 1555 1555 2.82
LINK O ILE N 163 MG MG N9006 1555 1555 2.42
LINK O ASP N 166 MG MG N9006 1555 1555 3.09
LINK O SER N 169 MG MG N9006 1555 1555 2.66
LINK O HOH N 556 MG MG N9006 1555 1555 2.87
LINK OE2 GLU R 105 MG MG Z9012 1555 1555 2.36
LINK O HOH R1666 MG MG Z9012 1555 1555 2.24
LINK OG1 THR U 13 MG MG U9011 1555 1555 2.47
LINK O TYR U 123 MG MG U9011 1555 1555 2.30
LINK O ARG U 126 MG MG U9011 1555 1555 1.90
LINK O ALA U 127 MG MG U9020 1555 1555 1.79
LINK O TYR U 128 MG MG U9020 1555 1555 3.12
LINK N TYR U 128 MG MG U9020 1555 1555 2.26
LINK O MET U 129 MG MG U9011 1555 1555 2.10
LINK O HOH U1558 MG MG U9011 1555 1555 2.24
LINK O ILE V 163 MG MG V9017 1555 1555 2.08
LINK O ASP V 166 MG MG V9017 1555 1555 2.21
LINK O SER V 169 MG MG V9017 1555 1555 2.04
LINK O HOH V2268 MG MG W9013 1555 1555 2.98
LINK O ALA W 163 MG MG W9015 1555 1555 2.25
LINK O ASP W 166 MG MG W9015 1555 1555 2.41
LINK O SER W 169 MG MG W9015 1555 1555 2.41
LINK MG MG W9013 O HOH W9026 1555 1555 2.53
LINK MG MG W9013 O HOH W9075 1555 1555 2.49
LINK MG MG W9013 O HOH W9113 1555 1555 2.91
LINK MG MG W9015 O HOH W9055 1555 1555 2.38
LINK MG MG W9015 O HOH W9057 1555 1555 2.24
LINK O ALA Y 163 MG MG Y9018 1555 1555 2.21
LINK O ASP Y 166 MG MG Y9018 1555 1555 2.21
LINK O SER Y 169 MG MG Y9018 1555 1555 2.45
LINK MG MG Y9018 O HOH Y9024 1555 1555 2.99
LINK OG SER Z 75 MG MG Z9012 1555 1555 2.54
LINK OG SER Z 78 MG MG Z9012 1555 1555 2.66
LINK O THR Z 163 MG MG Z9014 1555 1555 2.32
LINK O HIS Z 166 MG MG Z9014 1555 1555 2.32
LINK O VAL Z 169 MG MG Z9014 1555 1555 2.34
LINK O HOH Z 849 MG MG Z9014 1555 1555 1.90
LINK O HOH Z 975 MG MG Z9014 1555 1555 3.04
LINK O HOH Z1650 MG MG Z9012 1555 1555 2.02
LINK O HOH Z1667 MG MG Z9012 1555 1555 2.27
LINK O HOH Z1710 MG MG Z9014 1555 1555 2.42
LINK O ILE 2 163 MG MG 29016 1555 1555 2.41
LINK O ASP 2 166 MG MG 29016 1555 1555 2.48
LINK O SER 2 169 MG MG 29016 1555 1555 2.47
SITE 1 AC1 5 THR G 13 TYR G 123 ARG G 126 MET G 129
SITE 2 AC1 5 HOH G9019
SITE 1 AC2 6 GLU D 105 HOH D 254 SER L 75 SER L 78
SITE 2 AC2 6 HOH L9010 HOH L9015
SITE 1 AC3 5 HOH H 814 SER I 131 HOH I9030 HOH I9067
SITE 2 AC3 5 HOH I9093
SITE 1 AC4 7 THR L 163 HIS L 166 ILE L 167 VAL L 169
SITE 2 AC4 7 HOH L9031 HOH L9104 HOH L9106
SITE 1 AC5 5 ALA I 163 ASP I 166 SER I 169 HOH I9011
SITE 2 AC5 5 HOH I9013
SITE 1 AC6 5 ARG N 19 ILE N 163 ASP N 166 SER N 169
SITE 2 AC6 5 HOH N 556
SITE 1 AC7 6 GLY H 162 ILE H 163 ASP H 166 SER H 169
SITE 2 AC7 6 HOH H1721 ASP Z 194
SITE 1 AC8 6 ARG K 19 ALA K 163 ASP K 166 SER K 169
SITE 2 AC8 6 HOH K9080 ASP W 194
SITE 1 AC9 1 LYS F 173
SITE 1 BC1 4 TYR A 8 ALA G 127 TYR G 128 MET G 129
SITE 1 BC2 6 THR U 13 TYR U 123 ARG U 126 ALA U 127
SITE 2 BC2 6 MET U 129 HOH U1558
SITE 1 BC3 6 GLU R 105 HOH R1666 SER Z 75 SER Z 78
SITE 2 BC3 6 HOH Z1650 HOH Z1667
SITE 1 BC4 5 HOH V2268 SER W 131 HOH W9026 HOH W9075
SITE 2 BC4 5 HOH W9113
SITE 1 BC5 7 THR Z 163 HIS Z 166 ILE Z 167 VAL Z 169
SITE 2 BC5 7 HOH Z 849 HOH Z 975 HOH Z1710
SITE 1 BC6 5 ALA W 163 ASP W 166 SER W 169 HOH W9055
SITE 2 BC6 5 HOH W9057
SITE 1 BC7 4 ARG 2 19 ILE 2 163 ASP 2 166 SER 2 169
SITE 1 BC8 6 ASP L 194 HOH L9038 GLY V 162 ILE V 163
SITE 2 BC8 6 ASP V 166 SER V 169
SITE 1 BC9 6 ASP I 194 ARG Y 19 ALA Y 163 ASP Y 166
SITE 2 BC9 6 SER Y 169 HOH Y9024
SITE 1 CC1 1 LYS T 173
SITE 1 CC2 4 TYR O 8 ALA U 127 TYR U 128 MET U 129
CRYST1 135.180 301.100 144.100 90.00 113.00 90.00 P 1 21 1 4
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 0.007398 0.000000 0.003140 0.00000
SCALE2 0.000000 0.003321 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007539 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
