HEADER RIBOSOME 14-JUN-07 2QA4
TITLE A MORE COMPLETE STRUCTURE OF THE THE L7/L12 STALK OF THE HALOARCULA
TITLE 2 MARISMORTUI 50S LARGE RIBOSOMAL SUBUNIT
CAVEAT 2QA4 CHIRALITY ERRORS AT SEVERAL RESIDUES IN CHAINS 0,I
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 23S RIBOSOMAL RNA;
COMPND 3 CHAIN: 0;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: 5S RIBOSOMAL RNA;
COMPND 6 CHAIN: 9;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: 50S RIBOSOMAL PROTEIN L2P;
COMPND 9 CHAIN: A;
COMPND 10 MOL_ID: 4;
COMPND 11 MOLECULE: 50S RIBOSOMAL PROTEIN L3P;
COMPND 12 CHAIN: B;
COMPND 13 MOL_ID: 5;
COMPND 14 MOLECULE: 50S RIBOSOMAL PROTEIN L4P;
COMPND 15 CHAIN: C;
COMPND 16 MOL_ID: 6;
COMPND 17 MOLECULE: 50S RIBOSOMAL PROTEIN L5P;
COMPND 18 CHAIN: D;
COMPND 19 MOL_ID: 7;
COMPND 20 MOLECULE: 50S RIBOSOMAL PROTEIN L6P;
COMPND 21 CHAIN: E;
COMPND 22 MOL_ID: 8;
COMPND 23 MOLECULE: 50S RIBOSOMAL PROTEIN L7AE;
COMPND 24 CHAIN: F;
COMPND 25 MOL_ID: 9;
COMPND 26 MOLECULE: ACIDIC RIBOSOMAL PROTEIN P0 HOMO;
COMPND 27 CHAIN: G;
COMPND 28 MOL_ID: 10;
COMPND 29 MOLECULE: 50S RIBOSOMAL PROTEIN L10E;
COMPND 30 CHAIN: H;
COMPND 31 MOL_ID: 11;
COMPND 32 MOLECULE: 50S RIBOSOMAL PROTEIN L11P;
COMPND 33 CHAIN: I;
COMPND 34 MOL_ID: 12;
COMPND 35 MOLECULE: 50S RIBOSOMAL PROTEIN L13P;
COMPND 36 CHAIN: J;
COMPND 37 MOL_ID: 13;
COMPND 38 MOLECULE: 50S RIBOSOMAL PROTEIN L14P;
COMPND 39 CHAIN: K;
COMPND 40 MOL_ID: 14;
COMPND 41 MOLECULE: 50S RIBOSOMAL PROTEIN L15P;
COMPND 42 CHAIN: L;
COMPND 43 MOL_ID: 15;
COMPND 44 MOLECULE: 50S RIBOSOMAL PROTEIN L15E;
COMPND 45 CHAIN: M;
COMPND 46 MOL_ID: 16;
COMPND 47 MOLECULE: 50S RIBOSOMAL PROTEIN L18P;
COMPND 48 CHAIN: N;
COMPND 49 MOL_ID: 17;
COMPND 50 MOLECULE: 50S RIBOSOMAL PROTEIN L18E;
COMPND 51 CHAIN: O;
COMPND 52 MOL_ID: 18;
COMPND 53 MOLECULE: 50S RIBOSOMAL PROTEIN L19E;
COMPND 54 CHAIN: P;
COMPND 55 MOL_ID: 19;
COMPND 56 MOLECULE: 50S RIBOSOMAL PROTEIN L21E;
COMPND 57 CHAIN: Q;
COMPND 58 MOL_ID: 20;
COMPND 59 MOLECULE: 50S RIBOSOMAL PROTEIN L22P;
COMPND 60 CHAIN: R;
COMPND 61 MOL_ID: 21;
COMPND 62 MOLECULE: 50S RIBOSOMAL PROTEIN L23P;
COMPND 63 CHAIN: S;
COMPND 64 MOL_ID: 22;
COMPND 65 MOLECULE: 50S RIBOSOMAL PROTEIN L24P;
COMPND 66 CHAIN: T;
COMPND 67 MOL_ID: 23;
COMPND 68 MOLECULE: 50S RIBOSOMAL PROTEIN L24E;
COMPND 69 CHAIN: U;
COMPND 70 MOL_ID: 24;
COMPND 71 MOLECULE: 50S RIBOSOMAL PROTEIN L29P;
COMPND 72 CHAIN: V;
COMPND 73 MOL_ID: 25;
COMPND 74 MOLECULE: 50S RIBOSOMAL PROTEIN L30P;
COMPND 75 CHAIN: W;
COMPND 76 MOL_ID: 26;
COMPND 77 MOLECULE: 50S RIBOSOMAL PROTEIN L31E;
COMPND 78 CHAIN: X;
COMPND 79 MOL_ID: 27;
COMPND 80 MOLECULE: 50S RIBOSOMAL PROTEIN L32E;
COMPND 81 CHAIN: Y;
COMPND 82 MOL_ID: 28;
COMPND 83 MOLECULE: 50S RIBOSOMAL PROTEIN L37AE;
COMPND 84 CHAIN: Z;
COMPND 85 MOL_ID: 29;
COMPND 86 MOLECULE: 50S RIBOSOMAL PROTEIN L37E;
COMPND 87 CHAIN: 1;
COMPND 88 MOL_ID: 30;
COMPND 89 MOLECULE: 50S RIBOSOMAL PROTEIN L39E;
COMPND 90 CHAIN: 2;
COMPND 91 MOL_ID: 31;
COMPND 92 MOLECULE: 50S RIBOSOMAL PROTEIN L44E;
COMPND 93 CHAIN: 3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 3 ORGANISM_TAXID: 2238;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 6 ORGANISM_TAXID: 2238;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 9 ORGANISM_TAXID: 2238;
SOURCE 10 MOL_ID: 4;
SOURCE 11 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 12 ORGANISM_TAXID: 2238;
SOURCE 13 MOL_ID: 5;
SOURCE 14 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 15 ORGANISM_TAXID: 2238;
SOURCE 16 MOL_ID: 6;
SOURCE 17 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 18 ORGANISM_TAXID: 2238;
SOURCE 19 MOL_ID: 7;
SOURCE 20 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 21 ORGANISM_TAXID: 2238;
SOURCE 22 MOL_ID: 8;
SOURCE 23 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 24 ORGANISM_TAXID: 2238;
SOURCE 25 MOL_ID: 9;
SOURCE 26 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 27 ORGANISM_TAXID: 2238;
SOURCE 28 MOL_ID: 10;
SOURCE 29 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 30 ORGANISM_TAXID: 2238;
SOURCE 31 MOL_ID: 11;
SOURCE 32 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 33 ORGANISM_TAXID: 2238;
SOURCE 34 MOL_ID: 12;
SOURCE 35 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 36 ORGANISM_TAXID: 2238;
SOURCE 37 MOL_ID: 13;
SOURCE 38 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 39 ORGANISM_TAXID: 2238;
SOURCE 40 MOL_ID: 14;
SOURCE 41 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 42 ORGANISM_TAXID: 2238;
SOURCE 43 MOL_ID: 15;
SOURCE 44 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 45 ORGANISM_TAXID: 2238;
SOURCE 46 MOL_ID: 16;
SOURCE 47 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 48 ORGANISM_TAXID: 2238;
SOURCE 49 MOL_ID: 17;
SOURCE 50 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 51 ORGANISM_TAXID: 2238;
SOURCE 52 MOL_ID: 18;
SOURCE 53 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 54 ORGANISM_TAXID: 2238;
SOURCE 55 MOL_ID: 19;
SOURCE 56 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 57 ORGANISM_TAXID: 2238;
SOURCE 58 MOL_ID: 20;
SOURCE 59 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 60 ORGANISM_TAXID: 2238;
SOURCE 61 MOL_ID: 21;
SOURCE 62 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 63 ORGANISM_TAXID: 2238;
SOURCE 64 MOL_ID: 22;
SOURCE 65 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 66 ORGANISM_TAXID: 2238;
SOURCE 67 MOL_ID: 23;
SOURCE 68 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 69 ORGANISM_TAXID: 2238;
SOURCE 70 MOL_ID: 24;
SOURCE 71 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 72 ORGANISM_TAXID: 2238;
SOURCE 73 MOL_ID: 25;
SOURCE 74 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 75 ORGANISM_TAXID: 2238;
SOURCE 76 MOL_ID: 26;
SOURCE 77 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 78 ORGANISM_TAXID: 2238;
SOURCE 79 MOL_ID: 27;
SOURCE 80 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 81 ORGANISM_TAXID: 2238;
SOURCE 82 MOL_ID: 28;
SOURCE 83 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 84 ORGANISM_TAXID: 2238;
SOURCE 85 MOL_ID: 29;
SOURCE 86 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 87 ORGANISM_TAXID: 2238;
SOURCE 88 MOL_ID: 30;
SOURCE 89 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 90 ORGANISM_TAXID: 2238;
SOURCE 91 MOL_ID: 31;
SOURCE 92 ORGANISM_SCIENTIFIC: HALOARCULA MARISMORTUI;
SOURCE 93 ORGANISM_TAXID: 2238
KEYWDS LARGE RIBOSOMAL SUBUNIT, RIBONUCLEOPROTEIN, RIBOSOMAL PROTEIN, RNA-
KEYWDS 2 BINDING, RRNA-BINDING, TRNA-BINDING, METAL-BINDING, ZINC, ZINC-
KEYWDS 3 FINGER, RIBOSOME
EXPDTA X-RAY DIFFRACTION
AUTHOR T.A.STEITZ,J.M.KAVRAN
REVDAT 3 30-AUG-23 2QA4 1 REMARK SEQADV SHEET LINK
REVDAT 2 24-FEB-09 2QA4 1 VERSN
REVDAT 1 01-APR-08 2QA4 0
JRNL AUTH J.M.KAVRAN,T.A.STEITZ
JRNL TITL STRUCTURE OF THE BASE OF THE L7/L12 STALK OF THE HALOARCULA
JRNL TITL 2 MARISMORTUI LARGE RIBOSOMAL SUBUNIT: ANALYSIS OF L11
JRNL TITL 3 MOVEMENTS
JRNL REF J.MOL.BIOL. V. 371 1047 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17599351
JRNL DOI 10.1016/J.JMB.2007.05.091
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 361885
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.241
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 30438
REMARK 3 NUCLEIC ACID ATOMS : 61579
REMARK 3 HETEROGEN ATOMS : 231
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2QA4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000043340.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 361885
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.13400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: CNS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1JJ2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 289.02800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 289.02800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 107.24500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 151.21600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 107.24500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 151.21600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 289.02800
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 107.24500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 151.21600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 289.02800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 107.24500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 151.21600
REMARK 290 SMTRY3 8 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 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: 31-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 31-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 0, 9, A, B, C, D, E, F, G, H,
REMARK 350 AND CHAINS: I, J, K, L, M, N, O, P, Q,
REMARK 350 AND CHAINS: R, S, T, U, V, W, X, Y, Z, 1,
REMARK 350 AND CHAINS: 2, 3
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 U 0 2
REMARK 465 U 0 3
REMARK 465 G 0 4
REMARK 465 G 0 5
REMARK 465 C 0 6
REMARK 465 U 0 7
REMARK 465 A 0 8
REMARK 465 C 0 9
REMARK 465 C 0 126
REMARK 465 U 0 127
REMARK 465 A 0 628
REMARK 465 U 0 715
REMARK 465 G 0 971
REMARK 465 U 0 972
REMARK 465 G 0 973
REMARK 465 U 0 974
REMARK 465 C 0 975
REMARK 465 C 0 976
REMARK 465 G 0 977
REMARK 465 C 0 978
REMARK 465 C 0 979
REMARK 465 U 0 980
REMARK 465 C 0 981
REMARK 465 C 0 982
REMARK 465 G 0 983
REMARK 465 A 0 984
REMARK 465 G 0 985
REMARK 465 A 0 986
REMARK 465 G 0 987
REMARK 465 G 0 988
REMARK 465 A 0 989
REMARK 465 G 0 990
REMARK 465 U 0 991
REMARK 465 C 0 992
REMARK 465 G 0 993
REMARK 465 G 0 994
REMARK 465 C 0 995
REMARK 465 A 0 996
REMARK 465 C 0 997
REMARK 465 A 0 998
REMARK 465 U 0 1560
REMARK 465 U 0 1952
REMARK 465 A 0 1953
REMARK 465 A 0 1954
REMARK 465 C 0 1955
REMARK 465 U 0 1956
REMARK 465 A 0 1957
REMARK 465 U 0 1958
REMARK 465 G 0 1959
REMARK 465 A 0 1960
REMARK 465 C 0 1961
REMARK 465 C 0 1962
REMARK 465 C 0 1963
REMARK 465 A 0 2137
REMARK 465 C 0 2138
REMARK 465 G 0 2139
REMARK 465 U 0 2140
REMARK 465 G 0 2141
REMARK 465 G 0 2142
REMARK 465 U 0 2143
REMARK 465 C 0 2144
REMARK 465 G 0 2145
REMARK 465 C 0 2146
REMARK 465 C 0 2147
REMARK 465 G 0 2148
REMARK 465 A 0 2149
REMARK 465 U 0 2150
REMARK 465 G 0 2151
REMARK 465 U 0 2152
REMARK 465 G 0 2153
REMARK 465 C 0 2154
REMARK 465 A 0 2155
REMARK 465 G 0 2156
REMARK 465 C 0 2157
REMARK 465 A 0 2158
REMARK 465 U 0 2159
REMARK 465 A 0 2160
REMARK 465 G 0 2161
REMARK 465 G 0 2162
REMARK 465 U 0 2163
REMARK 465 A 0 2164
REMARK 465 G 0 2165
REMARK 465 G 0 2166
REMARK 465 A 0 2167
REMARK 465 G 0 2168
REMARK 465 A 0 2169
REMARK 465 C 0 2170
REMARK 465 A 0 2171
REMARK 465 C 0 2172
REMARK 465 U 0 2173
REMARK 465 A 0 2174
REMARK 465 C 0 2175
REMARK 465 A 0 2176
REMARK 465 C 0 2177
REMARK 465 A 0 2178
REMARK 465 G 0 2179
REMARK 465 G 0 2180
REMARK 465 U 0 2181
REMARK 465 A 0 2182
REMARK 465 C 0 2183
REMARK 465 C 0 2184
REMARK 465 C 0 2185
REMARK 465 G 0 2186
REMARK 465 C 0 2187
REMARK 465 G 0 2188
REMARK 465 C 0 2189
REMARK 465 U 0 2190
REMARK 465 A 0 2191
REMARK 465 G 0 2192
REMARK 465 C 0 2193
REMARK 465 G 0 2194
REMARK 465 G 0 2195
REMARK 465 G 0 2196
REMARK 465 C 0 2197
REMARK 465 C 0 2198
REMARK 465 A 0 2199
REMARK 465 C 0 2200
REMARK 465 C 0 2201
REMARK 465 G 0 2202
REMARK 465 A 0 2203
REMARK 465 G 0 2204
REMARK 465 U 0 2205
REMARK 465 C 0 2206
REMARK 465 A 0 2207
REMARK 465 A 0 2208
REMARK 465 C 0 2209
REMARK 465 A 0 2210
REMARK 465 G 0 2211
REMARK 465 U 0 2212
REMARK 465 G 0 2213
REMARK 465 A 0 2214
REMARK 465 A 0 2215
REMARK 465 A 0 2216
REMARK 465 U 0 2217
REMARK 465 A 0 2218
REMARK 465 C 0 2219
REMARK 465 U 0 2220
REMARK 465 A 0 2221
REMARK 465 C 0 2222
REMARK 465 C 0 2223
REMARK 465 C 0 2224
REMARK 465 G 0 2225
REMARK 465 U 0 2226
REMARK 465 C 0 2227
REMARK 465 G 0 2228
REMARK 465 G 0 2229
REMARK 465 U 0 2230
REMARK 465 G 0 2231
REMARK 465 A 0 2232
REMARK 465 C 0 2233
REMARK 465 U 0 2234
REMARK 465 G 0 2235
REMARK 465 C 0 2236
REMARK 465 A 0 2339
REMARK 465 C 0 2340
REMARK 465 A 0 2341
REMARK 465 G 0 2342
REMARK 465 A 0 2343
REMARK 465 A 0 2665
REMARK 465 U 0 2666
REMARK 465 A 0 2915
REMARK 465 G 0 2916
REMARK 465 C 0 2917
REMARK 465 C 0 2918
REMARK 465 A 0 2919
REMARK 465 U 0 2920
REMARK 465 C 0 2921
REMARK 465 A 0 2922
REMARK 465 U 0 2923
REMARK 465 MET A 0
REMARK 465 ASN A 238
REMARK 465 GLU A 239
REMARK 465 MET B 0
REMARK 465 MET D 0
REMARK 465 SER D 1
REMARK 465 SER D 2
REMARK 465 GLU D 3
REMARK 465 SER D 4
REMARK 465 GLU D 5
REMARK 465 SER D 6
REMARK 465 GLY D 7
REMARK 465 GLY D 8
REMARK 465 ASP D 9
REMARK 465 GLY D 30
REMARK 465 GLY D 31
REMARK 465 ARG D 32
REMARK 465 ASP D 33
REMARK 465 LEU D 34
REMARK 465 VAL D 108
REMARK 465 GLU D 109
REMARK 465 GLU D 110
REMARK 465 HIS D 111
REMARK 465 THR D 112
REMARK 465 GLU D 113
REMARK 465 PHE D 114
REMARK 465 PRO D 115
REMARK 465 SER D 116
REMARK 465 GLN D 117
REMARK 465 GLU D 118
REMARK 465 TYR D 119
REMARK 465 ASP D 120
REMARK 465 PRO D 121
REMARK 465 SER D 122
REMARK 465 ILE D 123
REMARK 465 GLY D 124
REMARK 465 ILE D 125
REMARK 465 TYR D 126
REMARK 465 GLY D 127
REMARK 465 SER D 175
REMARK 465 GLU D 176
REMARK 465 MET E 0
REMARK 465 ASN E 173
REMARK 465 ARG E 174
REMARK 465 GLY E 175
REMARK 465 ASP E 176
REMARK 465 ALA E 177
REMARK 465 MET F 0
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 ALA G 3
REMARK 465 GLU G 4
REMARK 465 SER G 5
REMARK 465 GLU G 6
REMARK 465 ALA G 120
REMARK 465 VAL G 133
REMARK 465 ASP G 134
REMARK 465 PRO G 135
REMARK 465 GLY G 136
REMARK 465 PRO G 137
REMARK 465 PHE G 138
REMARK 465 VAL G 139
REMARK 465 GLY G 140
REMARK 465 GLU G 141
REMARK 465 LEU G 142
REMARK 465 GLN G 143
REMARK 465 SER G 144
REMARK 465 VAL G 145
REMARK 465 GLY G 146
REMARK 465 ALA G 147
REMARK 465 ASP G 148
REMARK 465 ALA G 149
REMARK 465 ARG G 150
REMARK 465 ILE G 151
REMARK 465 GLN G 152
REMARK 465 GLU G 153
REMARK 465 GLY G 154
REMARK 465 SER G 155
REMARK 465 ILE G 156
REMARK 465 GLN G 157
REMARK 465 VAL G 158
REMARK 465 LEU G 159
REMARK 465 SER G 160
REMARK 465 ASP G 161
REMARK 465 SER G 162
REMARK 465 THR G 163
REMARK 465 VAL G 164
REMARK 465 LEU G 165
REMARK 465 ASP G 166
REMARK 465 THR G 167
REMARK 465 GLY G 168
REMARK 465 GLU G 169
REMARK 465 GLU G 170
REMARK 465 VAL G 171
REMARK 465 SER G 172
REMARK 465 GLN G 173
REMARK 465 GLU G 174
REMARK 465 LEU G 175
REMARK 465 SER G 176
REMARK 465 ASN G 177
REMARK 465 VAL G 178
REMARK 465 LEU G 179
REMARK 465 ASN G 180
REMARK 465 GLU G 181
REMARK 465 LEU G 182
REMARK 465 GLY G 183
REMARK 465 ILE G 184
REMARK 465 GLU G 185
REMARK 465 PRO G 186
REMARK 465 LYS G 187
REMARK 465 GLU G 188
REMARK 465 VAL G 189
REMARK 465 GLY G 190
REMARK 465 LEU G 191
REMARK 465 ASP G 192
REMARK 465 LEU G 193
REMARK 465 ARG G 194
REMARK 465 ALA G 195
REMARK 465 VAL G 196
REMARK 465 PHE G 197
REMARK 465 ALA G 198
REMARK 465 ASP G 199
REMARK 465 GLY G 200
REMARK 465 VAL G 201
REMARK 465 LEU G 202
REMARK 465 PHE G 203
REMARK 465 GLU G 204
REMARK 465 PRO G 205
REMARK 465 GLU G 206
REMARK 465 GLU G 207
REMARK 465 LEU G 208
REMARK 465 GLU G 209
REMARK 465 LEU G 210
REMARK 465 ASP G 211
REMARK 465 ILE G 212
REMARK 465 ASP G 213
REMARK 465 GLU G 214
REMARK 465 TYR G 215
REMARK 465 ARG G 216
REMARK 465 SER G 217
REMARK 465 ASP G 218
REMARK 465 ILE G 219
REMARK 465 GLN G 220
REMARK 465 ALA G 221
REMARK 465 ALA G 222
REMARK 465 ALA G 223
REMARK 465 GLY G 224
REMARK 465 ARG G 225
REMARK 465 ALA G 226
REMARK 465 PHE G 227
REMARK 465 ASN G 228
REMARK 465 LEU G 229
REMARK 465 SER G 230
REMARK 465 VAL G 231
REMARK 465 ASN G 232
REMARK 465 ALA G 233
REMARK 465 ASP G 234
REMARK 465 TYR G 235
REMARK 465 PRO G 236
REMARK 465 THR G 237
REMARK 465 ALA G 238
REMARK 465 THR G 239
REMARK 465 THR G 240
REMARK 465 ALA G 241
REMARK 465 PRO G 242
REMARK 465 THR G 243
REMARK 465 MET G 244
REMARK 465 LEU G 245
REMARK 465 GLN G 246
REMARK 465 SER G 247
REMARK 465 ASP G 248
REMARK 465 ARG G 249
REMARK 465 GLY G 250
REMARK 465 ASN G 251
REMARK 465 ALA G 252
REMARK 465 LYS G 253
REMARK 465 SER G 254
REMARK 465 LEU G 255
REMARK 465 ALA G 256
REMARK 465 LEU G 257
REMARK 465 GLN G 258
REMARK 465 ALA G 259
REMARK 465 ALA G 260
REMARK 465 ILE G 261
REMARK 465 GLU G 262
REMARK 465 ASP G 263
REMARK 465 PRO G 264
REMARK 465 GLU G 265
REMARK 465 VAL G 266
REMARK 465 VAL G 267
REMARK 465 PRO G 268
REMARK 465 ASP G 269
REMARK 465 LEU G 270
REMARK 465 VAL G 271
REMARK 465 SER G 272
REMARK 465 LYS G 273
REMARK 465 ALA G 274
REMARK 465 ASP G 275
REMARK 465 ALA G 276
REMARK 465 GLN G 277
REMARK 465 VAL G 278
REMARK 465 ARG G 279
REMARK 465 ALA G 280
REMARK 465 LEU G 281
REMARK 465 ALA G 282
REMARK 465 SER G 283
REMARK 465 GLN G 284
REMARK 465 ILE G 285
REMARK 465 ASP G 286
REMARK 465 ASP G 287
REMARK 465 GLU G 288
REMARK 465 GLU G 289
REMARK 465 ALA G 290
REMARK 465 LEU G 291
REMARK 465 PRO G 292
REMARK 465 GLU G 293
REMARK 465 GLU G 294
REMARK 465 LEU G 295
REMARK 465 GLN G 296
REMARK 465 GLY G 297
REMARK 465 VAL G 298
REMARK 465 GLU G 299
REMARK 465 ALA G 300
REMARK 465 ASP G 301
REMARK 465 VAL G 302
REMARK 465 ALA G 303
REMARK 465 THR G 304
REMARK 465 GLU G 305
REMARK 465 GLU G 306
REMARK 465 PRO G 307
REMARK 465 THR G 308
REMARK 465 ASP G 309
REMARK 465 ASP G 310
REMARK 465 GLN G 311
REMARK 465 ASP G 312
REMARK 465 ASP G 313
REMARK 465 ASP G 314
REMARK 465 THR G 315
REMARK 465 ALA G 316
REMARK 465 SER G 317
REMARK 465 GLU G 318
REMARK 465 ASP G 319
REMARK 465 ASP G 320
REMARK 465 ALA G 321
REMARK 465 ASP G 322
REMARK 465 ALA G 323
REMARK 465 ASP G 324
REMARK 465 ASP G 325
REMARK 465 ALA G 326
REMARK 465 ALA G 327
REMARK 465 GLU G 328
REMARK 465 GLU G 329
REMARK 465 ALA G 330
REMARK 465 ASP G 331
REMARK 465 ASP G 332
REMARK 465 ASP G 333
REMARK 465 ASP G 334
REMARK 465 ASP G 335
REMARK 465 ASP G 336
REMARK 465 ASP G 337
REMARK 465 GLU G 338
REMARK 465 ASP G 339
REMARK 465 ALA G 340
REMARK 465 GLY G 341
REMARK 465 ASP G 342
REMARK 465 ALA G 343
REMARK 465 LEU G 344
REMARK 465 GLY G 345
REMARK 465 ALA G 346
REMARK 465 MET G 347
REMARK 465 PHE G 348
REMARK 465 GLN H 100
REMARK 465 ALA H 101
REMARK 465 THR H 102
REMARK 465 GLY H 103
REMARK 465 ALA H 104
REMARK 465 GLY H 105
REMARK 465 ALA H 106
REMARK 465 ASP H 107
REMARK 465 ARG H 108
REMARK 465 VAL H 109
REMARK 465 SER H 110
REMARK 465 MET I 1
REMARK 465 ALA I 2
REMARK 465 GLY I 3
REMARK 465 THR I 4
REMARK 465 GLY I 25
REMARK 465 PRO I 26
REMARK 465 THR I 27
REMARK 465 ALA I 44
REMARK 465 PHE I 45
REMARK 465 ASP I 46
REMARK 465 GLY I 47
REMARK 465 THR I 48
REMARK 465 LEU I 131
REMARK 465 GLY I 132
REMARK 465 VAL I 133
REMARK 465 THR I 134
REMARK 465 ILE I 135
REMARK 465 GLU I 136
REMARK 465 GLY I 137
REMARK 465 GLU I 138
REMARK 465 ASN I 139
REMARK 465 PRO I 140
REMARK 465 ARG I 141
REMARK 465 GLU I 142
REMARK 465 PHE I 143
REMARK 465 LYS I 144
REMARK 465 GLU I 145
REMARK 465 ARG I 146
REMARK 465 ILE I 147
REMARK 465 ASP I 148
REMARK 465 ALA I 149
REMARK 465 GLY I 150
REMARK 465 GLU I 151
REMARK 465 TYR I 152
REMARK 465 ASP I 153
REMARK 465 ASP I 154
REMARK 465 VAL I 155
REMARK 465 PHE I 156
REMARK 465 ALA I 157
REMARK 465 ALA I 158
REMARK 465 GLU I 159
REMARK 465 ALA I 160
REMARK 465 GLN I 161
REMARK 465 ALA I 162
REMARK 465 MET J 1
REMARK 465 SER J 2
REMARK 465 VAL J 3
REMARK 465 MET L 0
REMARK 465 VAL L 84
REMARK 465 GLU L 85
REMARK 465 ASP L 86
REMARK 465 GLY L 87
REMARK 465 GLY L 88
REMARK 465 ALA L 151
REMARK 465 GLU L 152
REMARK 465 ALA L 153
REMARK 465 GLU L 154
REMARK 465 GLU L 155
REMARK 465 THR L 156
REMARK 465 GLU L 157
REMARK 465 ASP L 158
REMARK 465 ALA L 159
REMARK 465 ASP L 160
REMARK 465 ALA L 161
REMARK 465 ASP L 162
REMARK 465 GLU L 163
REMARK 465 GLU L 164
REMARK 465 MET M 0
REMARK 465 LYS M 195
REMARK 465 MET N 0
REMARK 465 MET O 0
REMARK 465 MET P 0
REMARK 465 ASN P 144
REMARK 465 HIS P 145
REMARK 465 GLY P 146
REMARK 465 ASP P 147
REMARK 465 ALA P 148
REMARK 465 MET Q 0
REMARK 465 MET R 0
REMARK 465 GLU R 151
REMARK 465 VAL R 152
REMARK 465 GLU R 153
REMARK 465 ASP R 154
REMARK 465 MET S 0
REMARK 465 GLY S 82
REMARK 465 VAL S 83
REMARK 465 PHE S 84
REMARK 465 MET T 0
REMARK 465 MET U 0
REMARK 465 PRO U 1
REMARK 465 ARG U 2
REMARK 465 THR U 3
REMARK 465 GLY U 57
REMARK 465 GLU U 58
REMARK 465 ALA U 59
REMARK 465 GLY U 60
REMARK 465 GLU U 61
REMARK 465 ALA U 62
REMARK 465 GLU U 63
REMARK 465 ASP U 64
REMARK 465 GLU U 65
REMARK 465 ALA U 66
REMARK 465 MET V 0
REMARK 465 LEU V 66
REMARK 465 GLN V 67
REMARK 465 GLU V 68
REMARK 465 ASN V 69
REMARK 465 GLU V 70
REMARK 465 MET X 0
REMARK 465 SER X 1
REMARK 465 ALA X 2
REMARK 465 SER X 3
REMARK 465 ASP X 4
REMARK 465 PHE X 5
REMARK 465 GLU X 6
REMARK 465 THR X 89
REMARK 465 ALA X 90
REMARK 465 GLU X 91
REMARK 465 MET Y 0
REMARK 465 ALA Y 1
REMARK 465 ASP Y 2
REMARK 465 ASN Y 3
REMARK 465 GLU Y 4
REMARK 465 GLU Y 5
REMARK 465 ASP Y 6
REMARK 465 VAL Y 7
REMARK 465 GLU Y 8
REMARK 465 ALA Y 9
REMARK 465 GLU Y 10
REMARK 465 GLU Y 11
REMARK 465 GLU Y 12
REMARK 465 TYR Y 13
REMARK 465 THR Y 14
REMARK 465 GLU Y 15
REMARK 465 LEU Y 16
REMARK 465 THR Y 17
REMARK 465 ASP Y 18
REMARK 465 ILE Y 19
REMARK 465 SER Y 20
REMARK 465 GLY Y 21
REMARK 465 VAL Y 22
REMARK 465 GLY Y 23
REMARK 465 PRO Y 24
REMARK 465 SER Y 25
REMARK 465 LYS Y 26
REMARK 465 ALA Y 27
REMARK 465 GLU Y 28
REMARK 465 SER Y 29
REMARK 465 LEU Y 30
REMARK 465 ARG Y 31
REMARK 465 GLU Y 32
REMARK 465 ALA Y 33
REMARK 465 GLY Y 34
REMARK 465 PHE Y 35
REMARK 465 GLU Y 36
REMARK 465 SER Y 37
REMARK 465 VAL Y 38
REMARK 465 GLU Y 39
REMARK 465 ASP Y 40
REMARK 465 VAL Y 41
REMARK 465 ARG Y 42
REMARK 465 GLY Y 43
REMARK 465 ALA Y 44
REMARK 465 ASP Y 45
REMARK 465 GLN Y 46
REMARK 465 SER Y 47
REMARK 465 ALA Y 48
REMARK 465 LEU Y 49
REMARK 465 ALA Y 50
REMARK 465 ASP Y 51
REMARK 465 VAL Y 52
REMARK 465 SER Y 53
REMARK 465 GLY Y 54
REMARK 465 ILE Y 55
REMARK 465 GLY Y 56
REMARK 465 ASN Y 57
REMARK 465 ALA Y 58
REMARK 465 LEU Y 59
REMARK 465 ALA Y 60
REMARK 465 ALA Y 61
REMARK 465 ARG Y 62
REMARK 465 ILE Y 63
REMARK 465 LYS Y 64
REMARK 465 ALA Y 65
REMARK 465 ASP Y 66
REMARK 465 VAL Y 67
REMARK 465 GLY Y 68
REMARK 465 GLY Y 69
REMARK 465 LEU Y 70
REMARK 465 GLU Y 71
REMARK 465 VAL Y 72
REMARK 465 GLU Y 73
REMARK 465 SER Y 74
REMARK 465 GLU Y 75
REMARK 465 THR Y 76
REMARK 465 GLU Y 77
REMARK 465 ALA Y 78
REMARK 465 GLU Y 79
REMARK 465 VAL Y 80
REMARK 465 GLU Y 81
REMARK 465 GLU Y 82
REMARK 465 GLU Y 83
REMARK 465 GLY Y 84
REMARK 465 GLY Y 85
REMARK 465 GLU Y 86
REMARK 465 GLU Y 87
REMARK 465 ALA Y 88
REMARK 465 PRO Y 89
REMARK 465 ASP Y 90
REMARK 465 GLU Y 91
REMARK 465 ASP Y 92
REMARK 465 VAL Y 93
REMARK 465 GLU Y 94
REMARK 465 GLU Y 237
REMARK 465 VAL Y 238
REMARK 465 SER Y 239
REMARK 465 GLU Y 240
REMARK 465 MET Z 1
REMARK 465 ALA Z 2
REMARK 465 SER Z 3
REMARK 465 LYS Z 4
REMARK 465 SER Z 5
REMARK 465 GLY Z 6
REMARK 465 LYS Z 7
REMARK 465 THR Z 8
REMARK 465 GLY Z 9
REMARK 465 ILE Z 83
REMARK 465 ARG Z 84
REMARK 465 ALA Z 85
REMARK 465 ALA Z 86
REMARK 465 LEU Z 87
REMARK 465 SER Z 88
REMARK 465 GLU Z 89
REMARK 465 ASP Z 90
REMARK 465 GLU Z 91
REMARK 465 GLU Z 92
REMARK 465 MET 1 0
REMARK 465 MET 2 0
REMARK 465 GLU 2 32
REMARK 465 VAL 2 33
REMARK 465 GLN 2 34
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 U 0 10 P OP1 OP2
REMARK 470 A 0 128 P OP1 OP2
REMARK 470 G 0 716 P OP1 OP2
REMARK 470 C 0 999 P OP1 OP2
REMARK 470 A 01161 P OP1 OP2
REMARK 470 A 01181 P OP1 OP2 O5' C5' C4' O4'
REMARK 470 A 01181 C1' N9 C5 C6 N6 N1 C2
REMARK 470 A 01181 N3 C4
REMARK 470 U 01561 P OP1 OP2
REMARK 470 U 01964 P OP1 OP2
REMARK 470 G 02237 P OP1 OP2
REMARK 470 G 02344 P OP1 OP2
REMARK 470 G 02667 P OP1 OP2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NE2 HIS G 54 CE2 TYR I 115 0.44
REMARK 500 CE1 HIS G 54 CE2 TYR I 115 1.14
REMARK 500 MG MG 0 2931 NA NA 0 3079 1.37
REMARK 500 CE1 HIS G 54 CZ TYR I 115 1.47
REMARK 500 NE2 HIS G 54 CD2 TYR I 115 1.56
REMARK 500 O HIS G 54 N GLY G 55 1.57
REMARK 500 N7 G 0 824 MG MG 0 2933 1.59
REMARK 500 CE1 HIS G 54 CD2 TYR I 115 1.61
REMARK 500 OP2 G 0 1979 MG MG 0 2967 1.64
REMARK 500 NE2 HIS G 54 CZ TYR I 115 1.69
REMARK 500 OP1 U 0 1748 MG MG 0 2952 1.69
REMARK 500 C VAL G 33 OD2 ASP G 123 1.72
REMARK 500 CG2 VAL I 31 CB VAL I 34 1.73
REMARK 500 CD2 HIS G 54 CE2 TYR I 115 1.79
REMARK 500 CG2 VAL I 31 CG2 VAL I 34 1.82
REMARK 500 OG SER G 32 CD1 ILE G 124 1.83
REMARK 500 CG2 VAL G 35 OD1 ASN G 122 1.93
REMARK 500 N GLY G 34 OD2 ASP G 123 1.96
REMARK 500 SG CYS 1 22 CD CD 1 57 2.07
REMARK 500 CE1 HIS G 54 CE1 TYR I 115 2.11
REMARK 500 CA VAL G 33 OD2 ASP G 123 2.14
REMARK 500 SG CYS 1 19 CD CD 1 57 2.18
REMARK 500 ND1 HIS G 54 CE2 TYR I 115 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 LEU G 53 C HIS G 54 N 0.294
REMARK 500 HIS G 54 CB HIS G 54 CG 0.516
REMARK 500 HIS G 54 C GLY G 55 N -0.349
REMARK 500 LEU I 24 CA LEU I 24 CB 1.908
REMARK 500 LEU I 24 CB LEU I 24 CG 1.006
REMARK 500 LEU I 24 CG LEU I 24 CD1 1.868
REMARK 500 LEU I 24 CG LEU I 24 CD2 2.131
REMARK 500 LEU I 24 C LEU I 24 O 0.318
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 G 01167 O4' - C4' - C3' ANGL. DEV. = -11.4 DEGREES
REMARK 500 G 01167 C5' - C4' - O4' ANGL. DEV. = 5.7 DEGREES
REMARK 500 G 01167 C1' - O4' - C4' ANGL. DEV. = -5.9 DEGREES
REMARK 500 G 01167 N9 - C1' - C2' ANGL. DEV. = 9.5 DEGREES
REMARK 500 A 01174 O4' - C1' - N9 ANGL. DEV. = 4.2 DEGREES
REMARK 500 A 01193 C5' - C4' - C3' ANGL. DEV. = 10.3 DEGREES
REMARK 500 A 01193 C5' - C4' - O4' ANGL. DEV. = 9.1 DEGREES
REMARK 500 A 01193 C2' - C3' - O3' ANGL. DEV. = 10.3 DEGREES
REMARK 500 A 01193 N9 - C1' - C2' ANGL. DEV. = 9.9 DEGREES
REMARK 500 A 01504 C1' - O4' - C4' ANGL. DEV. = -6.0 DEGREES
REMARK 500 A 01504 N9 - C1' - C2' ANGL. DEV. = 9.0 DEGREES
REMARK 500 A 01829 N9 - C1' - C2' ANGL. DEV. = -6.8 DEGREES
REMARK 500 G 01878 N9 - C1' - C2' ANGL. DEV. = -6.8 DEGREES
REMARK 500 G 01979 C2' - C3' - O3' ANGL. DEV. = 10.8 DEGREES
REMARK 500 G 02810 N9 - C1' - C2' ANGL. DEV. = -6.8 DEGREES
REMARK 500 A 9 103 C5' - C4' - O4' ANGL. DEV. = 7.3 DEGREES
REMARK 500 PRO B 159 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 PRO B 252 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 PRO D 137 C - N - CA ANGL. DEV. = 11.0 DEGREES
REMARK 500 TYR G 30 CB - CA - C ANGL. DEV. = 15.1 DEGREES
REMARK 500 GLU G 31 N - CA - CB ANGL. DEV. = 14.3 DEGREES
REMARK 500 ALA G 39 CB - CA - C ANGL. DEV. = -10.2 DEGREES
REMARK 500 ASP G 52 N - CA - C ANGL. DEV. = -19.5 DEGREES
REMARK 500 LEU G 53 CA - C - N ANGL. DEV. = -37.2 DEGREES
REMARK 500 LEU G 53 O - C - N ANGL. DEV. = 17.1 DEGREES
REMARK 500 HIS G 54 CA - C - N ANGL. DEV. = 33.8 DEGREES
REMARK 500 HIS G 54 O - C - N ANGL. DEV. = -32.8 DEGREES
REMARK 500 GLY G 55 C - N - CA ANGL. DEV. = 43.7 DEGREES
REMARK 500 ASN G 82 CB - CA - C ANGL. DEV. = -14.4 DEGREES
REMARK 500 TYR G 84 N - CA - C ANGL. DEV. = 19.0 DEGREES
REMARK 500 VAL G 89 CB - CA - C ANGL. DEV. = 12.0 DEGREES
REMARK 500 LYS G 109 N - CA - C ANGL. DEV. = 16.3 DEGREES
REMARK 500 THR G 110 CB - CA - C ANGL. DEV. = -21.0 DEGREES
REMARK 500 THR G 110 N - CA - C ANGL. DEV. = 35.7 DEGREES
REMARK 500 PRO G 111 N - CA - C ANGL. DEV. = 20.8 DEGREES
REMARK 500 ASP G 123 CB - CA - C ANGL. DEV. = -12.9 DEGREES
REMARK 500 PRO G 127 C - N - CD ANGL. DEV. = -17.5 DEGREES
REMARK 500 LEU I 24 CB - CA - C ANGL. DEV. = -69.3 DEGREES
REMARK 500 LEU I 24 N - CA - CB ANGL. DEV. = 39.7 DEGREES
REMARK 500 LEU I 24 CA - CB - CG ANGL. DEV. = -58.4 DEGREES
REMARK 500 LEU I 24 CD1 - CG - CD2 ANGL. DEV. = -90.3 DEGREES
REMARK 500 LEU I 24 CB - CG - CD1 ANGL. DEV. = -49.6 DEGREES
REMARK 500 LEU I 24 CB - CG - CD2 ANGL. DEV. = -43.7 DEGREES
REMARK 500 PRO I 69 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 PRO N 109 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 PRO R 150 C - N - CA ANGL. DEV. = 10.4 DEGREES
REMARK 500 PRO V 43 C - N - CA ANGL. DEV. = 11.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 19 60.11 -67.72
REMARK 500 ASP A 34 -172.28 162.14
REMARK 500 ASP A 36 -7.63 88.51
REMARK 500 SER A 52 -5.42 64.02
REMARK 500 ASP A 62 15.43 -60.63
REMARK 500 LYS A 117 -49.01 -158.93
REMARK 500 ALA A 119 81.91 57.95
REMARK 500 VAL A 170 -37.84 70.12
REMARK 500 ALA A 181 35.24 -92.95
REMARK 500 PRO A 187 -162.88 -76.89
REMARK 500 HIS A 199 143.07 -177.39
REMARK 500 ASP A 227 90.44 -64.40
REMARK 500 ARG A 232 176.27 167.15
REMARK 500 GLN B 2 87.58 85.10
REMARK 500 SER B 4 175.54 -56.94
REMARK 500 ARG B 5 137.13 171.60
REMARK 500 ARG B 16 81.85 -54.40
REMARK 500 ASP B 33 -85.40 -96.85
REMARK 500 GLN B 39 45.92 -107.07
REMARK 500 PHE B 41 -157.68 -139.82
REMARK 500 GLU B 57 110.12 -33.14
REMARK 500 GLU B 63 125.81 -32.89
REMARK 500 GLU B 67 115.45 -174.10
REMARK 500 THR B 76 57.57 -119.13
REMARK 500 THR B 102 -156.94 -112.95
REMARK 500 ASP B 103 -32.04 -132.89
REMARK 500 SER B 107 -17.61 -43.78
REMARK 500 ASP B 114 75.62 -101.81
REMARK 500 ASP B 139 166.16 -44.20
REMARK 500 LYS B 158 104.87 -55.49
REMARK 500 MET B 162 145.59 -172.22
REMARK 500 GLU B 183 -49.56 -27.40
REMARK 500 ASP B 184 -83.51 -58.68
REMARK 500 ILE B 193 -61.98 -106.39
REMARK 500 THR B 206 160.95 -42.00
REMARK 500 THR B 263 74.31 -108.41
REMARK 500 THR B 279 140.64 -37.19
REMARK 500 PHE B 284 102.31 -58.41
REMARK 500 ASN B 286 12.84 55.89
REMARK 500 TYR B 287 -66.93 -127.99
REMARK 500 ASP B 291 105.44 -169.14
REMARK 500 LYS B 306 -5.29 95.85
REMARK 500 ALA B 314 123.77 -38.29
REMARK 500 LEU B 323 158.00 -44.90
REMARK 500 ASP B 324 75.99 21.30
REMARK 500 SER B 334 152.43 -45.79
REMARK 500 LEU C 8 15.87 -63.37
REMARK 500 ASP C 13 59.77 -141.77
REMARK 500 GLU C 15 138.20 -176.00
REMARK 500 PRO C 19 172.98 -51.27
REMARK 500
REMARK 500 THIS ENTRY HAS 263 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 HIS G 54 GLY G 55 86.18
REMARK 500 ASP G 123 ILE G 124 146.45
REMARK 500 ILE G 126 PRO G 127 120.65
REMARK 500 PRO G 127 GLU G 128 -69.82
REMARK 500 GLU G 128 GLY G 129 127.00
REMARK 500 PRO I 28 VAL I 29 -84.66
REMARK 500 ASP I 30 VAL I 31 119.82
REMARK 500 VAL I 31 GLN I 32 -120.78
REMARK 500 GLN I 32 ALA I 33 126.43
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 A 0 49 0.07 SIDE CHAIN
REMARK 500 G 0 79 0.05 SIDE CHAIN
REMARK 500 G 0 116 0.05 SIDE CHAIN
REMARK 500 A 0 191 0.06 SIDE CHAIN
REMARK 500 G 0 206 0.06 SIDE CHAIN
REMARK 500 G 0 246 0.06 SIDE CHAIN
REMARK 500 U 0 308 0.09 SIDE CHAIN
REMARK 500 G 0 315 0.06 SIDE CHAIN
REMARK 500 A 0 331 0.05 SIDE CHAIN
REMARK 500 A 0 436 0.07 SIDE CHAIN
REMARK 500 A 0 455 0.07 SIDE CHAIN
REMARK 500 G 0 471 0.06 SIDE CHAIN
REMARK 500 G 0 475 0.07 SIDE CHAIN
REMARK 500 G 0 482 0.06 SIDE CHAIN
REMARK 500 A 0 502 0.06 SIDE CHAIN
REMARK 500 G 0 506 0.06 SIDE CHAIN
REMARK 500 G 0 518 0.06 SIDE CHAIN
REMARK 500 A 0 521 0.07 SIDE CHAIN
REMARK 500 G 0 537 0.07 SIDE CHAIN
REMARK 500 G 0 564 0.07 SIDE CHAIN
REMARK 500 U 0 614 0.08 SIDE CHAIN
REMARK 500 U 0 619 0.07 SIDE CHAIN
REMARK 500 U 0 625 0.07 SIDE CHAIN
REMARK 500 U 0 626 0.08 SIDE CHAIN
REMARK 500 C 0 637 0.06 SIDE CHAIN
REMARK 500 A 0 761 0.05 SIDE CHAIN
REMARK 500 C 0 781 0.07 SIDE CHAIN
REMARK 500 A 0 818 0.07 SIDE CHAIN
REMARK 500 U 0 832 0.07 SIDE CHAIN
REMARK 500 A 0 857 0.08 SIDE CHAIN
REMARK 500 U 0 866 0.07 SIDE CHAIN
REMARK 500 A 0 874 0.07 SIDE CHAIN
REMARK 500 U 0 903 0.10 SIDE CHAIN
REMARK 500 U 0 942 0.08 SIDE CHAIN
REMARK 500 G 0 952 0.07 SIDE CHAIN
REMARK 500 G 01027 0.06 SIDE CHAIN
REMARK 500 G 01072 0.06 SIDE CHAIN
REMARK 500 U 01115 0.06 SIDE CHAIN
REMARK 500 G 01167 0.14 SIDE CHAIN
REMARK 500 U 01169 0.07 SIDE CHAIN
REMARK 500 A 01193 0.06 SIDE CHAIN
REMARK 500 U 01198 0.08 SIDE CHAIN
REMARK 500 U 01234 0.08 SIDE CHAIN
REMARK 500 U 01237 0.07 SIDE CHAIN
REMARK 500 A 01261 0.06 SIDE CHAIN
REMARK 500 U 01264 0.07 SIDE CHAIN
REMARK 500 G 01316 0.07 SIDE CHAIN
REMARK 500 G 01323 0.05 SIDE CHAIN
REMARK 500 A 01328 0.06 SIDE CHAIN
REMARK 500 U 01350 0.06 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 96 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LEU G 53 14.15
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 0 1 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 02533 OP2
REMARK 620 2 C 02534 OP2 66.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03037 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 0 40 O2'
REMARK 620 2 C 0 40 O2 118.8
REMARK 620 3 G 0 41 O4' 102.3 117.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03056 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 0 56 O6
REMARK 620 2 A 0 59 N3 70.4
REMARK 620 3 G 0 61 N7 143.7 138.0
REMARK 620 4 G 0 61 O6 93.9 88.3 70.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03052 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 0 130 O2
REMARK 620 2 U 0 146 O4 91.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03058 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 0 141 O4'
REMARK 620 2 C 0 141 O2 58.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03043 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 0 165 OP2
REMARK 620 2 A 0 166 O3' 78.2
REMARK 620 3 A 0 167 OP1 112.6 54.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02963 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 0 196 OP1
REMARK 620 2 C 0 228 O4' 108.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03059 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 0 218 O3'
REMARK 620 2 C 0 218 O2' 56.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03070 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 0 342 O2
REMARK 620 2 SER T 94 OG 61.9
REMARK 620 3 ASN T 95 OD1 159.0 109.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03060 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 0 386 O6
REMARK 620 2 G 0 387 O6 106.1
REMARK 620 3 U 0 402 O4 113.8 84.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03086 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 0 391 O2'
REMARK 620 2 U 0 391 O2 76.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03090 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 0 392 O4
REMARK 620 2 A 0 395 OP1 65.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03095 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 0 415 N3
REMARK 620 2 G 0 416 O4' 107.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03081 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 0 454 OP2
REMARK 620 2 C 0 478 OP1 79.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02926 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 0 456 O6
REMARK 620 2 A 0 459 OP1 88.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03088 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 0 464 O6
REMARK 620 2 G 0 475 OP2 133.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03087 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 0 544 O6
REMARK 620 2 U 0 611 O4 118.9
REMARK 620 3 U 0 612 O4 90.9 69.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03063 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 0 622 N7
REMARK 620 2 U 0 623 O4 92.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03073 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 0 624 O4'
REMARK 620 2 G 0 901 OP1 67.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02924 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 0 627 O6
REMARK 620 2 A 02483 OP1 139.7
REMARK 620 3 C 02534 OP1 77.7 65.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03035 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 0 630 N3
REMARK 620 2 A 0 631 O2' 170.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03097 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 0 633 OP1
REMARK 620 2 U 02539 OP2 133.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 03003 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 0 682 OP2
REMARK 620 2 G 0 683 OP2 107.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03075 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 0 768 O2'
REMARK 620 2 U 0 768 O2 78.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03053 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 0 776 O3'
REMARK 620 2 U 0 777 OP2 51.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02953 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 0 777 OP2
REMARK 620 2 C 0 778 OP2 71.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03089 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 0 814 O6
REMARK 620 2 U 0 815 O4 100.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02965 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 0 816 O6
REMARK 620 2 G 0 817 O6 64.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02928 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 0 822 OP2
REMARK 620 2 G 0 854 OP1 76.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02929 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 0 832 OP2
REMARK 620 2 A 01839 OP1 143.0
REMARK 620 3 A 01840 OP2 110.5 70.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02932 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 0 836 OP1
REMARK 620 2 U 02615 OP1 133.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02937 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 0 844 OP1
REMARK 620 2 A 01689 OP1 169.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02925 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 0 876 OP2
REMARK 620 2 G 0 877 OP2 79.2
REMARK 620 3 A 02624 OP1 87.9 91.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02935 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 0 877 OP1
REMARK 620 2 G 02623 OP1 87.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02994 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 0 880 OP1
REMARK 620 2 U 0 883 OP2 146.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03051 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 0 885 O2'
REMARK 620 2 G 02113 O4' 102.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02930 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 0 919 OP1
REMARK 620 2 C 02464 OP1 163.3
REMARK 620 3 A 02465 OP1 99.2 76.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03080 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 0 922 OP1
REMARK 620 2 A 0 923 O2' 131.4
REMARK 620 3 U 02109 OP2 98.3 129.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03078 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 0 941 O6
REMARK 620 2 U 0 942 O4 59.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03072 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 01043 O3'
REMARK 620 2 C 01044 OP2 55.8
REMARK 620 3 G 01045 OP2 94.8 98.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03032 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 01069 OP2
REMARK 620 2 G 01072 N7 62.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03104 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 01077 N7
REMARK 620 2 A 01079 OP1 80.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 03021 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 01106 OP2
REMARK 620 2 A 01107 OP2 80.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02947 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 01120 OP2
REMARK 620 2 G 01121 OP2 96.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA H 172 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 01133 O3'
REMARK 620 2 A 01133 O2' 61.5
REMARK 620 3 ILE H 157 O 161.3 133.0
REMARK 620 4 PRO H 159 O 89.7 149.8 73.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03076 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 01244 OP2
REMARK 620 2 THR J 47 N 108.0
REMARK 620 3 THR J 47 OG1 55.7 55.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02991 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 01286 OP1
REMARK 620 2 A 01287 OP1 73.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02940 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 01291 OP1
REMARK 620 2 G 01292 OP2 74.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03074 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 01296 OP1
REMARK 620 2 GLY L 14 O 107.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03038 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 01394 O2
REMARK 620 2 U 01432 O4 71.7
REMARK 620 3 U 01724 O2 132.4 78.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02997 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 01420 OP1
REMARK 620 2 C 01421 OP2 81.3
REMARK 620 3 G 01438 OP1 74.5 132.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02950 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 01448 OP2
REMARK 620 2 U 01677 O4 75.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02983 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 01489 OP2
REMARK 620 2 G 01491 O6 139.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02951 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 01503 OP1
REMARK 620 2 C 01679 OP1 79.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03094 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 01576 O6
REMARK 620 2 U 01577 O4 71.4
REMARK 620 3 G 01618 O6 152.9 98.4
REMARK 620 4 G 01619 O6 75.6 90.5 79.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02938 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 01678 OP1
REMARK 620 2 C 01679 OP2 67.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03064 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 01706 O6
REMARK 620 2 G 01707 O6 60.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03067 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 01741 O4
REMARK 620 2 G 02033 O2' 62.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02955 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 01748 OP2
REMARK 620 2 U 01749 O4 73.7
REMARK 620 3 G 02585 OP1 78.2 138.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03055 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 01831 O3'
REMARK 620 2 U 01831 O2' 66.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02927 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 01836 OP1
REMARK 620 2 U 01838 OP1 91.9
REMARK 620 3 A 01839 OP2 136.6 66.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02986 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 01845 OP1
REMARK 620 2 G 01884 O6 110.0
REMARK 620 3 ASN A 188 O 82.0 167.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 241 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 01873 OP2
REMARK 620 2 ASP A 26 OD1 86.0
REMARK 620 3 ASP A 26 OD2 123.5 55.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02978 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 01883 OP1
REMARK 620 2 U 02012 O2' 134.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03061 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 01894 O2
REMARK 620 2 U 01897 O4 72.6
REMARK 620 3 G 01898 O6 93.7 84.9
REMARK 620 4 U 01939 O4 57.2 129.8 98.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03062 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 01896 N7
REMARK 620 2 G 01896 O6 74.1
REMARK 620 3 U 01897 O4 86.2 64.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03054 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 01971 O6
REMARK 620 2 A 02010 OP2 84.2
REMARK 620 3 U 02012 O4 164.4 80.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02966 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 02088 O3'
REMARK 620 2 A 02089 OP1 65.4
REMARK 620 3 GLY R 65 O 93.4 130.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03036 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 02093 N7
REMARK 620 2 G 02093 O6 72.2
REMARK 620 3 G 02094 N7 86.6 92.5
REMARK 620 4 G 02094 O6 147.6 82.0 75.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K 03031 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 02102 O6
REMARK 620 2 G 02482 O6 102.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03083 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 02110 OP2
REMARK 620 2 U 02277 OP1 116.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02972 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 02248 OP1
REMARK 620 2 C 02248 OP2 70.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03066 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 02540 O6
REMARK 620 2 G 02611 O2' 82.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03046 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 02543 N7
REMARK 620 2 G 02544 N7 85.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03101 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 02585 O6
REMARK 620 2 U 02586 O4 79.9
REMARK 620 3 G 02592 O6 105.9 83.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02948 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 02608 OP1
REMARK 620 2 G 02609 OP1 71.7
REMARK 620 3 U 02610 OP2 95.4 97.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03048 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 02611 N7
REMARK 620 2 U 02615 O4 82.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03079 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 02611 OP1
REMARK 620 2 A 02612 OP1 58.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02945 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 02617 OP2
REMARK 620 2 G 02618 OP2 96.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA R 155 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 02659 O3'
REMARK 620 2 VAL R 72 O 113.0
REMARK 620 3 TRP R 75 O 67.0 95.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03065 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 02660 OP1
REMARK 620 2 VAL R 72 O 97.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 03071 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 02663 O2
REMARK 620 2 A 02811 O3' 129.7
REMARK 620 3 A 02811 O2' 171.3 57.3
REMARK 620 4 A 02816 O2' 81.4 90.3 104.7
REMARK 620 5 G 02817 OP2 87.5 142.8 85.6 97.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02970 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 02746 OP2
REMARK 620 2 G 02750 OP2 73.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 02977 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 02757 OP1
REMARK 620 2 ASN B 335 O 92.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 9 123 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 9 56 OP2
REMARK 620 2 A 9 57 OP2 78.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA 9 126 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 9 57 N3
REMARK 620 2 A 9 57 OP2 110.0
REMARK 620 3 C 9 59 N4 117.8 113.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 242 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 201 O
REMARK 620 2 GLY A 202 O 66.6
REMARK 620 3 GLY A 203 O 97.8 64.2
REMARK 620 4 HIS A 208 O 92.7 158.5 115.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 247 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 45 OD1
REMARK 620 2 ASP C 45 OD2 51.2
REMARK 620 3 LYS C 96 O 96.3 86.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA J 146 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL J 61 O
REMARK 620 2 TYR J 69 O 140.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA L 165 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA L 33 O
REMARK 620 2 GLU L 39 OE1 92.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA M 197 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER M 106 OG
REMARK 620 2 PRO M 110 O 150.1
REMARK 620 3 LEU M 112 O 94.5 71.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA Q 96 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP Q 20 O
REMARK 620 2 SER Q 24 OG 143.9
REMARK 620 3 SER Q 46 OG 121.4 82.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA R 156 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLN R 61 O
REMARK 620 2 ASN R 63 OD1 77.3
REMARK 620 3 ASN R 63 ND2 100.0 46.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG T 120 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER T 114 O
REMARK 620 2 ASP T 117 O 85.0
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 0 2932
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 0 2939
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 0 2950
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 0 2966
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 338
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 0 2977
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 0 2978
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 0 2979
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 240
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 0 2986
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 133
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG T 120
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 3 93
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Y 241
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 0 3025
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 0 3027
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K M 196
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA 0 3034
REMARK 800
REMARK 800 SITE_IDENTIFIER: LC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 247
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA H 172
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA S 85
REMARK 800
REMARK 800 SITE_IDENTIFIER: MC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA 0 3045
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA 0 3047
REMARK 800
REMARK 800 SITE_IDENTIFIER: NC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA 0 3049
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA R 155
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA 0 3070
REMARK 800
REMARK 800 SITE_IDENTIFIER: PC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 242
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA J 146
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA M 197
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA Q 96
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA 0 3074
REMARK 800
REMARK 800 SITE_IDENTIFIER: QC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA 0 3076
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA 0 3084
REMARK 800
REMARK 800 SITE_IDENTIFIER: RC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA 0 3086
REMARK 800
REMARK 800 SITE_IDENTIFIER: SC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA 0 3088
REMARK 800
REMARK 800 SITE_IDENTIFIER: SC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA 0 3090
REMARK 800
REMARK 800 SITE_IDENTIFIER: TC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA 0 3099
REMARK 800
REMARK 800 SITE_IDENTIFIER: TC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA L 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: TC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA R 156
REMARK 800
REMARK 800 SITE_IDENTIFIER: UC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD U 67
REMARK 800
REMARK 800 SITE_IDENTIFIER: UC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD 1 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: UC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD Z 93
REMARK 800
REMARK 800 SITE_IDENTIFIER: UC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL J 147
REMARK 800
REMARK 800 SITE_IDENTIFIER: UC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL J 148
REMARK 800
REMARK 800 SITE_IDENTIFIER: UC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL 3 95
REMARK 800
REMARK 800 SITE_IDENTIFIER: UC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL N 187
REMARK 800
REMARK 800 SITE_IDENTIFIER: VC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL Q 97
REMARK 800
REMARK 800 SITE_IDENTIFIER: VC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL K 134
REMARK 800
REMARK 800 SITE_IDENTIFIER: VC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL 0 3108
REMARK 800
REMARK 800 SITE_IDENTIFIER: VC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL 0 3110
REMARK 800
REMARK 800 SITE_IDENTIFIER: VC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL 0 3111
REMARK 800
REMARK 800 SITE_IDENTIFIER: VC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL M 198
REMARK 800
REMARK 800 SITE_IDENTIFIER: VC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 339
REMARK 800
REMARK 800 SITE_IDENTIFIER: WC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL Y 242
REMARK 800
REMARK 800 SITE_IDENTIFIER: WC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL J 149
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUE A 1207 AND RESIDUE C 1208 CHAIN 0 ARE NOT LINKED. DISTANCE
REMARK 999 OF O3'-P BOND IS 2.51A. DISTANCE OF C-N BOND BETWEEN RESIDUE G LEU
REMARK 999 53 AND RESIDUE G HIS 54 IS 1.63A. DISTANCE OF C-N BOND BETWEEN
REMARK 999 RESIDUE G HIS 54 AND RESIDUE G GLY 55 IS 0.99A.
DBREF 2QA4 0 2 2923 GB 3377779 AF034620 2597 5518
DBREF 2QA4 9 1 122 GB 3377779 AF034620 5658 5779
DBREF 2QA4 A 0 239 UNP P20276 RL2_HALMA 1 240
DBREF 2QA4 B 0 337 UNP P20279 RL3_HALMA 1 338
DBREF 2QA4 C 1 246 UNP P12735 RL4_HALMA 1 246
DBREF 2QA4 D 0 176 UNP P14124 RL5_HALMA 1 177
DBREF 2QA4 E 0 177 UNP P14135 RL6_HALMA 1 178
DBREF 2QA4 F 0 119 UNP P12743 RL7A_HALMA 1 120
DBREF 2QA4 G 1 348 UNP P15825 RLA0_HALMA 1 348
DBREF 2QA4 H 1 171 UNP P60617 RL10_HALMA 4 177
DBREF 2QA4 I 1 162 UNP P14122 RL11_HALMA 1 162
DBREF 2QA4 J 1 145 UNP P29198 RL13_HALMA 1 145
DBREF 2QA4 K 1 132 UNP P22450 RL14_HALMA 1 132
DBREF 2QA4 L 0 164 UNP P12737 RL15_HALMA 1 165
DBREF 2QA4 M 0 195 UNP P60618 RL15E_HALMA 1 196
DBREF 2QA4 N 0 186 UNP P14123 RL18_HALMA 1 187
DBREF 2QA4 O 0 115 UNP P12733 RL18E_HALMA 1 116
DBREF 2QA4 P 0 148 UNP P14119 RL19_HALMA 1 149
DBREF 2QA4 Q 0 95 UNP P12734 RL21_HALMA 1 96
DBREF 2QA4 R 0 154 UNP P10970 RL22_HALMA 1 155
DBREF 2QA4 S 0 84 UNP P12732 RL23_HALMA 1 85
DBREF 2QA4 T 0 119 UNP P10972 RL24_HALMA 1 120
DBREF 2QA4 U 0 66 UNP P14116 RL24E_HALMA 1 67
DBREF 2QA4 V 0 70 UNP P10971 RL29_HALMA 1 71
DBREF 2QA4 W 1 154 UNP P14121 RL30_HALMA 1 154
DBREF 2QA4 X 0 91 UNP P18138 RL31_HALMA 1 92
DBREF 2QA4 Y 0 240 UNP P12736 RL32_HALMA 1 241
DBREF 2QA4 Z 1 92 UNP P60619 RL37A_HALMA 1 92
DBREF 2QA4 1 0 56 UNP P32410 RL37_HALMA 1 57
DBREF 2QA4 2 0 49 UNP P22452 RL39_HALMA 1 50
DBREF 2QA4 3 1 92 UNP P32411 RL44_HALMA 1 92
SEQADV 2QA4 C 0 560 GB 3377779 U 3155 CONFLICT
SEQADV 2QA4 LEU C 73 UNP P12735 GLN 73 CONFLICT
SEQADV 2QA4 ASP G 248 UNP P15825 ALA 248 CONFLICT
SEQADV 2QA4 ASP H 164 UNP P60617 INSERTION
SEQADV 2QA4 SER H 165 UNP P60617 LYS 167 CONFLICT
SEQADV 2QA4 SER H 166 UNP P60617 VAL 168 CONFLICT
SEQADV 2QA4 PRO H 167 UNP P60617 GLU 169 CONFLICT
SEQADV 2QA4 ALA H 168 UNP P60617 ARG 170 CONFLICT
SEQADV 2QA4 H UNP P60617 GLU 172 DELETION
SEQADV 2QA4 H UNP P60617 GLU 173 DELETION
SEQADV 2QA4 H UNP P60617 LEU 174 DELETION
SEQADV 2QA4 H UNP P60617 LEU 175 DELETION
SEQADV 2QA4 ASN H 170 UNP P60617 ILE 176 CONFLICT
SEQADV 2QA4 LEU K 44 UNP P22450 HIS 44 CONFLICT
SEQADV 2QA4 GLU M 13 UNP P60618 LYS 14 CONFLICT
SEQADV 2QA4 ALA M 194 UNP P60618 GLY 195 CONFLICT
SEQADV 2QA4 ARG Z 10 UNP P60619 SER 10 CONFLICT
SEQRES 1 0 2922 U U G G C U A C U A U G C
SEQRES 2 0 2922 C A G C U G G U G G A U U
SEQRES 3 0 2922 G C U C G G C U C A G G C
SEQRES 4 0 2922 G C U G A U G A A G G A C
SEQRES 5 0 2922 G U G C C A A G C U G C G
SEQRES 6 0 2922 A U A A G C C A U G G G G
SEQRES 7 0 2922 A G C C G C A C G G A G G
SEQRES 8 0 2922 C G A A G A A C C A U G G
SEQRES 9 0 2922 A U U U C C G A A U G A G
SEQRES 10 0 2922 A A U C U C U C U A A C A
SEQRES 11 0 2922 A U U G C U U C G C G C A
SEQRES 12 0 2922 A U G A G G A A C C C C G
SEQRES 13 0 2922 A G A A C U G A A A C A U
SEQRES 14 0 2922 C U C A G U A U C G G G A
SEQRES 15 0 2922 G G A A C A G A A A A C G
SEQRES 16 0 2922 C A A U G U G A U G U C G
SEQRES 17 0 2922 U U A G U A A C C G C G A
SEQRES 18 0 2922 G U G A A C G C G A U A C
SEQRES 19 0 2922 A G C C C A A A C C G A A
SEQRES 20 0 2922 G C C C U C A C G G G C A
SEQRES 21 0 2922 A U G U G G U G U C A G G
SEQRES 22 0 2922 G C U A C C U C U C A U C
SEQRES 23 0 2922 A G C C G A C C G U C U C
SEQRES 24 0 2922 G A C G A A G U C U C U U
SEQRES 25 0 2922 G G A A C A G A G C G U G
SEQRES 26 0 2922 A U A C A G G G U G A C A
SEQRES 27 0 2922 A C C C C G U A C U C G A
SEQRES 28 0 2922 G A C C A G U A C G A C G
SEQRES 29 0 2922 U G C G G U A G U G C C A
SEQRES 30 0 2922 G A G U A G C G G G G G U
SEQRES 31 0 2922 U G G A U A U C C C U C G
SEQRES 32 0 2922 C G A A U A A C G C A G G
SEQRES 33 0 2922 C A U C G A C U G C G A A
SEQRES 34 0 2922 G G C U A A A C A C A A C
SEQRES 35 0 2922 C U G A G A C C G A U A G
SEQRES 36 0 2922 U G A A C A A G U A G U G
SEQRES 37 0 2922 U G A A C G A A C G C U G
SEQRES 38 0 2922 C A A A G U A C C C U C A
SEQRES 39 0 2922 G A A G G G A G G C G A A
SEQRES 40 0 2922 A U A G A G C A U G A A A
SEQRES 41 0 2922 U C A G U U G G C G A U C
SEQRES 42 0 2922 G A G C G A C A G G G C A
SEQRES 43 0 2922 U A C A A G G U C C C U C
SEQRES 44 0 2922 G A C G A A U G A C C G A
SEQRES 45 0 2922 C G C G C G A G C G U C C
SEQRES 46 0 2922 A G U A A G A C U C A C G
SEQRES 47 0 2922 G G A A G C C G A U G U U
SEQRES 48 0 2922 C U G U C G U A C G U U U
SEQRES 49 0 2922 U G A A A A A C G A G C C
SEQRES 50 0 2922 A G G G A G U G U G U C U
SEQRES 51 0 2922 G C A U G G C A A G U C U
SEQRES 52 0 2922 A A C C G G A G U A U C C
SEQRES 53 0 2922 G G G G A G G C A C A G G
SEQRES 54 0 2922 G A A A C C G A C A U G G
SEQRES 55 0 2922 C C G C A G G G C U U U G
SEQRES 56 0 2922 C C C G A G G G C C G C C
SEQRES 57 0 2922 G U C U U C A A G G G C G
SEQRES 58 0 2922 G G G A G C C A U G U G G
SEQRES 59 0 2922 A C A C G A C C C G A A U
SEQRES 60 0 2922 C C G G A C G A U C U A C
SEQRES 61 0 2922 G C A U G G A C A A G A U
SEQRES 62 0 2922 G A A G C G U G C C G A A
SEQRES 63 0 2922 A G G C A C G U G G A A G
SEQRES 64 0 2922 U C U G U U A G A G U U G
SEQRES 65 0 2922 G U G U C C U A C A A U A
SEQRES 66 0 2922 C C C U C U C G U G A U C
SEQRES 67 0 2922 U A U G U G U A G G G G U
SEQRES 68 0 2922 G A A A G G C C C A U C G
SEQRES 69 0 2922 A G U C C G G C A A C A G
SEQRES 70 0 2922 C U G G U U C C A A U C G
SEQRES 71 0 2922 A A A C A U G U C G A A G
SEQRES 72 0 2922 C A U G A C C U C C G C C
SEQRES 73 0 2922 G A G G U A G U C U G U G
SEQRES 74 0 2922 A G G U A G A G C G A C C
SEQRES 75 0 2922 G A U U G G U G U G U C C
SEQRES 76 0 2922 G C C U C C G A G A G G A
SEQRES 77 0 2922 G U C G G C A C A C C U G
SEQRES 78 0 2922 U C A A A C U C C A A A C
SEQRES 79 0 2922 U U A C A G A C G C C G U
SEQRES 80 0 2922 U U G A C G C G G G G A U
SEQRES 81 0 2922 U C C G G U G C G C G G G
SEQRES 82 0 2922 G U A A G C C U G U G U A
SEQRES 83 0 2922 C C A G G A G G G G A A C
SEQRES 84 0 2922 A A C C C A G A G A U A G
SEQRES 85 0 2922 G U U A A G G U C C C C A
SEQRES 86 0 2922 A G U G U G G A U U A A G
SEQRES 87 0 2922 U G U A A U C C U C U G A
SEQRES 88 0 2922 A G G U G G U C U C G A G
SEQRES 89 0 2922 C C C U A G A C A G C C G
SEQRES 90 0 2922 G G A G G U G A G C U U A
SEQRES 91 0 2922 G A A G C A G C U A C C C
SEQRES 92 0 2922 U C U A A G A A A A G C G
SEQRES 93 0 2922 U A A C A G C U U A C C G
SEQRES 94 0 2922 G C C G A G G U U U G A G
SEQRES 95 0 2922 G C G C C C A A A A U G A
SEQRES 96 0 2922 U C G G G A C U C A A A U
SEQRES 97 0 2922 C C A C C A C C G A G A C
SEQRES 98 0 2922 C U G U C C G U A C C A C
SEQRES 99 0 2922 U C A U A C U G G U A A U
SEQRES 100 0 2922 C G A G U A G A U U G G C
SEQRES 101 0 2922 G C U C U A A U U G G A U
SEQRES 102 0 2922 G G A A G U A G G G G U G
SEQRES 103 0 2922 A A A A C U C C U A U G G
SEQRES 104 0 2922 A C C G A U U A G U G A C
SEQRES 105 0 2922 G A A A A U C C U G G C C
SEQRES 106 0 2922 A U A G U A G C A G C G A
SEQRES 107 0 2922 U A G U C G G G U G A G A
SEQRES 108 0 2922 A C C C C G A C G G C C U
SEQRES 109 0 2922 A A U G G A U A A G G G U
SEQRES 110 0 2922 U C C U C A G C A C U G C
SEQRES 111 0 2922 U G A U C A G C U G A G G
SEQRES 112 0 2922 G U U A G C C G G U C C U
SEQRES 113 0 2922 A A G U C A U A C C G C A
SEQRES 114 0 2922 A C U C G A C U A U G A C
SEQRES 115 0 2922 G A A A U G G G A A A C G
SEQRES 116 0 2922 G G U U A A U A U U C C C
SEQRES 117 0 2922 G U G C C A C U A U G C A
SEQRES 118 0 2922 G U G A A A G U U G A C G
SEQRES 119 0 2922 C C C U G G G G U C G A U
SEQRES 120 0 2922 C A C G C U G G G C A U U
SEQRES 121 0 2922 C G C C C A G U C G A A C
SEQRES 122 0 2922 C G U C C A A C U C C G U
SEQRES 123 0 2922 G G A A G C C G U A A U G
SEQRES 124 0 2922 G C A G G A A G C G G A C
SEQRES 125 0 2922 G A A C G G C G G C A U A
SEQRES 126 0 2922 G G G A A A C G U G A U U
SEQRES 127 0 2922 C A A C C U G G G G C C C
SEQRES 128 0 2922 A U G A A A A G A C G A G
SEQRES 129 0 2922 C A U A G U G U C C G U A
SEQRES 130 0 2922 C C G A G A A C C G A C A
SEQRES 131 0 2922 C A G G U G U C C A U G G
SEQRES 132 0 2922 C G G C G A A A G C C A A
SEQRES 133 0 2922 G G C C U G U C G G G A G
SEQRES 134 0 2922 C A A C C A A C G U U A G
SEQRES 135 0 2922 G G A A U U C G G C A A G
SEQRES 136 0 2922 U U A G U C C C G U A C C
SEQRES 137 0 2922 U U C G G A A G A A G G G
SEQRES 138 0 2922 A U G C C U G C U C C G G
SEQRES 139 0 2922 A A C G G A G C A G G U C
SEQRES 140 0 2922 G C A G U G A C U C G G A
SEQRES 141 0 2922 A G C U C G G A C U G U C
SEQRES 142 0 2922 U A G U A A C A A C A U A
SEQRES 143 0 2922 G G U G A C C G C A A A U
SEQRES 144 0 2922 C C G C A A G G A C U C G
SEQRES 145 0 2922 U A C G G U C A C U G A A
SEQRES 146 0 2922 U C C U G C C C A G U G C
SEQRES 147 0 2922 A G G U A U C U G A A C A
SEQRES 148 0 2922 C C U C G U A C A A G A G
SEQRES 149 0 2922 G A C G A A G G A C C U G
SEQRES 150 0 2922 U C A A C G G C G G G G G
SEQRES 151 0 2922 U A A C U A U G A C C C U
SEQRES 152 0 2922 C U U A A G G U A G C G U
SEQRES 153 0 2922 A G U A C C U U G C C G C
SEQRES 154 0 2922 A U C A G U A G C G G C U
SEQRES 155 0 2922 U G C A U G A A U G G A U
SEQRES 156 0 2922 U A A C C A G A G C U U C
SEQRES 157 0 2922 A C U G U C C C A A C G U
SEQRES 158 0 2922 U G G G C C C G G U G A A
SEQRES 159 0 2922 C U G U A C A U U C C A G
SEQRES 160 0 2922 U G C G G A G U C U G G A
SEQRES 161 0 2922 G A C A C C C A G G G G G
SEQRES 162 0 2922 A A G C G A A G A C C C U
SEQRES 163 0 2922 A U G G A G C U U U A C U
SEQRES 164 0 2922 G C A G G C U G U C G C U
SEQRES 165 0 2922 G A G A C G U G G U C G C
SEQRES 166 0 2922 C G A U G U G C A G C A U
SEQRES 167 0 2922 A G G U A G G A G A C A C
SEQRES 168 0 2922 U A C A C A G G U A C C C
SEQRES 169 0 2922 G C G C U A G C G G G C C
SEQRES 170 0 2922 A C C G A G U C A A C A G
SEQRES 171 0 2922 U G A A A U A C U A C C C
SEQRES 172 0 2922 G U C G G U G A C U G C G
SEQRES 173 0 2922 A C U C U C A C U C C G G
SEQRES 174 0 2922 G A G G A G G A C A C C G
SEQRES 175 0 2922 A U A G C C G G G C A G U
SEQRES 176 0 2922 U U G A C U G G G G C G G
SEQRES 177 0 2922 U A C G C G C U C G A A A
SEQRES 178 0 2922 A G A U A U C G A G C G C
SEQRES 179 0 2922 G C C C U A U G G C U A U
SEQRES 180 0 2922 C U C A G C C G G G A C A
SEQRES 181 0 2922 G A G A C C C G G C G A A
SEQRES 182 0 2922 G A G U G C A A G A G C A
SEQRES 183 0 2922 A A A G A U A G C U U G A
SEQRES 184 0 2922 C A G U G U U C U U C C C
SEQRES 185 0 2922 A A C G A G G A A C G C U
SEQRES 186 0 2922 G A C G C G A A A G C G U
SEQRES 187 0 2922 G G U C U A G C G A A C C
SEQRES 188 0 2922 A A U U A G C C U G C U U
SEQRES 189 0 2922 G A U G C G G G C A A U U
SEQRES 190 0 2922 G A U G A C A G A A A A G
SEQRES 191 0 2922 C U A C C C U A G G G A U
SEQRES 192 0 2922 A A C A G A G U C G U C A
SEQRES 193 0 2922 C U C G C A A G A G C A C
SEQRES 194 0 2922 A U A U C G A C C G A G U
SEQRES 195 0 2922 G G C U U G C U A C C U C
SEQRES 196 0 2922 G A U G U C G G U U C C C
SEQRES 197 0 2922 U C C A U C C U G C C C G
SEQRES 198 0 2922 U G C A G A A G C G G G C
SEQRES 199 0 2922 A A G G G U G A G G U OMU OMG
SEQRES 200 0 2922 U U C G C C U A U U A A A
SEQRES 201 0 2922 G G A G G U C G U G A G C
SEQRES 202 0 2922 U G G G UR3 U PSU A G A C C G
SEQRES 203 0 2922 U C G U G A G A C A G G U
SEQRES 204 0 2922 C G G C U G C U A U C U A
SEQRES 205 0 2922 C U G G G U G U G U A A U
SEQRES 206 0 2922 G G U G U C U G A C A A G
SEQRES 207 0 2922 A A C G A C C G U A U A G
SEQRES 208 0 2922 U A C G A G A G G A A C U
SEQRES 209 0 2922 A C G G U U G G U G G C C
SEQRES 210 0 2922 A C U G G U G U A C C G G
SEQRES 211 0 2922 U U G U U C G A G A G A G
SEQRES 212 0 2922 C A C G U G C C G G G U A
SEQRES 213 0 2922 G C C A C G C C A C A C G
SEQRES 214 0 2922 G G G U A A G A G C U G A
SEQRES 215 0 2922 A C G C A U C U A A G C U
SEQRES 216 0 2922 C G A A A C C C A C U U G
SEQRES 217 0 2922 G A A A A G A G A C A C C
SEQRES 218 0 2922 G C C G A G G U C C C G C
SEQRES 219 0 2922 G U A C A A G A C G C G G
SEQRES 220 0 2922 U C G A U A G A C U C G G
SEQRES 221 0 2922 G G U G U G C G C G U C G
SEQRES 222 0 2922 A G G U A A C G A G A C G
SEQRES 223 0 2922 U U A A G C C C A C G A G
SEQRES 224 0 2922 C A C U A A C A G A C C A
SEQRES 225 0 2922 A A G C C A U C A U
SEQRES 1 9 122 U U A G G C G G C C A C A
SEQRES 2 9 122 G C G G U G G G G U U G C
SEQRES 3 9 122 C U C C C G U A C C C A U
SEQRES 4 9 122 C C C G A A C A C G G A A
SEQRES 5 9 122 G A U A A G C C C A C C A
SEQRES 6 9 122 G C G U U C C G G G G A G
SEQRES 7 9 122 U A C U G G A G U G C G C
SEQRES 8 9 122 G A G C C U C U G G G A A
SEQRES 9 9 122 A C C C G G U U C G C C G
SEQRES 10 9 122 C C A C C
SEQRES 1 A 240 MET GLY ARG ARG ILE GLN GLY GLN ARG ARG GLY ARG GLY
SEQRES 2 A 240 THR SER THR PHE ARG ALA PRO SER HIS ARG TYR LYS ALA
SEQRES 3 A 240 ASP LEU GLU HIS ARG LYS VAL GLU ASP GLY ASP VAL ILE
SEQRES 4 A 240 ALA GLY THR VAL VAL ASP ILE GLU HIS ASP PRO ALA ARG
SEQRES 5 A 240 SER ALA PRO VAL ALA ALA VAL GLU PHE GLU ASP GLY ASP
SEQRES 6 A 240 ARG ARG LEU ILE LEU ALA PRO GLU GLY VAL GLY VAL GLY
SEQRES 7 A 240 ASP GLU LEU GLN VAL GLY VAL SER ALA GLU ILE ALA PRO
SEQRES 8 A 240 GLY ASN THR LEU PRO LEU ALA GLU ILE PRO GLU GLY VAL
SEQRES 9 A 240 PRO VAL CYS ASN VAL GLU SER SER PRO GLY ASP GLY GLY
SEQRES 10 A 240 LYS PHE ALA ARG ALA SER GLY VAL ASN ALA GLN LEU LEU
SEQRES 11 A 240 THR HIS ASP ARG ASN VAL ALA VAL VAL LYS LEU PRO SER
SEQRES 12 A 240 GLY GLU MET LYS ARG LEU ASP PRO GLN CYS ARG ALA THR
SEQRES 13 A 240 ILE GLY VAL VAL ALA GLY GLY GLY ARG THR ASP LYS PRO
SEQRES 14 A 240 PHE VAL LYS ALA GLY ASN LYS HIS HIS LYS MET LYS ALA
SEQRES 15 A 240 ARG GLY THR LYS TRP PRO ASN VAL ARG GLY VAL ALA MET
SEQRES 16 A 240 ASN ALA VAL ASP HIS PRO PHE GLY GLY GLY GLY ARG GLN
SEQRES 17 A 240 HIS PRO GLY LYS PRO LYS SER ILE SER ARG ASN ALA PRO
SEQRES 18 A 240 PRO GLY ARG LYS VAL GLY ASP ILE ALA SER LYS ARG THR
SEQRES 19 A 240 GLY ARG GLY GLY ASN GLU
SEQRES 1 B 338 MET PRO GLN PRO SER ARG PRO ARG LYS GLY SER LEU GLY
SEQRES 2 B 338 PHE GLY PRO ARG LYS ARG SER THR SER GLU THR PRO ARG
SEQRES 3 B 338 PHE ASN SER TRP PRO SER ASP ASP GLY GLN PRO GLY VAL
SEQRES 4 B 338 GLN GLY PHE ALA GLY TYR LYS ALA GLY MET THR HIS VAL
SEQRES 5 B 338 VAL LEU VAL ASN ASP GLU PRO ASN SER PRO ARG GLU GLY
SEQRES 6 B 338 MET GLU GLU THR VAL PRO VAL THR VAL ILE GLU THR PRO
SEQRES 7 B 338 PRO MET ARG ALA VAL ALA LEU ARG ALA TYR GLU ASP THR
SEQRES 8 B 338 PRO TYR GLY GLN ARG PRO LEU THR GLU VAL TRP THR ASP
SEQRES 9 B 338 GLU PHE HIS SER GLU LEU ASP ARG THR LEU ASP VAL PRO
SEQRES 10 B 338 GLU ASP HIS ASP PRO ASP ALA ALA GLU GLU GLN ILE ARG
SEQRES 11 B 338 ASP ALA HIS GLU ALA GLY ASP LEU GLY ASP LEU ARG LEU
SEQRES 12 B 338 ILE THR HIS THR VAL PRO ASP ALA VAL PRO SER VAL PRO
SEQRES 13 B 338 LYS LYS LYS PRO ASP VAL MET GLU THR ARG VAL GLY GLY
SEQRES 14 B 338 GLY SER VAL SER ASP ARG LEU ASP HIS ALA LEU ASP ILE
SEQRES 15 B 338 VAL GLU ASP GLY GLY GLU HIS ALA MET ASN ASP ILE PHE
SEQRES 16 B 338 ARG ALA GLY GLU TYR ALA ASP VAL ALA GLY VAL THR LYS
SEQRES 17 B 338 GLY LYS GLY THR GLN GLY PRO VAL LYS ARG TRP GLY VAL
SEQRES 18 B 338 GLN LYS ARG LYS GLY LYS HIS ALA ARG GLN GLY TRP ARG
SEQRES 19 B 338 ARG ARG ILE GLY ASN LEU GLY PRO TRP ASN PRO SER ARG
SEQRES 20 B 338 VAL ARG SER THR VAL PRO GLN GLN GLY GLN THR GLY TYR
SEQRES 21 B 338 HIS GLN ARG THR GLU LEU ASN LYS ARG LEU ILE ASP ILE
SEQRES 22 B 338 GLY GLU GLY ASP GLU PRO THR VAL ASP GLY GLY PHE VAL
SEQRES 23 B 338 ASN TYR GLY GLU VAL ASP GLY PRO TYR THR LEU VAL LYS
SEQRES 24 B 338 GLY SER VAL PRO GLY PRO ASP LYS ARG LEU VAL ARG PHE
SEQRES 25 B 338 ARG PRO ALA VAL ARG PRO ASN ASP GLN PRO ARG LEU ASP
SEQRES 26 B 338 PRO GLU VAL ARG TYR VAL SER ASN GLU SER ASN GLN GLY
SEQRES 1 C 246 MET GLN ALA THR ILE TYR ASP LEU ASP GLY ASN THR ASP
SEQRES 2 C 246 GLY GLU VAL ASP LEU PRO ASP VAL PHE GLU THR PRO VAL
SEQRES 3 C 246 ARG SER ASP LEU ILE GLY LYS ALA VAL ARG ALA ALA GLN
SEQRES 4 C 246 ALA ASN ARG LYS GLN ASP TYR GLY SER ASP GLU TYR ALA
SEQRES 5 C 246 GLY LEU ARG THR PRO ALA GLU SER PHE GLY SER GLY ARG
SEQRES 6 C 246 GLY GLN ALA HIS VAL PRO LYS LEU ASP GLY ARG ALA ARG
SEQRES 7 C 246 ARG VAL PRO GLN ALA VAL LYS GLY ARG SER ALA HIS PRO
SEQRES 8 C 246 PRO LYS THR GLU LYS ASP ARG SER LEU ASP LEU ASN ASP
SEQRES 9 C 246 LYS GLU ARG GLN LEU ALA VAL ARG SER ALA LEU ALA ALA
SEQRES 10 C 246 THR ALA ASP ALA ASP LEU VAL ALA ASP ARG GLY HIS GLU
SEQRES 11 C 246 PHE ASP ARG ASP GLU VAL PRO VAL VAL VAL SER ASP ASP
SEQRES 12 C 246 PHE GLU ASP LEU VAL LYS THR GLN GLU VAL VAL SER LEU
SEQRES 13 C 246 LEU GLU ALA LEU ASP VAL HIS ALA ASP ILE ASP ARG ALA
SEQRES 14 C 246 ASP GLU THR LYS ILE LYS ALA GLY GLN GLY SER ALA ARG
SEQRES 15 C 246 GLY ARG LYS TYR ARG ARG PRO ALA SER ILE LEU PHE VAL
SEQRES 16 C 246 THR SER ASP GLU PRO SER THR ALA ALA ARG ASN LEU ALA
SEQRES 17 C 246 GLY ALA ASP VAL ALA THR ALA SER GLU VAL ASN THR GLU
SEQRES 18 C 246 ASP LEU ALA PRO GLY GLY ALA PRO GLY ARG LEU THR VAL
SEQRES 19 C 246 PHE THR GLU SER ALA LEU ALA GLU VAL ALA GLU ARG
SEQRES 1 D 177 MET SER SER GLU SER GLU SER GLY GLY ASP PHE HIS GLU
SEQRES 2 D 177 MET ARG GLU PRO ARG ILE GLU LYS VAL VAL VAL HIS MET
SEQRES 3 D 177 GLY ILE GLY HIS GLY GLY ARG ASP LEU ALA ASN ALA GLU
SEQRES 4 D 177 ASP ILE LEU GLY GLU ILE THR GLY GLN MET PRO VAL ARG
SEQRES 5 D 177 THR LYS ALA LYS ARG THR VAL GLY GLU PHE ASP ILE ARG
SEQRES 6 D 177 GLU GLY ASP PRO ILE GLY ALA LYS VAL THR LEU ARG ASP
SEQRES 7 D 177 GLU MET ALA GLU GLU PHE LEU GLN THR ALA LEU PRO LEU
SEQRES 8 D 177 ALA GLU LEU ALA THR SER GLN PHE ASP ASP THR GLY ASN
SEQRES 9 D 177 PHE SER PHE GLY VAL GLU GLU HIS THR GLU PHE PRO SER
SEQRES 10 D 177 GLN GLU TYR ASP PRO SER ILE GLY ILE TYR GLY LEU ASP
SEQRES 11 D 177 VAL THR VAL ASN LEU VAL ARG PRO GLY TYR ARG VAL ALA
SEQRES 12 D 177 LYS ARG ASP LYS ALA SER ARG SER ILE PRO THR LYS HIS
SEQRES 13 D 177 ARG LEU ASN PRO ALA ASP ALA VAL ALA PHE ILE GLU SER
SEQRES 14 D 177 THR TYR ASP VAL GLU VAL SER GLU
SEQRES 1 E 178 MET PRO ARG VAL GLU LEU GLU ILE PRO GLU ASP VAL ASP
SEQRES 2 E 178 ALA GLU GLN ASP HIS LEU ASP ILE THR VAL GLU GLY ASP
SEQRES 3 E 178 ASN GLY SER VAL THR ARG ARG LEU TRP TYR PRO ASP ILE
SEQRES 4 E 178 ASP VAL SER VAL ASP GLY ASP THR VAL VAL ILE GLU SER
SEQRES 5 E 178 ASP GLU ASP ASN ALA LYS THR MET SER THR ILE GLY THR
SEQRES 6 E 178 PHE GLN SER HIS ILE GLU ASN MET PHE HIS GLY VAL THR
SEQRES 7 E 178 GLU GLY TRP GLU TYR GLY MET GLU VAL PHE TYR SER HIS
SEQRES 8 E 178 PHE PRO MET GLN VAL ASN VAL GLU GLY ASP GLU VAL VAL
SEQRES 9 E 178 ILE GLU ASN PHE LEU GLY GLU LYS ALA PRO ARG ARG THR
SEQRES 10 E 178 THR ILE HIS GLY ASP THR ASP VAL GLU ILE ASP GLY GLU
SEQRES 11 E 178 GLU LEU THR VAL SER GLY PRO ASP ILE GLU ALA VAL GLY
SEQRES 12 E 178 GLN THR ALA ALA ASP ILE GLU GLN LEU THR ARG ILE ASN
SEQRES 13 E 178 ASP LYS ASP VAL ARG VAL PHE GLN ASP GLY VAL TYR ILE
SEQRES 14 E 178 THR ARG LYS PRO ASN ARG GLY ASP ALA
SEQRES 1 F 120 MET PRO VAL TYR VAL ASP PHE ASP VAL PRO ALA ASP LEU
SEQRES 2 F 120 GLU ASP ASP ALA LEU GLU ALA LEU GLU VAL ALA ARG ASP
SEQRES 3 F 120 THR GLY ALA VAL LYS LYS GLY THR ASN GLU THR THR LYS
SEQRES 4 F 120 SER ILE GLU ARG GLY SER ALA GLU LEU VAL PHE VAL ALA
SEQRES 5 F 120 GLU ASP VAL GLN PRO GLU GLU ILE VAL MET HIS ILE PRO
SEQRES 6 F 120 GLU LEU ALA ASP GLU LYS GLY VAL PRO PHE ILE PHE VAL
SEQRES 7 F 120 GLU GLN GLN ASP ASP LEU GLY HIS ALA ALA GLY LEU GLU
SEQRES 8 F 120 VAL GLY SER ALA ALA ALA ALA VAL THR ASP ALA GLY GLU
SEQRES 9 F 120 ALA ASP ALA ASP VAL GLU ASP ILE ALA ASP LYS VAL GLU
SEQRES 10 F 120 GLU LEU ARG
SEQRES 1 G 348 MET SER ALA GLU SER GLU ARG LYS THR GLU THR ILE PRO
SEQRES 2 G 348 GLU TRP LYS GLN GLU GLU VAL ASP ALA ILE VAL GLU MET
SEQRES 3 G 348 ILE GLU SER TYR GLU SER VAL GLY VAL VAL ASN ILE ALA
SEQRES 4 G 348 GLY ILE PRO SER ARG GLN LEU GLN ASP MET ARG ARG ASP
SEQRES 5 G 348 LEU HIS GLY THR ALA GLU LEU ARG VAL SER ARG ASN THR
SEQRES 6 G 348 LEU LEU GLU ARG ALA LEU ASP ASP VAL ASP ASP GLY LEU
SEQRES 7 G 348 GLU ASP LEU ASN GLY TYR ILE THR GLY GLN VAL GLY LEU
SEQRES 8 G 348 ILE GLY THR ASP ASP ASN PRO PHE SER LEU PHE GLN GLU
SEQRES 9 G 348 LEU GLU ALA SER LYS THR PRO ALA PRO ILE GLY ALA GLY
SEQRES 10 G 348 GLU VAL ALA PRO ASN ASP ILE VAL ILE PRO GLU GLY ASP
SEQRES 11 G 348 THR GLY VAL ASP PRO GLY PRO PHE VAL GLY GLU LEU GLN
SEQRES 12 G 348 SER VAL GLY ALA ASP ALA ARG ILE GLN GLU GLY SER ILE
SEQRES 13 G 348 GLN VAL LEU SER ASP SER THR VAL LEU ASP THR GLY GLU
SEQRES 14 G 348 GLU VAL SER GLN GLU LEU SER ASN VAL LEU ASN GLU LEU
SEQRES 15 G 348 GLY ILE GLU PRO LYS GLU VAL GLY LEU ASP LEU ARG ALA
SEQRES 16 G 348 VAL PHE ALA ASP GLY VAL LEU PHE GLU PRO GLU GLU LEU
SEQRES 17 G 348 GLU LEU ASP ILE ASP GLU TYR ARG SER ASP ILE GLN ALA
SEQRES 18 G 348 ALA ALA GLY ARG ALA PHE ASN LEU SER VAL ASN ALA ASP
SEQRES 19 G 348 TYR PRO THR ALA THR THR ALA PRO THR MET LEU GLN SER
SEQRES 20 G 348 ASP ARG GLY ASN ALA LYS SER LEU ALA LEU GLN ALA ALA
SEQRES 21 G 348 ILE GLU ASP PRO GLU VAL VAL PRO ASP LEU VAL SER LYS
SEQRES 22 G 348 ALA ASP ALA GLN VAL ARG ALA LEU ALA SER GLN ILE ASP
SEQRES 23 G 348 ASP GLU GLU ALA LEU PRO GLU GLU LEU GLN GLY VAL GLU
SEQRES 24 G 348 ALA ASP VAL ALA THR GLU GLU PRO THR ASP ASP GLN ASP
SEQRES 25 G 348 ASP ASP THR ALA SER GLU ASP ASP ALA ASP ALA ASP ASP
SEQRES 26 G 348 ALA ALA GLU GLU ALA ASP ASP ASP ASP ASP ASP ASP GLU
SEQRES 27 G 348 ASP ALA GLY ASP ALA LEU GLY ALA MET PHE
SEQRES 1 H 171 LYS PRO ALA SER MET TYR ARG ASP ILE ASP LYS PRO ALA
SEQRES 2 H 171 TYR THR ARG ARG GLU TYR ILE THR GLY ILE PRO GLY SER
SEQRES 3 H 171 LYS ILE ALA GLN HIS LYS MET GLY ARG LYS GLN LYS ASP
SEQRES 4 H 171 ALA ASP ASP TYR PRO VAL GLN ILE SER LEU ILE VAL GLU
SEQRES 5 H 171 GLU THR VAL GLN LEU ARG HIS GLY SER LEU GLU ALA SER
SEQRES 6 H 171 ARG LEU SER ALA ASN ARG HIS LEU ILE LYS GLU LEU GLY
SEQRES 7 H 171 GLU GLU GLY ASP TYR LYS MET THR LEU ARG LYS PHE PRO
SEQRES 8 H 171 HIS GLN VAL LEU ARG GLU ASN LYS GLN ALA THR GLY ALA
SEQRES 9 H 171 GLY ALA ASP ARG VAL SER ASP GLY MET ARG ALA ALA PHE
SEQRES 10 H 171 GLY LYS ILE VAL GLY THR ALA ALA ARG VAL GLN ALA GLY
SEQRES 11 H 171 GLU GLN LEU PHE THR ALA TYR CYS ASN VAL GLU ASP ALA
SEQRES 12 H 171 GLU HIS VAL LYS GLU ALA PHE ARG ARG ALA TYR ASN LYS
SEQRES 13 H 171 ILE THR PRO SER CYS ARG ILE ASP SER SER PRO ALA GLY
SEQRES 14 H 171 ASN ALA
SEQRES 1 I 162 MET ALA GLY THR ILE GLU VAL LEU VAL PRO GLY GLY GLU
SEQRES 2 I 162 ALA ASN PRO GLY PRO PRO LEU GLY PRO GLU LEU GLY PRO
SEQRES 3 I 162 THR PRO VAL ASP VAL GLN ALA VAL VAL GLN GLU ILE ASN
SEQRES 4 I 162 ASP GLN THR ALA ALA PHE ASP GLY THR GLU VAL PRO VAL
SEQRES 5 I 162 THR VAL LYS TYR ASP ASP ASP GLY SER PHE GLU ILE GLU
SEQRES 6 I 162 VAL GLY VAL PRO PRO THR ALA GLU LEU ILE LYS ASP GLU
SEQRES 7 I 162 ALA GLY PHE GLU THR GLY SER GLY GLU PRO GLN GLU ASP
SEQRES 8 I 162 PHE VAL ALA ASP LEU SER VAL ASP GLN VAL LYS GLN ILE
SEQRES 9 I 162 ALA GLU GLN LYS HIS PRO ASP LEU LEU SER TYR ASP LEU
SEQRES 10 I 162 THR ASN ALA ALA LYS GLU VAL VAL GLY THR CYS THR SER
SEQRES 11 I 162 LEU GLY VAL THR ILE GLU GLY GLU ASN PRO ARG GLU PHE
SEQRES 12 I 162 LYS GLU ARG ILE ASP ALA GLY GLU TYR ASP ASP VAL PHE
SEQRES 13 I 162 ALA ALA GLU ALA GLN ALA
SEQRES 1 J 145 MET SER VAL ALA GLU PHE ASP ALA ASP VAL ILE VAL ASP
SEQRES 2 J 145 ALA ARG ASP CYS ILE MET GLY ARG VAL ALA SER GLN VAL
SEQRES 3 J 145 ALA GLU GLN ALA LEU ASP GLY GLU THR VAL ALA VAL VAL
SEQRES 4 J 145 ASN ALA GLU ARG ALA VAL ILE THR GLY ARG GLU GLU GLN
SEQRES 5 J 145 ILE VAL GLU LYS TYR GLU LYS ARG VAL ASP ILE GLY ASN
SEQRES 6 J 145 ASP ASN GLY TYR PHE TYR PRO LYS ARG PRO ASP GLY ILE
SEQRES 7 J 145 PHE LYS ARG THR ILE ARG GLY MET LEU PRO HIS LYS LYS
SEQRES 8 J 145 GLN ARG GLY ARG GLU ALA PHE GLU SER VAL ARG VAL TYR
SEQRES 9 J 145 LEU GLY ASN PRO TYR ASP GLU ASP GLY GLU VAL LEU ASP
SEQRES 10 J 145 GLY THR SER LEU ASP ARG LEU SER ASN ILE LYS PHE VAL
SEQRES 11 J 145 THR LEU GLY GLU ILE SER GLU THR LEU GLY ALA ASN LYS
SEQRES 12 J 145 THR TRP
SEQRES 1 K 132 MET GLU ALA LEU GLY ALA ASP VAL THR GLN GLY LEU GLU
SEQRES 2 K 132 LYS GLY SER LEU ILE THR CYS ALA ASP ASN THR GLY ALA
SEQRES 3 K 132 ARG GLU LEU LYS VAL ILE SER VAL HIS GLY TYR SER GLY
SEQRES 4 K 132 THR LYS ASN ARG LEU PRO LYS ALA GLY LEU GLY ASP LYS
SEQRES 5 K 132 ILE THR VAL SER VAL THR LYS GLY THR PRO GLU MET ARG
SEQRES 6 K 132 ARG GLN VAL LEU GLU ALA VAL VAL VAL ARG GLN ARG LYS
SEQRES 7 K 132 PRO ILE ARG ARG PRO ASP GLY THR ARG VAL LYS PHE GLU
SEQRES 8 K 132 ASP ASN ALA ALA VAL ILE VAL ASP GLU ASN GLU ASP PRO
SEQRES 9 K 132 ARG GLY THR GLU LEU LYS GLY PRO ILE ALA ARG GLU VAL
SEQRES 10 K 132 ALA GLN ARG PHE GLY SER VAL ALA SER ALA ALA THR MET
SEQRES 11 K 132 ILE VAL
SEQRES 1 L 165 MET THR SER LYS LYS LYS ARG GLN ARG GLY SER ARG THR
SEQRES 2 L 165 HIS GLY GLY GLY SER HIS LYS ASN ARG ARG GLY ALA GLY
SEQRES 3 L 165 HIS ARG GLY GLY ARG GLY ASP ALA GLY ARG ASP LYS HIS
SEQRES 4 L 165 GLU PHE HIS ASN HIS GLU PRO LEU GLY LYS SER GLY PHE
SEQRES 5 L 165 LYS ARG PRO GLN LYS VAL GLN GLU GLU ALA ALA THR ILE
SEQRES 6 L 165 ASP VAL ARG GLU ILE ASP GLU ASN VAL THR LEU LEU ALA
SEQRES 7 L 165 ALA ASP ASP VAL ALA GLU VAL GLU ASP GLY GLY PHE ARG
SEQRES 8 L 165 VAL ASP VAL ARG ASP VAL VAL GLU GLU ALA ASP ASP ALA
SEQRES 9 L 165 ASP TYR VAL LYS VAL LEU GLY ALA GLY GLN VAL ARG HIS
SEQRES 10 L 165 GLU LEU THR LEU ILE ALA ASP ASP PHE SER GLU GLY ALA
SEQRES 11 L 165 ARG GLU LYS VAL GLU GLY ALA GLY GLY SER VAL GLU LEU
SEQRES 12 L 165 THR ASP LEU GLY GLU GLU ARG GLN ALA GLU ALA GLU GLU
SEQRES 13 L 165 THR GLU ASP ALA ASP ALA ASP GLU GLU
SEQRES 1 M 196 MET ALA ARG SER ALA TYR SER TYR ILE ARG ASP ALA TRP
SEQRES 2 M 196 GLU ASN PRO GLY ASP GLY GLN LEU ALA GLU LEU GLN TRP
SEQRES 3 M 196 GLN ARG GLN GLN GLU TRP ARG ASN GLU GLY ALA VAL GLU
SEQRES 4 M 196 ARG ILE GLU ARG PRO THR ARG LEU ASP LYS ALA ARG SER
SEQRES 5 M 196 GLN GLY TYR LYS ALA LYS GLN GLY VAL ILE VAL ALA ARG
SEQRES 6 M 196 VAL SER VAL ARG LYS GLY SER ALA ARG LYS ARG ARG HIS
SEQRES 7 M 196 LYS ALA GLY ARG ARG SER LYS ARG GLN GLY VAL THR ARG
SEQRES 8 M 196 ILE THR ARG ARG LYS ASP ILE GLN ARG VAL ALA GLU GLU
SEQRES 9 M 196 ARG ALA SER ARG THR PHE PRO ASN LEU ARG VAL LEU ASN
SEQRES 10 M 196 SER TYR SER VAL GLY GLN ASP GLY ARG GLN LYS TRP HIS
SEQRES 11 M 196 GLU VAL ILE LEU ILE ASP PRO ASN HIS PRO ALA ILE GLN
SEQRES 12 M 196 ASN ASP ASP ASP LEU SER TRP ILE CYS ALA ASP ASP GLN
SEQRES 13 M 196 ALA ASP ARG VAL PHE ARG GLY LEU THR GLY ALA GLY ARG
SEQRES 14 M 196 ARG ASN ARG GLY LEU SER GLY LYS GLY LYS GLY SER GLU
SEQRES 15 M 196 LYS THR ARG PRO SER LEU ARG SER ASN GLY GLY LYS ALA
SEQRES 16 M 196 LYS
SEQRES 1 N 187 MET ALA THR GLY PRO ARG TYR LYS VAL PRO MET ARG ARG
SEQRES 2 N 187 ARG ARG GLU ALA ARG THR ASP TYR HIS GLN ARG LEU ARG
SEQRES 3 N 187 LEU LEU LYS SER GLY LYS PRO ARG LEU VAL ALA ARG LYS
SEQRES 4 N 187 SER ASN LYS HIS VAL ARG ALA GLN LEU VAL THR LEU GLY
SEQRES 5 N 187 PRO ASN GLY ASP ASP THR LEU ALA SER ALA HIS SER SER
SEQRES 6 N 187 ASP LEU ALA GLU TYR GLY TRP GLU ALA PRO THR GLY ASN
SEQRES 7 N 187 MET PRO SER ALA TYR LEU THR GLY LEU LEU ALA GLY LEU
SEQRES 8 N 187 ARG ALA GLN GLU ALA GLY VAL GLU GLU ALA VAL LEU ASP
SEQRES 9 N 187 ILE GLY LEU ASN SER PRO THR PRO GLY SER LYS VAL PHE
SEQRES 10 N 187 ALA ILE GLN GLU GLY ALA ILE ASP ALA GLY LEU ASP ILE
SEQRES 11 N 187 PRO HIS ASN ASP ASP VAL LEU ALA ASP TRP GLN ARG THR
SEQRES 12 N 187 ARG GLY ALA HIS ILE ALA GLU TYR ASP GLU GLN LEU GLU
SEQRES 13 N 187 GLU PRO LEU TYR SER GLY ASP PHE ASP ALA ALA ASP LEU
SEQRES 14 N 187 PRO GLU HIS PHE ASP GLU LEU ARG GLU THR LEU LEU ASP
SEQRES 15 N 187 GLY ASP ILE GLU LEU
SEQRES 1 O 116 MET SER LYS THR ASN PRO ARG LEU SER SER LEU ILE ALA
SEQRES 2 O 116 ASP LEU LYS SER ALA ALA ARG SER SER GLY GLY ALA VAL
SEQRES 3 O 116 TRP GLY ASP VAL ALA GLU ARG LEU GLU LYS PRO ARG ARG
SEQRES 4 O 116 THR HIS ALA GLU VAL ASN LEU GLY ARG ILE GLU ARG TYR
SEQRES 5 O 116 ALA GLN GLU ASP GLU THR VAL VAL VAL PRO GLY LYS VAL
SEQRES 6 O 116 LEU GLY SER GLY VAL LEU GLN LYS ASP VAL THR VAL ALA
SEQRES 7 O 116 ALA VAL ASP PHE SER GLY THR ALA GLU THR LYS ILE ASP
SEQRES 8 O 116 GLN VAL GLY GLU ALA VAL SER LEU GLU GLN ALA ILE GLU
SEQRES 9 O 116 ASN ASN PRO GLU GLY SER HIS VAL ARG VAL ILE ARG
SEQRES 1 P 149 MET THR ASP LEU SER ALA GLN LYS ARG LEU ALA ALA ASP
SEQRES 2 P 149 VAL LEU ASP VAL GLY LYS ASN ARG VAL TRP PHE ASN PRO
SEQRES 3 P 149 GLU ARG GLN GLY ASP ILE ALA ASP ALA ILE THR ARG GLU
SEQRES 4 P 149 ASP VAL ARG GLU LEU VAL ASP GLU GLY ALA ILE GLN ALA
SEQRES 5 P 149 LYS ASP LYS LYS GLY ASN SER ARG GLY ARG ALA ARG GLU
SEQRES 6 P 149 ARG GLN LYS LYS ARG ALA TYR GLY HIS GLN LYS GLY ALA
SEQRES 7 P 149 GLY SER ARG LYS GLY LYS ALA GLY ALA ARG GLN ASN SER
SEQRES 8 P 149 LYS GLU ASP TRP GLU SER ARG ILE ARG ALA GLN ARG THR
SEQRES 9 P 149 LYS LEU ARG GLU LEU ARG ASP GLU GLY THR LEU SER SER
SEQRES 10 P 149 SER GLN TYR ARG ASP LEU TYR ASP LYS ALA GLY GLY GLY
SEQRES 11 P 149 GLU PHE ASP SER VAL ALA ASP LEU GLU ARG TYR ILE ASP
SEQRES 12 P 149 ALA ASN HIS GLY ASP ALA
SEQRES 1 Q 96 MET PRO SER SER ASN GLY PRO LEU GLU GLY THR ARG GLY
SEQRES 2 Q 96 LYS LEU LYS ASN LYS PRO ARG ASP ARG GLY THR SER PRO
SEQRES 3 Q 96 PRO GLN ARG ALA VAL GLU GLU PHE ASP ASP GLY GLU LYS
SEQRES 4 Q 96 VAL HIS LEU LYS ILE ASP PRO SER VAL PRO ASN GLY ARG
SEQRES 5 Q 96 PHE HIS PRO ARG PHE ASP GLY GLN THR GLY THR VAL GLU
SEQRES 6 Q 96 GLY LYS GLN GLY ASP ALA TYR LYS VAL ASP ILE VAL ASP
SEQRES 7 Q 96 GLY GLY LYS GLU LYS THR ILE ILE VAL THR ALA ALA HIS
SEQRES 8 Q 96 LEU ARG ARG GLN GLU
SEQRES 1 R 155 MET GLY ILE SER TYR SER VAL GLU ALA ASP PRO ASP THR
SEQRES 2 R 155 THR ALA LYS ALA MET LEU ARG GLU ARG GLN MET SER PHE
SEQRES 3 R 155 LYS HIS SER LYS ALA ILE ALA ARG GLU ILE LYS GLY LYS
SEQRES 4 R 155 THR ALA GLY GLU ALA VAL ASP TYR LEU GLU ALA VAL ILE
SEQRES 5 R 155 GLU GLY ASP GLN PRO VAL PRO PHE LYS GLN HIS ASN SER
SEQRES 6 R 155 GLY VAL GLY HIS LYS SER LYS VAL ASP GLY TRP ASP ALA
SEQRES 7 R 155 GLY ARG TYR PRO GLU LYS ALA SER LYS ALA PHE LEU ASP
SEQRES 8 R 155 LEU LEU GLU ASN ALA VAL GLY ASN ALA ASP HIS GLN GLY
SEQRES 9 R 155 PHE ASP GLY GLU ALA MET THR ILE LYS HIS VAL ALA ALA
SEQRES 10 R 155 HIS LYS VAL GLY GLU GLN GLN GLY ARG LYS PRO ARG ALA
SEQRES 11 R 155 MET GLY ARG ALA SER ALA TRP ASN SER PRO GLN VAL ASP
SEQRES 12 R 155 VAL GLU LEU ILE LEU GLU GLU PRO GLU VAL GLU ASP
SEQRES 1 S 85 MET SER TRP ASP VAL ILE LYS HIS PRO HIS VAL THR GLU
SEQRES 2 S 85 LYS ALA MET ASN ASP MET ASP PHE GLN ASN LYS LEU GLN
SEQRES 3 S 85 PHE ALA VAL ASP ASP ARG ALA SER LYS GLY GLU VAL ALA
SEQRES 4 S 85 ASP ALA VAL GLU GLU GLN TYR ASP VAL THR VAL GLU GLN
SEQRES 5 S 85 VAL ASN THR GLN ASN THR MET ASP GLY GLU LYS LYS ALA
SEQRES 6 S 85 VAL VAL ARG LEU SER GLU ASP ASP ASP ALA GLN GLU VAL
SEQRES 7 S 85 ALA SER ARG ILE GLY VAL PHE
SEQRES 1 T 120 MET SER LYS GLN PRO ASP LYS GLN ARG LYS SER GLN ARG
SEQRES 2 T 120 ARG ALA PRO LEU HIS GLU ARG HIS LYS GLN VAL ARG ALA
SEQRES 3 T 120 THR LEU SER ALA ASP LEU ARG GLU GLU TYR GLY GLN ARG
SEQRES 4 T 120 ASN VAL ARG VAL ASN ALA GLY ASP THR VAL GLU VAL LEU
SEQRES 5 T 120 ARG GLY ASP PHE ALA GLY GLU GLU GLY GLU VAL ILE ASN
SEQRES 6 T 120 VAL ASP LEU ASP LYS ALA VAL ILE HIS VAL GLU ASP VAL
SEQRES 7 T 120 THR LEU GLU LYS THR ASP GLY GLU GLU VAL PRO ARG PRO
SEQRES 8 T 120 LEU ASP THR SER ASN VAL ARG VAL THR ASP LEU ASP LEU
SEQRES 9 T 120 GLU ASP GLU LYS ARG GLU ALA ARG LEU GLU SER GLU ASP
SEQRES 10 T 120 ASP SER ALA
SEQRES 1 U 67 MET PRO ARG THR ARG GLU CYS ASP TYR CYS GLY THR ASP
SEQRES 2 U 67 ILE GLU PRO GLY THR GLY THR MET PHE VAL HIS LYS ASP
SEQRES 3 U 67 GLY ALA THR THR HIS PHE CYS SER SER LYS CYS GLU ASN
SEQRES 4 U 67 ASN ALA ASP LEU GLY ARG GLU ALA ARG ASN LEU GLU TRP
SEQRES 5 U 67 THR ASP THR ALA ARG GLY GLU ALA GLY GLU ALA GLU ASP
SEQRES 6 U 67 GLU ALA
SEQRES 1 V 71 MET THR VAL LEU HIS VAL GLN GLU ILE ARG ASP MET THR
SEQRES 2 V 71 PRO ALA GLU ARG GLU ALA GLU LEU ASP ASP LEU LYS THR
SEQRES 3 V 71 GLU LEU LEU ASN ALA ARG ALA VAL GLN ALA ALA GLY GLY
SEQRES 4 V 71 ALA PRO GLU ASN PRO GLY ARG ILE LYS GLU LEU ARG LYS
SEQRES 5 V 71 ALA ILE ALA ARG ILE LYS THR ILE GLN GLY GLU GLU GLY
SEQRES 6 V 71 ASP LEU GLN GLU ASN GLU
SEQRES 1 W 154 MET HIS ALA LEU VAL GLN LEU ARG GLY GLU VAL ASN MET
SEQRES 2 W 154 HIS THR ASP ILE GLN ASP THR LEU GLU MET LEU ASN ILE
SEQRES 3 W 154 HIS HIS VAL ASN HIS CYS THR LEU VAL PRO GLU THR ASP
SEQRES 4 W 154 ALA TYR ARG GLY MET VAL ALA LYS VAL ASN ASP PHE VAL
SEQRES 5 W 154 ALA PHE GLY GLU PRO SER GLN GLU THR LEU GLU THR VAL
SEQRES 6 W 154 LEU ALA THR ARG ALA GLU PRO LEU GLU GLY ASP ALA ASP
SEQRES 7 W 154 VAL ASP ASP GLU TRP VAL ALA GLU HIS THR ASP TYR ASP
SEQRES 8 W 154 ASP ILE SER GLY LEU ALA PHE ALA LEU LEU SER GLU GLU
SEQRES 9 W 154 THR THR LEU ARG GLU GLN GLY LEU SER PRO THR LEU ARG
SEQRES 10 W 154 LEU HIS PRO PRO ARG GLY GLY HIS ASP GLY VAL LYS HIS
SEQRES 11 W 154 PRO VAL LYS GLU GLY GLY GLN LEU GLY LYS HIS ASP THR
SEQRES 12 W 154 GLU GLY ILE ASP ASP LEU LEU GLU ALA MET ARG
SEQRES 1 X 92 MET SER ALA SER ASP PHE GLU GLU ARG VAL VAL THR ILE
SEQRES 2 X 92 PRO LEU ARG ASP ALA ARG ALA GLU PRO ASN HIS LYS ARG
SEQRES 3 X 92 ALA ASP LYS ALA MET ILE LEU ILE ARG GLU HIS LEU ALA
SEQRES 4 X 92 LYS HIS PHE SER VAL ASP GLU ASP ALA VAL ARG LEU ASP
SEQRES 5 X 92 PRO SER ILE ASN GLU ALA ALA TRP ALA ARG GLY ARG ALA
SEQRES 6 X 92 ASN THR PRO SER LYS ILE ARG VAL ARG ALA ALA ARG PHE
SEQRES 7 X 92 GLU GLU GLU GLY GLU ALA ILE VAL GLU ALA GLU THR ALA
SEQRES 8 X 92 GLU
SEQRES 1 Y 241 MET ALA ASP ASN GLU GLU ASP VAL GLU ALA GLU GLU GLU
SEQRES 2 Y 241 TYR THR GLU LEU THR ASP ILE SER GLY VAL GLY PRO SER
SEQRES 3 Y 241 LYS ALA GLU SER LEU ARG GLU ALA GLY PHE GLU SER VAL
SEQRES 4 Y 241 GLU ASP VAL ARG GLY ALA ASP GLN SER ALA LEU ALA ASP
SEQRES 5 Y 241 VAL SER GLY ILE GLY ASN ALA LEU ALA ALA ARG ILE LYS
SEQRES 6 Y 241 ALA ASP VAL GLY GLY LEU GLU VAL GLU SER GLU THR GLU
SEQRES 7 Y 241 ALA GLU VAL GLU GLU GLU GLY GLY GLU GLU ALA PRO ASP
SEQRES 8 Y 241 GLU ASP VAL GLU THR GLU LEU GLN ALA ARG GLY LEU THR
SEQRES 9 Y 241 GLU LYS THR PRO ASP LEU SER ASP GLU ASP ALA ARG LEU
SEQRES 10 Y 241 LEU THR GLN ARG HIS ARG VAL GLY LYS PRO GLN PHE ASN
SEQRES 11 Y 241 ARG GLN ASP HIS HIS LYS LYS LYS ARG VAL SER THR SER
SEQRES 12 Y 241 TRP ARG LYS PRO ARG GLY GLN LEU SER LYS GLN ARG ARG
SEQRES 13 Y 241 GLY ILE LYS GLY LYS GLY ASP THR VAL GLU ALA GLY PHE
SEQRES 14 Y 241 ARG SER PRO THR ALA VAL ARG GLY LYS HIS PRO SER GLY
SEQRES 15 Y 241 PHE GLU GLU VAL ARG VAL HIS ASN VAL ASP ASP LEU GLU
SEQRES 16 Y 241 GLY VAL ASP GLY ASP THR GLU ALA VAL ARG ILE ALA SER
SEQRES 17 Y 241 LYS VAL GLY ALA ARG LYS ARG GLU ARG ILE GLU GLU GLU
SEQRES 18 Y 241 ALA GLU ASP ALA GLY ILE ARG VAL LEU ASN PRO THR TYR
SEQRES 19 Y 241 VAL GLU VAL GLU VAL SER GLU
SEQRES 1 Z 92 MET ALA SER LYS SER GLY LYS THR GLY ARG SER GLY ARG
SEQRES 2 Z 92 PHE GLY ALA ARG TYR GLY ARG VAL SER ARG ARG ARG VAL
SEQRES 3 Z 92 ALA GLU ILE GLU SER GLU MET ASN GLU ASP HIS ALA CYS
SEQRES 4 Z 92 PRO ASN CYS GLY GLU ASP ARG VAL ASP ARG GLN GLY THR
SEQRES 5 Z 92 GLY ILE TRP GLN CYS SER TYR CYS ASP TYR LYS PHE THR
SEQRES 6 Z 92 GLY GLY SER TYR LYS PRO GLU THR PRO GLY GLY LYS THR
SEQRES 7 Z 92 VAL ARG ARG SER ILE ARG ALA ALA LEU SER GLU ASP GLU
SEQRES 8 Z 92 GLU
SEQRES 1 1 57 MET THR GLY ALA GLY THR PRO SER GLN GLY LYS LYS ASN
SEQRES 2 1 57 THR THR THR HIS THR LYS CYS ARG ARG CYS GLY GLU LYS
SEQRES 3 1 57 SER TYR HIS THR LYS LYS LYS VAL CYS SER SER CYS GLY
SEQRES 4 1 57 PHE GLY LYS SER ALA LYS ARG ARG ASP TYR GLU TRP GLN
SEQRES 5 1 57 SER LYS ALA GLY GLU
SEQRES 1 2 50 MET GLY LYS LYS SER LYS ALA THR LYS LYS ARG LEU ALA
SEQRES 2 2 50 LYS LEU ASP ASN GLN ASN SER ARG VAL PRO ALA TRP VAL
SEQRES 3 2 50 MET LEU LYS THR ASP ARG GLU VAL GLN ARG ASN HIS LYS
SEQRES 4 2 50 ARG ARG HIS TRP ARG ARG ASN ASP THR ASP GLU
SEQRES 1 3 92 MET GLN MET PRO ARG ARG PHE ASN THR TYR CYS PRO HIS
SEQRES 2 3 92 CYS ASN GLU HIS GLN GLU HIS GLU VAL GLU LYS VAL ARG
SEQRES 3 3 92 SER GLY ARG GLN THR GLY MET LYS TRP ILE ASP ARG GLN
SEQRES 4 3 92 ARG GLU ARG ASN SER GLY ILE GLY ASN ASP GLY LYS PHE
SEQRES 5 3 92 SER LYS VAL PRO GLY GLY ASP LYS PRO THR LYS LYS THR
SEQRES 6 3 92 ASP LEU LYS TYR ARG CYS GLY GLU CYS GLY LYS ALA HIS
SEQRES 7 3 92 LEU ARG GLU GLY TRP ARG ALA GLY ARG LEU GLU PHE GLN
SEQRES 8 3 92 GLU
MODRES 2QA4 OMU 0 2587 U O2'-METHYLURIDINE 5'-MONOPHOSPHATE
MODRES 2QA4 OMG 0 2588 G O2'-METHYLGUANOSINE-5'-MONOPHOSPHATE
MODRES 2QA4 UR3 0 2619 U 3-METHYLURIDINE-5'-MONOPHOSHATE
MODRES 2QA4 PSU 0 2621 U PSEUDOURIDINE-5'-MONOPHOSPHATE
HET OMU 02587 21
HET OMG 02588 24
HET UR3 02619 21
HET PSU 02621 20
HET MG 0 1 1
HET MG 02924 1
HET MG 02925 1
HET MG 02926 1
HET MG 02927 1
HET MG 02928 1
HET MG 02929 1
HET MG 02930 1
HET MG 02931 1
HET MG 02932 1
HET MG 02933 1
HET MG 02934 1
HET MG 02935 1
HET MG 02936 1
HET MG 02937 1
HET MG 02938 1
HET MG 02939 1
HET MG 02940 1
HET MG 02941 1
HET MG 02942 1
HET MG 02943 1
HET MG 02944 1
HET MG 02945 1
HET MG 02946 1
HET MG 02947 1
HET MG 02948 1
HET MG 02949 1
HET MG 02950 1
HET MG 02951 1
HET MG 02952 1
HET MG 02953 1
HET MG 02954 1
HET MG 02955 1
HET MG 02956 1
HET MG 02957 1
HET MG 02958 1
HET MG 02959 1
HET MG 02960 1
HET MG 02961 1
HET MG 02962 1
HET MG 02963 1
HET MG 02964 1
HET MG 02965 1
HET MG 02966 1
HET MG 02967 1
HET MG 02968 1
HET MG 02969 1
HET MG 02970 1
HET MG 02971 1
HET MG 02972 1
HET MG 02973 1
HET MG 02974 1
HET MG 02975 1
HET MG 02976 1
HET MG 02977 1
HET MG 02978 1
HET MG 02979 1
HET MG 02980 1
HET MG 02981 1
HET MG 02982 1
HET MG 02983 1
HET MG 02984 1
HET MG 02985 1
HET MG 02986 1
HET MG 02987 1
HET MG 02988 1
HET MG 02989 1
HET MG 02990 1
HET MG 02991 1
HET MG 02992 1
HET MG 02993 1
HET MG 02994 1
HET MG 02995 1
HET MG 02996 1
HET MG 02997 1
HET MG 02998 1
HET MG 02999 1
HET MG 03000 1
HET MG 03001 1
HET MG 03002 1
HET MG 03003 1
HET MG 03004 1
HET MG 03005 1
HET MG 03006 1
HET MG 03007 1
HET MG 03008 1
HET MG 03009 1
HET MG 03010 1
HET MG 03011 1
HET MG 03012 1
HET MG 03013 1
HET MG 03014 1
HET MG 03015 1
HET MG 03016 1
HET MG 03017 1
HET MG 03018 1
HET MG 03019 1
HET MG 03020 1
HET MG 03021 1
HET MG 03022 1
HET MG 03023 1
HET MG 03024 1
HET MG 03025 1
HET MG 03026 1
HET MG 03027 1
HET MG 03028 1
HET MG 03029 1
HET MG 03030 1
HET K 03031 1
HET NA 03032 1
HET NA 03033 1
HET NA 03034 1
HET NA 03035 1
HET NA 03036 1
HET NA 03037 1
HET NA 03038 1
HET NA 03039 1
HET NA 03040 1
HET NA 03041 1
HET NA 03042 1
HET NA 03043 1
HET NA 03044 1
HET NA 03045 1
HET NA 03046 1
HET NA 03047 1
HET NA 03048 1
HET NA 03049 1
HET NA 03050 1
HET NA 03051 1
HET NA 03052 1
HET NA 03053 1
HET NA 03054 1
HET NA 03055 1
HET NA 03056 1
HET NA 03057 1
HET NA 03058 1
HET NA 03059 1
HET NA 03060 1
HET NA 03061 1
HET NA 03062 1
HET NA 03063 1
HET NA 03064 1
HET NA 03065 1
HET NA 03066 1
HET NA 03067 1
HET NA 03068 1
HET NA 03069 1
HET NA 03070 1
HET NA 03071 1
HET NA 03072 1
HET NA 03073 1
HET NA 03074 1
HET NA 03075 1
HET NA 03076 1
HET NA 03077 1
HET NA 03078 1
HET NA 03079 1
HET NA 03080 1
HET NA 03081 1
HET NA 03082 1
HET NA 03083 1
HET NA 03084 1
HET NA 03085 1
HET NA 03086 1
HET NA 03087 1
HET NA 03088 1
HET NA 03089 1
HET NA 03090 1
HET NA 03091 1
HET NA 03092 1
HET NA 03093 1
HET NA 03094 1
HET NA 03095 1
HET NA 03096 1
HET NA 03097 1
HET NA 03098 1
HET NA 03099 1
HET NA 03100 1
HET NA 03101 1
HET NA 03102 1
HET NA 03103 1
HET NA 03104 1
HET CL 03105 1
HET CL 03106 1
HET CL 03107 1
HET CL 03108 1
HET CL 03109 1
HET CL 03110 1
HET CL 03111 1
HET CL 03112 1
HET MG 9 123 1
HET NA 9 124 1
HET NA 9 125 1
HET NA 9 126 1
HET MG A 240 1
HET MG A 241 1
HET NA A 242 1
HET CL A 243 1
HET MG B 338 1
HET CL B 339 1
HET NA C 247 1
HET NA H 172 1
HET NA J 146 1
HET CL J 147 1
HET CL J 148 1
HET CL J 149 1
HET MG K 133 1
HET CL K 134 1
HET NA L 165 1
HET CL L 166 1
HET K M 196 1
HET NA M 197 1
HET CL M 198 1
HET CL N 187 1
HET CD O 116 1
HET CL O 117 1
HET NA Q 96 1
HET CL Q 97 1
HET NA R 155 1
HET NA R 156 1
HET CL R 157 1
HET NA S 85 1
HET MG T 120 1
HET CD U 67 1
HET MG Y 241 1
HET CL Y 242 1
HET CD Z 93 1
HET CD 1 57 1
HET MG 3 93 1
HET CD 3 94 1
HET CL 3 95 1
HETNAM OMU O2'-METHYLURIDINE 5'-MONOPHOSPHATE
HETNAM OMG O2'-METHYLGUANOSINE-5'-MONOPHOSPHATE
HETNAM UR3 3-METHYLURIDINE-5'-MONOPHOSHATE
HETNAM PSU PSEUDOURIDINE-5'-MONOPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM K POTASSIUM ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM CD CADMIUM ION
FORMUL 1 OMU C10 H15 N2 O9 P
FORMUL 1 OMG C11 H16 N5 O8 P
FORMUL 1 UR3 C10 H15 N2 O9 P
FORMUL 1 PSU C9 H13 N2 O9 P
FORMUL 32 MG 116(MG 2+)
FORMUL 40 K 2(K 1+)
FORMUL 41 NA 86(NA 1+)
FORMUL 14 CL 22(CL 1-)
FORMUL 46 CD 5(CD 2+)
HELIX 1 1 ILE A 4 GLY A 12 1 9
HELIX 2 2 PRO A 19 TYR A 23 5 5
HELIX 3 3 ALA A 97 ILE A 99 5 3
HELIX 4 4 LYS A 171 ALA A 181 1 11
HELIX 5 5 SER B 10 GLY B 14 5 5
HELIX 6 6 GLU B 108 THR B 112 5 5
HELIX 7 7 ASP B 122 GLY B 135 1 14
HELIX 8 8 VAL B 147 VAL B 151 5 5
HELIX 9 9 SER B 170 GLY B 185 1 16
HELIX 10 10 ALA B 189 PHE B 194 1 6
HELIX 11 11 GLY B 213 GLY B 219 1 7
HELIX 12 12 GLY B 225 GLN B 230 5 6
HELIX 13 13 PRO C 19 THR C 24 5 6
HELIX 14 14 ARG C 27 ARG C 42 1 16
HELIX 15 15 ASN C 103 ASP C 120 1 18
HELIX 16 16 ASP C 120 ARG C 127 1 8
HELIX 17 17 ASP C 142 LEU C 147 5 6
HELIX 18 18 LYS C 149 ASP C 161 1 13
HELIX 19 19 HIS C 163 ASP C 170 1 8
HELIX 20 20 GLY C 177 GLY C 183 5 7
HELIX 21 21 SER C 201 ASN C 206 1 6
HELIX 22 22 ASN C 219 ALA C 224 1 6
HELIX 23 23 PRO C 225 ALA C 228 5 4
HELIX 24 24 GLU C 237 ALA C 244 1 8
HELIX 25 25 GLU C 245 ARG C 246 5 2
HELIX 26 26 PHE D 10 ARG D 14 5 5
HELIX 27 27 ALA D 37 GLY D 42 1 6
HELIX 28 28 ASP D 77 LEU D 88 1 12
HELIX 29 29 PRO D 89 ALA D 91 5 3
HELIX 30 30 TYR D 139 ARG D 144 1 6
HELIX 31 31 ASN D 158 SER D 168 1 11
HELIX 32 32 ASN E 55 THR E 77 1 23
HELIX 33 33 ASN E 106 GLU E 110 5 5
HELIX 34 34 ASP E 137 LEU E 151 1 15
HELIX 35 35 PRO F 9 GLY F 27 1 19
HELIX 36 36 GLY F 32 GLY F 43 1 12
HELIX 37 37 GLU F 57 HIS F 62 1 6
HELIX 38 38 HIS F 62 GLU F 69 1 8
HELIX 39 39 GLN F 80 ALA F 87 1 8
HELIX 40 40 ALA F 104 ARG F 119 1 16
HELIX 41 41 PRO G 13 SER G 29 1 17
HELIX 42 42 PRO G 42 ARG G 50 1 9
HELIX 43 43 ARG G 63 ASP G 73 1 11
HELIX 44 44 LEU G 78 TYR G 84 1 7
HELIX 45 45 PHE G 99 SER G 108 1 10
HELIX 46 46 PRO H 2 TYR H 6 5 5
HELIX 47 47 ASP H 39 TYR H 43 5 5
HELIX 48 48 HIS H 59 GLY H 78 1 20
HELIX 49 49 ASP H 142 TYR H 154 1 13
HELIX 50 50 ASN H 155 ILE H 157 5 3
HELIX 51 55 ILE J 18 LEU J 31 1 14
HELIX 52 56 ASN J 40 ARG J 43 5 4
HELIX 53 57 ARG J 49 ILE J 63 1 15
HELIX 54 58 ARG J 74 GLY J 85 1 12
HELIX 55 59 LYS J 91 SER J 100 1 10
HELIX 56 60 LEU J 132 GLY J 140 1 9
HELIX 57 61 ARG K 115 PHE K 121 1 7
HELIX 58 62 PHE K 121 SER K 126 1 6
HELIX 59 63 SER L 2 GLN L 7 1 6
HELIX 60 64 PRO L 54 GLN L 58 5 5
HELIX 61 65 VAL L 66 GLU L 71 1 6
HELIX 62 66 ARG L 94 VAL L 96 5 3
HELIX 63 67 SER L 126 GLY L 135 1 10
HELIX 64 68 ALA M 4 TRP M 12 1 9
HELIX 65 69 ASP M 17 ARG M 32 1 16
HELIX 66 70 ARG M 45 GLY M 53 1 9
HELIX 67 71 ARG M 82 GLN M 86 5 5
HELIX 68 72 ASP M 96 PHE M 109 1 14
HELIX 69 73 HIS M 138 ASP M 144 1 7
HELIX 70 74 LEU M 147 ALA M 156 5 10
HELIX 71 75 ARG M 158 GLY M 162 5 5
HELIX 72 76 THR M 164 ARG M 171 1 8
HELIX 73 77 LEU M 187 GLY M 191 5 5
HELIX 74 78 MET N 10 GLU N 15 1 6
HELIX 75 79 ASP N 19 LEU N 27 1 9
HELIX 76 80 LYS N 28 GLY N 30 5 3
HELIX 77 81 SER N 63 GLY N 70 5 8
HELIX 78 82 ASN N 77 GLY N 96 1 20
HELIX 79 83 SER N 113 GLY N 126 1 14
HELIX 80 84 ASN N 132 LEU N 136 5 5
HELIX 81 85 ASP N 138 GLY N 144 1 7
HELIX 82 86 GLY N 144 GLN N 153 1 10
HELIX 83 87 PRO N 169 LEU N 180 1 12
HELIX 84 88 ASN O 4 SER O 21 1 18
HELIX 85 89 ALA O 24 LYS O 35 1 12
HELIX 86 90 PRO O 36 HIS O 40 5 5
HELIX 87 91 ASN O 44 ALA O 52 1 9
HELIX 88 92 SER O 82 GLY O 93 1 12
HELIX 89 93 LEU O 98 ASN O 105 1 8
HELIX 90 94 LEU P 3 LEU P 14 1 12
HELIX 91 95 ARG P 27 ASP P 33 1 7
HELIX 92 96 THR P 36 GLU P 46 1 11
HELIX 93 97 ARG P 59 TYR P 71 1 13
HELIX 94 98 GLY P 76 ARG P 80 5 5
HELIX 95 99 LYS P 83 GLN P 88 1 6
HELIX 96 100 ASN P 89 GLY P 112 1 24
HELIX 97 101 SER P 117 GLY P 127 1 11
HELIX 98 102 VAL P 134 ASP P 142 1 9
HELIX 99 103 THR Q 87 ALA Q 89 5 3
HELIX 100 104 SER R 24 LYS R 36 1 13
HELIX 101 105 THR R 39 GLY R 53 1 15
HELIX 102 106 PRO R 81 HIS R 101 1 21
HELIX 103 107 ALA R 129 GLY R 131 5 3
HELIX 104 108 THR S 11 ASN S 22 1 12
HELIX 105 109 SER S 33 ASP S 46 1 14
HELIX 106 110 ASP S 73 ARG S 80 1 8
HELIX 107 111 GLN T 3 ARG T 13 1 11
HELIX 108 112 LEU T 16 GLN T 22 5 7
HELIX 109 113 SER T 28 GLY T 36 1 9
HELIX 110 114 ASP T 92 SER T 94 5 3
HELIX 111 115 ASP T 105 SER T 114 1 10
HELIX 112 116 SER U 33 ASP U 41 1 9
HELIX 113 117 HIS V 4 MET V 11 1 8
HELIX 114 118 THR V 12 ALA V 35 1 24
HELIX 115 119 PRO V 43 GLY V 64 1 22
HELIX 116 120 HIS W 14 LEU W 24 1 11
HELIX 117 121 THR W 38 ASN W 49 1 12
HELIX 118 122 SER W 58 ARG W 69 1 12
HELIX 119 123 ASP W 80 THR W 88 1 9
HELIX 120 124 ASP W 92 SER W 102 1 11
HELIX 121 125 ASP W 142 MET W 153 1 12
HELIX 122 126 PRO X 21 HIS X 23 5 3
HELIX 123 127 LYS X 24 PHE X 41 1 18
HELIX 124 128 ASP X 51 TRP X 59 1 9
HELIX 125 129 SER Y 110 GLY Y 124 1 15
HELIX 126 130 GLU Y 165 ARG Y 169 5 5
HELIX 127 131 ASN Y 189 GLU Y 194 5 6
HELIX 128 132 GLY Y 210 ALA Y 224 1 15
HELIX 129 133 ARG Z 10 GLY Z 15 5 6
HELIX 130 134 GLY Z 19 GLU Z 30 1 12
HELIX 131 135 LYS Z 77 SER Z 82 1 6
HELIX 132 136 GLY 1 4 GLY 1 9 1 6
HELIX 133 137 TYR 1 48 SER 1 52 5 5
HELIX 134 138 ALA 2 6 GLN 2 17 1 12
HELIX 135 139 PRO 2 22 ASP 2 30 1 9
HELIX 136 140 TRP 3 35 SER 3 44 1 10
HELIX 137 141 ASP 3 49 LYS 3 54 5 6
SHEET 1 A 4 ARG A 65 ILE A 68 0
SHEET 2 A 4 PRO A 54 PHE A 60 -1 N ALA A 56 O ILE A 68
SHEET 3 A 4 ALA A 39 HIS A 47 -1 N GLU A 46 O VAL A 55
SHEET 4 A 4 GLU A 79 GLN A 81 -1 O LEU A 80 N GLY A 40
SHEET 1 B 4 THR A 93 PRO A 95 0
SHEET 2 B 4 ARG A 153 ILE A 156 -1 O ALA A 154 N LEU A 94
SHEET 3 B 4 PRO A 104 CYS A 106 -1 N CYS A 106 O THR A 155
SHEET 4 B 4 ALA A 126 GLN A 127 -1 O ALA A 126 N VAL A 105
SHEET 1 C 2 VAL A 137 LYS A 139 0
SHEET 2 C 2 MET A 145 ARG A 147 -1 O LYS A 146 N VAL A 138
SHEET 1 D 2 SER A 214 ILE A 215 0
SHEET 2 D 2 ASP A 227 ILE A 228 1 O ASP A 227 N ILE A 215
SHEET 1 E 8 VAL B 327 VAL B 330 0
SHEET 2 E 8 PHE B 41 VAL B 54 -1 N VAL B 52 O TYR B 329
SHEET 3 E 8 LEU B 308 PRO B 313 -1 O VAL B 309 N GLY B 43
SHEET 4 E 8 TYR B 199 VAL B 205 -1 N ASP B 201 O ARG B 312
SHEET 5 E 8 GLN B 261 ASP B 271 -1 O LYS B 267 N ALA B 200
SHEET 6 E 8 TYR B 294 LYS B 298 -1 O LEU B 296 N ASP B 271
SHEET 7 E 8 GLU B 66 GLU B 75 -1 N THR B 72 O VAL B 297
SHEET 8 E 8 PHE B 41 VAL B 54 -1 N GLY B 47 O VAL B 73
SHEET 1 F 4 GLY B 93 TRP B 101 0
SHEET 2 F 4 MET B 79 THR B 90 -1 N ALA B 86 O LEU B 97
SHEET 3 F 4 LEU B 137 HIS B 145 -1 O ARG B 141 N ARG B 85
SHEET 4 F 4 VAL B 161 VAL B 166 -1 O MET B 162 N THR B 144
SHEET 1 G 3 GLY B 93 TRP B 101 0
SHEET 2 G 3 MET B 79 THR B 90 -1 N ALA B 86 O LEU B 97
SHEET 3 G 3 GLU B 187 HIS B 188 -1 O HIS B 188 N MET B 79
SHEET 1 H 2 GLY B 210 GLN B 212 0
SHEET 2 H 2 GLY B 255 THR B 257 -1 O GLY B 255 N GLN B 212
SHEET 1 I 6 THR C 12 VAL C 16 0
SHEET 2 I 6 ALA C 3 TYR C 6 -1 N ALA C 3 O VAL C 16
SHEET 3 I 6 VAL C 138 VAL C 140 1 O VAL C 139 N THR C 4
SHEET 4 I 6 THR C 233 THR C 236 1 O PHE C 235 N VAL C 140
SHEET 5 I 6 LEU C 193 THR C 196 1 N VAL C 195 O THR C 236
SHEET 6 I 6 ASP C 211 THR C 214 1 O ALA C 213 N THR C 196
SHEET 1 J 2 LYS C 72 LEU C 73 0
SHEET 2 J 2 ARG C 76 ALA C 77 -1 O ARG C 76 N LEU C 73
SHEET 1 K 2 LYS C 173 ILE C 174 0
SHEET 2 K 2 TYR C 186 ARG C 187 -1 O ARG C 187 N LYS C 173
SHEET 1 L 4 THR D 74 LEU D 75 0
SHEET 2 L 4 ILE D 18 VAL D 22 -1 N VAL D 21 O LEU D 75
SHEET 3 L 4 THR D 131 LEU D 134 -1 O ASN D 133 N LYS D 20
SHEET 4 L 4 PHE D 104 SER D 105 -1 N PHE D 104 O VAL D 132
SHEET 1 M 3 MET D 25 GLY D 26 0
SHEET 2 M 3 PRO D 68 LYS D 72 -1 O ALA D 71 N MET D 25
SHEET 3 M 3 VAL D 50 LYS D 53 -1 N THR D 52 O ILE D 69
SHEET 1 N 3 ARG E 2 GLU E 6 0
SHEET 2 N 3 THR E 46 SER E 51 -1 O VAL E 47 N LEU E 5
SHEET 3 N 3 ILE E 38 ASP E 43 -1 N SER E 41 O VAL E 48
SHEET 1 O 3 ASP E 12 ASP E 16 0
SHEET 2 O 3 ASP E 19 GLU E 23 -1 O GLU E 23 N ASP E 12
SHEET 3 O 3 SER E 28 ARG E 32 -1 O ARG E 31 N ILE E 20
SHEET 1 P 4 ASP E 123 ASP E 127 0
SHEET 2 P 4 GLU E 130 GLY E 135 -1 O SER E 134 N ASP E 123
SHEET 3 P 4 TRP E 80 MET E 84 -1 N TYR E 82 O VAL E 133
SHEET 4 P 4 ILE E 168 ARG E 170 -1 O THR E 169 N GLY E 83
SHEET 1 Q 3 GLN E 94 GLU E 98 0
SHEET 2 Q 3 GLU E 101 GLU E 105 -1 O VAL E 103 N ASN E 96
SHEET 3 Q 3 ARG E 114 THR E 117 -1 O ARG E 114 N ILE E 104
SHEET 1 R 4 VAL F 29 LYS F 30 0
SHEET 2 R 4 ALA F 95 VAL F 98 -1 O ALA F 97 N LYS F 30
SHEET 3 R 4 VAL F 48 ALA F 51 -1 N PHE F 49 O ALA F 96
SHEET 4 R 4 PHE F 74 VAL F 77 1 O VAL F 77 N VAL F 50
SHEET 1 S 2 ASN G 37 ILE G 38 0
SHEET 2 S 2 VAL G 89 GLY G 90 -1 O GLY G 90 N ASN G 37
SHEET 1 T 4 LYS H 84 LEU H 87 0
SHEET 2 T 4 GLN H 132 CYS H 138 -1 O TYR H 137 N LYS H 84
SHEET 3 T 4 VAL H 45 VAL H 51 -1 N LEU H 49 O PHE H 134
SHEET 4 T 4 CYS H 161 SER H 165 -1 O ASP H 164 N SER H 48
SHEET 1 U 3 VAL H 55 ARG H 58 0
SHEET 2 U 3 GLY H 122 VAL H 127 -1 O ALA H 125 N LEU H 57
SHEET 3 U 3 GLN H 93 LEU H 95 -1 N LEU H 95 O GLY H 122
SHEET 1 V 1 LEU I 8 VAL I 9 0
SHEET 1 W 3 VAL J 10 ASP J 13 0
SHEET 2 W 3 VAL J 36 VAL J 39 1 O VAL J 39 N VAL J 12
SHEET 3 W 3 ARG J 102 VAL J 103 1 O ARG J 102 N VAL J 38
SHEET 1 X 2 VAL J 45 THR J 47 0
SHEET 2 X 2 PHE J 129 THR J 131 -1 O VAL J 130 N ILE J 46
SHEET 1 Y 2 LEU K 12 GLU K 13 0
SHEET 2 Y 2 LYS K 46 ALA K 47 -1 O ALA K 47 N LEU K 12
SHEET 1 Z 6 LEU K 17 CYS K 20 0
SHEET 2 Z 6 ALA K 26 VAL K 34 -1 O LEU K 29 N ILE K 18
SHEET 3 Z 6 LYS K 52 GLY K 60 -1 O SER K 56 N LYS K 30
SHEET 4 Z 6 VAL K 68 ARG K 75 -1 O LEU K 69 N VAL K 55
SHEET 5 Z 6 ALA K 94 VAL K 98 -1 O ALA K 94 N VAL K 74
SHEET 6 Z 6 LEU K 17 CYS K 20 1 N THR K 19 O ALA K 95
SHEET 1 AA 4 ILE K 80 ARG K 81 0
SHEET 2 AA 4 ARG K 87 LYS K 89 -1 O VAL K 88 N ILE K 80
SHEET 3 AA 4 THR U 19 VAL U 22 1 O MET U 20 N ARG K 87
SHEET 4 AA 4 THR U 28 PHE U 31 -1 O THR U 29 N PHE U 21
SHEET 1 AB 2 ILE K 113 ALA K 114 0
SHEET 2 AB 2 ILE K 131 VAL K 132 1 O VAL K 132 N ILE K 113
SHEET 1 AC 2 ALA L 62 ASP L 65 0
SHEET 2 AC 2 VAL L 106 LEU L 109 1 O LEU L 109 N ILE L 64
SHEET 1 AD 3 ARG L 90 ASP L 92 0
SHEET 2 AD 3 THR L 119 ALA L 122 1 O ILE L 121 N VAL L 91
SHEET 3 AD 3 SER L 139 LEU L 142 1 O GLU L 141 N LEU L 120
SHEET 1 AE 4 VAL M 37 ILE M 40 0
SHEET 2 AE 4 VAL M 60 ARG M 68 -1 O ARG M 64 N GLU M 38
SHEET 3 AE 4 GLN M 126 ILE M 134 -1 O LEU M 133 N ILE M 61
SHEET 4 AE 4 ARG M 113 GLN M 122 -1 N TYR M 118 O GLU M 130
SHEET 1 AF 4 ASP N 56 THR N 57 0
SHEET 2 AF 4 VAL N 43 THR N 49 -1 N THR N 49 O ASP N 56
SHEET 3 AF 4 ARG N 33 LYS N 38 -1 N ARG N 33 O VAL N 48
SHEET 4 AF 4 VAL N 101 ASP N 103 1 O VAL N 101 N LEU N 34
SHEET 1 AG 4 ALA O 41 VAL O 43 0
SHEET 2 AG 4 THR O 57 VAL O 64 1 O LYS O 63 N ALA O 41
SHEET 3 AG 4 THR O 75 PHE O 81 1 O ALA O 77 N VAL O 58
SHEET 4 AG 4 GLU O 94 SER O 97 1 O VAL O 96 N VAL O 76
SHEET 1 AH 3 ALA O 41 VAL O 43 0
SHEET 2 AH 3 THR O 57 VAL O 64 1 O LYS O 63 N ALA O 41
SHEET 3 AH 3 VAL O 111 VAL O 113 1 O ARG O 112 N VAL O 59
SHEET 1 AI 2 VAL P 21 PHE P 23 0
SHEET 2 AI 2 ILE P 49 ALA P 51 -1 O GLN P 50 N TRP P 22
SHEET 1 AJ 5 LYS Q 80 VAL Q 86 0
SHEET 2 AJ 5 ALA Q 70 ASP Q 77 -1 N VAL Q 73 O ILE Q 84
SHEET 3 AJ 5 THR Q 60 GLN Q 67 -1 N GLN Q 67 O ALA Q 70
SHEET 4 AJ 5 LYS Q 38 LEU Q 41 -1 N VAL Q 39 O GLY Q 61
SHEET 5 AJ 5 LEU Q 91 ARG Q 93 -1 O ARG Q 92 N HIS Q 40
SHEET 1 AK 3 THR R 13 ARG R 21 0
SHEET 2 AK 3 SER R 138 GLU R 148 -1 O VAL R 141 N ARG R 21
SHEET 3 AK 3 THR R 110 GLN R 122 -1 N HIS R 113 O ILE R 146
SHEET 1 AL 2 VAL R 57 PRO R 58 0
SHEET 2 AL 2 GLY R 78 ARG R 79 -1 O ARG R 79 N VAL R 57
SHEET 1 AM 2 ARG R 125 PRO R 127 0
SHEET 2 AM 2 ALA R 133 ALA R 135 -1 O SER R 134 N LYS R 126
SHEET 1 AN 4 ILE S 5 PRO S 8 0
SHEET 2 AN 4 LYS S 23 VAL S 28 -1 O ALA S 27 N LYS S 6
SHEET 3 AN 4 LYS S 62 LEU S 68 -1 O VAL S 66 N LEU S 24
SHEET 4 AN 4 VAL S 49 ASN S 53 -1 N ASN S 53 O VAL S 65
SHEET 1 AO 2 ARG T 24 THR T 26 0
SHEET 2 AO 2 ASN T 39 ARG T 41 -1 O VAL T 40 N ALA T 25
SHEET 1 AP 4 VAL T 71 VAL T 74 0
SHEET 2 AP 4 GLU T 59 ASP T 66 -1 N ASN T 64 O HIS T 73
SHEET 3 AP 4 THR T 47 VAL T 50 -1 N VAL T 48 O GLY T 60
SHEET 4 AP 4 VAL T 96 ASP T 100 -1 O ARG T 97 N GLU T 49
SHEET 1 AQ 2 THR T 78 GLU T 80 0
SHEET 2 AQ 2 GLU T 86 PRO T 88 -1 O VAL T 87 N LEU T 79
SHEET 1 AR 5 LEU W 116 ARG W 117 0
SHEET 2 AR 5 HIS W 31 VAL W 35 -1 N CYS W 32 O LEU W 116
SHEET 3 AR 5 HIS W 2 GLN W 6 -1 N HIS W 2 O VAL W 35
SHEET 4 AR 5 VAL W 52 PHE W 54 -1 O ALA W 53 N VAL W 5
SHEET 5 AR 5 GLY W 139 LYS W 140 1 O GLY W 139 N PHE W 54
SHEET 1 AS 3 ARG X 8 PRO X 13 0
SHEET 2 AS 3 LYS X 69 PHE X 77 -1 O ILE X 70 N ILE X 12
SHEET 3 AS 3 GLU X 82 GLU X 86 -1 O GLU X 86 N ARG X 73
SHEET 1 AT 2 GLU Y 96 ALA Y 99 0
SHEET 2 AT 2 TYR Y 233 VAL Y 236 -1 O VAL Y 234 N GLN Y 98
SHEET 1 AU 2 GLU Y 183 VAL Y 187 0
SHEET 2 AU 2 GLU Y 201 ILE Y 205 1 O ARG Y 204 N VAL Y 185
SHEET 1 AV 3 VAL Z 47 ARG Z 49 0
SHEET 2 AV 3 ILE Z 54 CYS Z 57 -1 O GLN Z 56 N ASP Z 48
SHEET 3 AV 3 LYS Z 63 THR Z 65 -1 O PHE Z 64 N TRP Z 55
SHEET 1 AW 2 HIS 1 16 LYS 1 18 0
SHEET 2 AW 2 LYS 1 25 HIS 1 28 -1 O TYR 1 27 N THR 1 17
SHEET 1 AX 2 GLN 3 2 PRO 3 4 0
SHEET 2 AX 2 GLU 3 89 GLN 3 91 1 O GLU 3 89 N MET 3 3
SHEET 1 AY 3 ARG 3 6 CYS 3 11 0
SHEET 2 AY 3 GLU 3 16 LYS 3 24 -1 O HIS 3 20 N PHE 3 7
SHEET 3 AY 3 LEU 3 67 CYS 3 71 -1 O ARG 3 70 N GLU 3 21
LINK O3' U 02586 P OMU 02587 1555 1555 1.60
LINK O3' OMU 02587 P OMG 02588 1555 1555 1.62
LINK O3' OMG 02588 P U 02589 1555 1555 1.60
LINK O3' G 02618 P UR3 02619 1555 1555 1.61
LINK O3' UR3 02619 P U 02620 1555 1555 1.60
LINK O3' U 02620 P PSU 02621 1555 1555 1.61
LINK O3' PSU 02621 P A 02622 1555 1555 1.60
LINK MG MG 0 1 OP2 C 02533 1555 1555 2.27
LINK MG MG 0 1 OP2 C 02534 1555 1555 2.29
LINK OP1 G 0 28 MG MG 02934 1555 1555 2.12
LINK O2' C 0 40 NA NA 03037 1555 1555 2.44
LINK O2 C 0 40 NA NA 03037 1555 1555 2.05
LINK O4' G 0 41 NA NA 03037 1555 1555 2.71
LINK O6 G 0 56 NA NA 03056 1555 1555 2.98
LINK N3 A 0 59 NA NA 03056 1555 1555 2.69
LINK N7 G 0 61 NA NA 03056 1555 1555 2.43
LINK O6 G 0 61 NA NA 03056 1555 1555 2.87
LINK O2 U 0 108 NA NA 03057 1555 1555 2.98
LINK OP2 U 0 115 MG MG 02961 1555 1555 1.99
LINK O2 C 0 130 NA NA 03052 1555 1555 2.82
LINK O4' C 0 141 NA NA 03058 1555 1555 2.48
LINK O2 C 0 141 NA NA 03058 1555 1555 2.67
LINK O4 U 0 146 NA NA 03052 1555 1555 2.44
LINK OP1 C 0 162 MG MG 02976 1555 1555 2.28
LINK OP2 A 0 165 NA NA 03043 1555 1555 2.36
LINK O3' A 0 166 NA NA 03043 1555 1555 2.99
LINK OP1 A 0 167 NA NA 03043 1555 1555 2.24
LINK OP2 C 0 168 MG MG 02995 1555 1555 2.37
LINK O4 U 0 172 K K M 196 1555 1555 2.87
LINK OP2 G 0 175 MG MG 02981 1555 1555 2.20
LINK OP1 G 0 196 MG MG 02963 1555 1555 2.49
LINK N3 C 0 197 NA NA 03103 1555 1555 2.44
LINK O3' C 0 218 NA NA 03059 1555 1555 2.86
LINK O2' C 0 218 NA NA 03059 1555 1555 2.72
LINK O4' C 0 228 MG MG 02963 1555 1555 2.06
LINK OP1 C 0 240 MG MG 02949 1555 1555 1.97
LINK O2 C 0 342 NA NA 03070 1555 1555 2.56
LINK O6 G 0 386 NA NA 03060 1555 1555 2.28
LINK O6 G 0 387 NA NA 03060 1555 1555 2.06
LINK O2' U 0 391 NA NA 03086 1555 1555 2.91
LINK O2 U 0 391 NA NA 03086 1555 1555 2.86
LINK O4 U 0 392 NA NA 03090 1555 1555 2.77
LINK OP1 A 0 395 NA NA 03090 1555 1555 2.87
LINK O4 U 0 402 NA NA 03060 1555 1555 2.59
LINK N3 A 0 415 NA NA 03095 1555 1555 3.00
LINK O4' G 0 416 NA NA 03095 1555 1555 2.18
LINK OP2 U 0 454 NA NA 03081 1555 1555 2.70
LINK O6 G 0 456 MG MG 02926 1555 1555 2.07
LINK OP2 G 0 456 MG MG 02939 1555 1555 2.42
LINK OP1 A 0 459 MG MG 02926 1555 1555 1.88
LINK O6 G 0 464 NA NA 03088 1555 1555 2.34
LINK O6 G 0 471 MG MG 02975 1555 1555 2.12
LINK OP2 G 0 475 NA NA 03088 1555 1555 2.79
LINK OP1 C 0 478 NA NA 03081 1555 1555 2.75
LINK OP2 U 0 517 MG MG 03005 1555 1555 1.93
LINK OP1 U 0 533 MG MG 03002 1555 1555 2.27
LINK O6 G 0 544 NA NA 03087 1555 1555 2.88
LINK O4 U 0 611 NA NA 03087 1555 1555 2.61
LINK O4 U 0 612 NA NA 03087 1555 1555 2.42
LINK N7 G 0 622 NA NA 03063 1555 1555 2.62
LINK O4 U 0 623 NA NA 03063 1555 1555 2.80
LINK O4' U 0 624 NA NA 03073 1555 1555 2.97
LINK O6 G 0 627 MG MG 02924 1555 1555 2.17
LINK N3 A 0 630 NA NA 03035 1555 1555 2.59
LINK O2' A 0 631 NA NA 03035 1555 1555 2.83
LINK OP1 C 0 633 NA NA 03097 1555 1555 2.15
LINK N7 G 0 636 NA NA 03085 1555 1555 2.31
LINK OP2 A 0 643 NA NA 03034 1555 1555 2.96
LINK OP2 A 0 682 MG MG 03003 1555 1555 2.32
LINK OP2 G 0 683 MG MG 03003 1555 1555 2.08
LINK N7 G 0 683 NA NA 03068 1555 1555 2.64
LINK O2' U 0 768 NA NA 03075 1555 1555 2.75
LINK O2 U 0 768 NA NA 03075 1555 1555 2.98
LINK O3' A 0 776 NA NA 03053 1555 1555 2.97
LINK OP2 U 0 777 MG MG 02953 1555 1555 2.18
LINK OP2 U 0 777 NA NA 03053 1555 1555 2.87
LINK OP2 C 0 778 MG MG 02953 1555 1555 2.10
LINK O6 G 0 814 NA NA 03089 1555 1555 2.14
LINK O4 U 0 815 NA NA 03089 1555 1555 2.88
LINK O6 G 0 816 MG MG 02965 1555 1555 2.45
LINK O6 G 0 817 MG MG 02965 1555 1555 2.32
LINK O6 G 0 817 MG MG 03020 1555 1555 2.22
LINK OP2 C 0 822 MG MG 02928 1555 1555 2.33
LINK OP2 U 0 832 MG MG 02929 1555 1555 1.80
LINK O4 U 0 832 NA NA 03100 1555 1555 2.92
LINK OP1 G 0 836 MG MG 02932 1555 1555 1.76
LINK OP1 U 0 837 NA NA 03049 1555 1555 2.46
LINK OP1 U 0 837 NA NA 03082 1555 1555 2.97
LINK OP1 A 0 844 MG MG 02937 1555 1555 1.97
LINK OP1 G 0 854 MG MG 02928 1555 1555 2.23
LINK N7 G 0 854 MG MG 02933 1555 1555 1.91
LINK OP2 A 0 876 MG MG 02925 1555 1555 2.03
LINK OP2 G 0 877 MG MG 02925 1555 1555 2.37
LINK OP1 G 0 877 MG MG 02935 1555 1555 2.13
LINK OP1 C 0 880 MG MG 02994 1555 1555 2.09
LINK OP2 U 0 883 MG MG 02994 1555 1555 1.96
LINK O2' G 0 885 NA NA 03051 1555 1555 2.85
LINK OP2 G 0 887 NA NA 03096 1555 1555 2.30
LINK N7 G 0 892 NA NA 03069 1555 1555 2.98
LINK O2' C 0 896 NA NA 03044 1555 1555 2.83
LINK OP1 G 0 901 NA NA 03073 1555 1555 2.93
LINK OP1 U 0 919 MG MG 02930 1555 1555 1.85
LINK O4 U 0 919 NA NA 03093 1555 1555 2.71
LINK OP1 A 0 922 NA NA 03080 1555 1555 2.82
LINK O2' A 0 923 NA NA 03080 1555 1555 2.69
LINK O6 G 0 941 NA NA 03078 1555 1555 2.97
LINK O4 U 0 942 NA NA 03078 1555 1555 2.58
LINK OP2 G 0 956 MG MG 02958 1555 1555 2.03
LINK O3' C 01043 NA NA 03072 1555 1555 2.97
LINK OP2 C 01044 NA NA 03072 1555 1555 2.14
LINK OP2 G 01045 NA NA 03072 1555 1555 2.43
LINK OP2 C 01069 NA NA 03032 1555 1555 2.46
LINK N7 G 01072 NA NA 03032 1555 1555 2.94
LINK N7 G 01077 NA NA 03104 1555 1555 2.48
LINK OP1 A 01079 NA NA 03104 1555 1555 2.09
LINK OP2 A 01106 MG MG 03021 1555 1555 2.43
LINK OP2 A 01107 MG MG 03021 1555 1555 2.41
LINK OP2 U 01120 MG MG 02947 1555 1555 2.26
LINK OP2 U 01120 NA NA 03033 1555 1555 2.41
LINK OP2 G 01121 MG MG 02947 1555 1555 2.01
LINK O3' A 01133 NA NA H 172 1555 1555 2.81
LINK O2' A 01133 NA NA H 172 1555 1555 2.76
LINK OP2 U 01244 NA NA 03076 1555 1555 2.55
LINK OP2 C 01257 MG MG 03010 1555 1555 2.16
LINK OP1 A 01286 MG MG 02991 1555 1555 1.91
LINK OP1 A 01287 MG MG 02991 1555 1555 2.49
LINK OP1 A 01291 MG MG 02940 1555 1555 2.22
LINK OP2 G 01292 MG MG 02940 1555 1555 2.18
LINK OP1 A 01296 NA NA 03074 1555 1555 2.40
LINK OP2 A 01369 MG MG 02982 1555 1555 2.15
LINK O2 C 01394 NA NA 03038 1555 1555 2.43
LINK O3' G 01416 NA NA 03045 1555 1555 2.82
LINK OP1 C 01420 MG MG 02997 1555 1555 2.39
LINK OP2 C 01421 MG MG 02997 1555 1555 2.17
LINK O4 U 01432 NA NA 03038 1555 1555 2.89
LINK OP2 A 01437 MG MG 02998 1555 1555 2.42
LINK OP1 G 01438 MG MG 02997 1555 1555 2.13
LINK OP2 A 01448 MG MG 02950 1555 1555 2.15
LINK OP2 G 01484 MG MG 02957 1555 1555 1.88
LINK OP2 G 01489 MG MG 02983 1555 1555 2.31
LINK O6 G 01491 MG MG 02983 1555 1555 2.10
LINK OP1 U 01503 MG MG 02951 1555 1555 2.45
LINK O6 G 01576 NA NA 03094 1555 1555 2.90
LINK O4 U 01577 NA NA 03094 1555 1555 2.82
LINK O6 G 01618 NA NA 03094 1555 1555 2.66
LINK O6 G 01619 NA NA 03094 1555 1555 2.10
LINK O4 U 01677 MG MG 02950 1555 1555 2.24
LINK OP1 A 01678 MG MG 02938 1555 1555 2.36
LINK OP2 C 01679 MG MG 02938 1555 1555 2.00
LINK OP1 C 01679 MG MG 02951 1555 1555 2.48
LINK OP2 A 01684 MG MG 02996 1555 1555 1.91
LINK OP1 A 01689 MG MG 02937 1555 1555 1.96
LINK O6 G 01706 NA NA 03064 1555 1555 2.47
LINK O6 G 01707 NA NA 03064 1555 1555 2.58
LINK O2 U 01724 NA NA 03038 1555 1555 2.46
LINK O4 U 01741 NA NA 03067 1555 1555 2.54
LINK OP2 A 01742 MG MG 03000 1555 1555 2.24
LINK OP2 U 01748 MG MG 02955 1555 1555 2.48
LINK O4 U 01749 MG MG 02955 1555 1555 2.38
LINK OP2 A 01754 MG MG 02999 1555 1555 2.36
LINK N7 G 01794 MG MG 02968 1555 1555 2.34
LINK OP1 C 01830 MG MG 02942 1555 1555 2.20
LINK O3' U 01831 NA NA 03055 1555 1555 2.74
LINK O2' U 01831 NA NA 03055 1555 1555 2.09
LINK OP2 G 01832 NA NA 03091 1555 1555 2.08
LINK OP1 A 01836 MG MG 02927 1555 1555 1.96
LINK OP1 U 01838 MG MG 02927 1555 1555 2.48
LINK OP2 A 01839 MG MG 02927 1555 1555 2.23
LINK OP1 A 01839 MG MG 02929 1555 1555 2.25
LINK OP2 A 01840 MG MG 02929 1555 1555 2.35
LINK OP2 C 01844 MG MG 03008 1555 1555 2.47
LINK OP1 A 01845 MG MG 02986 1555 1555 2.34
LINK OP2 G 01873 MG MG A 241 1555 1555 1.89
LINK OP1 U 01883 MG MG 02978 1555 1555 2.48
LINK O6 G 01884 MG MG 02986 1555 1555 2.33
LINK O2 C 01894 NA NA 03061 1555 1555 2.61
LINK N7 G 01896 NA NA 03062 1555 1555 2.06
LINK O6 G 01896 NA NA 03062 1555 1555 2.92
LINK O4 U 01897 NA NA 03061 1555 1555 2.95
LINK O4 U 01897 NA NA 03062 1555 1555 2.72
LINK O6 G 01898 NA NA 03061 1555 1555 2.12
LINK O4 U 01939 NA NA 03061 1555 1555 2.67
LINK O6 G 01971 NA NA 03054 1555 1555 2.67
LINK OP2 A 02010 NA NA 03054 1555 1555 2.89
LINK O2' U 02012 MG MG 02978 1555 1555 2.44
LINK O4 U 02012 NA NA 03054 1555 1555 2.83
LINK O2' G 02033 NA NA 03067 1555 1555 2.54
LINK O3' C 02088 MG MG 02966 1555 1555 2.48
LINK OP1 A 02089 MG MG 02966 1555 1555 2.12
LINK N7 G 02093 NA NA 03036 1555 1555 2.69
LINK O6 G 02093 NA NA 03036 1555 1555 2.66
LINK N7 G 02094 NA NA 03036 1555 1555 2.60
LINK O6 G 02094 NA NA 03036 1555 1555 2.47
LINK OP2 G 02097 MG MG 02944 1555 1555 2.07
LINK O6 G 02102 K K 03031 1555 1555 2.46
LINK OP2 C 02105 MG MG 03019 1555 1555 2.35
LINK OP2 U 02109 NA NA 03080 1555 1555 2.84
LINK OP2 G 02110 NA NA 03083 1555 1555 2.43
LINK O4' G 02113 NA NA 03051 1555 1555 2.52
LINK OP1 U 02115 MG MG 02954 1555 1555 2.13
LINK OP1 C 02248 MG MG 02972 1555 1555 2.48
LINK OP2 C 02248 MG MG 02972 1555 1555 1.82
LINK OP1 U 02277 NA NA 03083 1555 1555 2.92
LINK O4 U 02282 MG MG 03016 1555 1555 2.24
LINK OP1 A 02303 MG MG 02956 1555 1555 1.97
LINK N7 G 02399 NA NA 03041 1555 1555 2.72
LINK OP1 C 02464 MG MG 02930 1555 1555 2.17
LINK OP1 A 02465 MG MG 02930 1555 1555 2.27
LINK O6 G 02482 K K 03031 1555 1555 2.40
LINK OP1 A 02483 MG MG 02924 1555 1555 2.04
LINK O6 G 02525 NA NA 03040 1555 1555 2.32
LINK OP1 C 02534 MG MG 02924 1555 1555 2.45
LINK OP2 G 02537 MG MG 02936 1555 1555 2.27
LINK OP2 U 02539 NA NA 03097 1555 1555 2.74
LINK O6 G 02540 NA NA 03066 1555 1555 2.36
LINK N7 G 02543 NA NA 03046 1555 1555 2.76
LINK N7 G 02544 NA NA 03046 1555 1555 2.83
LINK OP2 A 02553 MG MG 02959 1555 1555 1.94
LINK OP2 A 02568 MG MG 02987 1555 1555 2.24
LINK O6 G 02579 NA NA 03039 1555 1555 2.85
LINK OP1 G 02585 MG MG 02955 1555 1555 2.01
LINK O6 G 02585 NA NA 03101 1555 1555 2.85
LINK O4 U 02586 NA NA 03101 1555 1555 2.37
LINK O6 G 02592 NA NA 03101 1555 1555 2.80
LINK O2' U 02607 NA NA 03042 1555 1555 2.84
LINK OP1 C 02608 MG MG 02948 1555 1555 2.02
LINK OP1 G 02609 MG MG 02948 1555 1555 2.16
LINK N7 G 02609 MG MG 03024 1555 1555 1.85
LINK OP2 U 02610 MG MG 02948 1555 1555 1.91
LINK N7 G 02611 NA NA 03048 1555 1555 2.84
LINK O2' G 02611 NA NA 03066 1555 1555 2.85
LINK OP1 G 02611 NA NA 03079 1555 1555 2.90
LINK OP1 A 02612 MG MG 02931 1555 1555 1.91
LINK OP1 A 02612 NA NA 03079 1555 1555 2.89
LINK OP1 U 02615 MG MG 02932 1555 1555 2.20
LINK O4 U 02615 NA NA 03048 1555 1555 2.39
LINK OP2 G 02617 MG MG 02945 1555 1555 2.36
LINK OP2 G 02618 MG MG 02945 1555 1555 1.91
LINK OP1 G 02623 MG MG 02935 1555 1555 2.16
LINK OP1 A 02624 MG MG 02925 1555 1555 2.05
LINK O3' U 02659 NA NA R 155 1555 1555 2.87
LINK OP1 G 02660 NA NA 03065 1555 1555 2.50
LINK O2 U 02663 NA NA 03071 1555 1555 2.38
LINK OP2 A 02746 MG MG 02970 1555 1555 2.41
LINK OP2 G 02750 MG MG 02970 1555 1555 2.40
LINK OP1 A 02757 MG MG 02977 1555 1555 1.82
LINK O6 G 02773 NA NA 03102 1555 1555 2.66
LINK O3' A 02811 NA NA 03071 1555 1555 2.94
LINK O2' A 02811 NA NA 03071 1555 1555 2.57
LINK O2' A 02816 NA NA 03071 1555 1555 2.37
LINK OP2 G 02817 NA NA 03071 1555 1555 2.78
LINK MG MG 02966 O GLY R 65 1555 1555 2.18
LINK MG MG 02974 OP1 G 9 92 1555 1555 2.50
LINK MG MG 02977 O ASN B 335 1555 1555 2.03
LINK MG MG 02986 O ASN A 188 1555 1555 2.43
LINK NA NA 03065 O VAL R 72 1555 1555 2.50
LINK NA NA 03070 OG SER T 94 1555 1555 2.67
LINK NA NA 03070 OD1 ASN T 95 1555 1555 2.72
LINK NA NA 03074 O GLY L 14 1555 1555 2.64
LINK NA NA 03076 N THR J 47 1555 1555 2.91
LINK NA NA 03076 OG1 THR J 47 1555 1555 2.73
LINK O2 C 9 40 NA NA 9 124 1555 1555 2.75
LINK OP2 A 9 56 MG MG 9 123 1555 1555 2.11
LINK OP2 A 9 57 MG MG 9 123 1555 1555 2.33
LINK N3 A 9 57 NA NA 9 126 1555 1555 2.89
LINK OP2 A 9 57 NA NA 9 126 1555 1555 3.00
LINK N4 C 9 59 NA NA 9 126 1555 1555 2.97
LINK OD1 ASP A 26 MG MG A 241 1555 1555 2.50
LINK OD2 ASP A 26 MG MG A 241 1555 1555 2.15
LINK O ARG A 182 MG MG A 240 1555 1555 2.39
LINK O PHE A 201 NA NA A 242 1555 1555 2.77
LINK O GLY A 202 NA NA A 242 1555 1555 2.61
LINK O GLY A 203 NA NA A 242 1555 1555 2.80
LINK O HIS A 208 NA NA A 242 1555 1555 2.50
LINK OD1 ASP C 45 NA NA C 247 1555 1555 2.53
LINK OD2 ASP C 45 NA NA C 247 1555 1555 2.55
LINK O LYS C 96 NA NA C 247 1555 1555 2.75
LINK O ILE H 157 NA NA H 172 1555 1555 2.47
LINK O PRO H 159 NA NA H 172 1555 1555 2.79
LINK O VAL J 61 NA NA J 146 1555 1555 2.54
LINK O TYR J 69 NA NA J 146 1555 1555 2.94
LINK O ALA L 33 NA NA L 165 1555 1555 2.05
LINK OE1 GLU L 39 NA NA L 165 1555 1555 2.35
LINK OG SER M 106 NA NA M 197 1555 1555 2.59
LINK O PRO M 110 NA NA M 197 1555 1555 2.68
LINK O LEU M 112 NA NA M 197 1555 1555 2.69
LINK O ASP Q 20 NA NA Q 96 1555 1555 2.84
LINK OG SER Q 24 NA NA Q 96 1555 1555 2.72
LINK OG SER Q 46 NA NA Q 96 1555 1555 2.24
LINK O GLN R 61 NA NA R 156 1555 1555 2.99
LINK OD1 ASN R 63 NA NA R 156 1555 1555 2.85
LINK ND2 ASN R 63 NA NA R 156 1555 1555 2.88
LINK O VAL R 72 NA NA R 155 1555 1555 2.90
LINK O TRP R 75 NA NA R 155 1555 1555 2.34
LINK O SER T 114 MG MG T 120 1555 1555 2.49
LINK O ASP T 117 MG MG T 120 1555 1555 2.40
LINK O HIS Y 133 MG MG Y 241 1555 1555 2.24
LINK O GLY 3 45 MG MG 3 93 1555 1555 2.25
CISPEP 1 TRP A 186 PRO A 187 0 3.37
CISPEP 2 GLY B 14 PRO B 15 0 -0.46
CISPEP 3 ASN B 243 PRO B 244 0 1.20
CISPEP 4 VAL C 136 PRO C 137 0 1.33
CISPEP 5 GLN F 55 PRO F 56 0 0.49
CISPEP 6 ARG M 184 PRO M 185 0 0.48
SITE 1 BC1 1 GLN B 230
SITE 1 BC8 1 GLY C 86
SITE 1 CC9 1 THR S 54
SITE 1 EC2 1 GLY R 65
SITE 1 FC3 1 GLY B 337
SITE 1 FC4 1 ASN B 335
SITE 1 FC5 1 GLN A 207
SITE 1 FC6 1 GLN A 207
SITE 1 GC4 4 THR A 15 ARG A 182 GLY A 183 THR A 184
SITE 1 GC5 1 ASP A 26
SITE 1 GC6 2 ASN A 188 ARG A 190
SITE 1 GC8 1 ASN K 42
SITE 1 HC2 5 GLN T 37 ARG T 111 LEU T 112 SER T 114
SITE 2 HC2 5 ASP T 117
SITE 1 HC6 3 GLY 3 45 ILE 3 46 GLY 3 47
SITE 1 KC2 3 HIS Y 133 LYS Y 136 LYS Y 137
SITE 1 KC5 1 PRO M 185
SITE 1 KC6 1 LYS 3 54
SITE 1 LC1 1 ARG M 82
SITE 1 LC4 1 ARG L 8
SITE 1 LC5 2 ASP C 45 LYS C 96
SITE 1 MC1 4 TYR H 154 ILE H 157 THR H 158 PRO H 159
SITE 1 MC4 2 HIS S 7 GLU S 61
SITE 1 MC9 3 TRP 2 42 ASN 2 45 ASP 2 46
SITE 1 NC2 1 ASP L 36
SITE 1 NC4 1 ARG B 229
SITE 1 PC2 2 TRP R 75 ASP R 76
SITE 1 PC7 2 SER T 94 ASN T 95
SITE 1 PC9 4 PHE A 201 GLY A 202 GLY A 203 HIS A 208
SITE 1 QC1 4 ARG J 60 ILE J 63 TYR J 69 TYR J 71
SITE 1 QC2 4 SER M 106 PRO M 110 LEU M 112 ASP M 157
SITE 1 QC3 5 ASN Q 16 ASP Q 20 GLY Q 22 SER Q 24
SITE 2 QC3 5 SER Q 46
SITE 1 QC7 1 GLY L 14
SITE 1 QC9 2 ILE J 46 THR J 47
SITE 1 RC8 1 GLY C 66
SITE 1 RC9 1 LYS M 193
SITE 1 SC2 1 ARG C 55
SITE 1 SC4 1 ARG 3 42
SITE 1 TC2 2 HIS L 18 ARG L 21
SITE 1 TC4 5 GLY L 28 GLY L 31 ASP L 32 ALA L 33
SITE 2 TC4 5 GLU L 39
SITE 1 TC9 3 LYS R 60 GLN R 61 ASN R 63
SITE 1 UC1 4 CYS U 6 CYS U 9 CYS U 32 CYS U 36
SITE 1 UC2 4 CYS 1 19 CYS 1 22 CYS 1 34 CYS 1 37
SITE 1 UC3 3 CYS Z 39 CYS Z 42 CYS Z 60
SITE 1 UC4 3 ASN J 126 ILE J 127 LYS J 128
SITE 1 UC5 3 PRO J 88 LYS J 90 LYS J 91
SITE 1 UC7 2 LYS 3 24 ASP 3 66
SITE 1 UC9 2 LYS N 38 ASN N 107
SITE 1 VC1 3 PHE Q 52 HIS Q 53 PHE Q 56
SITE 1 VC2 3 LYS K 14 ILE K 32 SER K 33
SITE 1 VC4 1 HIS L 13
SITE 1 VC6 1 LYS J 56
SITE 1 VC7 1 ARG Y 122
SITE 1 VC8 2 SER M 106 ARG M 158
SITE 1 VC9 2 LYS B 224 HIS B 227
SITE 1 WC1 1 ARG Y 169
SITE 1 WC2 2 ASN J 65 GLY J 68
CRYST1 214.490 302.432 578.056 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004662 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003307 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001730 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
