HEADER RIBOSOME 26-OCT-09 2WWQ
TITLE E.COLI 70S RIBOSOME STALLED DURING TRANSLATION OF TNAC
TITLE 2 LEADER PEPTIDE. THIS FILE CONTAINS THE 50S, THE P-SITE
TITLE 3 TRNA AND THE TNAC LEADER PEPTIDE (PART 2 OF 2).
SPLIT 2WWL 2WWQ
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 23S RIBOSOMAL RNA;
COMPND 3 CHAIN: B;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: 5S RIBOSOMAL RNA;
COMPND 6 CHAIN: A;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: 50S RIBOSOMAL PROTEIN L1;
COMPND 9 CHAIN: 5;
COMPND 10 MOL_ID: 4;
COMPND 11 MOLECULE: 50S RIBOSOMAL PROTEIN L2;
COMPND 12 CHAIN: C;
COMPND 13 MOL_ID: 5;
COMPND 14 MOLECULE: 50S RIBOSOMAL PROTEIN L3;
COMPND 15 CHAIN: D;
COMPND 16 MOL_ID: 6;
COMPND 17 MOLECULE: 50S RIBOSOMAL PROTEIN L4;
COMPND 18 CHAIN: E;
COMPND 19 MOL_ID: 7;
COMPND 20 MOLECULE: 50S RIBOSOMAL PROTEIN L5;
COMPND 21 CHAIN: F;
COMPND 22 MOL_ID: 8;
COMPND 23 MOLECULE: 50S RIBOSOMAL PROTEIN L6;
COMPND 24 CHAIN: G;
COMPND 25 MOL_ID: 9;
COMPND 26 MOLECULE: 50S RIBOSOMAL PROTEIN L9;
COMPND 27 CHAIN: H;
COMPND 28 MOL_ID: 10;
COMPND 29 MOLECULE: 50S RIBOSOMAL PROTEIN L11;
COMPND 30 CHAIN: I;
COMPND 31 MOL_ID: 11;
COMPND 32 MOLECULE: 50S RIBOSOMAL PROTEIN L13;
COMPND 33 CHAIN: J;
COMPND 34 MOL_ID: 12;
COMPND 35 MOLECULE: 50S RIBOSOMAL PROTEIN L14;
COMPND 36 CHAIN: K;
COMPND 37 MOL_ID: 13;
COMPND 38 MOLECULE: 50S RIBOSOMAL PROTEIN L15;
COMPND 39 CHAIN: L;
COMPND 40 FRAGMENT: RESIDUES 2-144;
COMPND 41 MOL_ID: 14;
COMPND 42 MOLECULE: 50S RIBOSOMAL PROTEIN L16;
COMPND 43 CHAIN: M;
COMPND 44 MOL_ID: 15;
COMPND 45 MOLECULE: 50S RIBOSOMAL PROTEIN L17;
COMPND 46 CHAIN: N;
COMPND 47 MOL_ID: 16;
COMPND 48 MOLECULE: 50S RIBOSOMAL PROTEIN L18;
COMPND 49 CHAIN: O;
COMPND 50 FRAGMENT: RESIDUES 2-117;
COMPND 51 MOL_ID: 17;
COMPND 52 MOLECULE: 50S RIBOSOMAL PROTEIN L19;
COMPND 53 CHAIN: P;
COMPND 54 MOL_ID: 18;
COMPND 55 MOLECULE: 50S RIBOSOMAL PROTEIN L20;
COMPND 56 CHAIN: Q;
COMPND 57 MOL_ID: 19;
COMPND 58 MOLECULE: 50S RIBOSOMAL PROTEIN L21;
COMPND 59 CHAIN: R;
COMPND 60 MOL_ID: 20;
COMPND 61 MOLECULE: 50S RIBOSOMAL PROTEIN L22;
COMPND 62 CHAIN: S;
COMPND 63 MOL_ID: 21;
COMPND 64 MOLECULE: 50S RIBOSOMAL PROTEIN L23;
COMPND 65 CHAIN: T;
COMPND 66 MOL_ID: 22;
COMPND 67 MOLECULE: 50S RIBOSOMAL PROTEIN L24;
COMPND 68 CHAIN: U;
COMPND 69 MOL_ID: 23;
COMPND 70 MOLECULE: 50S RIBOSOMAL PROTEIN L25;
COMPND 71 CHAIN: W;
COMPND 72 MOL_ID: 24;
COMPND 73 MOLECULE: 50S RIBOSOMAL PROTEIN L27;
COMPND 74 CHAIN: Y;
COMPND 75 FRAGMENT: RESIDUES 7-85;
COMPND 76 MOL_ID: 25;
COMPND 77 MOLECULE: 50S RIBOSOMAL PROTEIN L28;
COMPND 78 CHAIN: 0;
COMPND 79 MOL_ID: 26;
COMPND 80 MOLECULE: 50S RIBOSOMAL PROTEIN L29;
COMPND 81 CHAIN: 1;
COMPND 82 MOL_ID: 27;
COMPND 83 MOLECULE: 50S RIBOSOMAL PROTEIN L30;
COMPND 84 CHAIN: 2;
COMPND 85 MOL_ID: 28;
COMPND 86 MOLECULE: 50S RIBOSOMAL PROTEIN L32;
COMPND 87 CHAIN: 3;
COMPND 88 MOL_ID: 29;
COMPND 89 MOLECULE: 50S RIBOSOMAL PROTEIN L33;
COMPND 90 CHAIN: 4;
COMPND 91 MOL_ID: 30;
COMPND 92 MOLECULE: 50S RIBOSOMAL PROTEIN L34;
COMPND 93 CHAIN: 6;
COMPND 94 MOL_ID: 31;
COMPND 95 MOLECULE: 50S RIBOSOMAL PROTEIN L35;
COMPND 96 CHAIN: 7;
COMPND 97 MOL_ID: 32;
COMPND 98 MOLECULE: 50S RIBOSOMAL PROTEIN L36;
COMPND 99 CHAIN: 8;
COMPND 100 MOL_ID: 33;
COMPND 101 MOLECULE: MRNA;
COMPND 102 CHAIN: X;
COMPND 103 MOL_ID: 34;
COMPND 104 MOLECULE: P-SITE TRNA 2;
COMPND 105 CHAIN: V;
COMPND 106 MOL_ID: 35;
COMPND 107 MOLECULE: NASCENT TNAC LEADER PEPTIDE 5;
COMPND 108 CHAIN: Z
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 6 ORGANISM_TAXID: 562;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 9 ORGANISM_TAXID: 562;
SOURCE 10 MOL_ID: 4;
SOURCE 11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 12 ORGANISM_TAXID: 562;
SOURCE 13 MOL_ID: 5;
SOURCE 14 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 15 ORGANISM_TAXID: 562;
SOURCE 16 MOL_ID: 6;
SOURCE 17 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 18 ORGANISM_TAXID: 562;
SOURCE 19 MOL_ID: 7;
SOURCE 20 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 21 ORGANISM_TAXID: 562;
SOURCE 22 MOL_ID: 8;
SOURCE 23 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 24 ORGANISM_TAXID: 562;
SOURCE 25 MOL_ID: 9;
SOURCE 26 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 27 ORGANISM_TAXID: 562;
SOURCE 28 MOL_ID: 10;
SOURCE 29 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 30 ORGANISM_TAXID: 562;
SOURCE 31 MOL_ID: 11;
SOURCE 32 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 33 ORGANISM_TAXID: 562;
SOURCE 34 MOL_ID: 12;
SOURCE 35 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 36 ORGANISM_TAXID: 562;
SOURCE 37 MOL_ID: 13;
SOURCE 38 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 39 ORGANISM_TAXID: 562;
SOURCE 40 MOL_ID: 14;
SOURCE 41 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 42 ORGANISM_TAXID: 562;
SOURCE 43 MOL_ID: 15;
SOURCE 44 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 45 ORGANISM_TAXID: 562;
SOURCE 46 MOL_ID: 16;
SOURCE 47 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 48 ORGANISM_TAXID: 562;
SOURCE 49 MOL_ID: 17;
SOURCE 50 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 51 ORGANISM_TAXID: 562;
SOURCE 52 MOL_ID: 18;
SOURCE 53 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 54 ORGANISM_TAXID: 562;
SOURCE 55 MOL_ID: 19;
SOURCE 56 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 57 ORGANISM_TAXID: 562;
SOURCE 58 MOL_ID: 20;
SOURCE 59 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 60 ORGANISM_TAXID: 562;
SOURCE 61 MOL_ID: 21;
SOURCE 62 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 63 ORGANISM_TAXID: 562;
SOURCE 64 MOL_ID: 22;
SOURCE 65 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 66 ORGANISM_TAXID: 562;
SOURCE 67 MOL_ID: 23;
SOURCE 68 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 69 ORGANISM_TAXID: 562;
SOURCE 70 MOL_ID: 24;
SOURCE 71 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 72 ORGANISM_TAXID: 562;
SOURCE 73 MOL_ID: 25;
SOURCE 74 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 75 ORGANISM_TAXID: 562;
SOURCE 76 MOL_ID: 26;
SOURCE 77 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 78 ORGANISM_TAXID: 562;
SOURCE 79 MOL_ID: 27;
SOURCE 80 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 81 ORGANISM_TAXID: 562;
SOURCE 82 MOL_ID: 28;
SOURCE 83 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 84 ORGANISM_TAXID: 562;
SOURCE 85 MOL_ID: 29;
SOURCE 86 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 87 ORGANISM_TAXID: 562;
SOURCE 88 MOL_ID: 30;
SOURCE 89 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 90 ORGANISM_TAXID: 562;
SOURCE 91 MOL_ID: 31;
SOURCE 92 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 93 ORGANISM_TAXID: 562;
SOURCE 94 MOL_ID: 32;
SOURCE 95 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 96 ORGANISM_TAXID: 562;
SOURCE 97 MOL_ID: 33;
SOURCE 98 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 99 ORGANISM_TAXID: 562;
SOURCE 100 MOL_ID: 34;
SOURCE 101 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 102 ORGANISM_TAXID: 562;
SOURCE 103 MOL_ID: 35;
SOURCE 104 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 105 ORGANISM_TAXID: 562
KEYWDS RIBOSOMAL PROTEIN, RIBONUCLEOPROTEIN, NUCLEOTIDE-BINDING,
KEYWDS 2 PROTEIN BIOSYNTHESIS, TRANSLATION, ZINC-FINGER, TNAC, 70S
KEYWDS 3 RIBOSOME, STALLING, RIBOSOME
EXPDTA ELECTRON MICROSCOPY
AUTHOR B.SEIDELT,C.A.INNIS,D.N.WILSON,M.GARTMANN,J.ARMACHE,E.VILLA,
AUTHOR 2 L.G.TRABUCO,T.BECKER,T.MIELKE,K.SCHULTEN,T.A.STEITZ,
AUTHOR 3 R.BECKMANN
REVDAT 1 14-APR-10 2WWQ 0
JRNL AUTH B.SEIDELT,C.A.INNIS,D.N.WILSON,M.GARTMANN,
JRNL AUTH 2 J.ARMACHE,E.VILLA,L.G.TRABUCO,T.BECKER,T.MIELKE,
JRNL AUTH 3 K.SCHULTEN,T.A.STEITZ,R.BECKMANN
JRNL TITL STRUCTURAL INSIGHT INTO NASCENT POLYPEPTIDE CHAIN-
JRNL TITL 2 MEDIATED TRANSLATIONAL STALLING.
JRNL REF SCIENCE V. 326 1412 2009
JRNL REFN ISSN 0036-8075
JRNL PMID 19933110
JRNL DOI 10.1126/SCIENCE.1177662
REMARK 2
REMARK 2 RESOLUTION. 5.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : SPIDER
REMARK 3 RECONSTRUCTION SCHEMA : PROJECTION MATCHING
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 3FIH,3FIK
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FITTING
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : MDFF
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 5.8
REMARK 3 NUMBER OF PARTICLES : 263000
REMARK 3 CTF CORRECTION METHOD : DEFOCUS GROUP VOLUMES
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 2WWQ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-OCT-09.
REMARK 100 THE PDBE ID CODE IS EBI-41520.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : VITREOUS ICE
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : NULL
REMARK 245 NAME OF SAMPLE : TNAC STALLED 70S RIBOSOME
REMARK 245 WITH P-SITE TRNA.
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : HOLEY CARBON
REMARK 245 SAMPLE VITRIFICATION DETAILS : VITRIFICATION 1 --
REMARK 245 CRYOGEN ETHANE
REMARK 245 SAMPLE BUFFER : 50MM TRIS-HCL PH 8.0,
REMARK 245 10MM MG-ACETATE, 50MM KCL,
REMARK 245 10MM NH4CL, 2MM EGTA,
REMARK 245 2MM L-TRYPTOPHAN AND 10MM
REMARK 245 DDT
REMARK 245 PH : NULL
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 128
REMARK 245 TEMPERATURE (KELVIN) : 95
REMARK 245 MICROSCOPE MODEL : FEI TECNAI F30
REMARK 245 DETECTOR TYPE : KODAK SO163
REMARK 245 MINIMUM DEFOCUS (NM) : 1000
REMARK 245 MAXIMUM DEFOCUS (NM) : 3000
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.26
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 20
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 39000
REMARK 245 CALIBRATED MAGNIFICATION : 38900
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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 QUATERNARY STRUCTURE FOR THIS ENTRY: 35MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, K,
REMARK 350 AND CHAINS: L, M, N, O, P, Q, R, S, T, U, V,
REMARK 350 AND CHAINS: W, X, Y, Z, 1, 2, 3, 4, 5, 6, 7
REMARK 350 AND CHAINS: 8, 0
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 C A 3
REMARK 465 G A 6
REMARK 465 VAL G 8
REMARK 465 ALA U 1
REMARK 465 ARG U 5
REMARK 465 ASP U 7
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 GLU K 121 O
REMARK 470 5MU V 54 C5M
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 N2 G V 35 C2 C X 18 2.08
REMARK 500 O3' A V 76 C ALA Z 24 1.32
REMARK 500 O3' A V 76 O ALA Z 24 1.20
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 ARG 0 10 NE ARG 0 10 CZ 0.081
REMARK 500 ARG 0 71 NE ARG 0 71 CZ 0.091
REMARK 500 GLU 1 12 CB GLU 1 12 CG 0.120
REMARK 500 ARG 1 47 CZ ARG 1 47 NH2 0.095
REMARK 500 ARG 2 30 CZ ARG 2 30 NH1 0.085
REMARK 500 ARG 3 16 NE ARG 3 16 CZ 0.081
REMARK 500 TYR 3 47 CG TYR 3 47 CD2 0.079
REMARK 500 ARG 3 49 NE ARG 3 49 CZ 0.086
REMARK 500 PHE 4 19 CG PHE 4 19 CD1 0.099
REMARK 500 TYR 5 21 CG TYR 5 21 CD2 0.089
REMARK 500 GLY 5 49 N GLY 5 49 CA 0.090
REMARK 500 ARG 5 74 NE ARG 5 74 CZ 0.084
REMARK 500 GLY 5 159 CA GLY 5 159 C -0.114
REMARK 500 ARG 6 12 CD ARG 6 12 NE 0.120
REMARK 500 ARG 6 12 NE ARG 6 12 CZ 0.079
REMARK 500 ARG 6 28 CD ARG 6 28 NE 0.117
REMARK 500 ARG 7 12 CZ ARG 7 12 NH1 0.088
REMARK 500 ARG 7 39 CZ ARG 7 39 NH1 0.084
REMARK 500 ARG 7 39 NE ARG 7 39 CZ 0.102
REMARK 500 ARG 8 24 CD ARG 8 24 NE 0.108
REMARK 500 CYS 8 27 CB CYS 8 27 SG 0.129
REMARK 500 G A 2 C2' G A 2 C1' -0.096
REMARK 500 G A 2 N7 G A 2 C5 -0.037
REMARK 500 C A 4 C2 C A 4 N3 0.076
REMARK 500 C A 4 C4' C A 4 C3' 0.078
REMARK 500 C A 4 C5 C A 4 C6 -0.052
REMARK 500 C A 4 N1 C A 4 C6 -0.042
REMARK 500 C A 4 N3 C A 4 C4 0.054
REMARK 500 U A 5 C2 U A 5 N3 0.066
REMARK 500 U A 5 N3 U A 5 C4 0.074
REMARK 500 U A 5 P U A 5 O5' -0.061
REMARK 500 G A 7 C2 G A 7 N3 0.054
REMARK 500 G A 7 C5' G A 7 C4' -0.048
REMARK 500 C A 8 C2' C A 8 C1' -0.052
REMARK 500 C A 8 N3 C A 8 C4 0.050
REMARK 500 G A 9 N1 G A 9 C2 0.053
REMARK 500 G A 9 N9 G A 9 C4 -0.050
REMARK 500 G A 10 N1 G A 10 C2 0.055
REMARK 500 G A 10 N7 G A 10 C5 -0.070
REMARK 500 G A 10 N9 G A 10 C8 0.058
REMARK 500 C A 11 C2 C A 11 N3 -0.050
REMARK 500 C A 11 N1 C A 11 C6 0.070
REMARK 500 C A 11 N3 C A 11 C4 0.055
REMARK 500 C A 12 C2' C A 12 C1' -0.058
REMARK 500 G A 13 C2 G A 13 N2 0.072
REMARK 500 G A 13 C8 G A 13 N7 -0.070
REMARK 500 G A 13 N9 G A 13 C4 -0.049
REMARK 500 C A 12 O3' G A 13 P -0.126
REMARK 500 A A 15 C5 A A 15 C6 -0.062
REMARK 500 A A 15 N7 A A 15 C5 -0.052
REMARK 500
REMARK 500 THIS ENTRY HAS 6650 BOND DEVIATIONS.
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 ARG 0 10 NE - CZ - NH2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG 0 17 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG 0 26 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG 0 26 NE - CZ - NH2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 PHE 0 45 CB - CG - CD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 PHE 0 45 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG 0 49 NE - CZ - NH1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG 0 49 NE - CZ - NH2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG 0 56 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ASP 0 59 CB - CG - OD2 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ASP 0 64 O - C - N ANGL. DEV. = 10.4 DEGREES
REMARK 500 ARG 0 73 NE - CZ - NH1 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG 0 73 NE - CZ - NH2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG 1 7 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG 1 7 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 PHE 1 26 CB - CG - CD1 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ARG 1 29 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG 1 47 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP 1 49 CB - CG - OD1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG 1 52 NE - CZ - NH2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 THR 2 9 CA - CB - CG2 ANGL. DEV. = -10.0 DEGREES
REMARK 500 ARG 2 30 NE - CZ - NH2 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG 2 44 NE - CZ - NH1 ANGL. DEV. = -4.8 DEGREES
REMARK 500 PHE 2 52 CB - CG - CD1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 PHE 2 52 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG 3 12 NE - CZ - NH2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 SER 3 28 N - CA - CB ANGL. DEV. = 11.7 DEGREES
REMARK 500 ARG 3 39 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 THR 3 43 CA - CB - CG2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 TYR 3 48 CG - CD1 - CE1 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ARG 3 49 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG 3 49 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG 3 51 N - CA - CB ANGL. DEV. = 14.5 DEGREES
REMARK 500 ARG 3 51 NE - CZ - NH2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG 4 5 N - CA - CB ANGL. DEV. = 15.2 DEGREES
REMARK 500 ARG 4 5 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 TYR 4 20 CB - CG - CD1 ANGL. DEV. = -8.3 DEGREES
REMARK 500 TYR 4 20 CB - CG - CD2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 PHE 4 38 CB - CG - CD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG 4 43 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG 5 7 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG 5 7 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 MET 5 8 CG - SD - CE ANGL. DEV. = -10.7 DEGREES
REMARK 500 ARG 5 9 NE - CZ - NH1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 TYR 5 21 CB - CG - CD1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 PHE 5 38 CB - CG - CD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP 5 43 CB - CG - OD1 ANGL. DEV. = 8.5 DEGREES
REMARK 500 ASP 5 43 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ASP 5 51 CB - CG - OD1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG 5 53 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 12521 ANGLE DEVIATIONS.
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 ARG 0 2 51.11 -100.77
REMARK 500 THR 0 7 -14.91 -153.15
REMARK 500 ARG 0 17 106.95 60.21
REMARK 500 HIS 0 19 14.06 -67.35
REMARK 500 ALA 0 20 20.15 -150.90
REMARK 500 LEU 0 21 44.20 77.00
REMARK 500 THR 0 24 125.87 -173.98
REMARK 500 ARG 0 26 -11.17 -155.71
REMARK 500 ARG 0 27 123.84 76.12
REMARK 500 LEU 0 32 123.47 68.41
REMARK 500 GLU 0 40 -3.04 80.11
REMARK 500 GLU 0 42 -21.64 -152.13
REMARK 500 THR 0 65 -36.37 -159.27
REMARK 500 LEU 0 70 -53.78 69.87
REMARK 500 LYS 1 2 -95.32 -69.03
REMARK 500 ARG 1 23 42.16 73.61
REMARK 500 GLU 1 24 -9.03 -159.94
REMARK 500 LEU 1 37 127.64 56.88
REMARK 500 GLN 1 38 65.33 -100.09
REMARK 500 GLN 1 39 74.43 -108.22
REMARK 500 VAL 1 46 -60.63 70.62
REMARK 500 ARG 1 48 41.30 -72.84
REMARK 500 ASP 1 49 -44.26 -149.05
REMARK 500 LEU 1 57 -50.92 74.03
REMARK 500 GLN 2 8 -69.07 -103.84
REMARK 500 ARG 2 10 -136.56 -149.70
REMARK 500 LYS 2 18 36.21 -84.87
REMARK 500 HIS 2 19 -58.70 -132.40
REMARK 500 ARG 2 29 3.20 -160.47
REMARK 500 GLN 3 3 170.55 -55.01
REMARK 500 ASN 3 5 156.60 62.85
REMARK 500 ALA 3 20 164.77 168.36
REMARK 500 HIS 3 41 -161.00 -160.57
REMARK 500 ALA 3 44 13.77 91.50
REMARK 500 ASP 3 45 16.47 -148.07
REMARK 500 TYR 3 48 -26.53 -142.82
REMARK 500 ARG 3 49 27.67 -168.55
REMARK 500 ARG 3 51 104.81 76.81
REMARK 500 ALA 3 55 12.94 -151.10
REMARK 500 LYS 4 24 148.38 -170.10
REMARK 500 THR 4 28 13.59 -148.10
REMARK 500 LYS 4 29 78.04 -169.64
REMARK 500 LEU 4 33 140.98 69.55
REMARK 500 LYS 4 37 -162.29 179.00
REMARK 500 ARG 4 43 46.57 39.55
REMARK 500 LYS 4 49 -169.76 -100.60
REMARK 500 GLU 4 50 159.76 74.23
REMARK 500 LEU 5 4 78.47 -115.32
REMARK 500 ARG 5 53 -117.49 -98.01
REMARK 500 LYS 5 54 -64.68 -127.27
REMARK 500
REMARK 500 THIS ENTRY HAS 555 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 ALA 0 52 LYS 0 53 145.27
REMARK 500 SER 4 13 ALA 4 14 137.16
REMARK 500 LYS 4 37 PHE 4 38 -148.64
REMARK 500 THR 5 144 VAL 5 145 145.52
REMARK 500 ARG 6 39 ALA 6 40 -149.00
REMARK 500 GLU D 89 PHE D 90 -147.40
REMARK 500 THR D 151 PRO D 152 140.23
REMARK 500 LYS E 57 LYS E 58 -147.58
REMARK 500 ARG E 88 PRO E 89 149.21
REMARK 500 GLU F 18 PHE F 19 -139.54
REMARK 500 ASP F 173 PHE F 174 148.67
REMARK 500 THR G 83 LYS G 84 -145.81
REMARK 500 VAL H 31 PRO H 32 37.33
REMARK 500 GLY J 112 PRO J 113 -145.64
REMARK 500 ARG K 70 ARG K 71 148.16
REMARK 500 ARG K 71 PRO K 72 -51.23
REMARK 500 ASN K 88 ASN K 89 -148.10
REMARK 500 GLY M 37 ARG M 38 -148.51
REMARK 500 THR N 95 ARG N 96 148.21
REMARK 500 ASN P 51 ARG P 52 -138.41
REMARK 500 VAL P 60 ARG P 61 136.70
REMARK 500 GLY Q 6 VAL Q 7 149.24
REMARK 500 PHE Y 68 GLU Y 69 138.93
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 ARG 0 36 0.09 SIDE CHAIN
REMARK 500 ARG 0 49 0.10 SIDE CHAIN
REMARK 500 ARG 0 73 0.13 SIDE CHAIN
REMARK 500 PHE 1 26 0.09 SIDE CHAIN
REMARK 500 ARG 3 12 0.09 SIDE CHAIN
REMARK 500 ARG 3 51 0.09 SIDE CHAIN
REMARK 500 TYR 4 48 0.07 SIDE CHAIN
REMARK 500 ARG 5 9 0.08 SIDE CHAIN
REMARK 500 ARG 5 60 0.08 SIDE CHAIN
REMARK 500 ARG 5 71 0.09 SIDE CHAIN
REMARK 500 ARG 5 164 0.12 SIDE CHAIN
REMARK 500 TYR 5 208 0.15 SIDE CHAIN
REMARK 500 ARG 6 12 0.08 SIDE CHAIN
REMARK 500 ARG 6 28 0.10 SIDE CHAIN
REMARK 500 HIS 7 25 0.07 SIDE CHAIN
REMARK 500 G A 2 0.10 SIDE CHAIN
REMARK 500 C A 4 0.13 SIDE CHAIN
REMARK 500 U A 5 0.10 SIDE CHAIN
REMARK 500 G A 7 0.07 SIDE CHAIN
REMARK 500 G A 10 0.06 SIDE CHAIN
REMARK 500 C A 12 0.08 SIDE CHAIN
REMARK 500 G A 16 0.09 SIDE CHAIN
REMARK 500 C A 17 0.10 SIDE CHAIN
REMARK 500 G A 18 0.07 SIDE CHAIN
REMARK 500 G A 21 0.09 SIDE CHAIN
REMARK 500 G A 24 0.13 SIDE CHAIN
REMARK 500 C A 26 0.09 SIDE CHAIN
REMARK 500 C A 27 0.08 SIDE CHAIN
REMARK 500 C A 31 0.07 SIDE CHAIN
REMARK 500 C A 37 0.10 SIDE CHAIN
REMARK 500 U A 40 0.08 SIDE CHAIN
REMARK 500 G A 41 0.09 SIDE CHAIN
REMARK 500 G A 44 0.12 SIDE CHAIN
REMARK 500 A A 45 0.10 SIDE CHAIN
REMARK 500 C A 47 0.05 SIDE CHAIN
REMARK 500 C A 49 0.10 SIDE CHAIN
REMARK 500 G A 51 0.08 SIDE CHAIN
REMARK 500 G A 54 0.17 SIDE CHAIN
REMARK 500 A A 58 0.06 SIDE CHAIN
REMARK 500 A A 59 0.10 SIDE CHAIN
REMARK 500 G A 61 0.07 SIDE CHAIN
REMARK 500 G A 64 0.06 SIDE CHAIN
REMARK 500 A A 66 0.08 SIDE CHAIN
REMARK 500 C A 68 0.10 SIDE CHAIN
REMARK 500 C A 70 0.12 SIDE CHAIN
REMARK 500 C A 71 0.08 SIDE CHAIN
REMARK 500 G A 72 0.12 SIDE CHAIN
REMARK 500 G A 75 0.09 SIDE CHAIN
REMARK 500 A A 78 0.07 SIDE CHAIN
REMARK 500 G A 79 0.07 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 1488 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 SER Y 34 11.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 LEU 0 32 23.8 L L OUTSIDE RANGE
REMARK 500 SER 1 10 23.1 L L OUTSIDE RANGE
REMARK 500 ARG 1 23 25.0 L L OUTSIDE RANGE
REMARK 500 VAL 1 46 24.9 L L OUTSIDE RANGE
REMARK 500 LEU 1 57 24.0 L L OUTSIDE RANGE
REMARK 500 THR 2 9 22.1 L L OUTSIDE RANGE
REMARK 500 ASP 2 39 24.6 L L OUTSIDE RANGE
REMARK 500 ALA 3 44 23.5 L L OUTSIDE RANGE
REMARK 500 ARG 3 51 19.9 L L OUTSIDE RANGE
REMARK 500 GLU 4 50 24.2 L L OUTSIDE RANGE
REMARK 500 THR 5 144 24.7 L L OUTSIDE RANGE
REMARK 500 VAL 5 178 22.9 L L OUTSIDE RANGE
REMARK 500 GLU 5 187 23.2 L L OUTSIDE RANGE
REMARK 500 LYS 5 210 23.8 L L OUTSIDE RANGE
REMARK 500 A B1088 -45.3 D D OUTSIDE RANGE
REMARK 500 ALA C 154 24.9 L L OUTSIDE RANGE
REMARK 500 THR D 91 24.3 L L OUTSIDE RANGE
REMARK 500 VAL D 107 24.7 L L OUTSIDE RANGE
REMARK 500 ILE E 148 17.0 L L OUTSIDE RANGE
REMARK 500 LEU F 48 23.5 L L OUTSIDE RANGE
REMARK 500 ALA F 58 24.6 L L OUTSIDE RANGE
REMARK 500 ARG F 79 23.7 L L OUTSIDE RANGE
REMARK 500 ILE G 140 23.1 L L OUTSIDE RANGE
REMARK 500 LEU H 15 24.3 L L OUTSIDE RANGE
REMARK 500 THR H 96 24.1 L L OUTSIDE RANGE
REMARK 500 VAL J 105 21.1 L L OUTSIDE RANGE
REMARK 500 LYS L 29 22.3 L L OUTSIDE RANGE
REMARK 500 THR L 30 24.2 L L OUTSIDE RANGE
REMARK 500 LYS L 36 24.0 L L OUTSIDE RANGE
REMARK 500 GLU L 86 24.8 L L OUTSIDE RANGE
REMARK 500 THR L 117 24.0 L L OUTSIDE RANGE
REMARK 500 VAL M 57 24.4 L L OUTSIDE RANGE
REMARK 500 ASP O 2 23.5 L L OUTSIDE RANGE
REMARK 500 GLU O 55 24.5 L L OUTSIDE RANGE
REMARK 500 LEU O 106 24.8 L L OUTSIDE RANGE
REMARK 500 THR P 59 21.8 L L OUTSIDE RANGE
REMARK 500 THR P 103 23.9 L L OUTSIDE RANGE
REMARK 500 ILE Q 73 22.1 L L OUTSIDE RANGE
REMARK 500 ARG Q 91 23.6 L L OUTSIDE RANGE
REMARK 500 GLU R 16 22.2 L L OUTSIDE RANGE
REMARK 500 PHE R 53 24.3 L L OUTSIDE RANGE
REMARK 500 HIS S 9 24.2 L L OUTSIDE RANGE
REMARK 500 VAL S 45 23.5 L L OUTSIDE RANGE
REMARK 500 ASN S 61 21.9 L L OUTSIDE RANGE
REMARK 500 THR S 72 24.4 L L OUTSIDE RANGE
REMARK 500 LYS T 19 24.1 L L OUTSIDE RANGE
REMARK 500 THR T 29 24.2 L L OUTSIDE RANGE
REMARK 500 THR T 86 24.6 L L OUTSIDE RANGE
REMARK 500 SER W 17 20.5 L L OUTSIDE RANGE
REMARK 500 ASP W 45 23.3 L L OUTSIDE RANGE
REMARK 500
REMARK 500 THIS ENTRY HAS 51 CHIRALITY DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "WA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DFU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF E.COLI RIBOSOMAL
REMARK 900 PROTEIN L25 COMPLEXEDWITH A 5S RRNA FRAGMENT
REMARK 900 AT 1.8 A RESOLUTION
REMARK 900 RELATED ID: 2J28 RELATED DB: PDB
REMARK 900 MODEL OF E. COLI SRP BOUND TO 70S RNCS
REMARK 900 RELATED ID: 2VHM RELATED DB: PDB
REMARK 900 STRUCTURE OF PDF BINDING HELIX IN COMPLEX
REMARK 900 WITH THE RIBOSOME
REMARK 900 RELATED ID: 2VRH RELATED DB: PDB
REMARK 900 STRUCTURE OF THE E. COLI TRIGGER FACTOR
REMARK 900 BOUND TO A TRANSLATING RIBOSOME
REMARK 900 RELATED ID: 1B75 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF RIBOSOMAL PROTEIN L25
REMARK 900 FROMESCHERICHIA COLI
REMARK 900 RELATED ID: 487D RELATED DB: PDB
REMARK 900 SEVEN RIBOSOMAL PROTEINS FITTED TO A CRYO-
REMARK 900 ELECTRONMICROSCOPIC MAP OF THE LARGE 50S
REMARK 900 SUBUNIT AT 7.5 ANGSTROMSRESOLUTION
REMARK 900 RELATED ID: 2AW4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE BACTERIAL RIBOSOME
REMARK 900 FROMESCHERICHIA COLI AT 3.5 A RESOLUTION.
REMARK 900 THIS FILE CONTAINSTHE 50S SUBUNIT OF ONE
REMARK 900 70S RIBOSOME. THE ENTIRE CRYSTALSTRUCTURE
REMARK 900 CONTAINS TWO 70S RIBOSOMES AND IS DESCRIBED
REMARK 900 INREMARK 400.
REMARK 900 RELATED ID: 1P86 RELATED DB: PDB
REMARK 900 REAL SPACE REFINED COORDINATES OF THE 50S
REMARK 900 SUBUNIT FITTEDINTO THE LOW RESOLUTION CRYO-
REMARK 900 EM MAP OF THE INITIATION-LIKESTATE OF E.
REMARK 900 COLI 70S RIBOSOME
REMARK 900 RELATED ID: 1P85 RELATED DB: PDB
REMARK 900 REAL SPACE REFINED COORDINATES OF THE 50S
REMARK 900 SUBUNIT FITTEDINTO THE LOW RESOLUTION CRYO-
REMARK 900 EM MAP OF THE EF-G.GTP STATEOF E. COLI
REMARK 900 70S RIBOSOME
REMARK 900 RELATED ID: 1D6K RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF THE 5S RRNA E-
REMARK 900 LOOP/L25 COMPLEX
REMARK 900 RELATED ID: 2VHN RELATED DB: PDB
REMARK 900 STRUCTURE OF PDF BINDING HELIX IN COMPLEX
REMARK 900 WITH THE RIBOSOME
REMARK 900 RELATED ID: 2AWB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE BACTERIAL RIBOSOME
REMARK 900 FROMESCHERICHIA COLI AT 3.5 A RESOLUTION.
REMARK 900 THIS FILE CONTAINSTHE 50S SUBUNIT OF THE
REMARK 900 SECOND 70S RIBOSOME. THE ENTIRECRYSTAL
REMARK 900 STRUCTURE CONTAINS TWO 70S RIBOSOMES AND
REMARK 900 IS DESCRIBED IN REMARK 400.
REMARK 900 RELATED ID: 2WWL RELATED DB: PDB
REMARK 900 E.COLI 70S RIBOSOME STALLED DURING
REMARK 900 TRANSLATION OF TNAC LEADER PEPTIDE
REMARK 900 RELATED ID: EMD-1657 RELATED DB: EMDB
REMARK 900 STRUCTURAL INSIGHT INTO NASCENT POLYPEPTIDE
REMARK 900 CHAIN-MEDIATED TRANSLATIONAL STALLING
DBREF 2WWQ 0 1 77 UNP P0A7M2 RL28_ECOLI 2 78
DBREF 2WWQ 1 1 63 UNP P0A7M6 RL29_ECOLI 1 63
DBREF 2WWQ 2 1 58 UNP P0AG51 RL30_ECOLI 2 59
DBREF 2WWQ 3 1 56 UNP P0A7N4 RL32_ECOLI 2 57
DBREF 2WWQ 4 3 52 UNP P0A7N9 RL33_ECOLI 4 53
DBREF 2WWQ 5 1 234 UNP P0A7L0 RL1_ECOLI 1 234
DBREF 2WWQ 6 1 46 UNP P0A7P5 RL34_ECOLI 1 46
DBREF 2WWQ 7 1 64 UNP P0A7Q1 RL35_ECOLI 2 65
DBREF 2WWQ 8 1 38 UNP P0A7Q6 RL36_ECOLI 1 38
DBREF1 2WWQ A 2 118 GB CP001396
DBREF2 2WWQ A 238859724 228756 228872
DBREF1 2WWQ B 1 2903 GB CP001396
DBREF2 2WWQ B 238859724 2613011 2610109
DBREF 2WWQ C 1 271 UNP P60422 RL2_ECOLI 2 272
DBREF 2WWQ D 1 209 UNP P60438 RL3_ECOLI 1 209
DBREF 2WWQ E 1 201 UNP P60723 RL4_ECOLI 1 201
DBREF 2WWQ F 1 178 UNP P62399 RL5_ECOLI 2 179
DBREF 2WWQ G 1 176 UNP P0AG55 RL6_ECOLI 2 177
DBREF 2WWQ H 1 149 UNP P0A7R1 RL9_ECOLI 1 149
DBREF 2WWQ I 1 141 UNP P0A7J7 RL11_ECOLI 2 142
DBREF 2WWQ J 1 142 UNP P0AA10 RL13_ECOLI 1 142
DBREF 2WWQ K 1 121 UNP P0ADY3 RL14_ECOLI 2 122
DBREF 2WWQ L 2 144 UNP P02413 RL15_ECOLI 2 144
DBREF 2WWQ M 1 136 UNP P0ADY7 RL16_ECOLI 1 136
DBREF 2WWQ N 1 120 UNP P0AG44 RL17_ECOLI 1 120
DBREF 2WWQ O 2 117 UNP P0C018 RL18_ECOLI 2 117
DBREF 2WWQ P 1 114 UNP P0A7K6 RL19_ECOLI 2 115
DBREF 2WWQ Q 1 117 UNP P0A7L3 RL20_ECOLI 2 118
DBREF 2WWQ R 1 103 UNP P0AG48 RL21_ECOLI 1 103
DBREF 2WWQ S 1 110 UNP P61175 RL22_ECOLI 1 110
DBREF 2WWQ T 1 93 UNP P0ADZ0 RL23_ECOLI 1 93
DBREF 2WWQ U 1 102 UNP P60624 RL24_ECOLI 2 103
DBREF1 2WWQ V 1 76 GB CP001396
DBREF2 2WWQ V 238859724 2170038 2170114
DBREF 2WWQ W 1 94 UNP P68919 RL25_ECOLI 1 94
DBREF 2WWQ X 12 22 PDB 2WWQ 2WWQ 12 22
DBREF 2WWQ Y 6 84 UNP P0A7L8 RL27_ECOLI 7 85
DBREF 2WWQ Z 5 24 PDB 2WWQ 2WWQ 5 24
SEQRES 1 0 77 SER ARG VAL CYS GLN VAL THR GLY LYS ARG PRO VAL THR
SEQRES 2 0 77 GLY ASN ASN ARG SER HIS ALA LEU ASN ALA THR LYS ARG
SEQRES 3 0 77 ARG PHE LEU PRO ASN LEU HIS SER HIS ARG PHE TRP VAL
SEQRES 4 0 77 GLU SER GLU LYS ARG PHE VAL THR LEU ARG VAL SER ALA
SEQRES 5 0 77 LYS GLY MET ARG VAL ILE ASP LYS LYS GLY ILE ASP THR
SEQRES 6 0 77 VAL LEU ALA GLU LEU ARG ALA ARG GLY GLU LYS TYR
SEQRES 1 1 63 MET LYS ALA LYS GLU LEU ARG GLU LYS SER VAL GLU GLU
SEQRES 2 1 63 LEU ASN THR GLU LEU LEU ASN LEU LEU ARG GLU GLN PHE
SEQRES 3 1 63 ASN LEU ARG MET GLN ALA ALA SER GLY GLN LEU GLN GLN
SEQRES 4 1 63 SER HIS LEU LEU LYS GLN VAL ARG ARG ASP VAL ALA ARG
SEQRES 5 1 63 VAL LYS THR LEU LEU ASN GLU LYS ALA GLY ALA
SEQRES 1 2 58 ALA LYS THR ILE LYS ILE THR GLN THR ARG SER ALA ILE
SEQRES 2 2 58 GLY ARG LEU PRO LYS HIS LYS ALA THR LEU LEU GLY LEU
SEQRES 3 2 58 GLY LEU ARG ARG ILE GLY HIS THR VAL GLU ARG GLU ASP
SEQRES 4 2 58 THR PRO ALA ILE ARG GLY MET ILE ASN ALA VAL SER PHE
SEQRES 5 2 58 MET VAL LYS VAL GLU GLU
SEQRES 1 3 56 ALA VAL GLN GLN ASN LYS PRO THR ARG SER LYS ARG GLY
SEQRES 2 3 56 MET ARG ARG SER HIS ASP ALA LEU THR ALA VAL THR SER
SEQRES 3 3 56 LEU SER VAL ASP LYS THR SER GLY GLU LYS HIS LEU ARG
SEQRES 4 3 56 HIS HIS ILE THR ALA ASP GLY TYR TYR ARG GLY ARG LYS
SEQRES 5 3 56 VAL ILE ALA LYS
SEQRES 1 4 50 GLY ILE ARG GLU LYS ILE LYS LEU VAL SER SER ALA GLY
SEQRES 2 4 50 THR GLY HIS PHE TYR THR THR THR LYS ASN LYS ARG THR
SEQRES 3 4 50 LYS PRO GLU LYS LEU GLU LEU LYS LYS PHE ASP PRO VAL
SEQRES 4 4 50 VAL ARG GLN HIS VAL ILE TYR LYS GLU ALA LYS
SEQRES 1 5 234 MET ALA LYS LEU THR LYS ARG MET ARG VAL ILE ARG GLU
SEQRES 2 5 234 LYS VAL ASP ALA THR LYS GLN TYR ASP ILE ASN GLU ALA
SEQRES 3 5 234 ILE ALA LEU LEU LYS GLU LEU ALA THR ALA LYS PHE VAL
SEQRES 4 5 234 GLU SER VAL ASP VAL ALA VAL ASN LEU GLY ILE ASP ALA
SEQRES 5 5 234 ARG LYS SER ASP GLN ASN VAL ARG GLY ALA THR VAL LEU
SEQRES 6 5 234 PRO HIS GLY THR GLY ARG SER VAL ARG VAL ALA VAL PHE
SEQRES 7 5 234 THR GLN GLY ALA ASN ALA GLU ALA ALA LYS ALA ALA GLY
SEQRES 8 5 234 ALA GLU LEU VAL GLY MET GLU ASP LEU ALA ASP GLN ILE
SEQRES 9 5 234 LYS LYS GLY GLU MET ASN PHE ASP VAL VAL ILE ALA SER
SEQRES 10 5 234 PRO ASP ALA MET ARG VAL VAL GLY GLN LEU GLY GLN VAL
SEQRES 11 5 234 LEU GLY PRO ARG GLY LEU MET PRO ASN PRO LYS VAL GLY
SEQRES 12 5 234 THR VAL THR PRO ASN VAL ALA GLU ALA VAL LYS ASN ALA
SEQRES 13 5 234 LYS ALA GLY GLN VAL ARG TYR ARG ASN ASP LYS ASN GLY
SEQRES 14 5 234 ILE ILE HIS THR THR ILE GLY LYS VAL ASP PHE ASP ALA
SEQRES 15 5 234 ASP LYS LEU LYS GLU ASN LEU GLU ALA LEU LEU VAL ALA
SEQRES 16 5 234 LEU LYS LYS ALA LYS PRO THR GLN ALA LYS GLY VAL TYR
SEQRES 17 5 234 ILE LYS LYS VAL SER ILE SER THR THR MET GLY ALA GLY
SEQRES 18 5 234 VAL ALA VAL ASP GLN ALA GLY LEU SER ALA SER VAL ASN
SEQRES 1 6 46 MET LYS ARG THR PHE GLN PRO SER VAL LEU LYS ARG ASN
SEQRES 2 6 46 ARG SER HIS GLY PHE ARG ALA ARG MET ALA THR LYS ASN
SEQRES 3 6 46 GLY ARG GLN VAL LEU ALA ARG ARG ARG ALA LYS GLY ARG
SEQRES 4 6 46 ALA ARG LEU THR VAL SER LYS
SEQRES 1 7 64 PRO LYS ILE LYS THR VAL ARG GLY ALA ALA LYS ARG PHE
SEQRES 2 7 64 LYS LYS THR GLY LYS GLY GLY PHE LYS HIS LYS HIS ALA
SEQRES 3 7 64 ASN LEU ARG HIS ILE LEU THR LYS LYS ALA THR LYS ARG
SEQRES 4 7 64 LYS ARG HIS LEU ARG PRO LYS ALA MET VAL SER LYS GLY
SEQRES 5 7 64 ASP LEU GLY LEU VAL ILE ALA CYS LEU PRO TYR ALA
SEQRES 1 8 38 MET LYS VAL ARG ALA SER VAL LYS LYS LEU CYS ARG ASN
SEQRES 2 8 38 CYS LYS ILE VAL LYS ARG ASP GLY VAL ILE ARG VAL ILE
SEQRES 3 8 38 CYS SER ALA GLU PRO LYS HIS LYS GLN ARG GLN GLY
SEQRES 1 A 117 G C C U G G C G G C C G U
SEQRES 2 A 117 A G C G C G G U G G U C C
SEQRES 3 A 117 C A C C U G A C C C C A U
SEQRES 4 A 117 G C C G A A C U C A G A A
SEQRES 5 A 117 G U G A A A C G C C G U A
SEQRES 6 A 117 G C G C C G A U G G U A G
SEQRES 7 A 117 U G U G G G G U C U C C C
SEQRES 8 A 117 C A U G C G A G A G U A G
SEQRES 9 A 117 G G A A C U G C C A G G C
SEQRES 1 B 2903 G G U U A A G C G A C U A
SEQRES 2 B 2903 A G C G U A C A C G G U G
SEQRES 3 B 2903 G A U G C C C U G G C A G
SEQRES 4 B 2903 U C A G A G G C G A U G A
SEQRES 5 B 2903 A G G A C G U G C U A A U
SEQRES 6 B 2903 C U G C G A U A A G C G U
SEQRES 7 B 2903 C G G U A A G G U G A U A
SEQRES 8 B 2903 U G A A C C G U U A U A A
SEQRES 9 B 2903 C C G G C G A U U U C C G
SEQRES 10 B 2903 A A U G G G G A A A C C C
SEQRES 11 B 2903 A G U G U G U U U C G A C
SEQRES 12 B 2903 A C A C U A U C A U U A A
SEQRES 13 B 2903 C U G A A U C C A U A G G
SEQRES 14 B 2903 U U A A U G A G G C G A A
SEQRES 15 B 2903 C C G G G G G A A C U G A
SEQRES 16 B 2903 A A C A U C U A A G U A C
SEQRES 17 B 2903 C C C G A G G A A A A G A
SEQRES 18 B 2903 A A U C A A C C G A G A U
SEQRES 19 B 2903 U C C C C C A G U A G C G
SEQRES 20 B 2903 G C G A G C G A A C G G G
SEQRES 21 B 2903 G A G C A G C C C A G A G
SEQRES 22 B 2903 C C U G A A U C A G U G U
SEQRES 23 B 2903 G U G U G U U A G U G G A
SEQRES 24 B 2903 A G C G U C U G G A A A G
SEQRES 25 B 2903 G C G C G C G A U A C A G
SEQRES 26 B 2903 G G U G A C A G C C C C G
SEQRES 27 B 2903 U A C A C A A A A A U G C
SEQRES 28 B 2903 A C A U G C U G U G A G C
SEQRES 29 B 2903 U C G A U G A G U A G G G
SEQRES 30 B 2903 C G G G A C A C G U G G U
SEQRES 31 B 2903 A U C C U G U C U G A A U
SEQRES 32 B 2903 A U G G G G G G A C C A U
SEQRES 33 B 2903 C C U C C A A G G C U A A
SEQRES 34 B 2903 A U A C U C C U G A C U G
SEQRES 35 B 2903 A C C G A U A G U G A A C
SEQRES 36 B 2903 C A G U A C C G U G A G G
SEQRES 37 B 2903 G A A A G G C G A A A A G
SEQRES 38 B 2903 A A C C C C G G C G A G G
SEQRES 39 B 2903 G G A G U G A A A A A G A
SEQRES 40 B 2903 A C C U G A A A C C G U G
SEQRES 41 B 2903 U A C G U A C A A G C A G
SEQRES 42 B 2903 U G G G A G C A C G C U U
SEQRES 43 B 2903 A G G C G U G U G A C U G
SEQRES 44 B 2903 C G U A C C U U U U G U A
SEQRES 45 B 2903 U A A U G G G U C A G C G
SEQRES 46 B 2903 A C U U A U A U U C U G U
SEQRES 47 B 2903 A G C A A G G U U A A C C
SEQRES 48 B 2903 G A A U A G G G G A G C C
SEQRES 49 B 2903 G A A G G G A A A C C G A
SEQRES 50 B 2903 G U C U U A A C U G G G C
SEQRES 51 B 2903 G U U A A G U U G C A G G
SEQRES 52 B 2903 G U A U A G A C C C G A A
SEQRES 53 B 2903 A C C C G G U G A U C U A
SEQRES 54 B 2903 G C C A U G G G C A G G U
SEQRES 55 B 2903 U G A A G G U U G G G U A
SEQRES 56 B 2903 A C A C U A A C U G G A G
SEQRES 57 B 2903 G A C C G A A C C G A C U
SEQRES 58 B 2903 A A U G U U G A A A A A U
SEQRES 59 B 2903 U A G C G G A U G A C U U
SEQRES 60 B 2903 G U G G C U G G G G G U G
SEQRES 61 B 2903 A A A G G C C A A U C A A
SEQRES 62 B 2903 A C C G G G A G A U A G C
SEQRES 63 B 2903 U G G U U C U C C C C G A
SEQRES 64 B 2903 A A G C U A U U U A G G U
SEQRES 65 B 2903 A G C G C C U C G U G A A
SEQRES 66 B 2903 U U C A U C U C C G G G G
SEQRES 67 B 2903 G U A G A G C A C U G U U
SEQRES 68 B 2903 U C G G C A A G G G G G U
SEQRES 69 B 2903 C A U C C C G A C U U A C
SEQRES 70 B 2903 C A A C C C G A U G C A A
SEQRES 71 B 2903 A C U G C G A A U A C C G
SEQRES 72 B 2903 G A G A A U G U U A U C A
SEQRES 73 B 2903 C G G G A G A C A C A C G
SEQRES 74 B 2903 G C G G G U G C U A A C G
SEQRES 75 B 2903 U C C G U C G U G A A G A
SEQRES 76 B 2903 G G G A A A C A A C C C A
SEQRES 77 B 2903 G A C C G C C A G C U A A
SEQRES 78 B 2903 G G U C C C A A A G U C A
SEQRES 79 B 2903 U G G U U A A G U G G G A
SEQRES 80 B 2903 A A C G A U G U G G G A A
SEQRES 81 B 2903 G G C C C A G A C A G C C
SEQRES 82 B 2903 A G G A U G U U G G C U U
SEQRES 83 B 2903 A G A A G C A G C C A U C
SEQRES 84 B 2903 A U U U A A A G A A A G C
SEQRES 85 B 2903 G U A A U A G C U C A C U
SEQRES 86 B 2903 G G U C G A G U C G G C C
SEQRES 87 B 2903 U G C G C G G A A G A U G
SEQRES 88 B 2903 U A A C G G G G C U A A A
SEQRES 89 B 2903 C C A U G C A C C G A A G
SEQRES 90 B 2903 C U G C G G C A G C G A C
SEQRES 91 B 2903 G C U U A U G C G U U G U
SEQRES 92 B 2903 U G G G U A G G G G A G C
SEQRES 93 B 2903 G U U C U G U A A G C C U
SEQRES 94 B 2903 G C G A A G G U G U G C U
SEQRES 95 B 2903 G U G A G G C A U G C U G
SEQRES 96 B 2903 G A G G U A U C A G A A G
SEQRES 97 B 2903 U G C G A A U G C U G A C
SEQRES 98 B 2903 A U A A G U A A C G A U A
SEQRES 99 B 2903 A A G C G G G U G A A A A
SEQRES 100 B 2903 G C C C G C U C G C C G G
SEQRES 101 B 2903 A A G A C C A A G G G U U
SEQRES 102 B 2903 C C U G U C C A A C G U U
SEQRES 103 B 2903 A A U C G G G G C A G G G
SEQRES 104 B 2903 U G A G U C G A C C C C U
SEQRES 105 B 2903 A A G G C G A G G C C G A
SEQRES 106 B 2903 A A G G C G U A G U C G A
SEQRES 107 B 2903 U G G G A A A C A G G U U
SEQRES 108 B 2903 A A U A U U C C U G U A C
SEQRES 109 B 2903 U U G G U G U U A C U G C
SEQRES 110 B 2903 G A A G G G G G G A C G G
SEQRES 111 B 2903 A G A A G G C U A U G U U
SEQRES 112 B 2903 G G C C G G G C G A C G G
SEQRES 113 B 2903 U U G U C C C G G U U U A
SEQRES 114 B 2903 A G C G U G U A G G C U G
SEQRES 115 B 2903 G U U U U C C A G G C A A
SEQRES 116 B 2903 A U C C G G A A A A U C A
SEQRES 117 B 2903 A G G C U G A G G C G U G
SEQRES 118 B 2903 A U G A C G A G G C A C U
SEQRES 119 B 2903 A C G G U G C U G A A G C
SEQRES 120 B 2903 A A C A A A U G C C C U G
SEQRES 121 B 2903 C U U C C A G G A A A A G
SEQRES 122 B 2903 C C U C U A A G C A U C A
SEQRES 123 B 2903 G G U A A C A U C A A A U
SEQRES 124 B 2903 C G U A C C C C A A A C C
SEQRES 125 B 2903 G A C A C A G G U G G U C
SEQRES 126 B 2903 A G G U A G A G A A U A C
SEQRES 127 B 2903 C A A G G C G C U U G A G
SEQRES 128 B 2903 A G A A C U C G G G U G A
SEQRES 129 B 2903 A G G A A C U A G G C A A
SEQRES 130 B 2903 A A U G G U G C C G U A A
SEQRES 131 B 2903 C U U C G G G A G A A G G
SEQRES 132 B 2903 C A C G C U G A U A U G U
SEQRES 133 B 2903 A G G U G A G G U C C C U
SEQRES 134 B 2903 C G C G G A U G G A G C U
SEQRES 135 B 2903 G A A A U C A G U C G A A
SEQRES 136 B 2903 G A U A C C A G C U G G C
SEQRES 137 B 2903 U G C A A C U G U U U A U
SEQRES 138 B 2903 U A A A A A C A C A G C A
SEQRES 139 B 2903 C U G U G C A A A C A C G
SEQRES 140 B 2903 A A A G U G G A C G U A U
SEQRES 141 B 2903 A C G G U G U G A C G C C
SEQRES 142 B 2903 U G C C C G G U G C C G G
SEQRES 143 B 2903 A A G G U U A A U U G A U
SEQRES 144 B 2903 G G G G U U A G C G C A A
SEQRES 145 B 2903 G C G A A G C U C U U G A
SEQRES 146 B 2903 U C G A A G C C C C G G U
SEQRES 147 B 2903 A A A C G G C G G C C G U
SEQRES 148 B 2903 A A C U A U A A C G G U C
SEQRES 149 B 2903 C U A A G G U A G C G A A
SEQRES 150 B 2903 A U U C C U U G U C G G G
SEQRES 151 B 2903 U A A G U U C C G A C C U
SEQRES 152 B 2903 G C A C G A A U G G C G U
SEQRES 153 B 2903 A A U G A U G G C C A G G
SEQRES 154 B 2903 C U G U C U C C A C C C G
SEQRES 155 B 2903 A G A C U C A G U G A A A
SEQRES 156 B 2903 U U G A A C U C G C U G U
SEQRES 157 B 2903 G A A G A U G C A G U G U
SEQRES 158 B 2903 A C C C G C G G C A A G A
SEQRES 159 B 2903 C G G A A A G A C C C C G
SEQRES 160 B 2903 U G A A C C U U U A C U A
SEQRES 161 B 2903 U A G C U U G A C A C U G
SEQRES 162 B 2903 A A C A U U G A G C C U U
SEQRES 163 B 2903 G A U G U G U A G G A U A
SEQRES 164 B 2903 G G U G G G A G G C U U U
SEQRES 165 B 2903 G A A G U G U G G A C G C
SEQRES 166 B 2903 C A G U C U G C A U G G A
SEQRES 167 B 2903 G C C G A C C U U G A A A
SEQRES 168 B 2903 U A C C A C C C U U U A A
SEQRES 169 B 2903 U G U U U G A U G U U C U
SEQRES 170 B 2903 A A C G U U G A C C C G U
SEQRES 171 B 2903 A A U C C G G G U U G C G
SEQRES 172 B 2903 G A C A G U G U C U G G U
SEQRES 173 B 2903 G G G U A G U U U G A C U
SEQRES 174 B 2903 G G G G C G G U C U C C U
SEQRES 175 B 2903 C C U A A A G A G U A A C
SEQRES 176 B 2903 G G A G G A G C A C G A A
SEQRES 177 B 2903 G G U U G G C U A A U C C
SEQRES 178 B 2903 U G G U C G G A C A U C A
SEQRES 179 B 2903 G G A G G U U A G U G C A
SEQRES 180 B 2903 A U G G C A U A A G C C A
SEQRES 181 B 2903 G C U U G A C U G C G A G
SEQRES 182 B 2903 C G U G A C G G C G C G A
SEQRES 183 B 2903 G C A G G U G C G A A A G
SEQRES 184 B 2903 C A G G U C A U A G U G A
SEQRES 185 B 2903 U C C G G U G G U U C U G
SEQRES 186 B 2903 A A U G G A A G G G C C A
SEQRES 187 B 2903 U C G C U C A A C G G A U
SEQRES 188 B 2903 A A A A G G U A C U C C G
SEQRES 189 B 2903 G G G A U A A C A G G C U
SEQRES 190 B 2903 G A U A C C G C C C A A G
SEQRES 191 B 2903 A G U U C A U A U C G A C
SEQRES 192 B 2903 G G C G G U G U U U G G C
SEQRES 193 B 2903 A C C U C G A U G U C G G
SEQRES 194 B 2903 C U C A U C A C A U C C U
SEQRES 195 B 2903 G G G G C U G A A G U A G
SEQRES 196 B 2903 G U C C C A A G G G U A U
SEQRES 197 B 2903 G G C U G U U C G C C A U
SEQRES 198 B 2903 U U A A A G U G G U A C G
SEQRES 199 B 2903 C G A G C U G G G U U U A
SEQRES 200 B 2903 G A A C G U C G U G A G A
SEQRES 201 B 2903 C A G U U C G G U C C C U
SEQRES 202 B 2903 A U C U G C C G U G G G C
SEQRES 203 B 2903 G C U G G A G A A C U G A
SEQRES 204 B 2903 G G G G G G C U G C U C C
SEQRES 205 B 2903 U A G U A C G A G A G G A
SEQRES 206 B 2903 C C G G A G U G G A C G C
SEQRES 207 B 2903 A U C A C U G G U G U U C
SEQRES 208 B 2903 G G G U U G U C A U G C C
SEQRES 209 B 2903 A A U G G C A C U G C C C
SEQRES 210 B 2903 G G U A G C U A A A U G C
SEQRES 211 B 2903 G G A A G A G A U A A G U
SEQRES 212 B 2903 G C U G A A A G C A U C U
SEQRES 213 B 2903 A A G C A C G A A A C U U
SEQRES 214 B 2903 G C C C C G A G A U G A G
SEQRES 215 B 2903 U U C U C C C U G A C C C
SEQRES 216 B 2903 U U U A A G G G U C C U G
SEQRES 217 B 2903 A A G G A A C G U U G A A
SEQRES 218 B 2903 G A C G A C G A C G U U G
SEQRES 219 B 2903 A U A G G C C G G G U G U
SEQRES 220 B 2903 G U A A G C G C A G C G A
SEQRES 221 B 2903 U G C G U U G A G C U A A
SEQRES 222 B 2903 C C G G U A C U A A U G A
SEQRES 223 B 2903 A C C G U G A G G C U U A
SEQRES 224 B 2903 A C C U
SEQRES 1 C 271 ALA VAL VAL LYS CYS LYS PRO THR SER PRO GLY ARG ARG
SEQRES 2 C 271 HIS VAL VAL LYS VAL VAL ASN PRO GLU LEU HIS LYS GLY
SEQRES 3 C 271 LYS PRO PHE ALA PRO LEU LEU GLU LYS ASN SER LYS SER
SEQRES 4 C 271 GLY GLY ARG ASN ASN ASN GLY ARG ILE THR THR ARG HIS
SEQRES 5 C 271 ILE GLY GLY GLY HIS LYS GLN ALA TYR ARG ILE VAL ASP
SEQRES 6 C 271 PHE LYS ARG ASN LYS ASP GLY ILE PRO ALA VAL VAL GLU
SEQRES 7 C 271 ARG LEU GLU TYR ASP PRO ASN ARG SER ALA ASN ILE ALA
SEQRES 8 C 271 LEU VAL LEU TYR LYS ASP GLY GLU ARG ARG TYR ILE LEU
SEQRES 9 C 271 ALA PRO LYS GLY LEU LYS ALA GLY ASP GLN ILE GLN SER
SEQRES 10 C 271 GLY VAL ASP ALA ALA ILE LYS PRO GLY ASN THR LEU PRO
SEQRES 11 C 271 MET ARG ASN ILE PRO VAL GLY SER THR VAL HIS ASN VAL
SEQRES 12 C 271 GLU MET LYS PRO GLY LYS GLY GLY GLN LEU ALA ARG SER
SEQRES 13 C 271 ALA GLY THR TYR VAL GLN ILE VAL ALA ARG ASP GLY ALA
SEQRES 14 C 271 TYR VAL THR LEU ARG LEU ARG SER GLY GLU MET ARG LYS
SEQRES 15 C 271 VAL GLU ALA ASP CYS ARG ALA THR LEU GLY GLU VAL GLY
SEQRES 16 C 271 ASN ALA GLU HIS MET LEU ARG VAL LEU GLY LYS ALA GLY
SEQRES 17 C 271 ALA ALA ARG TRP ARG GLY VAL ARG PRO THR VAL ARG GLY
SEQRES 18 C 271 THR ALA MET ASN PRO VAL ASP HIS PRO HIS GLY GLY GLY
SEQRES 19 C 271 GLU GLY ARG ASN PHE GLY LYS HIS PRO VAL THR PRO TRP
SEQRES 20 C 271 GLY VAL GLN THR LYS GLY LYS LYS THR ARG SER ASN LYS
SEQRES 21 C 271 ARG THR ASP LYS PHE ILE VAL ARG ARG ARG SER
SEQRES 1 D 209 MET ILE GLY LEU VAL GLY LYS LYS VAL GLY MET THR ARG
SEQRES 2 D 209 ILE PHE THR GLU ASP GLY VAL SER ILE PRO VAL THR VAL
SEQRES 3 D 209 ILE GLU VAL GLU ALA ASN ARG VAL THR GLN VAL LYS ASP
SEQRES 4 D 209 LEU ALA ASN ASP GLY TYR ARG ALA ILE GLN VAL THR THR
SEQRES 5 D 209 GLY ALA LYS LYS ALA ASN ARG VAL THR LYS PRO GLU ALA
SEQRES 6 D 209 GLY HIS PHE ALA LYS ALA GLY VAL GLU ALA GLY ARG GLY
SEQRES 7 D 209 LEU TRP GLU PHE ARG LEU ALA GLU GLY GLU GLU PHE THR
SEQRES 8 D 209 VAL GLY GLN SER ILE SER VAL GLU LEU PHE ALA ASP VAL
SEQRES 9 D 209 LYS LYS VAL ASP VAL THR GLY THR SER LYS GLY LYS GLY
SEQRES 10 D 209 PHE ALA GLY THR VAL LYS ARG TRP ASN PHE ARG THR GLN
SEQRES 11 D 209 ASP ALA THR HIS GLY ASN SER LEU SER HIS ARG VAL PRO
SEQRES 12 D 209 GLY SER ILE GLY GLN ASN GLN THR PRO GLY LYS VAL PHE
SEQRES 13 D 209 LYS GLY LYS LYS MET ALA GLY GLN MET GLY ASN GLU ARG
SEQRES 14 D 209 VAL THR VAL GLN SER LEU ASP VAL VAL ARG VAL ASP ALA
SEQRES 15 D 209 GLU ARG ASN LEU LEU LEU VAL LYS GLY ALA VAL PRO GLY
SEQRES 16 D 209 ALA THR GLY SER ASP LEU ILE VAL LYS PRO ALA VAL LYS
SEQRES 17 D 209 ALA
SEQRES 1 E 201 MET GLU LEU VAL LEU LYS ASP ALA GLN SER ALA LEU THR
SEQRES 2 E 201 VAL SER GLU THR THR PHE GLY ARG ASP PHE ASN GLU ALA
SEQRES 3 E 201 LEU VAL HIS GLN VAL VAL VAL ALA TYR ALA ALA GLY ALA
SEQRES 4 E 201 ARG GLN GLY THR ARG ALA GLN LYS THR ARG ALA GLU VAL
SEQRES 5 E 201 THR GLY SER GLY LYS LYS PRO TRP ARG GLN LYS GLY THR
SEQRES 6 E 201 GLY ARG ALA ARG SER GLY SER ILE LYS SER PRO ILE TRP
SEQRES 7 E 201 ARG SER GLY GLY VAL THR PHE ALA ALA ARG PRO GLN ASP
SEQRES 8 E 201 HIS SER GLN LYS VAL ASN LYS LYS MET TYR ARG GLY ALA
SEQRES 9 E 201 LEU LYS SER ILE LEU SER GLU LEU VAL ARG GLN ASP ARG
SEQRES 10 E 201 LEU ILE VAL VAL GLU LYS PHE SER VAL GLU ALA PRO LYS
SEQRES 11 E 201 THR LYS LEU LEU ALA GLN LYS LEU LYS ASP MET ALA LEU
SEQRES 12 E 201 GLU ASP VAL LEU ILE ILE THR GLY GLU LEU ASP GLU ASN
SEQRES 13 E 201 LEU PHE LEU ALA ALA ARG ASN LEU HIS LYS VAL ASP VAL
SEQRES 14 E 201 ARG ASP ALA THR GLY ILE ASP PRO VAL SER LEU ILE ALA
SEQRES 15 E 201 PHE ASP LYS VAL VAL MET THR ALA ASP ALA VAL LYS GLN
SEQRES 16 E 201 VAL GLU GLU MET LEU ALA
SEQRES 1 F 178 ALA LYS LEU HIS ASP TYR TYR LYS ASP GLU VAL VAL LYS
SEQRES 2 F 178 LYS LEU MET THR GLU PHE ASN TYR ASN SER VAL MET GLN
SEQRES 3 F 178 VAL PRO ARG VAL GLU LYS ILE THR LEU ASN MET GLY VAL
SEQRES 4 F 178 GLY GLU ALA ILE ALA ASP LYS LYS LEU LEU ASP ASN ALA
SEQRES 5 F 178 ALA ALA ASP LEU ALA ALA ILE SER GLY GLN LYS PRO LEU
SEQRES 6 F 178 ILE THR LYS ALA ARG LYS SER VAL ALA GLY PHE LYS ILE
SEQRES 7 F 178 ARG GLN GLY TYR PRO ILE GLY CYS LYS VAL THR LEU ARG
SEQRES 8 F 178 GLY GLU ARG MET TRP GLU PHE PHE GLU ARG LEU ILE THR
SEQRES 9 F 178 ILE ALA VAL PRO ARG ILE ARG ASP PHE ARG GLY LEU SER
SEQRES 10 F 178 ALA LYS SER PHE ASP GLY ARG GLY ASN TYR SER MET GLY
SEQRES 11 F 178 VAL ARG GLU GLN ILE ILE PHE PRO GLU ILE ASP TYR ASP
SEQRES 12 F 178 LYS VAL ASP ARG VAL ARG GLY LEU ASP ILE THR ILE THR
SEQRES 13 F 178 THR THR ALA LYS SER ASP GLU GLU GLY ARG ALA LEU LEU
SEQRES 14 F 178 ALA ALA PHE ASP PHE PRO PHE ARG LYS
SEQRES 1 G 176 SER ARG VAL ALA LYS ALA PRO VAL VAL VAL PRO ALA GLY
SEQRES 2 G 176 VAL ASP VAL LYS ILE ASN GLY GLN VAL ILE THR ILE LYS
SEQRES 3 G 176 GLY LYS ASN GLY GLU LEU THR ARG THR LEU ASN ASP ALA
SEQRES 4 G 176 VAL GLU VAL LYS HIS ALA ASP ASN THR LEU THR PHE GLY
SEQRES 5 G 176 PRO ARG ASP GLY TYR ALA ASP GLY TRP ALA GLN ALA GLY
SEQRES 6 G 176 THR ALA ARG ALA LEU LEU ASN SER MET VAL ILE GLY VAL
SEQRES 7 G 176 THR GLU GLY PHE THR LYS LYS LEU GLN LEU VAL GLY VAL
SEQRES 8 G 176 GLY TYR ARG ALA ALA VAL LYS GLY ASN VAL ILE ASN LEU
SEQRES 9 G 176 SER LEU GLY PHE SER HIS PRO VAL ASP HIS GLN LEU PRO
SEQRES 10 G 176 ALA GLY ILE THR ALA GLU CYS PRO THR GLN THR GLU ILE
SEQRES 11 G 176 VAL LEU LYS GLY ALA ASP LYS GLN VAL ILE GLY GLN VAL
SEQRES 12 G 176 ALA ALA ASP LEU ARG ALA TYR ARG ARG PRO GLU PRO TYR
SEQRES 13 G 176 LYS GLY LYS GLY VAL ARG TYR ALA ASP GLU VAL VAL ARG
SEQRES 14 G 176 THR LYS GLU ALA LYS LYS LYS
SEQRES 1 H 149 MET GLN VAL ILE LEU LEU ASP LYS VAL ALA ASN LEU GLY
SEQRES 2 H 149 SER LEU GLY ASP GLN VAL ASN VAL LYS ALA GLY TYR ALA
SEQRES 3 H 149 ARG ASN PHE LEU VAL PRO GLN GLY LYS ALA VAL PRO ALA
SEQRES 4 H 149 THR LYS LYS ASN ILE GLU PHE PHE GLU ALA ARG ARG ALA
SEQRES 5 H 149 GLU LEU GLU ALA LYS LEU ALA GLU VAL LEU ALA ALA ALA
SEQRES 6 H 149 ASN ALA ARG ALA GLU LYS ILE ASN ALA LEU GLU THR VAL
SEQRES 7 H 149 THR ILE ALA SER LYS ALA GLY ASP GLU GLY LYS LEU PHE
SEQRES 8 H 149 GLY SER ILE GLY THR ARG ASP ILE ALA ASP ALA VAL THR
SEQRES 9 H 149 ALA ALA GLY VAL GLU VAL ALA LYS SER GLU VAL ARG LEU
SEQRES 10 H 149 PRO ASN GLY VAL LEU ARG THR THR GLY GLU HIS GLU VAL
SEQRES 11 H 149 SER PHE GLN VAL HIS SER GLU VAL PHE ALA LYS VAL ILE
SEQRES 12 H 149 VAL ASN VAL VAL ALA GLU
SEQRES 1 I 141 ALA LYS LYS VAL GLN ALA TYR VAL LYS LEU GLN VAL ALA
SEQRES 2 I 141 ALA GLY MET ALA ASN PRO SER PRO PRO VAL GLY PRO ALA
SEQRES 3 I 141 LEU GLY GLN GLN GLY VAL ASN ILE MET GLU PHE CYS LYS
SEQRES 4 I 141 ALA PHE ASN ALA LYS THR ASP SER ILE GLU LYS GLY LEU
SEQRES 5 I 141 PRO ILE PRO VAL VAL ILE THR VAL TYR ALA ASP ARG SER
SEQRES 6 I 141 PHE THR PHE VAL THR LYS THR PRO PRO ALA ALA VAL LEU
SEQRES 7 I 141 LEU LYS LYS ALA ALA GLY ILE LYS SER GLY SER GLY LYS
SEQRES 8 I 141 PRO ASN LYS ASP LYS VAL GLY LYS ILE SER ARG ALA GLN
SEQRES 9 I 141 LEU GLN GLU ILE ALA GLN THR LYS ALA ALA ASP MET THR
SEQRES 10 I 141 GLY ALA ASP ILE GLU ALA MET THR ARG SER ILE GLU GLY
SEQRES 11 I 141 THR ALA ARG SER MET GLY LEU VAL VAL GLU ASP
SEQRES 1 J 142 MET LYS THR PHE THR ALA LYS PRO GLU THR VAL LYS ARG
SEQRES 2 J 142 ASP TRP TYR VAL VAL ASP ALA THR GLY LYS THR LEU GLY
SEQRES 3 J 142 ARG LEU ALA THR GLU LEU ALA ARG ARG LEU ARG GLY LYS
SEQRES 4 J 142 HIS LYS ALA GLU TYR THR PRO HIS VAL ASP THR GLY ASP
SEQRES 5 J 142 TYR ILE ILE VAL LEU ASN ALA ASP LYS VAL ALA VAL THR
SEQRES 6 J 142 GLY ASN LYS ARG THR ASP LYS VAL TYR TYR HIS HIS THR
SEQRES 7 J 142 GLY HIS ILE GLY GLY ILE LYS GLN ALA THR PHE GLU GLU
SEQRES 8 J 142 MET ILE ALA ARG ARG PRO GLU ARG VAL ILE GLU ILE ALA
SEQRES 9 J 142 VAL LYS GLY MET LEU PRO LYS GLY PRO LEU GLY ARG ALA
SEQRES 10 J 142 MET PHE ARG LYS LEU LYS VAL TYR ALA GLY ASN GLU HIS
SEQRES 11 J 142 ASN HIS ALA ALA GLN GLN PRO GLN VAL LEU ASP ILE
SEQRES 1 K 121 MET ILE GLN GLU GLN THR MET LEU ASN VAL ALA ASP ASN
SEQRES 2 K 121 SER GLY ALA ARG ARG VAL MET CYS ILE LYS VAL LEU GLY
SEQRES 3 K 121 GLY SER HIS ARG ARG TYR ALA GLY VAL GLY ASP ILE ILE
SEQRES 4 K 121 LYS ILE THR ILE LYS GLU ALA ILE PRO ARG GLY LYS VAL
SEQRES 5 K 121 LYS LYS GLY ASP VAL LEU LYS ALA VAL VAL VAL ARG THR
SEQRES 6 K 121 LYS LYS GLY VAL ARG ARG PRO ASP GLY SER VAL ILE ARG
SEQRES 7 K 121 PHE ASP GLY ASN ALA CYS VAL LEU LEU ASN ASN ASN SER
SEQRES 8 K 121 GLU GLN PRO ILE GLY THR ARG ILE PHE GLY PRO VAL THR
SEQRES 9 K 121 ARG GLU LEU ARG SER GLU LYS PHE MET LYS ILE ILE SER
SEQRES 10 K 121 LEU ALA PRO GLU
SEQRES 1 L 143 ARG LEU ASN THR LEU SER PRO ALA GLU GLY SER LYS LYS
SEQRES 2 L 143 ALA GLY LYS ARG LEU GLY ARG GLY ILE GLY SER GLY LEU
SEQRES 3 L 143 GLY LYS THR GLY GLY ARG GLY HIS LYS GLY GLN LYS SER
SEQRES 4 L 143 ARG SER GLY GLY GLY VAL ARG ARG GLY PHE GLU GLY GLY
SEQRES 5 L 143 GLN MET PRO LEU TYR ARG ARG LEU PRO LYS PHE GLY PHE
SEQRES 6 L 143 THR SER ARG LYS ALA ALA ILE THR ALA GLU ILE ARG LEU
SEQRES 7 L 143 SER ASP LEU ALA LYS VAL GLU GLY GLY VAL VAL ASP LEU
SEQRES 8 L 143 ASN THR LEU LYS ALA ALA ASN ILE ILE GLY ILE GLN ILE
SEQRES 9 L 143 GLU PHE ALA LYS VAL ILE LEU ALA GLY GLU VAL THR THR
SEQRES 10 L 143 PRO VAL THR VAL ARG GLY LEU ARG VAL THR LYS GLY ALA
SEQRES 11 L 143 ARG ALA ALA ILE GLU ALA ALA GLY GLY LYS ILE GLU GLU
SEQRES 1 M 136 MET LEU GLN PRO LYS ARG THR LYS PHE ARG LYS MET HIS
SEQRES 2 M 136 LYS GLY ARG ASN ARG GLY LEU ALA GLN GLY THR ASP VAL
SEQRES 3 M 136 SER PHE GLY SER PHE GLY LEU LYS ALA VAL GLY ARG GLY
SEQRES 4 M 136 ARG LEU THR ALA ARG GLN ILE GLU ALA ALA ARG ARG ALA
SEQRES 5 M 136 MET THR ARG ALA VAL LYS ARG GLN GLY LYS ILE TRP ILE
SEQRES 6 M 136 ARG VAL PHE PRO ASP LYS PRO ILE THR GLU LYS PRO LEU
SEQRES 7 M 136 ALA VAL ARG MET GLY LYS GLY LYS GLY ASN VAL GLU TYR
SEQRES 8 M 136 TRP VAL ALA LEU ILE GLN PRO GLY LYS VAL LEU TYR GLU
SEQRES 9 M 136 MET ASP GLY VAL PRO GLU GLU LEU ALA ARG GLU ALA PHE
SEQRES 10 M 136 LYS LEU ALA ALA ALA LYS LEU PRO ILE LYS THR THR PHE
SEQRES 11 M 136 VAL THR LYS THR VAL MET
SEQRES 1 N 120 MET ARG HIS ARG LYS SER GLY ARG GLN LEU ASN ARG ASN
SEQRES 2 N 120 SER SER HIS ARG GLN ALA MET PHE ARG ASN MET ALA GLY
SEQRES 3 N 120 SER LEU VAL ARG HIS GLU ILE ILE LYS THR THR LEU PRO
SEQRES 4 N 120 LYS ALA LYS GLU LEU ARG ARG VAL VAL GLU PRO LEU ILE
SEQRES 5 N 120 THR LEU ALA LYS THR ASP SER VAL ALA ASN ARG ARG LEU
SEQRES 6 N 120 ALA PHE ALA ARG THR ARG ASP ASN GLU ILE VAL ALA LYS
SEQRES 7 N 120 LEU PHE ASN GLU LEU GLY PRO ARG PHE ALA SER ARG ALA
SEQRES 8 N 120 GLY GLY TYR THR ARG ILE LEU LYS CYS GLY PHE ARG ALA
SEQRES 9 N 120 GLY ASP ASN ALA PRO MET ALA TYR ILE GLU LEU VAL ASP
SEQRES 10 N 120 ARG SER GLU
SEQRES 1 O 116 ASP LYS LYS SER ALA ARG ILE ARG ARG ALA THR ARG ALA
SEQRES 2 O 116 ARG ARG LYS LEU GLN GLU LEU GLY ALA THR ARG LEU VAL
SEQRES 3 O 116 VAL HIS ARG THR PRO ARG HIS ILE TYR ALA GLN VAL ILE
SEQRES 4 O 116 ALA PRO ASN GLY SER GLU VAL LEU VAL ALA ALA SER THR
SEQRES 5 O 116 VAL GLU LYS ALA ILE ALA GLU GLN LEU LYS TYR THR GLY
SEQRES 6 O 116 ASN LYS ASP ALA ALA ALA ALA VAL GLY LYS ALA VAL ALA
SEQRES 7 O 116 GLU ARG ALA LEU GLU LYS GLY ILE LYS ASP VAL SER PHE
SEQRES 8 O 116 ASP ARG SER GLY PHE GLN TYR HIS GLY ARG VAL GLN ALA
SEQRES 9 O 116 LEU ALA ASP ALA ALA ARG GLU ALA GLY LEU GLN PHE
SEQRES 1 P 114 SER ASN ILE ILE LYS GLN LEU GLU GLN GLU GLN MET LYS
SEQRES 2 P 114 GLN ASP VAL PRO SER PHE ARG PRO GLY ASP THR VAL GLU
SEQRES 3 P 114 VAL LYS VAL TRP VAL VAL GLU GLY SER LYS LYS ARG LEU
SEQRES 4 P 114 GLN ALA PHE GLU GLY VAL VAL ILE ALA ILE ARG ASN ARG
SEQRES 5 P 114 GLY LEU HIS SER ALA PHE THR VAL ARG LYS ILE SER ASN
SEQRES 6 P 114 GLY GLU GLY VAL GLU ARG VAL PHE GLN THR HIS SER PRO
SEQRES 7 P 114 VAL VAL ASP SER ILE SER VAL LYS ARG ARG GLY ALA VAL
SEQRES 8 P 114 ARG LYS ALA LYS LEU TYR TYR LEU ARG GLU ARG THR GLY
SEQRES 9 P 114 LYS ALA ALA ARG ILE LYS GLU ARG LEU ASN
SEQRES 1 Q 117 ALA ARG VAL LYS ARG GLY VAL ILE ALA ARG ALA ARG HIS
SEQRES 2 Q 117 LYS LYS ILE LEU LYS GLN ALA LYS GLY TYR TYR GLY ALA
SEQRES 3 Q 117 ARG SER ARG VAL TYR ARG VAL ALA PHE GLN ALA VAL ILE
SEQRES 4 Q 117 LYS ALA GLY GLN TYR ALA TYR ARG ASP ARG ARG GLN ARG
SEQRES 5 Q 117 LYS ARG GLN PHE ARG GLN LEU TRP ILE ALA ARG ILE ASN
SEQRES 6 Q 117 ALA ALA ALA ARG GLN ASN GLY ILE SER TYR SER LYS PHE
SEQRES 7 Q 117 ILE ASN GLY LEU LYS LYS ALA SER VAL GLU ILE ASP ARG
SEQRES 8 Q 117 LYS ILE LEU ALA ASP ILE ALA VAL PHE ASP LYS VAL ALA
SEQRES 9 Q 117 PHE THR ALA LEU VAL GLU LYS ALA LYS ALA ALA LEU ALA
SEQRES 1 R 103 MET TYR ALA VAL PHE GLN SER GLY GLY LYS GLN HIS ARG
SEQRES 2 R 103 VAL SER GLU GLY GLN THR VAL ARG LEU GLU LYS LEU ASP
SEQRES 3 R 103 ILE ALA THR GLY GLU THR VAL GLU PHE ALA GLU VAL LEU
SEQRES 4 R 103 MET ILE ALA ASN GLY GLU GLU VAL LYS ILE GLY VAL PRO
SEQRES 5 R 103 PHE VAL ASP GLY GLY VAL ILE LYS ALA GLU VAL VAL ALA
SEQRES 6 R 103 HIS GLY ARG GLY GLU LYS VAL LYS ILE VAL LYS PHE ARG
SEQRES 7 R 103 ARG ARG LYS HIS TYR ARG LYS GLN GLN GLY HIS ARG GLN
SEQRES 8 R 103 TRP PHE THR ASP VAL LYS ILE THR GLY ILE SER ALA
SEQRES 1 S 110 MET GLU THR ILE ALA LYS HIS ARG HIS ALA ARG SER SER
SEQRES 2 S 110 ALA GLN LYS VAL ARG LEU VAL ALA ASP LEU ILE ARG GLY
SEQRES 3 S 110 LYS LYS VAL SER GLN ALA LEU ASP ILE LEU THR TYR THR
SEQRES 4 S 110 ASN LYS LYS ALA ALA VAL LEU VAL LYS LYS VAL LEU GLU
SEQRES 5 S 110 SER ALA ILE ALA ASN ALA GLU HIS ASN ASP GLY ALA ASP
SEQRES 6 S 110 ILE ASP ASP LEU LYS VAL THR LYS ILE PHE VAL ASP GLU
SEQRES 7 S 110 GLY PRO SER MET LYS ARG ILE MET PRO ARG ALA LYS GLY
SEQRES 8 S 110 ARG ALA ASP ARG ILE LEU LYS ARG THR SER HIS ILE THR
SEQRES 9 S 110 VAL VAL VAL SER ASP ARG
SEQRES 1 T 93 MET ILE ARG GLU GLU ARG LEU LEU LYS VAL LEU ARG ALA
SEQRES 2 T 93 PRO HIS VAL SER GLU LYS ALA SER THR ALA MET GLU LYS
SEQRES 3 T 93 SER ASN THR ILE VAL LEU LYS VAL ALA LYS ASP ALA THR
SEQRES 4 T 93 LYS ALA GLU ILE LYS ALA ALA VAL GLN LYS LEU PHE GLU
SEQRES 5 T 93 VAL GLU VAL GLU VAL VAL ASN THR LEU VAL VAL LYS GLY
SEQRES 6 T 93 LYS VAL LYS ARG HIS GLY GLN ARG ILE GLY ARG ARG SER
SEQRES 7 T 93 ASP TRP LYS LYS ALA TYR VAL THR LEU LYS GLU GLY GLN
SEQRES 8 T 93 ASN LEU
SEQRES 1 U 102 ALA ALA LYS ILE ARG ARG ASP ASP GLU VAL ILE VAL LEU
SEQRES 2 U 102 THR GLY LYS ASP LYS GLY LYS ARG GLY LYS VAL LYS ASN
SEQRES 3 U 102 VAL LEU SER SER GLY LYS VAL ILE VAL GLU GLY ILE ASN
SEQRES 4 U 102 LEU VAL LYS LYS HIS GLN LYS PRO VAL PRO ALA LEU ASN
SEQRES 5 U 102 GLN PRO GLY GLY ILE VAL GLU LYS GLU ALA ALA ILE GLN
SEQRES 6 U 102 VAL SER ASN VAL ALA ILE PHE ASN ALA ALA THR GLY LYS
SEQRES 7 U 102 ALA ASP ARG VAL GLY PHE ARG PHE GLU ASP GLY LYS LYS
SEQRES 8 U 102 VAL ARG PHE PHE LYS SER ASN SER GLU THR ILE
SEQRES 1 V 77 C G G C A C G U A G C G C
SEQRES 2 V 77 A G C C U G G U A G C G C
SEQRES 3 V 77 A C C G U C A U G G G G U
SEQRES 4 V 77 G U C G G G G G U C G G A
SEQRES 5 V 77 G G 5MU U C A A A U C C U C
SEQRES 6 V 77 U C G U G C C G A C C A
SEQRES 1 W 94 MET PHE THR ILE ASN ALA GLU VAL ARG LYS GLU GLN GLY
SEQRES 2 W 94 LYS GLY ALA SER ARG ARG LEU ARG ALA ALA ASN LYS PHE
SEQRES 3 W 94 PRO ALA ILE ILE TYR GLY GLY LYS GLU ALA PRO LEU ALA
SEQRES 4 W 94 ILE GLU LEU ASP HIS ASP LYS VAL MET ASN MET GLN ALA
SEQRES 5 W 94 LYS ALA GLU PHE TYR SER GLU VAL LEU THR ILE VAL VAL
SEQRES 6 W 94 ASP GLY LYS GLU ILE LYS VAL LYS ALA GLN ASP VAL GLN
SEQRES 7 W 94 ARG HIS PRO TYR LYS PRO LYS LEU GLN HIS ILE ASP PHE
SEQRES 8 W 94 VAL ARG ALA
SEQRES 1 X 11 A A A A C C C A G U A
SEQRES 1 Y 79 GLY GLY SER THR ARG ASN GLY ARG ASP SER GLU ALA LYS
SEQRES 2 Y 79 ARG LEU GLY VAL LYS ARG PHE GLY GLY GLU SER VAL LEU
SEQRES 3 Y 79 ALA GLY SER ILE ILE VAL ARG GLN ARG GLY THR LYS PHE
SEQRES 4 Y 79 HIS ALA GLY ALA ASN VAL GLY CYS GLY ARG ASP HIS THR
SEQRES 5 Y 79 LEU PHE ALA LYS ALA ASP GLY LYS VAL LYS PHE GLU VAL
SEQRES 6 Y 79 LYS GLY PRO LYS ASN ARG LYS PHE ILE SER ILE GLU ALA
SEQRES 7 Y 79 GLU
SEQRES 1 Z 20 ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA
SEQRES 2 Z 20 ALA ALA ALA ALA ALA ALA ALA
MODRES 2WWQ 5MU V 54 U 5-METHYLURIDINE 5'-MONOPHOSPHATE
HET 5MU V 54 20
HETNAM 5MU 5-METHYLURIDINE 5'-MONOPHOSPHATE
FORMUL 31 5MU C10 H15 N2 O9 P
HELIX 1 1 LYS 0 53 GLY 0 62 1 10
HELIX 2 2 GLY 0 62 LEU 0 67 1 6
HELIX 3 3 MET 1 1 ARG 1 7 1 7
HELIX 4 4 LYS 1 9 LEU 1 22 1 14
HELIX 5 5 GLN 1 25 ALA 1 33 1 9
HELIX 6 6 GLN 1 39 LEU 1 42 5 4
HELIX 7 7 LEU 1 43 LEU 1 56 1 14
HELIX 8 8 HIS 2 19 LEU 2 26 1 8
HELIX 9 9 ALA 2 42 VAL 2 50 1 9
HELIX 10 10 SER 2 51 VAL 2 54 5 4
HELIX 11 11 THR 3 8 MET 3 14 1 7
HELIX 12 12 ARG 3 15 ASP 3 19 5 5
HELIX 13 13 THR 5 5 GLU 5 13 1 9
HELIX 14 14 ASP 5 22 LEU 5 33 1 12
HELIX 15 15 ASN 5 83 GLY 5 91 1 9
HELIX 16 16 MET 5 97 GLY 5 107 1 11
HELIX 17 17 SER 5 117 VAL 5 124 1 8
HELIX 18 18 VAL 5 149 GLY 5 159 1 11
HELIX 19 19 ASP 5 181 ALA 5 199 1 19
HELIX 20 20 SER 6 8 ARG 6 14 1 7
HELIX 21 21 LYS 6 25 LYS 6 37 1 13
HELIX 22 22 GLY 7 8 ARG 7 12 5 5
HELIX 23 23 ALA 7 36 HIS 7 42 1 7
HELIX 24 24 ASP 7 53 VAL 7 57 5 5
HELIX 25 25 GLU 8 30 HIS 8 33 5 4
HELIX 26 26 PHE C 29 LEU C 33 5 5
HELIX 27 27 LYS C 206 TRP C 212 1 7
HELIX 28 28 ARG C 220 MET C 224 5 5
HELIX 29 29 ASN C 225 HIS C 229 5 5
HELIX 30 30 ARG C 261 LYS C 264 5 4
HELIX 31 31 LYS D 62 LYS D 70 1 9
HELIX 32 32 SER D 97 ASP D 103 5 7
HELIX 33 33 ASN E 24 GLY E 38 1 15
HELIX 34 34 ASN E 97 ILE E 108 1 12
HELIX 35 35 ILE E 108 VAL E 113 1 6
HELIX 36 36 LYS E 132 ASP E 140 1 9
HELIX 37 37 ASP E 154 ARG E 162 1 9
HELIX 38 38 ASP E 176 ALA E 182 1 7
HELIX 39 39 THR E 189 LEU E 200 1 12
HELIX 40 40 ALA F 1 ASP F 9 1 9
HELIX 41 41 ASP F 9 PHE F 19 1 11
HELIX 42 42 LYS F 47 SER F 60 1 14
HELIX 43 43 ARG F 91 PHE F 99 1 9
HELIX 44 44 SER F 161 ALA F 170 1 10
HELIX 45 45 SER G 1 ALA G 6 5 6
HELIX 46 46 TRP G 61 VAL G 78 1 18
HELIX 47 47 ASP G 136 ALA G 149 1 14
HELIX 48 48 LYS H 42 LEU H 58 1 17
HELIX 49 49 ALA H 63 ALA H 74 1 12
HELIX 50 50 GLY H 95 ILE H 99 5 5
HELIX 51 51 GLY I 24 GLN I 29 1 6
HELIX 52 52 ASN I 33 ASP I 46 1 14
HELIX 53 53 PRO I 74 GLY I 84 1 11
HELIX 54 54 SER I 101 ALA I 113 1 13
HELIX 55 55 ASP I 120 MET I 135 1 16
HELIX 56 56 LEU J 28 ARG J 37 1 10
HELIX 57 57 THR J 88 ARG J 95 1 8
HELIX 58 58 GLU J 98 GLY J 107 1 10
HELIX 59 59 GLY J 112 LYS J 121 1 10
HELIX 60 60 HIS J 132 GLN J 136 5 5
HELIX 61 61 THR K 104 ARG K 108 5 5
HELIX 62 62 LYS K 114 LEU K 118 5 5
HELIX 63 63 PRO L 56 ARG L 60 5 5
HELIX 64 64 SER L 80 LEU L 82 5 3
HELIX 65 65 ALA M 43 LYS M 58 1 16
HELIX 66 66 PRO M 109 ALA M 121 1 13
HELIX 67 67 ASN N 13 GLU N 32 1 20
HELIX 68 68 LEU N 38 LYS N 56 1 19
HELIX 69 69 VAL N 60 LEU N 65 1 6
HELIX 70 70 ALA N 66 ALA N 68 5 3
HELIX 71 71 GLU N 74 GLU N 82 1 9
HELIX 72 72 ASP O 2 ARG O 10 1 9
HELIX 73 73 ARG O 13 GLY O 22 1 10
HELIX 74 74 GLU O 55 GLU O 60 1 6
HELIX 75 75 ALA O 73 LEU O 83 1 11
HELIX 76 76 ASN P 2 GLU P 10 1 9
HELIX 77 77 TYR P 97 THR P 103 1 7
HELIX 78 78 ILE Q 8 GLN Q 19 1 12
HELIX 79 79 GLY Q 25 VAL Q 30 1 6
HELIX 80 80 TYR Q 31 ALA Q 34 5 4
HELIX 81 81 PHE Q 35 ASN Q 71 1 37
HELIX 82 82 SER Q 74 SER Q 86 1 13
HELIX 83 83 ASP Q 101 ALA Q 117 1 17
HELIX 84 84 SER S 13 ARG S 25 1 13
HELIX 85 85 ILE S 35 THR S 39 5 5
HELIX 86 86 ALA S 43 HIS S 60 1 18
HELIX 87 87 GLU T 4 LEU T 8 5 5
HELIX 88 88 THR T 22 SER T 27 1 6
HELIX 89 89 LYS T 40 LEU T 50 1 11
HELIX 90 90 GLY W 13 ALA W 22 1 10
HELIX 91 91 ASP W 43 LYS W 53 1 11
HELIX 92 92 ALA W 54 SER W 58 5 5
SHEET 1 0A 2 HIS 0 33 TRP 0 38 0
SHEET 2 0A 2 PHE 0 45 VAL 0 50 -1 O VAL 0 46 N PHE 0 37
SHEET 1 2A 2 THR 2 3 ILE 2 6 0
SHEET 2 2A 2 VAL 2 35 GLU 2 38 -1 O VAL 2 35 N ILE 2 6
SHEET 1 3A 2 LEU 3 27 SER 3 28 0
SHEET 2 3A 2 HIS 3 37 LEU 3 38 -1 O HIS 3 37 N SER 3 28
SHEET 1 4A 4 PHE 4 19 LYS 4 24 0
SHEET 2 4A 4 GLU 4 6 SER 4 12 -1 O GLU 4 6 N LYS 4 24
SHEET 3 4A 4 GLN 4 44 LYS 4 49 -1 O LYS 4 49 N VAL 4 11
SHEET 4 4A 4 LEU 4 35 ASP 4 39 -1 O LEU 4 35 N TYR 4 48
SHEET 1 5A 5 GLN 5 20 TYR 5 21 0
SHEET 2 5A 5 GLY 5 221 VAL 5 224 1 O ALA 5 223 N TYR 5 21
SHEET 3 5A 5 ILE 5 209 THR 5 216 -1 O VAL 5 212 N VAL 5 224
SHEET 4 5A 5 SER 5 41 LEU 5 48 -1 O ASP 5 43 N SER 5 215
SHEET 5 5A 5 ILE 5 170 LYS 5 177 -1 O ILE 5 171 N VAL 5 46
SHEET 1 5B 2 GLY 5 61 VAL 5 64 0
SHEET 2 5B 2 GLN 5 160 TYR 5 163 -1 O VAL 5 161 N THR 5 63
SHEET 1 5C 3 LEU 5 94 VAL 5 95 0
SHEET 2 5C 3 VAL 5 75 PHE 5 78 1 N VAL 5 77 O LEU 5 94
SHEET 3 5C 3 VAL 5 113 ALA 5 116 1 O VAL 5 113 N ALA 5 76
SHEET 1 7A 2 LYS 7 22 HIS 7 23 0
SHEET 2 7A 2 ALA 7 47 MET 7 48 -1 O ALA 7 47 N HIS 7 23
SHEET 1 8A 2 LYS 8 2 VAL 8 3 0
SHEET 2 8A 2 GLN 8 35 GLN 8 37 1 N ARG 8 36 O LYS 8 2
SHEET 1 8B 2 VAL 8 17 LYS 8 18 0
SHEET 2 8B 2 ILE 8 23 ARG 8 24 -1 O ARG 8 24 N VAL 8 17
SHEET 1 CA 2 VAL C 3 LYS C 4 0
SHEET 2 CA 2 VAL C 16 LYS C 17 -1 O LYS C 17 N VAL C 3
SHEET 1 CB 3 ALA C 75 VAL C 77 0
SHEET 2 CB 3 ALA C 91 TYR C 95 -1 O LEU C 94 N VAL C 76
SHEET 3 CB 3 ARG C 100 ILE C 103 -1 O ARG C 101 N VAL C 93
SHEET 1 CC 8 GLN C 116 SER C 117 0
SHEET 2 CC 8 ASN C 127 PRO C 130 1 N THR C 128 O GLN C 116
SHEET 3 CC 8 ARG C 188 LEU C 191 -1 O ALA C 189 N LEU C 129
SHEET 4 CC 8 THR C 139 HIS C 141 -1 O HIS C 141 N THR C 190
SHEET 5 CC 8 VAL C 161 ALA C 165 -1 O VAL C 161 N VAL C 140
SHEET 6 CC 8 VAL C 171 LEU C 175 -1 O THR C 172 N ALA C 165
SHEET 7 CC 8 GLU C 179 VAL C 183 -1 O GLU C 179 N LEU C 175
SHEET 8 CC 8 ILE C 266 ARG C 268 -1 N VAL C 267 O MET C 180
SHEET 1 DA 5 VAL D 177 ASP D 181 0
SHEET 2 DA 5 LEU D 186 VAL D 189 -1 O LEU D 186 N ASP D 181
SHEET 3 DA 5 SER D 21 GLU D 28 -1 O THR D 25 N VAL D 189
SHEET 4 DA 5 GLY D 6 PHE D 15 -1 O LYS D 7 N GLU D 28
SHEET 5 DA 5 ASP D 200 LEU D 201 -1 O LEU D 201 N GLY D 6
SHEET 1 DB 3 VAL D 34 VAL D 37 0
SHEET 2 DB 3 ALA D 47 VAL D 50 -1 O GLN D 49 N THR D 35
SHEET 3 DB 3 PHE D 82 ARG D 83 -1 O PHE D 82 N ILE D 48
SHEET 1 DC 2 GLY D 111 THR D 112 0
SHEET 2 DC 2 ARG D 169 VAL D 170 -1 O VAL D 170 N GLY D 111
SHEET 1 EA 2 LEU E 118 VAL E 120 0
SHEET 2 EA 2 VAL E 186 MET E 188 1 O VAL E 186 N ILE E 119
SHEET 1 FA 5 LEU F 65 LYS F 68 0
SHEET 2 FA 5 PRO F 83 THR F 89 -1 N ILE F 84 O THR F 67
SHEET 3 FA 5 THR F 34 MET F 37 -1 O LEU F 35 N VAL F 88
SHEET 4 FA 5 ASP F 152 THR F 154 -1 O ASP F 152 N ASN F 36
SHEET 5 FA 5 SER F 128 GLY F 130 -1 O MET F 129 N ILE F 153
SHEET 1 GA 2 ASP G 15 ILE G 18 0
SHEET 2 GA 2 ILE G 23 LYS G 26 -1 O THR G 24 N LYS G 17
SHEET 1 HA 3 GLN H 18 ASN H 20 0
SHEET 2 HA 3 GLN H 2 LEU H 5 -1 O VAL H 3 N VAL H 19
SHEET 3 HA 3 ALA H 36 ALA H 39 -1 O VAL H 37 N ILE H 4
SHEET 1 HB 2 GLN H 133 HIS H 135 0
SHEET 2 HB 2 VAL H 138 PHE H 139 -1 O VAL H 138 N VAL H 134
SHEET 1 IA 3 VAL I 8 VAL I 12 0
SHEET 2 IA 3 ILE I 54 VAL I 60 -1 O ILE I 54 N VAL I 12
SHEET 3 IA 3 PHE I 66 THR I 70 -1 O THR I 67 N THR I 59
SHEET 1 IB 2 GLY I 98 LYS I 99 0
SHEET 2 IB 2 LEU I 137 VAL I 138 1 N VAL I 138 O GLY I 98
SHEET 1 JA 2 TYR J 16 VAL J 17 0
SHEET 2 JA 2 GLN J 138 VAL J 139 1 O GLN J 138 N VAL J 17
SHEET 1 JB 2 ILE J 54 ILE J 55 0
SHEET 2 JB 2 LEU J 122 LYS J 123 1 N LYS J 123 O ILE J 54
SHEET 1 KA 5 ASN K 9 VAL K 10 0
SHEET 2 KA 5 ALA K 83 LEU K 87 1 N CYS K 84 O ASN K 9
SHEET 3 KA 5 VAL K 57 VAL K 62 -1 O LYS K 59 N LEU K 87
SHEET 4 KA 5 ILE K 38 ILE K 43 -1 O ILE K 39 N ALA K 60
SHEET 5 KA 5 VAL K 19 LYS K 23 -1 O MET K 20 N THR K 42
SHEET 1 KB 3 VAL K 69 ARG K 71 0
SHEET 2 KB 3 SER K 75 PHE K 79 -1 O SER K 75 N ARG K 71
SHEET 3 KB 3 VAL P 69 ARG P 71 -1 O GLU P 70 N ARG K 78
SHEET 1 LA 3 THR L 74 ARG L 78 0
SHEET 2 LA 3 PHE L 107 ILE L 111 1 O PHE L 107 N ALA L 75
SHEET 3 LA 3 ARG L 126 VAL L 127 1 O ARG L 126 N VAL L 110
SHEET 1 MA 4 ILE M 63 ILE M 65 0
SHEET 2 MA 4 TYR M 103 MET M 105 -1 O GLU M 104 N TRP M 64
SHEET 3 MA 4 PHE M 31 VAL M 36 -1 O PHE M 31 N MET M 105
SHEET 4 MA 4 LYS M 127 VAL M 131 -1 O LYS M 127 N VAL M 36
SHEET 1 MB 2 GLY M 39 LEU M 41 0
SHEET 2 MB 2 ALA M 94 ILE M 96 -1 O ALA M 94 N LEU M 41
SHEET 1 MC 2 THR M 74 GLU M 75 0
SHEET 2 MC 2 ASN M 88 VAL M 89 -1 O ASN M 88 N GLU M 75
SHEET 1 NA 3 ILE N 33 THR N 37 0
SHEET 2 NA 3 MET N 110 GLU N 114 -1 O ALA N 111 N THR N 36
SHEET 3 NA 3 LYS N 99 GLY N 101 -1 N CYS N 100 O MET N 110
SHEET 1 OA 4 VAL O 47 SER O 52 0
SHEET 2 OA 4 ILE O 35 ILE O 40 -1 O ALA O 37 N ALA O 51
SHEET 3 OA 4 THR O 24 ARG O 30 -1 O ARG O 25 N ILE O 40
SHEET 4 OA 4 VAL O 90 ASP O 93 1 O SER O 91 N LEU O 26
SHEET 1 PA 3 LEU P 39 PHE P 42 0
SHEET 2 PA 3 GLU P 26 TRP P 30 -1 N VAL P 27 O PHE P 42
SHEET 3 PA 3 SER P 82 SER P 84 -1 O SER P 82 N LYS P 28
SHEET 1 PB 2 GLY P 89 ALA P 90 0
SHEET 2 PB 2 LYS P 110 GLU P 111 -1 O LYS P 110 N ALA P 90
SHEET 1 RA 2 PHE R 5 GLN R 6 0
SHEET 2 RA 2 GLN R 11 HIS R 12 -1 O HIS R 12 N PHE R 5
SHEET 1 RB 3 VAL R 20 GLU R 23 0
SHEET 2 RB 3 TRP R 92 VAL R 96 -1 O THR R 94 N LEU R 22
SHEET 3 RB 3 GLY R 67 ARG R 68 -1 O GLY R 67 N PHE R 93
SHEET 1 RC 2 VAL R 72 ARG R 78 0
SHEET 2 RC 2 TYR R 83 HIS R 89 -1 O TYR R 83 N ARG R 78
SHEET 1 SA 3 LYS S 6 ARG S 11 0
SHEET 2 SA 3 THR S 100 ASP S 109 -1 O SER S 101 N ALA S 10
SHEET 3 SA 3 LEU S 69 GLU S 78 -1 N LYS S 70 O SER S 108
SHEET 1 SB 2 MET S 82 PRO S 87 0
SHEET 2 SB 2 ALA S 93 LYS S 98 -1 O ASP S 94 N MET S 86
SHEET 1 TA 3 VAL T 31 LYS T 33 0
SHEET 2 TA 3 TRP T 80 TYR T 84 -1 O ALA T 83 N LEU T 32
SHEET 3 TA 3 ASN T 59 VAL T 63 -1 O ASN T 59 N TYR T 84
SHEET 1 UA 4 GLU U 9 VAL U 10 0
SHEET 2 UA 4 GLY U 22 LEU U 28 -1 O GLY U 22 N VAL U 10
SHEET 3 UA 4 LYS U 32 VAL U 35 -1 O LYS U 32 N LEU U 28
SHEET 4 UA 4 ILE U 64 GLN U 65 -1 O ILE U 64 N VAL U 33
SHEET 1 UB 2 LEU U 40 VAL U 41 0
SHEET 2 UB 2 LYS U 60 GLU U 61 -1 O LYS U 60 N VAL U 41
SHEET 1 UC 2 GLY U 83 GLU U 87 0
SHEET 2 UC 2 LYS U 91 PHE U 94 -1 O VAL U 92 N PHE U 86
SHEET 1 WA 7 ASN W 5 VAL W 8 0
SHEET 2 WA 7 LEU W 61 VAL W 65 1 O VAL W 64 N ALA W 6
SHEET 3 WA 7 LYS W 68 ALA W 74 -1 O LYS W 68 N VAL W 65
SHEET 4 WA 7 ASP W 90 VAL W 92 -1 O VAL W 92 N LYS W 73
SHEET 5 WA 7 PHE W 26 TYR W 31 1 O ILE W 29 N PHE W 91
SHEET 6 WA 7 LEU W 38 LEU W 42 -1 O LEU W 38 N ILE W 30
SHEET 7 WA 7 ASN W 5 VAL W 8 -1 O GLU W 7 N GLU W 41
SHEET 1 YA 3 HIS Y 45 ALA Y 46 0
SHEET 2 YA 3 ILE Y 79 GLU Y 82 1 O ILE Y 79 N ALA Y 46
SHEET 3 YA 3 LYS Y 65 VAL Y 66 -1 O LYS Y 65 N GLU Y 82
LINK O3' G V 53 P 5MU V 54 1555 1555 1.59
LINK O3' 5MU V 54 P U V 55 1555 1555 1.58
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
