HEADER RIBOSOME 11-DEC-08 3FIH
TITLE TERNARY COMPLEX-BOUND E.COLI 70S RIBOSOME. THIS ENTRY CONSISTS OF THE
TITLE 2 30S SUBUNIT, TRNAS AND THE TERNARY COMPLEX.
SPLIT 3FIK 3FIH
CAVEAT 3FIH CHIRALITY ERRORS AT C1' CENTER OF C 17, C1' CENTER OF U 47,
CAVEAT 2 3FIH C3' CENTER OF G 70 IN CHAIN V AND C1' CENTER OF C17 IN
CAVEAT 3 3FIH CHAIN W. THE CHIRALITY ERRORS ARE INHERITED FROM STARTING
CAVEAT 4 3FIH MODEL 2J00
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 30S RIBOSOMAL PROTEIN S10;
COMPND 3 CHAIN: J;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: 30S RIBOSOMAL PROTEIN S11;
COMPND 6 CHAIN: K;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: 30S RIBOSOMAL PROTEIN S12;
COMPND 9 CHAIN: L;
COMPND 10 MOL_ID: 4;
COMPND 11 MOLECULE: 30S RIBOSOMAL PROTEIN S13;
COMPND 12 CHAIN: M;
COMPND 13 MOL_ID: 5;
COMPND 14 MOLECULE: 30S RIBOSOMAL PROTEIN S14;
COMPND 15 CHAIN: N;
COMPND 16 MOL_ID: 6;
COMPND 17 MOLECULE: 30S RIBOSOMAL PROTEIN S15;
COMPND 18 CHAIN: O;
COMPND 19 MOL_ID: 7;
COMPND 20 MOLECULE: 30S RIBOSOMAL PROTEIN S16;
COMPND 21 CHAIN: P;
COMPND 22 MOL_ID: 8;
COMPND 23 MOLECULE: 30S RIBOSOMAL PROTEIN S17;
COMPND 24 CHAIN: Q;
COMPND 25 MOL_ID: 9;
COMPND 26 MOLECULE: 30S RIBOSOMAL PROTEIN S18;
COMPND 27 CHAIN: R;
COMPND 28 MOL_ID: 10;
COMPND 29 MOLECULE: 30S RIBOSOMAL PROTEIN S19;
COMPND 30 CHAIN: S;
COMPND 31 MOL_ID: 11;
COMPND 32 MOLECULE: 30S RIBOSOMAL PROTEIN S20;
COMPND 33 CHAIN: T;
COMPND 34 MOL_ID: 12;
COMPND 35 MOLECULE: 30S RIBOSOMAL PROTEIN S21;
COMPND 36 CHAIN: U;
COMPND 37 MOL_ID: 13;
COMPND 38 MOLECULE: 30S RIBOSOMAL PROTEIN S2;
COMPND 39 CHAIN: B;
COMPND 40 MOL_ID: 14;
COMPND 41 MOLECULE: 30S RIBOSOMAL PROTEIN S3;
COMPND 42 CHAIN: C;
COMPND 43 MOL_ID: 15;
COMPND 44 MOLECULE: 30S RIBOSOMAL PROTEIN S4;
COMPND 45 CHAIN: D;
COMPND 46 MOL_ID: 16;
COMPND 47 MOLECULE: 30S RIBOSOMAL PROTEIN S5;
COMPND 48 CHAIN: E;
COMPND 49 MOL_ID: 17;
COMPND 50 MOLECULE: 30S RIBOSOMAL PROTEIN S6;
COMPND 51 CHAIN: F;
COMPND 52 MOL_ID: 18;
COMPND 53 MOLECULE: 30S RIBOSOMAL PROTEIN S7;
COMPND 54 CHAIN: G;
COMPND 55 MOL_ID: 19;
COMPND 56 MOLECULE: 30S RIBOSOMAL PROTEIN S8;
COMPND 57 CHAIN: H;
COMPND 58 MOL_ID: 20;
COMPND 59 MOLECULE: 30S RIBOSOMAL PROTEIN S9;
COMPND 60 CHAIN: I;
COMPND 61 MOL_ID: 21;
COMPND 62 MOLECULE: 16S RRNA;
COMPND 63 CHAIN: A;
COMPND 64 MOL_ID: 22;
COMPND 65 MOLECULE: A/T-SITE TRNA PHE;
COMPND 66 CHAIN: Y;
COMPND 67 ENGINEERED: YES;
COMPND 68 MOL_ID: 23;
COMPND 69 MOLECULE: P-SITE TRNA FMET (UNMODIFIED BASES EXCEPT FOR THYMINE 54);
COMPND 70 CHAIN: W;
COMPND 71 MOL_ID: 24;
COMPND 72 MOLECULE: MRNA;
COMPND 73 CHAIN: X;
COMPND 74 ENGINEERED: YES;
COMPND 75 MOL_ID: 25;
COMPND 76 MOLECULE: ELONGATION FACTOR TU;
COMPND 77 CHAIN: Z;
COMPND 78 MOL_ID: 26;
COMPND 79 MOLECULE: E-SITE TRNA PHE;
COMPND 80 CHAIN: V
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 SYNTHETIC: YES;
SOURCE 66 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN YEAST.;
SOURCE 67 MOL_ID: 23;
SOURCE 68 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 69 ORGANISM_TAXID: 562;
SOURCE 70 MOL_ID: 24;
SOURCE 71 SYNTHETIC: YES;
SOURCE 72 OTHER_DETAILS: MRNA WAS SYNTHETICALLY CONTSTRUCTED;
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
KEYWDS RIBOSOME, TERNARY COMPLEX, FLEXIBLE FITTING, CRYO-EM, 30S, 50S, TRNA,
KEYWDS 2 MRNA, EF-TU, 70S, RIBONUCLEOPROTEIN, RIBOSOMAL PROTEIN, RNA-BINDING,
KEYWDS 3 RRNA-BINDING, ANTIBIOTIC RESISTANCE, REPRESSOR, TRANSCRIPTION,
KEYWDS 4 TRANSCRIPTION REGULATION, TRANSCRIPTION TERMINATION, TRANSLATION
KEYWDS 5 REGULATION, TRNA-BINDING, METHYLATION, ENDONUCLEASE, HYDROLASE,
KEYWDS 6 NUCLEASE, CELL MEMBRANE, ELONGATION FACTOR, GTP-BINDING, MEMBRANE,
KEYWDS 7 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, PROTEIN BIOSYNTHESIS
EXPDTA ELECTRON MICROSCOPY
AUTHOR E.VILLA,J.SENGUPTA,L.G.TRABUCO,J.LEBARRON,W.T.BAXTER,T.R.SHAIKH,
AUTHOR 2 R.A.GRASSUCCI,P.NISSEN,M.EHRENBERG,K.SCHULTEN,J.FRANK
REVDAT 3 15-FEB-12 3FIH 1 REMARK VERSN
REVDAT 2 02-JUN-09 3FIH 1 ATOM
REVDAT 1 03-MAR-09 3FIH 0
JRNL AUTH E.VILLA,J.SENGUPTA,L.G.TRABUCO,J.LEBARRON,W.T.BAXTER,
JRNL AUTH 2 T.R.SHAIKH,R.A.GRASSUCCI,P.NISSEN,M.EHRENBERG,K.SCHULTEN,
JRNL AUTH 3 J.FRANK
JRNL TITL RIBOSOME-INDUCED CHANGES IN ELONGATION FACTOR TU
JRNL TITL 2 CONFORMATION CONTROL GTP HYDROLYSIS
JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 1063 2009
JRNL REFN ISSN 0027-8424
JRNL PMID 19122150
JRNL DOI 10.1073/PNAS.0811370106
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.TRABUCO,E.VILLA,K.MITRA,J.FRANK,K.SCHULTEN
REMARK 1 TITL FLEXIBLE FITTING OF ATOMIC STRUCTURES INTO ELECTRON
REMARK 1 TITL 2 MICROSCOPY MAPS USING MOLECULAR DYNAMICS.
REMARK 1 REF STRUCTURE V. 16 673 2008
REMARK 1 REFN ISSN 0969-2126
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.LEBARRON,R.A.GRASSUCCI,T.R.SHAIKH,W.T.BAXTER,J.SENGUPTA,
REMARK 1 AUTH 2 J.FRANK
REMARK 1 TITL EXPLORATION OF PARAMETERS IN CRYO-EM LEADING TO AN IMPROVED
REMARK 1 TITL 2 DENSITY MAP OF THE E. COLI RIBOSOME
REMARK 1 REF J.STRUCT.BIOL. V. 164 24 2008
REMARK 1 REFN ISSN 1047-8477
REMARK 2
REMARK 2 RESOLUTION. 6.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : MOLECULAR DYNAMICS FLEXIBLE FITTING
REMARK 3 (MDFF)
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 2I2U, 2I2V, 2J00, 1OB2
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FITTING
REMARK 3 REFINEMENT TARGET : CROSS CORRELATION, ROOT-MEAN
REMARK 3 SQUARE DEVIATION
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : SEE TRABUCO ET AL., STRUCTURE 16 (2008) 673-
REMARK 3 683.
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : 1.200
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 6.700
REMARK 3 NUMBER OF PARTICLES : NULL
REMARK 3 CTF CORRECTION METHOD : CORRECTION OF RECONSTRUCTION
REMARK 3 OF EACH DEFOCUS GROUP
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: SEE LEBARRON ET AL., JSB 164 (2008) 24-32.
REMARK 4
REMARK 4 3FIH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-08.
REMARK 100 THE RCSB ID CODE IS RCSB050631.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : VITREOUS ICE (CRYO EM)
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : ASYMMETRIC
REMARK 245 NAME OF SAMPLE : E. COLI RIBOSOME IN COMPLEX
REMARK 245 WITH THE TERNARY COMPLEX EF-TU
REMARK 245 AMINOACYL-TRNA GDP
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.08
REMARK 245 SAMPLE SUPPORT DETAILS : THIN CARBON ON 300 MESH
REMARK 245 QUANTIFOIL R2/4
REMARK 245 SAMPLE VITRIFICATION DETAILS : VITRIFICATION USING FEI
REMARK 245 VITROBOT; BLOT 3 SECONDS BEFORE
REMARK 245 PLUNGING WITH AN OFFSET OF -1MM
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : 31-AUG-06
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : 84.00
REMARK 245 MICROSCOPE MODEL : FEI POLARA 300
REMARK 245 DETECTOR TYPE : KODAK SO163 FILM
REMARK 245 MINIMUM DEFOCUS (NM) : 4520.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 1200.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : MAGNIFICATION
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 20.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 59000
REMARK 245 CALIBRATED MAGNIFICATION : 58279
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 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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: 26-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, K, L, M, N, O, P, Q, R,
REMARK 350 AND CHAINS: S, T, U, B, C, D, E, F, G,
REMARK 350 AND CHAINS: H, I, A, Y, W, X, Z, V
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 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 SER Z 1 OG
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 J 45 CZ ARG J 45 NH2 0.092
REMARK 500 HIS J 56 CG HIS J 56 CD2 0.084
REMARK 500 ARG J 62 NE ARG J 62 CZ 0.105
REMARK 500 TYR J 65 CZ TYR J 65 OH 0.107
REMARK 500 ARG J 72 CZ ARG J 72 NH2 0.085
REMARK 500 SER J 101 CA SER J 101 CB 0.110
REMARK 500 HIS K 23 CG HIS K 23 CD2 0.059
REMARK 500 ARG K 52 NE ARG K 52 CZ 0.087
REMARK 500 ARG K 121 CZ ARG K 121 NH2 0.091
REMARK 500 PRO K 123 CD PRO K 123 N -0.094
REMARK 500 ARG K 127 NE ARG K 127 CZ 0.083
REMARK 500 ARG L 55 NE ARG L 55 CZ 0.089
REMARK 500 ARG L 98 CZ ARG L 98 NH2 0.092
REMARK 500 ARG M 78 NE ARG M 78 CZ 0.099
REMARK 500 TYR M 85 CE1 TYR M 85 CZ 0.091
REMARK 500 ARG M 100 CZ ARG M 100 NH2 0.079
REMARK 500 ARG N 12 CZ ARG N 12 NH2 0.080
REMARK 500 ARG N 84 NE ARG N 84 CZ 0.084
REMARK 500 PRO N 93 N PRO N 93 CA -0.104
REMARK 500 ARG O 76 NE ARG O 76 CZ 0.096
REMARK 500 ARG O 87 CZ ARG O 87 NH2 0.083
REMARK 500 ARG P 8 NE ARG P 8 CZ 0.085
REMARK 500 ARG P 25 CD ARG P 25 NE 0.116
REMARK 500 ARG P 31 CZ ARG P 31 NH1 0.098
REMARK 500 GLY P 37 CA GLY P 37 C -0.120
REMARK 500 PHE P 39 CG PHE P 39 CD2 0.112
REMARK 500 ARG P 51 CZ ARG P 51 NH1 0.092
REMARK 500 ARG P 56 NE ARG P 56 CZ 0.085
REMARK 500 ARG Q 5 CD ARG Q 5 NE 0.105
REMARK 500 ARG Q 26 CZ ARG Q 26 NH2 0.078
REMARK 500 ARG Q 61 CZ ARG Q 61 NH2 0.097
REMARK 500 GLU Q 79 CG GLU Q 79 CD 0.100
REMARK 500 TYR R 50 CG TYR R 50 CD2 0.107
REMARK 500 TYR R 69 CZ TYR R 69 CE2 0.079
REMARK 500 ARG S 31 CZ ARG S 31 NH2 0.082
REMARK 500 ARG S 36 CD ARG S 36 NE 0.111
REMARK 500 ARG S 36 CZ ARG S 36 NH2 0.104
REMARK 500 ARG S 77 CZ ARG S 77 NH2 0.078
REMARK 500 ARG S 80 CD ARG S 80 NE 0.120
REMARK 500 ARG T 9 CZ ARG T 9 NH2 0.080
REMARK 500 ARG T 17 CZ ARG T 17 NH2 0.089
REMARK 500 ARG T 73 CD ARG T 73 NE 0.122
REMARK 500 GLU U 7 CG GLU U 7 CD 0.100
REMARK 500 ARG U 32 NE ARG U 32 CZ 0.084
REMARK 500 ARG U 34 NE ARG U 34 CZ 0.088
REMARK 500 TYR U 37 CG TYR U 37 CD2 0.081
REMARK 500 ARG B 34 NE ARG B 34 CZ 0.084
REMARK 500 SER B 85 CA SER B 85 CB 0.091
REMARK 500 ARG B 136 CD ARG B 136 NE 0.127
REMARK 500 ASP B 166 CA ASP B 166 CB 0.134
REMARK 500
REMARK 500 THIS ENTRY HAS 4090 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 J 5 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG J 9 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG J 9 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 PHE J 49 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 TYR J 65 CD1 - CG - CD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 TYR J 65 CB - CG - CD1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 TYR J 65 CG - CD2 - CE2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ARG K 12 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ALA K 24 N - CA - CB ANGL. DEV. = 9.6 DEGREES
REMARK 500 THR K 32 N - CA - CB ANGL. DEV. = 12.9 DEGREES
REMARK 500 ARG K 36 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 PHE K 51 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 ARG K 55 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG K 68 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 MET K 84 CG - SD - CE ANGL. DEV. = -11.1 DEGREES
REMARK 500 ARG K 97 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG K 121 NE - CZ - NH1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG K 121 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG K 126 NH1 - CZ - NH2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG K 126 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG L 8 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG L 13 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG L 13 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG L 30 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG L 35 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG L 49 CB - CG - CD ANGL. DEV. = 16.1 DEGREES
REMARK 500 TYR L 65 CB - CG - CD1 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG L 85 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG L 85 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG L 109 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG L 109 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG L 113 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 TYR L 116 CZ - CE2 - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG M 2 NE - CZ - NH1 ANGL. DEV. = -3.3 DEGREES
REMARK 500 TYR M 22 CG - CD2 - CE2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG M 28 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 GLU M 46 CB - CA - C ANGL. DEV. = -12.0 DEGREES
REMARK 500 ARG M 56 NE - CZ - NH2 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG M 69 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG M 69 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG M 78 N - CA - CB ANGL. DEV. = 11.1 DEGREES
REMARK 500 ARG M 78 NH1 - CZ - NH2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 ARG M 78 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG M 86 NE - CZ - NH2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG M 91 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG M 97 NE - CZ - NH2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG M 106 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG M 108 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG N 12 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG N 12 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 7521 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 J 16 41.66 -70.31
REMARK 500 LEU J 17 -50.72 -175.72
REMARK 500 THR J 22 -11.50 -149.32
REMARK 500 ALA J 34 -2.25 -157.25
REMARK 500 PRO J 41 179.87 -54.19
REMARK 500 ARG J 48 134.38 -175.35
REMARK 500 HIS J 56 128.96 179.15
REMARK 500 VAL J 57 -146.46 46.94
REMARK 500 ASN J 58 73.71 44.12
REMARK 500 ILE J 67 93.08 -176.04
REMARK 500 VAL J 74 -80.17 87.01
REMARK 500 ASP J 75 61.99 82.96
REMARK 500 ASP J 85 -77.01 -48.04
REMARK 500 SER K 16 -35.50 79.85
REMARK 500 ASP K 35 -173.92 -56.40
REMARK 500 LEU K 41 -53.25 -135.79
REMARK 500 PHE K 51 -129.07 -142.62
REMARK 500 ARG K 52 -119.66 -85.29
REMARK 500 SER K 54 7.33 -154.50
REMARK 500 SER K 57 -18.51 -150.57
REMARK 500 LYS K 79 -9.64 -148.65
REMARK 500 ALA K 101 28.41 -63.60
REMARK 500 ALA K 102 16.11 -146.96
REMARK 500 THR K 107 -3.76 -143.68
REMARK 500 ILE K 109 -24.41 -142.59
REMARK 500 ASN K 118 120.02 106.33
REMARK 500 CYS K 120 162.98 -44.23
REMARK 500 LYS K 125 175.68 57.54
REMARK 500 ALA L 22 0.85 -151.33
REMARK 500 GLU L 24 -148.42 29.45
REMARK 500 ALA L 25 7.34 -162.18
REMARK 500 ARG L 35 149.28 -170.89
REMARK 500 LYS L 43 148.21 80.62
REMARK 500 VAL L 62 -175.89 -53.02
REMARK 500 ALA L 100 152.29 63.65
REMARK 500 LEU L 101 -149.14 60.68
REMARK 500 TYR L 116 -6.28 76.09
REMARK 500 ARG M 2 -19.22 -148.32
REMARK 500 ILE M 3 -78.49 96.14
REMARK 500 ALA M 4 -21.24 -150.56
REMARK 500 ILE M 6 114.78 64.42
REMARK 500 ILE M 16 -70.18 -37.47
REMARK 500 THR M 19 -161.88 49.35
REMARK 500 ILE M 21 59.80 -152.65
REMARK 500 TYR M 22 110.53 71.32
REMARK 500 VAL M 24 107.31 -161.61
REMARK 500 SER M 29 -89.33 -59.83
REMARK 500 ASP M 41 57.38 -109.05
REMARK 500 GLU M 65 -154.11 44.68
REMARK 500 CYS M 84 160.05 -46.14
REMARK 500
REMARK 500 THIS ENTRY HAS 345 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 GLY K 89 PRO K 90 -142.68
REMARK 500 VAL L 20 PRO L 21 -140.66
REMARK 500 ASN M 104 ALA M 105 -147.22
REMARK 500 ASP O 20 THR O 21 -146.29
REMARK 500 PHE B 68 VAL B 69 -148.63
REMARK 500 TYR C 167 ARG C 168 139.38
REMARK 500 ASP G 14 PRO G 15 -147.85
REMARK 500 ILE H 125 CYS H 126 -149.88
REMARK 500 ASN Z 51 ALA Z 52 -32.03
REMARK 500 TYR Z 160 ASP Z 161 147.04
REMARK 500 LYS Z 208 PRO Z 209 141.42
REMARK 500 ASP Z 354 ASN Z 355 149.88
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 J 9 0.13 SIDE CHAIN
REMARK 500 ARG J 16 0.10 SIDE CHAIN
REMARK 500 ARG J 68 0.10 SIDE CHAIN
REMARK 500 PHE K 26 0.08 SIDE CHAIN
REMARK 500 ARG K 55 0.08 SIDE CHAIN
REMARK 500 ARG K 97 0.10 SIDE CHAIN
REMARK 500 ARG L 13 0.10 SIDE CHAIN
REMARK 500 ARG L 30 0.11 SIDE CHAIN
REMARK 500 ARG L 49 0.11 SIDE CHAIN
REMARK 500 ARG L 53 0.12 SIDE CHAIN
REMARK 500 TYR L 65 0.12 SIDE CHAIN
REMARK 500 ARG L 93 0.09 SIDE CHAIN
REMARK 500 ARG M 2 0.09 SIDE CHAIN
REMARK 500 TYR M 22 0.09 SIDE CHAIN
REMARK 500 ARG M 100 0.22 SIDE CHAIN
REMARK 500 ARG N 12 0.11 SIDE CHAIN
REMARK 500 ARG N 52 0.13 SIDE CHAIN
REMARK 500 ARG N 62 0.09 SIDE CHAIN
REMARK 500 ARG N 68 0.09 SIDE CHAIN
REMARK 500 ARG N 84 0.10 SIDE CHAIN
REMARK 500 ARG O 16 0.10 SIDE CHAIN
REMARK 500 ARG O 57 0.12 SIDE CHAIN
REMARK 500 ARG O 62 0.09 SIDE CHAIN
REMARK 500 ARG O 79 0.13 SIDE CHAIN
REMARK 500 HIS P 9 0.07 SIDE CHAIN
REMARK 500 TYR P 17 0.07 SIDE CHAIN
REMARK 500 ARG P 25 0.11 SIDE CHAIN
REMARK 500 HIS Q 30 0.10 SIDE CHAIN
REMARK 500 TYR R 22 0.12 SIDE CHAIN
REMARK 500 TYR R 31 0.10 SIDE CHAIN
REMARK 500 ARG R 47 0.10 SIDE CHAIN
REMARK 500 TYR R 69 0.07 SIDE CHAIN
REMARK 500 TYR S 79 0.07 SIDE CHAIN
REMARK 500 ARG T 9 0.09 SIDE CHAIN
REMARK 500 ARG T 17 0.12 SIDE CHAIN
REMARK 500 ARG T 24 0.10 SIDE CHAIN
REMARK 500 ARG U 6 0.10 SIDE CHAIN
REMARK 500 ARG U 20 0.10 SIDE CHAIN
REMARK 500 TYR U 37 0.12 SIDE CHAIN
REMARK 500 ARG U 44 0.09 SIDE CHAIN
REMARK 500 ARG U 46 0.12 SIDE CHAIN
REMARK 500 PHE B 29 0.10 SIDE CHAIN
REMARK 500 PHE B 89 0.08 SIDE CHAIN
REMARK 500 ARG B 107 0.09 SIDE CHAIN
REMARK 500 ARG C 53 0.10 SIDE CHAIN
REMARK 500 ARG C 71 0.08 SIDE CHAIN
REMARK 500 ARG C 155 0.12 SIDE CHAIN
REMARK 500 ARG C 163 0.13 SIDE CHAIN
REMARK 500 PHE D 19 0.08 SIDE CHAIN
REMARK 500 TYR D 50 0.14 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 908 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 ARG M 108 -11.20
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 U A 137 -45.3 D D OUTSIDE RANGE
REMARK 500 A A1394 -45.2 D D OUTSIDE RANGE
REMARK 500 C W 17 33.5 D L WRONG HAND
REMARK 500 U W 47 33.0 D L WRONG HAND
REMARK 500 VAL J 57 22.6 L L OUTSIDE RANGE
REMARK 500 VAL L 62 23.8 L L OUTSIDE RANGE
REMARK 500 ALA L 100 24.6 L L OUTSIDE RANGE
REMARK 500 TYR L 116 22.7 L L OUTSIDE RANGE
REMARK 500 ILE M 6 23.7 L L OUTSIDE RANGE
REMARK 500 TYR M 22 24.8 L L OUTSIDE RANGE
REMARK 500 ILE M 52 22.8 L L OUTSIDE RANGE
REMARK 500 ARG M 78 24.5 L L OUTSIDE RANGE
REMARK 500 VAL N 44 22.6 L L OUTSIDE RANGE
REMARK 500 ASP N 53 23.3 L L OUTSIDE RANGE
REMARK 500 ILE O 35 24.1 L L OUTSIDE RANGE
REMARK 500 HIS O 45 22.3 L L OUTSIDE RANGE
REMARK 500 GLU O 82 20.1 L L OUTSIDE RANGE
REMARK 500 LEU O 86 24.9 L L OUTSIDE RANGE
REMARK 500 GLU P 48 23.5 L L OUTSIDE RANGE
REMARK 500 LYS Q 18 23.8 L L OUTSIDE RANGE
REMARK 500 HIS S 13 24.8 L L OUTSIDE RANGE
REMARK 500 GLN T 54 24.1 L L OUTSIDE RANGE
REMARK 500 VAL U 31 24.9 L L OUTSIDE RANGE
REMARK 500 LEU B 213 23.9 L L OUTSIDE RANGE
REMARK 500 ASP C 82 23.9 L L OUTSIDE RANGE
REMARK 500 ASP C 111 23.9 L L OUTSIDE RANGE
REMARK 500 ASN E 69 24.2 L L OUTSIDE RANGE
REMARK 500 VAL E 116 23.5 L L OUTSIDE RANGE
REMARK 500 VAL F 18 23.7 L L OUTSIDE RANGE
REMARK 500 ARG G 118 24.9 L L OUTSIDE RANGE
REMARK 500 GLN I 49 23.1 L L OUTSIDE RANGE
REMARK 500 ASP I 55 24.7 L L OUTSIDE RANGE
REMARK 500 ILE Z 31 24.8 L L OUTSIDE RANGE
REMARK 500 ILE Z 49 22.3 L L OUTSIDE RANGE
REMARK 500 TYR Z 76 24.6 L L OUTSIDE RANGE
REMARK 500 ILE Z 92 24.1 L L OUTSIDE RANGE
REMARK 500 MET Z 98 20.2 L L OUTSIDE RANGE
REMARK 500 VAL Z 149 22.5 L L OUTSIDE RANGE
REMARK 500 MET Z 151 22.1 L L OUTSIDE RANGE
REMARK 500 ILE Z 281 23.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP Z 1397
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-5036 RELATED DB: EMDB
REMARK 900 6.7-A CRYO-EM MAP ON WHICH THIS MODEL IS BASED
REMARK 900 RELATED ID: 2I2U RELATED DB: PDB
REMARK 900 INITIAL COORDINATES USED FOR FITTING THE 30S INTO THE CRYO-
REMARK 900 EM MAP
REMARK 900 RELATED ID: 2I2V RELATED DB: PDB
REMARK 900 INITIAL COORDINATES USED FOR FITTING THE 50S INTO THE CRYO-
REMARK 900 EM MAP
REMARK 900 RELATED ID: 2J00 RELATED DB: PDB
REMARK 900 INITIAL COORDINATES USED FOR FITTING P- AND E-SITE TRNAS
REMARK 900 INTO THE CRYO-EM MAP
REMARK 900 RELATED ID: 1OB2 RELATED DB: PDB
REMARK 900 INITIAL COORDINATES USED FOR FITTING THE TERNARY COMPLEX
REMARK 900 INTO THE CRYO-EM MAP
DBREF 3FIH J 5 102 UNP P0A7R5 RS10_ECOLI 5 102
DBREF 3FIH K 12 128 UNP P0A7R9 RS11_ECOLI 13 129
DBREF 3FIH L 1 123 UNP P0A7S3 RS12_ECOLI 2 124
DBREF 3FIH M 1 113 UNP P0A7S9 RS13_ECOLI 2 114
DBREF 3FIH N 1 100 UNP P0AG59 RS14_ECOLI 2 101
DBREF 3FIH O 1 88 UNP Q8X9M2 RS15_ECO57 2 89
DBREF 3FIH P 1 80 UNP P0A7T3 RS16_ECOLI 1 80
DBREF 3FIH Q 3 82 UNP P0AG63 RS17_ECOLI 4 83
DBREF 3FIH R 19 73 UNP P0A7T7 RS18_ECOLI 20 74
DBREF 3FIH S 2 80 UNP P0A7U3 RS19_ECOLI 3 81
DBREF 3FIH T 2 86 UNP P0A7U7 RS20_ECOLI 3 87
DBREF 3FIH U 3 53 UNP P68679 RS21_ECOLI 4 54
DBREF 3FIH B 8 225 UNP P0A7V0 RS2_ECOLI 9 226
DBREF 3FIH C 1 206 UNP P0A7V3 RS3_ECOLI 2 207
DBREF 3FIH D 1 205 UNP P0A7V8 RS4_ECOLI 2 206
DBREF 3FIH E 9 158 UNP P0A7W1 RS5_ECOLI 10 159
DBREF 3FIH F 1 100 UNP P02358 RS6_ECOLI 1 100
DBREF 3FIH G 2 151 UNP P02359 RS7_ECOLI 3 152
DBREF 3FIH H 1 129 UNP P0A7W7 RS8_ECOLI 2 130
DBREF 3FIH I 3 129 UNP P0A7X3 RS9_ECOLI 4 130
DBREF 3FIH A 5 1534 GB 83754040 2AVY_A 5 1534
DBREF 3FIH Z 1 393 UNP P0A6N1 EFTU_ECOLI 2 394
SEQADV 3FIH N UNP P0AG59 SER 37 DELETION
SEQADV 3FIH N UNP P0AG59 ASP 38 DELETION
SEQADV 3FIH N UNP P0AG59 GLU 39 DELETION
SEQADV 3FIH N UNP P0AG59 ASP 40 DELETION
SEQRES 1 J 98 ARG ILE ARG ILE ARG LEU LYS ALA PHE ASP HIS ARG LEU
SEQRES 2 J 98 ILE ASP GLN ALA THR ALA GLU ILE VAL GLU THR ALA LYS
SEQRES 3 J 98 ARG THR GLY ALA GLN VAL ARG GLY PRO ILE PRO LEU PRO
SEQRES 4 J 98 THR ARG LYS GLU ARG PHE THR VAL LEU ILE SER PRO HIS
SEQRES 5 J 98 VAL ASN LYS ASP ALA ARG ASP GLN TYR GLU ILE ARG THR
SEQRES 6 J 98 HIS LEU ARG LEU VAL ASP ILE VAL GLU PRO THR GLU LYS
SEQRES 7 J 98 THR VAL ASP ALA LEU MET ARG LEU ASP LEU ALA ALA GLY
SEQRES 8 J 98 VAL ASP VAL GLN ILE SER LEU
SEQRES 1 K 117 ARG LYS GLN VAL SER ASP GLY VAL ALA HIS ILE HIS ALA
SEQRES 2 K 117 SER PHE ASN ASN THR ILE VAL THR ILE THR ASP ARG GLN
SEQRES 3 K 117 GLY ASN ALA LEU GLY TRP ALA THR ALA GLY GLY SER GLY
SEQRES 4 K 117 PHE ARG GLY SER ARG LYS SER THR PRO PHE ALA ALA GLN
SEQRES 5 K 117 VAL ALA ALA GLU ARG CYS ALA ASP ALA VAL LYS GLU TYR
SEQRES 6 K 117 GLY ILE LYS ASN LEU GLU VAL MET VAL LYS GLY PRO GLY
SEQRES 7 K 117 PRO GLY ARG GLU SER THR ILE ARG ALA LEU ASN ALA ALA
SEQRES 8 K 117 GLY PHE ARG ILE THR ASN ILE THR ASP VAL THR PRO ILE
SEQRES 9 K 117 PRO HIS ASN GLY CYS ARG PRO PRO LYS LYS ARG ARG VAL
SEQRES 1 L 123 ALA THR VAL ASN GLN LEU VAL ARG LYS PRO ARG ALA ARG
SEQRES 2 L 123 LYS VAL ALA LYS SER ASN VAL PRO ALA LEU GLU ALA CYS
SEQRES 3 L 123 PRO GLN LYS ARG GLY VAL CYS THR ARG VAL TYR THR THR
SEQRES 4 L 123 THR PRO LYS LYS PRO ASN SER ALA LEU ARG LYS VAL CYS
SEQRES 5 L 123 ARG VAL ARG LEU THR ASN GLY PHE GLU VAL THR SER TYR
SEQRES 6 L 123 ILE GLY GLY GLU GLY HIS ASN LEU GLN GLU HIS SER VAL
SEQRES 7 L 123 ILE LEU ILE ARG GLY GLY ARG VAL LYS ASP LEU PRO GLY
SEQRES 8 L 123 VAL ARG TYR HIS THR VAL ARG GLY ALA LEU ASP CYS SER
SEQRES 9 L 123 GLY VAL LYS ASP ARG LYS GLN ALA ARG SER LYS TYR GLY
SEQRES 10 L 123 VAL LYS ARG PRO LYS ALA
SEQRES 1 M 113 ALA ARG ILE ALA GLY ILE ASN ILE PRO ASP HIS LYS HIS
SEQRES 2 M 113 ALA VAL ILE ALA LEU THR SER ILE TYR GLY VAL GLY LYS
SEQRES 3 M 113 THR ARG SER LYS ALA ILE LEU ALA ALA ALA GLY ILE ALA
SEQRES 4 M 113 GLU ASP VAL LYS ILE SER GLU LEU SER GLU GLY GLN ILE
SEQRES 5 M 113 ASP THR LEU ARG ASP GLU VAL ALA LYS PHE VAL VAL GLU
SEQRES 6 M 113 GLY ASP LEU ARG ARG GLU ILE SER MET SER ILE LYS ARG
SEQRES 7 M 113 LEU MET ASP LEU GLY CYS TYR ARG GLY LEU ARG HIS ARG
SEQRES 8 M 113 ARG GLY LEU PRO VAL ARG GLY GLN ARG THR LYS THR ASN
SEQRES 9 M 113 ALA ARG THR ARG LYS GLY PRO ARG LYS
SEQRES 1 N 96 ALA LYS GLN SER MET LYS ALA ARG GLU VAL LYS ARG VAL
SEQRES 2 N 96 ALA LEU ALA ASP LYS TYR PHE ALA LYS ARG ALA GLU LEU
SEQRES 3 N 96 LYS ALA ILE ILE SER ASP VAL ASN ALA ARG TRP ASN ALA
SEQRES 4 N 96 VAL LEU LYS LEU GLN THR LEU PRO ARG ASP SER SER PRO
SEQRES 5 N 96 SER ARG GLN ARG ASN ARG CYS ARG GLN THR GLY ARG PRO
SEQRES 6 N 96 HIS GLY PHE LEU ARG LYS PHE GLY LEU SER ARG ILE LYS
SEQRES 7 N 96 VAL ARG GLU ALA ALA MET ARG GLY GLU ILE PRO GLY LEU
SEQRES 8 N 96 LYS LYS ALA SER TRP
SEQRES 1 O 88 SER LEU SER THR GLU ALA THR ALA LYS ILE VAL SER GLU
SEQRES 2 O 88 PHE GLY ARG ASP ALA ASN ASP THR GLY SER THR GLU VAL
SEQRES 3 O 88 GLN VAL ALA LEU LEU THR ALA GLN ILE ASN HIS LEU GLN
SEQRES 4 O 88 GLY HIS PHE ALA GLU HIS LYS LYS ASP HIS HIS SER ARG
SEQRES 5 O 88 ARG GLY LEU LEU ARG MET VAL SER GLN ARG ARG LYS LEU
SEQRES 6 O 88 LEU ASP TYR LEU LYS ARG LYS ASP VAL ALA ARG TYR THR
SEQRES 7 O 88 ARG LEU ILE GLU ARG LEU GLY LEU ARG ARG
SEQRES 1 P 80 MET VAL THR ILE ARG LEU ALA ARG HIS GLY ALA LYS LYS
SEQRES 2 P 80 ARG PRO PHE TYR GLN VAL VAL VAL ALA ASP SER ARG ASN
SEQRES 3 P 80 ALA ARG ASN GLY ARG PHE ILE GLU ARG VAL GLY PHE PHE
SEQRES 4 P 80 ASN PRO ILE ALA SER GLU LYS GLU GLU GLY THR ARG LEU
SEQRES 5 P 80 ASP LEU ASP ARG ILE ALA HIS TRP VAL GLY GLN GLY ALA
SEQRES 6 P 80 THR ILE SER ASP ARG VAL ALA ALA LEU ILE LYS GLU VAL
SEQRES 7 P 80 ASN LYS
SEQRES 1 Q 80 LYS ILE ARG THR LEU GLN GLY ARG VAL VAL SER ASP LYS
SEQRES 2 Q 80 MET GLU LYS SER ILE VAL VAL ALA ILE GLU ARG PHE VAL
SEQRES 3 Q 80 LYS HIS PRO ILE TYR GLY LYS PHE ILE LYS ARG THR THR
SEQRES 4 Q 80 LYS LEU HIS VAL HIS ASP GLU ASN ASN GLU CYS GLY ILE
SEQRES 5 Q 80 GLY ASP VAL VAL GLU ILE ARG GLU CYS ARG PRO LEU SER
SEQRES 6 Q 80 LYS THR LYS SER TRP THR LEU VAL ARG VAL VAL GLU LYS
SEQRES 7 Q 80 ALA VAL
SEQRES 1 R 55 GLU ILE ASP TYR LYS ASP ILE ALA THR LEU LYS ASN TYR
SEQRES 2 R 55 ILE THR GLU SER GLY LYS ILE VAL PRO SER ARG ILE THR
SEQRES 3 R 55 GLY THR ARG ALA LYS TYR GLN ARG GLN LEU ALA ARG ALA
SEQRES 4 R 55 ILE LYS ARG ALA ARG TYR LEU SER LEU LEU PRO TYR THR
SEQRES 5 R 55 ASP ARG HIS
SEQRES 1 S 79 ARG SER LEU LYS LYS GLY PRO PHE ILE ASP LEU HIS LEU
SEQRES 2 S 79 LEU LYS LYS VAL GLU LYS ALA VAL GLU SER GLY ASP LYS
SEQRES 3 S 79 LYS PRO LEU ARG THR TRP SER ARG ARG SER THR ILE PHE
SEQRES 4 S 79 PRO ASN MET ILE GLY LEU THR ILE ALA VAL HIS ASN GLY
SEQRES 5 S 79 ARG GLN HIS VAL PRO VAL PHE VAL THR ASP GLU MET VAL
SEQRES 6 S 79 GLY HIS LYS LEU GLY GLU PHE ALA PRO THR ARG THR TYR
SEQRES 7 S 79 ARG
SEQRES 1 T 85 ASN ILE LYS SER ALA LYS LYS ARG ALA ILE GLN SER GLU
SEQRES 2 T 85 LYS ALA ARG LYS HIS ASN ALA SER ARG ARG SER MET MET
SEQRES 3 T 85 ARG THR PHE ILE LYS LYS VAL TYR ALA ALA ILE GLU ALA
SEQRES 4 T 85 GLY ASP LYS ALA ALA ALA GLN LYS ALA PHE ASN GLU MET
SEQRES 5 T 85 GLN PRO ILE VAL ASP ARG GLN ALA ALA LYS GLY LEU ILE
SEQRES 6 T 85 HIS LYS ASN LYS ALA ALA ARG HIS LYS ALA ASN LEU THR
SEQRES 7 T 85 ALA GLN ILE ASN LYS LEU ALA
SEQRES 1 U 51 ILE LYS VAL ARG GLU ASN GLU PRO PHE ASP VAL ALA LEU
SEQRES 2 U 51 ARG ARG PHE LYS ARG SER CYS GLU LYS ALA GLY VAL LEU
SEQRES 3 U 51 ALA GLU VAL ARG ARG ARG GLU PHE TYR GLU LYS PRO THR
SEQRES 4 U 51 THR GLU ARG LYS ARG ALA LYS ALA SER ALA VAL LYS
SEQRES 1 B 218 MET LEU LYS ALA GLY VAL HIS PHE GLY HIS GLN THR ARG
SEQRES 2 B 218 TYR TRP ASN PRO LYS MET LYS PRO PHE ILE PHE GLY ALA
SEQRES 3 B 218 ARG ASN LYS VAL HIS ILE ILE ASN LEU GLU LYS THR VAL
SEQRES 4 B 218 PRO MET PHE ASN GLU ALA LEU ALA GLU LEU ASN LYS ILE
SEQRES 5 B 218 ALA SER ARG LYS GLY LYS ILE LEU PHE VAL GLY THR LYS
SEQRES 6 B 218 ARG ALA ALA SER GLU ALA VAL LYS ASP ALA ALA LEU SER
SEQRES 7 B 218 CYS ASP GLN PHE PHE VAL ASN HIS ARG TRP LEU GLY GLY
SEQRES 8 B 218 MET LEU THR ASN TRP LYS THR VAL ARG GLN SER ILE LYS
SEQRES 9 B 218 ARG LEU LYS ASP LEU GLU THR GLN SER GLN ASP GLY THR
SEQRES 10 B 218 PHE ASP LYS LEU THR LYS LYS GLU ALA LEU MET ARG THR
SEQRES 11 B 218 ARG GLU LEU GLU LYS LEU GLU ASN SER LEU GLY GLY ILE
SEQRES 12 B 218 LYS ASP MET GLY GLY LEU PRO ASP ALA LEU PHE VAL ILE
SEQRES 13 B 218 ASP ALA ASP HIS GLU HIS ILE ALA ILE LYS GLU ALA ASN
SEQRES 14 B 218 ASN LEU GLY ILE PRO VAL PHE ALA ILE VAL ASP THR ASN
SEQRES 15 B 218 SER ASP PRO ASP GLY VAL ASP PHE VAL ILE PRO GLY ASN
SEQRES 16 B 218 ASP ASP ALA ILE ARG ALA VAL THR LEU TYR LEU GLY ALA
SEQRES 17 B 218 VAL ALA ALA THR VAL ARG GLU GLY ARG SER
SEQRES 1 C 206 GLY GLN LYS VAL HIS PRO ASN GLY ILE ARG LEU GLY ILE
SEQRES 2 C 206 VAL LYS PRO TRP ASN SER THR TRP PHE ALA ASN THR LYS
SEQRES 3 C 206 GLU PHE ALA ASP ASN LEU ASP SER ASP PHE LYS VAL ARG
SEQRES 4 C 206 GLN TYR LEU THR LYS GLU LEU ALA LYS ALA SER VAL SER
SEQRES 5 C 206 ARG ILE VAL ILE GLU ARG PRO ALA LYS SER ILE ARG VAL
SEQRES 6 C 206 THR ILE HIS THR ALA ARG PRO GLY ILE VAL ILE GLY LYS
SEQRES 7 C 206 LYS GLY GLU ASP VAL GLU LYS LEU ARG LYS VAL VAL ALA
SEQRES 8 C 206 ASP ILE ALA GLY VAL PRO ALA GLN ILE ASN ILE ALA GLU
SEQRES 9 C 206 VAL ARG LYS PRO GLU LEU ASP ALA LYS LEU VAL ALA ASP
SEQRES 10 C 206 SER ILE THR SER GLN LEU GLU ARG ARG VAL MET PHE ARG
SEQRES 11 C 206 ARG ALA MET LYS ARG ALA VAL GLN ASN ALA MET ARG LEU
SEQRES 12 C 206 GLY ALA LYS GLY ILE LYS VAL GLU VAL SER GLY ARG LEU
SEQRES 13 C 206 GLY GLY ALA GLU ILE ALA ARG THR GLU TRP TYR ARG GLU
SEQRES 14 C 206 GLY ARG VAL PRO LEU HIS THR LEU ARG ALA ASP ILE ASP
SEQRES 15 C 206 TYR ASN THR SER GLU ALA HIS THR THR TYR GLY VAL ILE
SEQRES 16 C 206 GLY VAL LYS VAL TRP ILE PHE LYS GLY GLU ILE
SEQRES 1 D 205 ALA ARG TYR LEU GLY PRO LYS LEU LYS LEU SER ARG ARG
SEQRES 2 D 205 GLU GLY THR ASP LEU PHE LEU LYS SER GLY VAL ARG ALA
SEQRES 3 D 205 ILE ASP THR LYS CYS LYS ILE GLU GLN ALA PRO GLY GLN
SEQRES 4 D 205 HIS GLY ALA ARG LYS PRO ARG LEU SER ASP TYR GLY VAL
SEQRES 5 D 205 GLN LEU ARG GLU LYS GLN LYS VAL ARG ARG ILE TYR GLY
SEQRES 6 D 205 VAL LEU GLU ARG GLN PHE ARG ASN TYR TYR LYS GLU ALA
SEQRES 7 D 205 ALA ARG LEU LYS GLY ASN THR GLY GLU ASN LEU LEU ALA
SEQRES 8 D 205 LEU LEU GLU GLY ARG LEU ASP ASN VAL VAL TYR ARG MET
SEQRES 9 D 205 GLY PHE GLY ALA THR ARG ALA GLU ALA ARG GLN LEU VAL
SEQRES 10 D 205 SER HIS LYS ALA ILE MET VAL ASN GLY ARG VAL VAL ASN
SEQRES 11 D 205 ILE ALA SER TYR GLN VAL SER PRO ASN ASP VAL VAL SER
SEQRES 12 D 205 ILE ARG GLU LYS ALA LYS LYS GLN SER ARG VAL LYS ALA
SEQRES 13 D 205 ALA LEU GLU LEU ALA GLU GLN ARG GLU LYS PRO THR TRP
SEQRES 14 D 205 LEU GLU VAL ASP ALA GLY LYS MET GLU GLY THR PHE LYS
SEQRES 15 D 205 ARG LYS PRO GLU ARG SER ASP LEU SER ALA ASP ILE ASN
SEQRES 16 D 205 GLU HIS LEU ILE VAL GLU LEU TYR SER LYS
SEQRES 1 E 150 GLU LEU GLN GLU LYS LEU ILE ALA VAL ASN ARG VAL SER
SEQRES 2 E 150 LYS THR VAL LYS GLY GLY ARG ILE PHE SER PHE THR ALA
SEQRES 3 E 150 LEU THR VAL VAL GLY ASP GLY ASN GLY ARG VAL GLY PHE
SEQRES 4 E 150 GLY TYR GLY LYS ALA ARG GLU VAL PRO ALA ALA ILE GLN
SEQRES 5 E 150 LYS ALA MET GLU LYS ALA ARG ARG ASN MET ILE ASN VAL
SEQRES 6 E 150 ALA LEU ASN ASN GLY THR LEU GLN HIS PRO VAL LYS GLY
SEQRES 7 E 150 VAL HIS THR GLY SER ARG VAL PHE MET GLN PRO ALA SER
SEQRES 8 E 150 GLU GLY THR GLY ILE ILE ALA GLY GLY ALA MET ARG ALA
SEQRES 9 E 150 VAL LEU GLU VAL ALA GLY VAL HIS ASN VAL LEU ALA LYS
SEQRES 10 E 150 ALA TYR GLY SER THR ASN PRO ILE ASN VAL VAL ARG ALA
SEQRES 11 E 150 THR ILE ASP GLY LEU GLU ASN MET ASN SER PRO GLU MET
SEQRES 12 E 150 VAL ALA ALA LYS ARG GLY LYS
SEQRES 1 F 100 MET ARG HIS TYR GLU ILE VAL PHE MET VAL HIS PRO ASP
SEQRES 2 F 100 GLN SER GLU GLN VAL PRO GLY MET ILE GLU ARG TYR THR
SEQRES 3 F 100 ALA ALA ILE THR GLY ALA GLU GLY LYS ILE HIS ARG LEU
SEQRES 4 F 100 GLU ASP TRP GLY ARG ARG GLN LEU ALA TYR PRO ILE ASN
SEQRES 5 F 100 LYS LEU HIS LYS ALA HIS TYR VAL LEU MET ASN VAL GLU
SEQRES 6 F 100 ALA PRO GLN GLU VAL ILE ASP GLU LEU GLU THR THR PHE
SEQRES 7 F 100 ARG PHE ASN ASP ALA VAL ILE ARG SER MET VAL MET ARG
SEQRES 8 F 100 THR LYS HIS ALA VAL THR GLU ALA SER
SEQRES 1 G 150 ARG ARG ARG VAL ILE GLY GLN ARG LYS ILE LEU PRO ASP
SEQRES 2 G 150 PRO LYS PHE GLY SER GLU LEU LEU ALA LYS PHE VAL ASN
SEQRES 3 G 150 ILE LEU MET VAL ASP GLY LYS LYS SER THR ALA GLU SER
SEQRES 4 G 150 ILE VAL TYR SER ALA LEU GLU THR LEU ALA GLN ARG SER
SEQRES 5 G 150 GLY LYS SER GLU LEU GLU ALA PHE GLU VAL ALA LEU GLU
SEQRES 6 G 150 ASN VAL ARG PRO THR VAL GLU VAL LYS SER ARG ARG VAL
SEQRES 7 G 150 GLY GLY SER THR TYR GLN VAL PRO VAL GLU VAL ARG PRO
SEQRES 8 G 150 VAL ARG ARG ASN ALA LEU ALA MET ARG TRP ILE VAL GLU
SEQRES 9 G 150 ALA ALA ARG LYS ARG GLY ASP LYS SER MET ALA LEU ARG
SEQRES 10 G 150 LEU ALA ASN GLU LEU SER ASP ALA ALA GLU ASN LYS GLY
SEQRES 11 G 150 THR ALA VAL LYS LYS ARG GLU ASP VAL HIS ARG MET ALA
SEQRES 12 G 150 GLU ALA ASN LYS ALA PHE ALA
SEQRES 1 H 129 SER MET GLN ASP PRO ILE ALA ASP MET LEU THR ARG ILE
SEQRES 2 H 129 ARG ASN GLY GLN ALA ALA ASN LYS ALA ALA VAL THR MET
SEQRES 3 H 129 PRO SER SER LYS LEU LYS VAL ALA ILE ALA ASN VAL LEU
SEQRES 4 H 129 LYS GLU GLU GLY PHE ILE GLU ASP PHE LYS VAL GLU GLY
SEQRES 5 H 129 ASP THR LYS PRO GLU LEU GLU LEU THR LEU LYS TYR PHE
SEQRES 6 H 129 GLN GLY LYS ALA VAL VAL GLU SER ILE GLN ARG VAL SER
SEQRES 7 H 129 ARG PRO GLY LEU ARG ILE TYR LYS ARG LYS ASP GLU LEU
SEQRES 8 H 129 PRO LYS VAL MET ALA GLY LEU GLY ILE ALA VAL VAL SER
SEQRES 9 H 129 THR SER LYS GLY VAL MET THR ASP ARG ALA ALA ARG GLN
SEQRES 10 H 129 ALA GLY LEU GLY GLY GLU ILE ILE CYS TYR VAL ALA
SEQRES 1 I 127 ASN GLN TYR TYR GLY THR GLY ARG ARG LYS SER SER ALA
SEQRES 2 I 127 ALA ARG VAL PHE ILE LYS PRO GLY ASN GLY LYS ILE VAL
SEQRES 3 I 127 ILE ASN GLN ARG SER LEU GLU GLN TYR PHE GLY ARG GLU
SEQRES 4 I 127 THR ALA ARG MET VAL VAL ARG GLN PRO LEU GLU LEU VAL
SEQRES 5 I 127 ASP MET VAL GLU LYS LEU ASP LEU TYR ILE THR VAL LYS
SEQRES 6 I 127 GLY GLY GLY ILE SER GLY GLN ALA GLY ALA ILE ARG HIS
SEQRES 7 I 127 GLY ILE THR ARG ALA LEU MET GLU TYR ASP GLU SER LEU
SEQRES 8 I 127 ARG SER GLU LEU ARG LYS ALA GLY PHE VAL THR ARG ASP
SEQRES 9 I 127 ALA ARG GLN VAL GLU ARG LYS LYS VAL GLY LEU ARG LYS
SEQRES 10 I 127 ALA ARG ARG ARG PRO GLN PHE SER LYS ARG
SEQRES 1 A 1530 U G A A G A G U U U G A U
SEQRES 2 A 1530 C A U G G C U C A G A U U
SEQRES 3 A 1530 G A A C G C U G G C G G C
SEQRES 4 A 1530 A G G C C U A A C A C A U
SEQRES 5 A 1530 G C A A G U C G A A C G G
SEQRES 6 A 1530 U A A C A G G A A G A A G
SEQRES 7 A 1530 C U U G C U U C U U U G C
SEQRES 8 A 1530 U G A C G A G U G G C G G
SEQRES 9 A 1530 A C G G G U G A G U A A U
SEQRES 10 A 1530 G U C U G G G A A A C U G
SEQRES 11 A 1530 C C U G A U G G A G G G G
SEQRES 12 A 1530 G A U A A C U A C U G G A
SEQRES 13 A 1530 A A C G G U A G C U A A U
SEQRES 14 A 1530 A C C G C A U A A C G U C
SEQRES 15 A 1530 G C A A G A C C A A A G A
SEQRES 16 A 1530 G G G G G A C C U U C G G
SEQRES 17 A 1530 G C C U C U U G C C A U C
SEQRES 18 A 1530 G G A U G U G C C C A G A
SEQRES 19 A 1530 U G G G A U U A G C U A G
SEQRES 20 A 1530 U A G G U G G G G U A A C
SEQRES 21 A 1530 G G C U C A C C U A G G C
SEQRES 22 A 1530 G A C G A U C C C U A G C
SEQRES 23 A 1530 U G G U C U G A G A G G A
SEQRES 24 A 1530 U G A C C A G C C A C A C
SEQRES 25 A 1530 U G G A A C U G A G A C A
SEQRES 26 A 1530 C G G U C C A G A C U C C
SEQRES 27 A 1530 U A C G G G A G G C A G C
SEQRES 28 A 1530 A G U G G G G A A U A U U
SEQRES 29 A 1530 G C A C A A U G G G C G C
SEQRES 30 A 1530 A A G C C U G A U G C A G
SEQRES 31 A 1530 C C A U G C C G C G U G U
SEQRES 32 A 1530 A U G A A G A A G G C C U
SEQRES 33 A 1530 U C G G G U U G U A A A G
SEQRES 34 A 1530 U A C U U U C A G C G G G
SEQRES 35 A 1530 G A G G A A G G G A G U A
SEQRES 36 A 1530 A A G U U A A U A C C U U
SEQRES 37 A 1530 U G C U C A U U G A C G U
SEQRES 38 A 1530 U A C C C G C A G A A G A
SEQRES 39 A 1530 A G C A C C G G C U A A C
SEQRES 40 A 1530 U C C G U G C C A G C A G
SEQRES 41 A 1530 C C G C G G U A A U A C G
SEQRES 42 A 1530 G A G G G U G C A A G C G
SEQRES 43 A 1530 U U A A U C G G A A U U A
SEQRES 44 A 1530 C U G G G C G U A A A G C
SEQRES 45 A 1530 G C A C G C A G G C G G U
SEQRES 46 A 1530 U U G U U A A G U C A G A
SEQRES 47 A 1530 U G U G A A A U C C C C G
SEQRES 48 A 1530 G G C U C A A C C U G G G
SEQRES 49 A 1530 A A C U G C A U C U G A U
SEQRES 50 A 1530 A C U G G C A A G C U U G
SEQRES 51 A 1530 A G U C U C G U A G A G G
SEQRES 52 A 1530 G G G G U A G A A U U C C
SEQRES 53 A 1530 A G G U G U A G C G G U G
SEQRES 54 A 1530 A A A U G C G U A G A G A
SEQRES 55 A 1530 U C U G G A G G A A U A C
SEQRES 56 A 1530 C G G U G G C G A A G G C
SEQRES 57 A 1530 G G C C C C C U G G A C G
SEQRES 58 A 1530 A A G A C U G A C G C U C
SEQRES 59 A 1530 A G G U G C G A A A G C G
SEQRES 60 A 1530 U G G G G A G C A A A C A
SEQRES 61 A 1530 G G A U U A G A U A C C C
SEQRES 62 A 1530 U G G U A G U C C A C G C
SEQRES 63 A 1530 C G U A A A C G A U G U C
SEQRES 64 A 1530 G A C U U G G A G G U U G
SEQRES 65 A 1530 U G C C C U U G A G G C G
SEQRES 66 A 1530 U G G C U U C C G G A G C
SEQRES 67 A 1530 U A A C G C G U U A A G U
SEQRES 68 A 1530 C G A C C G C C U G G G G
SEQRES 69 A 1530 A G U A C G G C C G C A A
SEQRES 70 A 1530 G G U U A A A A C U C A A
SEQRES 71 A 1530 A U G A A U U G A C G G G
SEQRES 72 A 1530 G G C C C G C A C A A G C
SEQRES 73 A 1530 G G U G G A G C A U G U G
SEQRES 74 A 1530 G U U U A A U U C G A U G
SEQRES 75 A 1530 C A A C G C G A A G A A C
SEQRES 76 A 1530 C U U A C C U G G U C U U
SEQRES 77 A 1530 G A C A U C C A C G G A A
SEQRES 78 A 1530 G U U U U C A G A G A U G
SEQRES 79 A 1530 A G A A U G U G C C U U C
SEQRES 80 A 1530 G G G A A C C G U G A G A
SEQRES 81 A 1530 C A G G U G C U G C A U G
SEQRES 82 A 1530 G C U G U C G U C A G C U
SEQRES 83 A 1530 C G U G U U G U G A A A U
SEQRES 84 A 1530 G U U G G G U U A A G U C
SEQRES 85 A 1530 C C G C A A C G A G C G C
SEQRES 86 A 1530 A A C C C U U A U C C U U
SEQRES 87 A 1530 U G U U G C C A G C G G U
SEQRES 88 A 1530 C C G G C C G G G A A C U
SEQRES 89 A 1530 C A A A G G A G A C U G C
SEQRES 90 A 1530 C A G U G A U A A A C U G
SEQRES 91 A 1530 G A G G A A G G U G G G G
SEQRES 92 A 1530 A U G A C G U C A A G U C
SEQRES 93 A 1530 A U C A U G G C C C U U A
SEQRES 94 A 1530 C G A C C A G G G C U A C
SEQRES 95 A 1530 A C A C G U G C U A C A A
SEQRES 96 A 1530 U G G C G C A U A C A A A
SEQRES 97 A 1530 G A G A A G C G A C C U C
SEQRES 98 A 1530 G C G A G A G C A A G C G
SEQRES 99 A 1530 G A C C U C A U A A A G U
SEQRES 100 A 1530 G C G U C G U A G U C C G
SEQRES 101 A 1530 G A U U G G A G U C U G C
SEQRES 102 A 1530 A A C U C G A C U C C A U
SEQRES 103 A 1530 G A A G U C G G A A U C G
SEQRES 104 A 1530 C U A G U A A U C G U G G
SEQRES 105 A 1530 A U C A G A A U G C C A C
SEQRES 106 A 1530 G G U G A A U A C G U U C
SEQRES 107 A 1530 C C G G G C C U U G U A C
SEQRES 108 A 1530 A C A C C G C C C G U C A
SEQRES 109 A 1530 C A C C A U G G G A G U G
SEQRES 110 A 1530 G G U U G C A A A A G A A
SEQRES 111 A 1530 G U A G G U A G C U U A A
SEQRES 112 A 1530 C C U U C G G G A G G G C
SEQRES 113 A 1530 G C U U A C C A C U U U G
SEQRES 114 A 1530 U G A U U C A U G A C U G
SEQRES 115 A 1530 G G G U G A A G U C G U A
SEQRES 116 A 1530 A C A A G G U A A C C G U
SEQRES 117 A 1530 A G G G G A A C C U G C G
SEQRES 118 A 1530 G U U G G A U C A
SEQRES 1 Y 76 G C G G A U U U A G C U C
SEQRES 2 Y 76 A G U U G G G A G A G C G
SEQRES 3 Y 76 C C A G A C U G A A G A U
SEQRES 4 Y 76 C U G G A G G U C C U G U
SEQRES 5 Y 76 G U U C G A U C C A C A G
SEQRES 6 Y 76 A A U U C G C A C C A
SEQRES 1 W 76 G C C C G G A U A G C U C
SEQRES 2 W 76 A G U C G G U A G A G C A
SEQRES 3 W 76 G G G G A U U G A A A A U
SEQRES 4 W 76 C C C C G U G U C C U U G
SEQRES 5 W 76 G U U C G A U U C C G A G
SEQRES 6 W 76 U C C G G G C A C C A
SEQRES 1 X 11 A A A A A U G U U C A
SEQRES 1 Z 393 SER LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN
SEQRES 2 Z 393 VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR
SEQRES 3 Z 393 LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR
SEQRES 4 Z 393 GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN ALA
SEQRES 5 Z 393 PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR SER
SEQRES 6 Z 393 HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS
SEQRES 7 Z 393 VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET
SEQRES 8 Z 393 ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL
SEQRES 9 Z 393 VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU
SEQRES 10 Z 393 HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE
SEQRES 11 Z 393 ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU
SEQRES 12 Z 393 GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU
SEQRES 13 Z 393 LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE
SEQRES 14 Z 393 VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA
SEQRES 15 Z 393 GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU
SEQRES 16 Z 393 ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS
SEQRES 17 Z 393 PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER
SEQRES 18 Z 393 GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY
SEQRES 19 Z 393 ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE
SEQRES 20 Z 393 LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET
SEQRES 21 Z 393 PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN
SEQRES 22 Z 393 VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE
SEQRES 23 Z 393 GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS
SEQRES 24 Z 393 PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER
SEQRES 25 Z 393 LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY
SEQRES 26 Z 393 TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR
SEQRES 27 Z 393 GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET
SEQRES 28 Z 393 PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS
SEQRES 29 Z 393 PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG
SEQRES 30 Z 393 GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS
SEQRES 31 Z 393 VAL LEU SER
SEQRES 1 V 77 C G C G G G G U G G A G C
SEQRES 2 V 77 A G C C U G G U A G C U C
SEQRES 3 V 77 G U C G G G C U C A U A A
SEQRES 4 V 77 C C C G A A G G U C G U C
SEQRES 5 V 77 G G 5MU U C A A A U C C G G
SEQRES 6 V 77 C C C C C G C A A C C A
MODRES 3FIH 5MU V 54 U 5-METHYLURIDINE 5'-MONOPHOSPHATE
HET 5MU V 54 21
HET GDP Z1397 28
HETNAM 5MU 5-METHYLURIDINE 5'-MONOPHOSPHATE
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 26 5MU C10 H15 N2 O9 P
FORMUL 27 GDP C10 H15 N5 O11 P2
HELIX 1 1 ASP J 14 ASP J 19 1 6
HELIX 2 2 THR J 22 GLY J 33 1 12
HELIX 3 3 THR J 83 ARG J 89 1 7
HELIX 4 4 ALA K 46 GLY K 50 1 5
HELIX 5 5 THR K 58 LYS K 74 1 17
HELIX 6 6 GLU K 93 ALA K 101 1 9
HELIX 7 7 THR L 2 VAL L 7 1 6
HELIX 8 8 HIS M 13 THR M 19 1 7
HELIX 9 9 GLY M 25 GLY M 37 1 13
HELIX 10 10 GLY M 50 ALA M 60 1 11
HELIX 11 11 VAL M 64 GLY M 83 1 20
HELIX 12 12 CYS M 84 ARG M 89 1 6
HELIX 13 13 LYS N 2 ALA N 16 1 15
HELIX 14 14 ALA N 28 ASP N 32 5 5
HELIX 15 15 TRP N 41 LEU N 47 1 7
HELIX 16 16 ARG N 80 GLY N 90 1 11
HELIX 17 17 SER O 3 PHE O 14 1 12
HELIX 18 18 SER O 23 ASN O 36 1 14
HELIX 19 19 GLN O 39 GLU O 44 1 6
HELIX 20 20 ASP O 48 LYS O 70 1 23
HELIX 21 21 ASP O 73 GLY O 85 1 13
HELIX 22 22 SER P 68 ALA P 73 1 6
HELIX 23 23 ASP R 24 LYS R 29 1 6
HELIX 24 24 ARG R 47 TYR R 63 1 17
HELIX 25 25 LEU S 70 ALA S 74 5 5
HELIX 26 26 LYS T 8 ALA T 16 1 9
HELIX 27 27 LYS T 18 GLU T 39 1 22
HELIX 28 28 MET T 53 ALA T 62 1 10
HELIX 29 29 LEU T 78 ALA T 86 1 9
HELIX 30 30 ALA U 29 ARG U 33 5 5
HELIX 31 31 LYS B 44 ALA B 52 1 9
HELIX 32 32 VAL B 79 LEU B 84 1 6
HELIX 33 33 ASN B 102 LYS B 111 1 10
HELIX 34 34 ASP B 115 SER B 120 1 6
HELIX 35 35 GLN B 121 ASP B 126 5 6
HELIX 36 36 THR B 129 LYS B 142 1 14
HELIX 37 37 GLU B 168 ALA B 175 1 8
HELIX 38 38 ALA B 208 LEU B 213 1 6
HELIX 39 39 GLY B 214 VAL B 216 5 3
HELIX 40 40 LYS C 26 LEU C 46 1 21
HELIX 41 41 ASP C 82 ALA C 94 1 13
HELIX 42 42 ALA C 112 GLU C 124 1 13
HELIX 43 43 MET C 128 LEU C 143 1 16
HELIX 44 44 ARG C 155 ALA C 159 5 5
HELIX 45 45 PRO D 6 GLY D 15 1 10
HELIX 46 46 SER D 48 ILE D 63 1 16
HELIX 47 47 LEU D 67 ALA D 79 1 13
HELIX 48 48 ASN D 84 LEU D 93 1 10
HELIX 49 49 ARG D 96 ARG D 103 1 8
HELIX 50 50 THR D 109 HIS D 119 1 11
HELIX 51 51 GLU D 146 LYS D 149 5 4
HELIX 52 52 GLN D 151 ALA D 156 1 6
HELIX 53 53 ALA D 157 LEU D 158 5 2
HELIX 54 54 GLU D 159 ARG D 164 5 6
HELIX 55 55 ASN D 195 SER D 204 1 10
HELIX 56 56 PRO E 56 LYS E 65 1 10
HELIX 57 57 GLY E 108 ARG E 111 5 4
HELIX 58 58 ALA E 112 ALA E 117 1 6
HELIX 59 59 ASN E 131 VAL E 136 1 6
HELIX 60 60 ARG E 137 ALA E 138 5 2
HELIX 61 61 THR E 139 LEU E 143 5 5
HELIX 62 62 SER E 148 GLY E 157 1 10
HELIX 63 63 GLN F 17 GLY F 31 1 15
HELIX 64 64 PRO F 67 ARG F 79 1 13
HELIX 65 65 SER G 19 PHE G 25 1 7
HELIX 66 66 LYS G 35 SER G 53 1 19
HELIX 67 67 LEU G 58 ASN G 67 1 10
HELIX 68 68 ARG G 91 ALA G 106 1 16
HELIX 69 69 SER G 114 SER G 124 1 11
HELIX 70 70 GLY G 131 ALA G 144 1 14
HELIX 71 71 ASP H 4 ALA H 18 1 15
HELIX 72 72 SER H 29 GLU H 42 1 14
HELIX 73 73 VAL H 94 LEU H 98 5 5
HELIX 74 74 ASP H 112 ALA H 118 1 7
HELIX 75 75 SER I 33 PHE I 38 1 6
HELIX 76 76 THR I 42 VAL I 47 1 6
HELIX 77 77 ARG I 48 GLU I 52 5 5
HELIX 78 78 ILE I 71 THR I 83 1 13
HELIX 79 79 ARG I 94 LYS I 99 1 6
HELIX 80 80 GLY Z 23 LEU Z 35 1 13
HELIX 81 81 LEU Z 35 GLY Z 40 1 6
HELIX 82 82 ALA Z 52 GLY Z 59 1 8
HELIX 83 83 HIS Z 84 ASP Z 86 5 3
HELIX 84 84 TYR Z 87 ALA Z 96 1 10
HELIX 85 85 MET Z 112 GLY Z 126 1 15
HELIX 86 86 ASP Z 142 SER Z 158 1 17
HELIX 87 87 SER Z 173 ASP Z 181 1 9
HELIX 88 88 ASP Z 181 TYR Z 198 1 18
HELIX 89 89 LYS Z 282 ILE Z 286 5 5
SHEET 1 A 2 ILE J 8 ALA J 12 0
SHEET 2 A 2 VAL J 96 ILE J 100 -1 O ASP J 97 N LYS J 11
SHEET 1 B 3 THR J 50 VAL J 51 0
SHEET 2 B 3 ASP J 63 GLU J 66 -1 O ASP J 63 N VAL J 51
SHEET 3 B 3 LYS N 96 LYS N 97 -1 O LYS N 96 N GLU J 66
SHEET 1 C 4 ALA K 40 THR K 45 0
SHEET 2 C 4 ASN K 28 THR K 34 -1 N ILE K 33 O GLY K 42
SHEET 3 C 4 SER K 16 SER K 25 -1 N VAL K 19 O THR K 34
SHEET 4 C 4 ILE K 78 MET K 84 1 O GLU K 82 N ALA K 20
SHEET 1 D 6 LYS L 29 THR L 39 0
SHEET 2 D 6 ARG L 49 ARG L 55 -1 O ARG L 55 N VAL L 32
SHEET 3 D 6 THR L 63 ILE L 66 -1 O SER L 64 N CYS L 52
SHEET 4 D 6 TYR L 94 VAL L 97 1 O THR L 96 N TYR L 65
SHEET 5 D 6 ILE L 79 ILE L 81 -1 N LEU L 80 O VAL L 97
SHEET 6 D 6 LYS L 29 THR L 39 -1 N GLY L 31 O ILE L 79
SHEET 1 E 3 VAL P 2 ARG P 8 0
SHEET 2 E 3 TYR P 17 ASP P 23 -1 O ALA P 22 N THR P 3
SHEET 3 E 3 PHE P 32 PHE P 39 -1 O GLU P 34 N VAL P 21
SHEET 1 F 5 PHE Q 36 HIS Q 46 0
SHEET 2 F 5 SER Q 19 LYS Q 29 -1 N VAL Q 28 O ILE Q 37
SHEET 3 F 5 LEU Q 7 ASP Q 14 -1 N ARG Q 10 O ALA Q 23
SHEET 4 F 5 ILE Q 54 GLU Q 62 -1 O GLY Q 55 N VAL Q 11
SHEET 5 F 5 TRP Q 72 VAL Q 77 -1 O VAL Q 75 N GLU Q 59
SHEET 1 G 3 LEU S 30 THR S 32 0
SHEET 2 G 3 THR S 47 HIS S 51 1 O THR S 47 N LEU S 30
SHEET 3 G 3 HIS S 56 PHE S 60 -1 O VAL S 59 N ILE S 48
SHEET 1 H 2 THR C 66 THR C 69 0
SHEET 2 H 2 ASN C 101 GLU C 104 1 O ALA C 103 N ILE C 67
SHEET 1 I 3 ILE C 148 VAL C 152 0
SHEET 2 I 3 ILE C 195 ILE C 201 -1 O TRP C 200 N LYS C 149
SHEET 3 I 3 ASP C 182 ALA C 188 -1 N ASP C 182 O ILE C 201
SHEET 1 J 3 ARG D 127 VAL D 128 0
SHEET 2 J 3 ILE D 122 VAL D 124 -1 N VAL D 124 O ARG D 127
SHEET 3 J 3 VAL D 142 ILE D 144 -1 O SER D 143 N MET D 123
SHEET 1 K 2 GLN E 11 LEU E 14 0
SHEET 2 K 2 THR E 36 GLY E 39 -1 O VAL E 37 N LYS E 13
SHEET 1 L 2 ASN E 18 VAL E 20 0
SHEET 2 L 2 SER E 31 THR E 33 -1 O THR E 33 N ASN E 18
SHEET 1 M 3 VAL E 84 LYS E 85 0
SHEET 2 M 3 ARG E 92 GLN E 96 -1 O MET E 95 N VAL E 84
SHEET 3 M 3 LEU E 123 TYR E 127 -1 O LYS E 125 N PHE E 94
SHEET 1 N 3 VAL F 60 LEU F 61 0
SHEET 2 N 3 VAL F 7 VAL F 10 -1 N PHE F 8 O VAL F 60
SHEET 3 N 3 VAL F 84 MET F 88 -1 O ILE F 85 N MET F 9
SHEET 1 O 2 ARG G 77 VAL G 79 0
SHEET 2 O 2 SER G 82 TYR G 84 -1 O SER G 82 N VAL G 79
SHEET 1 P 3 ALA H 23 PRO H 27 0
SHEET 2 P 3 GLU H 57 LEU H 62 -1 O LEU H 58 N MET H 26
SHEET 3 P 3 ILE H 45 VAL H 50 -1 N LYS H 49 O GLU H 59
SHEET 1 Q 2 VAL H 102 SER H 104 0
SHEET 2 Q 2 VAL H 109 THR H 111 -1 O MET H 110 N VAL H 103
SHEET 1 R 3 TYR I 5 GLY I 7 0
SHEET 2 R 3 SER I 14 LYS I 21 -1 O ILE I 20 N TYR I 5
SHEET 3 R 3 ARG I 10 ARG I 11 -1 N ARG I 11 O SER I 14
SHEET 1 S 4 TYR I 5 GLY I 7 0
SHEET 2 S 4 SER I 14 LYS I 21 -1 O ILE I 20 N TYR I 5
SHEET 3 S 4 ASP I 61 VAL I 66 -1 O ASP I 61 N LYS I 21
SHEET 4 S 4 LYS I 26 ILE I 29 1 N VAL I 28 O LEU I 62
SHEET 1 T 2 GLU Z 3 LYS Z 4 0
SHEET 2 T 2 LYS Z 263 LEU Z 264 1 O LEU Z 264 N GLU Z 3
SHEET 1 U 3 HIS Z 11 VAL Z 14 0
SHEET 2 U 3 HIS Z 75 HIS Z 78 1 O ALA Z 77 N VAL Z 12
SHEET 3 U 3 VAL Z 67 ASP Z 70 -1 N TYR Z 69 O TYR Z 76
SHEET 1 V 4 THR Z 16 ILE Z 17 0
SHEET 2 V 4 ILE Z 102 ALA Z 106 1 O ILE Z 102 N ILE Z 17
SHEET 3 V 4 ILE Z 131 ASN Z 135 1 O PHE Z 133 N VAL Z 105
SHEET 4 V 4 VAL Z 170 GLY Z 172 1 O GLY Z 172 N LEU Z 134
SHEET 1 W 6 ASP Z 216 SER Z 219 0
SHEET 2 W 6 THR Z 225 ARG Z 230 -1 O THR Z 228 N ASP Z 216
SHEET 3 W 6 ASN Z 273 ARG Z 279 -1 O VAL Z 274 N GLY Z 229
SHEET 4 W 6 GLN Z 251 GLY Z 257 -1 N GLY Z 257 O LEU Z 277
SHEET 5 W 6 GLU Z 240 VAL Z 245 -1 N ILE Z 244 O GLN Z 251
SHEET 6 W 6 VAL Z 291 ALA Z 293 -1 O VAL Z 291 N VAL Z 245
SHEET 1 X 8 ASN Z 355 ILE Z 356 0
SHEET 2 X 8 PRO Z 300 ILE Z 310 -1 N VAL Z 308 O ILE Z 356
SHEET 3 X 8 ARG Z 381 VAL Z 391 -1 O LYS Z 390 N GLU Z 305
SHEET 4 X 8 ARG Z 373 GLU Z 378 -1 N ILE Z 376 O VAL Z 383
SHEET 5 X 8 GLN Z 329 PHE Z 332 -1 N GLN Z 329 O ARG Z 377
SHEET 6 X 8 THR Z 335 THR Z 340 -1 O VAL Z 337 N PHE Z 330
SHEET 7 X 8 VAL Z 359 ALA Z 367 -1 O ILE Z 363 N THR Z 338
SHEET 8 X 8 PRO Z 300 ILE Z 310 -1 N PHE Z 304 O VAL Z 360
LINK O3' G V 53 P 5MU V 54 1555 1555 1.58
LINK O3' 5MU V 54 P U V 55 1555 1555 1.61
CISPEP 1 ILE Z 199 PRO Z 200 0 -12.07
SITE 1 AC1 14 VAL Z 20 ASP Z 21 HIS Z 22 GLY Z 23
SITE 2 AC1 14 LYS Z 24 THR Z 25 THR Z 26 HIS Z 84
SITE 3 AC1 14 ASN Z 135 MET Z 139 SER Z 173 ALA Z 174
SITE 4 AC1 14 LEU Z 175 LYS Z 176
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
