HEADER RIBOSOME/HYDROLASE 30-MAY-11 2YKR
TITLE 30S RIBOSOMAL SUBUNIT WITH RSGA BOUND IN THE PRESENCE OF GMPPNP
CAVEAT 2YKR SER N 4 C-ALPHA IS PLANAR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 16S RRNA;
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: 30S RIBOSOMAL PROTEIN S2;
COMPND 6 CHAIN: B;
COMPND 7 FRAGMENT: RESIDUES 9-226;
COMPND 8 MOL_ID: 3;
COMPND 9 MOLECULE: 30S RIBOSOMAL PROTEIN S3;
COMPND 10 CHAIN: C;
COMPND 11 FRAGMENT: RESIDUES 2-207;
COMPND 12 MOL_ID: 4;
COMPND 13 MOLECULE: 30S RIBOSOMAL PROTEIN S4;
COMPND 14 CHAIN: D;
COMPND 15 FRAGMENT: RESIDUES 2-206;
COMPND 16 MOL_ID: 5;
COMPND 17 MOLECULE: 30S RIBOSOMAL PROTEIN S5;
COMPND 18 CHAIN: E;
COMPND 19 FRAGMENT: RESIDUES 10-159;
COMPND 20 MOL_ID: 6;
COMPND 21 MOLECULE: 30S RIBOSOMAL PROTEIN S6;
COMPND 22 CHAIN: F;
COMPND 23 FRAGMENT: RESIDUES 1-100;
COMPND 24 MOL_ID: 7;
COMPND 25 MOLECULE: 30S RIBOSOMAL PROTEIN S7;
COMPND 26 CHAIN: G;
COMPND 27 FRAGMENT: RESIDUES 2-152;
COMPND 28 MOL_ID: 8;
COMPND 29 MOLECULE: 30S RIBOSOMAL PROTEIN S8;
COMPND 30 CHAIN: H;
COMPND 31 FRAGMENT: RESIDUES 2-130;
COMPND 32 MOL_ID: 9;
COMPND 33 MOLECULE: 30S RIBOSOMAL PROTEIN S9;
COMPND 34 CHAIN: I;
COMPND 35 FRAGMENT: RESIDUES 4-130;
COMPND 36 MOL_ID: 10;
COMPND 37 MOLECULE: 30S RIBOSOMAL PROTEIN S10;
COMPND 38 CHAIN: J;
COMPND 39 FRAGMENT: RESIDUES 5-102;
COMPND 40 MOL_ID: 11;
COMPND 41 MOLECULE: 30S RIBOSOMAL PROTEIN S11;
COMPND 42 CHAIN: K;
COMPND 43 FRAGMENT: RESIDUES 13-129;
COMPND 44 MOL_ID: 12;
COMPND 45 MOLECULE: 30S RIBOSOMAL PROTEIN S12;
COMPND 46 CHAIN: L;
COMPND 47 FRAGMENT: RESIDUES 2-124;
COMPND 48 MOL_ID: 13;
COMPND 49 MOLECULE: 30S RIBOSOMAL PROTEIN S13;
COMPND 50 CHAIN: M;
COMPND 51 FRAGMENT: RESIDUES 2-115;
COMPND 52 MOL_ID: 14;
COMPND 53 MOLECULE: 30S RIBOSOMAL PROTEIN S14;
COMPND 54 CHAIN: N;
COMPND 55 FRAGMENT: RESIDUES 2-101;
COMPND 56 MOL_ID: 15;
COMPND 57 MOLECULE: 30S RIBOSOMAL PROTEIN S15;
COMPND 58 CHAIN: O;
COMPND 59 FRAGMENT: RESIDUES 2-89;
COMPND 60 MOL_ID: 16;
COMPND 61 MOLECULE: 30S RIBOSOMAL PROTEIN S16;
COMPND 62 CHAIN: P;
COMPND 63 MOL_ID: 17;
COMPND 64 MOLECULE: 30S RIBOSOMAL PROTEIN S17;
COMPND 65 CHAIN: Q;
COMPND 66 FRAGMENT: RESIDUES 4-83;
COMPND 67 MOL_ID: 18;
COMPND 68 MOLECULE: 30S RIBOSOMAL PROTEIN S18;
COMPND 69 CHAIN: R;
COMPND 70 FRAGMENT: RESIDUES 20-74;
COMPND 71 MOL_ID: 19;
COMPND 72 MOLECULE: 30S RIBOSOMAL PROTEIN S19;
COMPND 73 CHAIN: S;
COMPND 74 FRAGMENT: RESIDUES 3-81;
COMPND 75 MOL_ID: 20;
COMPND 76 MOLECULE: 30S RIBOSOMAL PROTEIN S20;
COMPND 77 CHAIN: T;
COMPND 78 FRAGMENT: RESIDUES 3-87;
COMPND 79 MOL_ID: 21;
COMPND 80 MOLECULE: 30S RIBOSOMAL PROTEIN S21;
COMPND 81 CHAIN: U;
COMPND 82 FRAGMENT: RESIDUES 4-54;
COMPND 83 MOL_ID: 22;
COMPND 84 MOLECULE: PUTATIVE RIBOSOME BIOGENESIS GTPASE RSGA;
COMPND 85 CHAIN: W;
COMPND 86 EC: 3.6.1.-;
COMPND 87 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 668369;
SOURCE 4 STRAIN: DH5ALPHA;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 7 ORGANISM_TAXID: 668369;
SOURCE 8 STRAIN: DH5ALPHA;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 11 ORGANISM_TAXID: 668369;
SOURCE 12 STRAIN: DH5ALPHA;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 15 ORGANISM_TAXID: 668369;
SOURCE 16 STRAIN: DH5ALPHA;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 19 ORGANISM_TAXID: 668369;
SOURCE 20 STRAIN: DH5ALPHA;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 23 ORGANISM_TAXID: 668369;
SOURCE 24 STRAIN: DH5ALPHA;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 27 ORGANISM_TAXID: 668369;
SOURCE 28 STRAIN: DH5ALPHA;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 31 ORGANISM_TAXID: 668369;
SOURCE 32 STRAIN: DH5ALPHA;
SOURCE 33 MOL_ID: 9;
SOURCE 34 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 35 ORGANISM_TAXID: 668369;
SOURCE 36 STRAIN: DH5ALPHA;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 39 ORGANISM_TAXID: 668369;
SOURCE 40 STRAIN: DH5ALPHA;
SOURCE 41 MOL_ID: 11;
SOURCE 42 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 43 ORGANISM_TAXID: 668369;
SOURCE 44 STRAIN: DH5ALPHA;
SOURCE 45 MOL_ID: 12;
SOURCE 46 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 47 ORGANISM_TAXID: 668369;
SOURCE 48 STRAIN: DH5ALPHA;
SOURCE 49 MOL_ID: 13;
SOURCE 50 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 51 ORGANISM_TAXID: 668369;
SOURCE 52 STRAIN: DH5ALPHA;
SOURCE 53 MOL_ID: 14;
SOURCE 54 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 55 ORGANISM_TAXID: 668369;
SOURCE 56 STRAIN: DH5ALPHA;
SOURCE 57 MOL_ID: 15;
SOURCE 58 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 59 ORGANISM_TAXID: 668369;
SOURCE 60 STRAIN: DH5ALPHA;
SOURCE 61 MOL_ID: 16;
SOURCE 62 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 63 ORGANISM_TAXID: 668369;
SOURCE 64 STRAIN: DH5ALPHA;
SOURCE 65 MOL_ID: 17;
SOURCE 66 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 67 ORGANISM_TAXID: 668369;
SOURCE 68 STRAIN: DH5ALPHA;
SOURCE 69 MOL_ID: 18;
SOURCE 70 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 71 ORGANISM_TAXID: 668369;
SOURCE 72 STRAIN: DH5ALPHA;
SOURCE 73 MOL_ID: 19;
SOURCE 74 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 75 ORGANISM_TAXID: 668369;
SOURCE 76 STRAIN: DH5ALPHA;
SOURCE 77 MOL_ID: 20;
SOURCE 78 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 79 ORGANISM_TAXID: 668369;
SOURCE 80 STRAIN: DH5ALPHA;
SOURCE 81 MOL_ID: 21;
SOURCE 82 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 83 ORGANISM_TAXID: 668369;
SOURCE 84 STRAIN: DH5ALPHA;
SOURCE 85 MOL_ID: 22;
SOURCE 86 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 87 ORGANISM_TAXID: 668369;
SOURCE 88 STRAIN: DH5ALPHA;
SOURCE 89 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 90 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 91 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 92 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 93 EXPRESSION_SYSTEM_VECTOR: PET28B
KEYWDS RIBOSOME-HYDROLASE COMPLEX, RIBOSOME BIOGENESIS, YJEQ, CIRCULARLY
KEYWDS 2 PERMUTATED GTPASE
EXPDTA ELECTRON MICROSCOPY
AUTHOR Q.GUO,Y.YUAN,Y.XU,B.FENG,L.LIU,K.CHEN,J.LEI,N.GAO
REVDAT 2 20-MAR-13 2YKR 1 REMARK CRYST1 SCALE1 SCALE2
REVDAT 2 2 SCALE3
REVDAT 1 24-AUG-11 2YKR 0
JRNL AUTH Q.GUO,Y.YUAN,Y.XU,B.FENG,L.LIU,K.CHEN,M.SUN,Z.YANG,J.LEI,
JRNL AUTH 2 N.GAO
JRNL TITL STRUCTURAL BASIS FOR THE FUNCTION OF A SMALL GTPASE RSGA ON
JRNL TITL 2 THE 30S RIBOSOMAL SUBUNIT MATURATION REVEALED BY
JRNL TITL 3 CRYOELECTRON MICROSCOPY.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 13100 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21788480
JRNL DOI 10.1073/PNAS.1104645108
REMARK 2
REMARK 2 RESOLUTION. 9.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : SPIDER
REMARK 3 RECONSTRUCTION SCHEMA : REFERENCE BASED
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 3OFA, 2RCN
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : X-RAY
REMARK 3 REFINEMENT TARGET : CROSS-CORELATION
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) : 2.90
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : 2.90
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 9.8
REMARK 3 NUMBER OF PARTICLES : 77483
REMARK 3 CTF CORRECTION METHOD : MAPS FROM EACH DEFOCUS GROUP
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD
REMARK 3 -1884. (DEPOSITION ID: 7882).
REMARK 4
REMARK 4 2YKR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAY-11.
REMARK 100 THE PDBE ID CODE IS EBI-47471.
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 : 30S RIBOSOMAL SUBUNIT WITH RSGA
REMARK 245 BOUND IN THE PRESENCE OF GMPPNP
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : OTHER
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.6
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : OTHER
REMARK 245 DETECTOR TYPE : FEI EAGLE 4K 4K CCD
REMARK 245 MINIMUM DEFOCUS (NM) : 2000
REMARK 245 MAXIMUM DEFOCUS (NM) : 3850
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.7
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 20
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 59000
REMARK 245 CALIBRATED MAGNIFICATION : NULL
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: 22-MERIC
REMARK 350 QUATERNARY STRUCTURE FOR THIS ENTRY: 22-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,
REMARK 350 AND CHAINS: J, K, L, M, N, O, P, Q, R,
REMARK 350 AND CHAINS: S, T, U, W,
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 ASP N 37
REMARK 465 GLU N 38
REMARK 465 ASP N 39
REMARK 465 MET W 1
REMARK 465 SER W 2
REMARK 465 LYS W 3
REMARK 465 ASN W 4
REMARK 465 LYS W 5
REMARK 465 LEU W 6
REMARK 465 SER W 7
REMARK 465 LYS W 8
REMARK 465 GLY W 9
REMARK 465 GLN W 10
REMARK 465 GLN W 11
REMARK 465 ARG W 12
REMARK 465 ARG W 13
REMARK 465 VAL W 14
REMARK 465 ASN W 15
REMARK 465 ALA W 16
REMARK 465 ASN W 17
REMARK 465 HIS W 18
REMARK 465 GLN W 19
REMARK 465 ARG W 20
REMARK 465 ARG W 21
REMARK 465 LEU W 22
REMARK 465 LYS W 23
REMARK 465 THR W 24
REMARK 465 SER W 25
REMARK 465 LYS W 26
REMARK 465 GLU W 27
REMARK 465 LYS W 28
REMARK 465 PRO W 29
REMARK 465 ASP W 30
REMARK 465 TYR W 31
REMARK 465 ASP W 32
REMARK 465 ASP W 33
REMARK 465 ASN W 34
REMARK 465 ALA W 87
REMARK 465 ALA W 88
REMARK 465 GLU W 89
REMARK 465 GLY W 90
REMARK 465 VAL W 91
REMARK 465 ASN W 92
REMARK 465 PHE W 112
REMARK 465 TYR W 113
REMARK 465 ASP W 114
REMARK 465 GLY W 115
REMARK 465 VAL W 239
REMARK 465 SER W 240
REMARK 465 ASP W 241
REMARK 465 ASN W 242
REMARK 465 SER W 243
REMARK 465 GLY W 244
REMARK 465 LEU W 245
REMARK 465 GLY W 246
REMARK 465 GLN W 247
REMARK 465 HIS W 248
REMARK 465 THR W 249
REMARK 465 THR W 250
REMARK 465 VAL W 339
REMARK 465 LYS W 340
REMARK 465 THR W 341
REMARK 465 ARG W 342
REMARK 465 LYS W 343
REMARK 465 ASN W 344
REMARK 465 PHE W 345
REMARK 465 SER W 346
REMARK 465 ASP W 347
REMARK 465 THR W 348
REMARK 465 ASP W 349
REMARK 465 ASP W 350
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 N 36 CA C O CB OG
REMARK 470 PRO W 86 CA C O CB CG CD
REMARK 470 ASP W 111 CA C O CB CG OD1 OD2
REMARK 470 ASP W 238 CA C O CB CG OD1 OD2
REMARK 470 GLN W 338 CA C O CB CG CD OE1 NE2
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 A A 2 C2' A A 2 C1' -0.055
REMARK 500 A A 2 C8 A A 2 N7 -0.053
REMARK 500 A A 2 N7 A A 2 C5 -0.069
REMARK 500 A A 2 N9 A A 2 C4 -0.039
REMARK 500 A A 3 C2' A A 3 C1' -0.082
REMARK 500 A A 3 C4' A A 3 C3' -0.073
REMARK 500 A A 3 C5' A A 3 C4' -0.054
REMARK 500 A A 3 N3 A A 3 C4 -0.053
REMARK 500 A A 3 N7 A A 3 C5 -0.048
REMARK 500 A A 3 N9 A A 3 C4 -0.057
REMARK 500 A A 3 O4' A A 3 C1' -0.095
REMARK 500 U A 5 C5' U A 5 C4' 0.102
REMARK 500 G A 6 N7 G A 6 C5 -0.051
REMARK 500 G A 6 P G A 6 O5' -0.093
REMARK 500 A A 7 C5' A A 7 C4' 0.084
REMARK 500 A A 8 C2' A A 8 C1' -0.056
REMARK 500 G A 9 C2' G A 9 C1' -0.076
REMARK 500 A A 8 O3' G A 9 P -0.091
REMARK 500 A A 10 C2' A A 10 C1' -0.099
REMARK 500 A A 10 N7 A A 10 C5 -0.037
REMARK 500 A A 10 N9 A A 10 C4 -0.037
REMARK 500 G A 11 N7 G A 11 C5 -0.048
REMARK 500 U A 13 C4' U A 13 C3' 0.069
REMARK 500 U A 13 C5' U A 13 C4' 0.082
REMARK 500 G A 15 N7 G A 15 C5 -0.048
REMARK 500 G A 15 P G A 15 O5' -0.068
REMARK 500 A A 16 C1' A A 16 N9 -0.103
REMARK 500 A A 16 C2' A A 16 C1' -0.096
REMARK 500 A A 16 C3' A A 16 C2' -0.073
REMARK 500 A A 16 N7 A A 16 C5 -0.070
REMARK 500 C A 18 C2' C A 18 C1' -0.077
REMARK 500 A A 19 C2' A A 19 C1' -0.086
REMARK 500 A A 19 N7 A A 19 C5 -0.046
REMARK 500 U A 20 C3' U A 20 C2' -0.074
REMARK 500 U A 20 P U A 20 O5' -0.092
REMARK 500 G A 21 C2' G A 21 C1' -0.074
REMARK 500 G A 21 C3' G A 21 C2' -0.111
REMARK 500 G A 21 N7 G A 21 C5 -0.043
REMARK 500 G A 21 N9 G A 21 C4 -0.049
REMARK 500 G A 21 P G A 21 O5' -0.095
REMARK 500 G A 22 C2' G A 22 C1' -0.090
REMARK 500 G A 22 C3' G A 22 C2' -0.109
REMARK 500 G A 22 C3' G A 22 O3' -0.088
REMARK 500 G A 22 C8 G A 22 N7 -0.041
REMARK 500 G A 22 N7 G A 22 C5 -0.076
REMARK 500 G A 22 P G A 22 O5' -0.071
REMARK 500 C A 23 C2' C A 23 C1' -0.088
REMARK 500 C A 23 C3' C A 23 C2' -0.107
REMARK 500 C A 23 C5' C A 23 C4' -0.047
REMARK 500 C A 23 P C A 23 O5' -0.071
REMARK 500
REMARK 500 THIS ENTRY HAS 4916 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 A A 2 C4 - C5 - C6 ANGL. DEV. = 3.1 DEGREES
REMARK 500 A A 2 C5 - C6 - N6 ANGL. DEV. = -9.3 DEGREES
REMARK 500 A A 2 N1 - C6 - N6 ANGL. DEV. = 9.6 DEGREES
REMARK 500 A A 3 N1 - C6 - N6 ANGL. DEV. = 6.2 DEGREES
REMARK 500 A A 3 P - O5' - C5' ANGL. DEV. = -11.1 DEGREES
REMARK 500 U A 4 C2 - N3 - C4 ANGL. DEV. = -4.6 DEGREES
REMARK 500 U A 4 C5' - C4' - C3' ANGL. DEV. = -8.5 DEGREES
REMARK 500 U A 4 C6 - N1 - C2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 U A 4 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 G A 6 C3' - C2' - C1' ANGL. DEV. = -4.6 DEGREES
REMARK 500 G A 6 C5 - C6 - O6 ANGL. DEV. = -4.5 DEGREES
REMARK 500 G A 6 N1 - C6 - O6 ANGL. DEV. = 7.0 DEGREES
REMARK 500 G A 6 O4' - C1' - N9 ANGL. DEV. = 5.8 DEGREES
REMARK 500 G A 6 O5' - C5' - C4' ANGL. DEV. = -6.3 DEGREES
REMARK 500 G A 6 C3' - O3' - P ANGL. DEV. = 14.6 DEGREES
REMARK 500 A A 7 C5 - C6 - N6 ANGL. DEV. = -7.6 DEGREES
REMARK 500 A A 7 N1 - C6 - N6 ANGL. DEV. = 9.1 DEGREES
REMARK 500 A A 7 O4' - C1' - N9 ANGL. DEV. = 6.3 DEGREES
REMARK 500 A A 8 C3' - C2' - C1' ANGL. DEV. = -5.2 DEGREES
REMARK 500 A A 8 C5 - C6 - N1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 A A 8 N1 - C6 - N6 ANGL. DEV. = 7.5 DEGREES
REMARK 500 A A 8 C3' - O3' - P ANGL. DEV. = 17.5 DEGREES
REMARK 500 G A 9 C5 - C6 - O6 ANGL. DEV. = -4.1 DEGREES
REMARK 500 G A 9 N1 - C6 - O6 ANGL. DEV. = 4.8 DEGREES
REMARK 500 G A 9 N3 - C2 - N2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 G A 9 N9 - C1' - C2' ANGL. DEV. = -7.3 DEGREES
REMARK 500 G A 9 O4' - C1' - N9 ANGL. DEV. = 8.5 DEGREES
REMARK 500 G A 9 O4' - C4' - C3' ANGL. DEV. = -7.1 DEGREES
REMARK 500 A A 10 C3' - C2' - C1' ANGL. DEV. = -6.7 DEGREES
REMARK 500 A A 10 N1 - C6 - N6 ANGL. DEV. = 5.3 DEGREES
REMARK 500 G A 11 C5' - C4' - C3' ANGL. DEV. = -13.4 DEGREES
REMARK 500 G A 11 C5' - C4' - O4' ANGL. DEV. = 5.5 DEGREES
REMARK 500 G A 11 C8 - N9 - C4 ANGL. DEV. = -3.8 DEGREES
REMARK 500 G A 11 N1 - C6 - O6 ANGL. DEV. = 5.5 DEGREES
REMARK 500 G A 11 N3 - C2 - N2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 G A 11 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 U A 12 O5' - C5' - C4' ANGL. DEV. = -6.8 DEGREES
REMARK 500 U A 13 C2 - N1 - C1' ANGL. DEV. = 10.9 DEGREES
REMARK 500 U A 13 C5' - C4' - C3' ANGL. DEV. = 11.6 DEGREES
REMARK 500 U A 13 C6 - N1 - C2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 U A 13 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 U A 14 C3' - O3' - P ANGL. DEV. = 9.4 DEGREES
REMARK 500 G A 15 C5 - C6 - O6 ANGL. DEV. = -3.9 DEGREES
REMARK 500 G A 15 C8 - N9 - C1' ANGL. DEV. = 8.1 DEGREES
REMARK 500 G A 15 N1 - C6 - O6 ANGL. DEV. = 5.2 DEGREES
REMARK 500 G A 15 N3 - C2 - N2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 A A 16 C4 - C5 - C6 ANGL. DEV. = 4.1 DEGREES
REMARK 500 A A 16 C5 - C6 - N1 ANGL. DEV. = -4.0 DEGREES
REMARK 500 A A 16 C5 - N7 - C8 ANGL. DEV. = 4.1 DEGREES
REMARK 500 A A 16 N1 - C6 - N6 ANGL. DEV. = 7.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 8724 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 LYS B 10 26.60 -145.99
REMARK 500 ALA B 11 -1.98 172.00
REMARK 500 HIS B 17 -0.93 -59.30
REMARK 500 GLN B 18 15.68 -58.58
REMARK 500 ASN B 23 122.40 -2.61
REMARK 500 LYS B 25 -55.18 -146.79
REMARK 500 LYS B 27 -13.44 -162.27
REMARK 500 ILE B 30 118.26 150.75
REMARK 500 ALA B 33 -9.28 -161.96
REMARK 500 ARG B 34 71.06 -163.70
REMARK 500 ASN B 35 123.58 106.71
REMARK 500 LYS B 36 106.85 -53.52
REMARK 500 VAL B 37 -151.61 -134.23
REMARK 500 HIS B 38 126.36 156.12
REMARK 500 ILE B 40 -131.80 -98.33
REMARK 500 ALA B 52 -78.66 -75.38
REMARK 500 ILE B 59 76.63 -108.85
REMARK 500 ALA B 60 -11.15 -157.06
REMARK 500 LYS B 63 150.22 74.68
REMARK 500 ILE B 66 -47.21 -25.67
REMARK 500 LEU B 67 105.30 67.56
REMARK 500 LYS B 72 -143.88 42.24
REMARK 500 ALA B 74 -88.70 -78.13
REMARK 500 SER B 76 -5.80 -164.82
REMARK 500 GLU B 77 -24.74 -147.38
REMARK 500 LYS B 80 102.93 -174.51
REMARK 500 ASP B 81 -99.58 -156.14
REMARK 500 ASP B 87 30.69 -150.48
REMARK 500 TRP B 95 -156.84 -114.97
REMARK 500 SER B 120 -6.04 -170.17
REMARK 500 ASP B 122 50.32 -91.12
REMARK 500 ASP B 126 -3.67 -140.13
REMARK 500 LYS B 127 -7.92 -162.88
REMARK 500 LEU B 128 -35.28 -133.29
REMARK 500 THR B 129 20.94 -151.46
REMARK 500 ALA B 133 63.75 -158.63
REMARK 500 LEU B 134 0.32 173.14
REMARK 500 LEU B 140 -77.92 -56.84
REMARK 500 LEU B 156 150.19 -3.77
REMARK 500 ASP B 158 62.36 -101.34
REMARK 500 ALA B 159 157.13 118.25
REMARK 500 HIS B 169 -87.35 -28.55
REMARK 500 ASP B 187 -146.67 -139.88
REMARK 500 ASP B 204 -9.64 -142.23
REMARK 500 ALA B 205 148.42 -34.71
REMARK 500 ALA B 208 -14.64 -151.55
REMARK 500 VAL B 209 -96.92 -96.03
REMARK 500 LEU B 211 -76.89 -54.81
REMARK 500 THR B 219 -59.72 -167.80
REMARK 500 GLN C 2 -84.92 -136.14
REMARK 500
REMARK 500 THIS ENTRY HAS 468 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 TRP B 95 LEU B 96 -137.77
REMARK 500 THR C 176 LEU C 177 -147.05
REMARK 500 PRO D 138 ASN D 139 -148.89
REMARK 500 ASP H 47 PHE H 48 146.76
REMARK 500 ALA L 22 LEU L 23 -143.64
REMARK 500 HIS M 13 ALA M 14 -148.60
REMARK 500 PHE Q 27 VAL Q 28 148.51
REMARK 500 HIS Q 44 VAL Q 45 -142.96
REMARK 500 SER R 65 LEU R 66 145.14
REMARK 500 SER T 5 ALA T 6 144.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 A A 2 0.14 SIDE CHAIN
REMARK 500 A A 3 0.28 SIDE CHAIN
REMARK 500 U A 4 0.34 SIDE CHAIN
REMARK 500 U A 5 0.17 SIDE CHAIN
REMARK 500 G A 6 0.15 SIDE CHAIN
REMARK 500 A A 7 0.09 SIDE CHAIN
REMARK 500 A A 8 0.14 SIDE CHAIN
REMARK 500 G A 9 0.07 SIDE CHAIN
REMARK 500 A A 10 0.08 SIDE CHAIN
REMARK 500 G A 11 0.19 SIDE CHAIN
REMARK 500 U A 12 0.07 SIDE CHAIN
REMARK 500 U A 13 0.16 SIDE CHAIN
REMARK 500 U A 14 0.16 SIDE CHAIN
REMARK 500 G A 15 0.08 SIDE CHAIN
REMARK 500 A A 16 0.05 SIDE CHAIN
REMARK 500 U A 17 0.09 SIDE CHAIN
REMARK 500 G A 21 0.22 SIDE CHAIN
REMARK 500 U A 24 0.17 SIDE CHAIN
REMARK 500 C A 25 0.11 SIDE CHAIN
REMARK 500 A A 28 0.11 SIDE CHAIN
REMARK 500 U A 29 0.10 SIDE CHAIN
REMARK 500 U A 30 0.30 SIDE CHAIN
REMARK 500 G A 31 0.09 SIDE CHAIN
REMARK 500 A A 32 0.12 SIDE CHAIN
REMARK 500 A A 33 0.14 SIDE CHAIN
REMARK 500 C A 34 0.07 SIDE CHAIN
REMARK 500 G A 35 0.09 SIDE CHAIN
REMARK 500 G A 38 0.20 SIDE CHAIN
REMARK 500 G A 39 0.10 SIDE CHAIN
REMARK 500 G A 42 0.18 SIDE CHAIN
REMARK 500 C A 43 0.09 SIDE CHAIN
REMARK 500 G A 45 0.08 SIDE CHAIN
REMARK 500 G A 46 0.15 SIDE CHAIN
REMARK 500 C A 47 0.15 SIDE CHAIN
REMARK 500 U A 49 0.43 SIDE CHAIN
REMARK 500 A A 50 0.22 SIDE CHAIN
REMARK 500 A A 51 0.10 SIDE CHAIN
REMARK 500 C A 52 0.18 SIDE CHAIN
REMARK 500 A A 53 0.14 SIDE CHAIN
REMARK 500 C A 54 0.14 SIDE CHAIN
REMARK 500 A A 55 0.13 SIDE CHAIN
REMARK 500 U A 56 0.40 SIDE CHAIN
REMARK 500 G A 57 0.12 SIDE CHAIN
REMARK 500 C A 58 0.08 SIDE CHAIN
REMARK 500 A A 60 0.17 SIDE CHAIN
REMARK 500 G A 61 0.10 SIDE CHAIN
REMARK 500 U A 62 0.16 SIDE CHAIN
REMARK 500 C A 63 0.15 SIDE CHAIN
REMARK 500 G A 64 0.08 SIDE CHAIN
REMARK 500 A A 66 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 1391 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 B 94 11.14
REMARK 500 TRP B 95 13.80
REMARK 500 ALA B 133 -10.04
REMARK 500 VAL C 96 11.22
REMARK 500 THR C 176 11.77
REMARK 500 PRO D 138 11.71
REMARK 500 SER H 106 -10.75
REMARK 500 GLN I 49 -10.40
REMARK 500 PRO I 124 11.68
REMARK 500 HIS J 56 10.02
REMARK 500 HIS M 13 10.70
REMARK 500 VAL M 96 -11.99
REMARK 500 PRO M 111 -11.90
REMARK 500 ASP N 32 -10.06
REMARK 500 ASN N 34 -10.33
REMARK 500 THR O 21 10.66
REMARK 500 LYS O 46 12.06
REMARK 500 ALA P 27 11.73
REMARK 500 ARG Q 39 10.09
REMARK 500 HIS Q 44 15.09
REMARK 500 HIS Q 46 -10.46
REMARK 500 THR S 47 10.29
REMARK 500 THR S 62 12.10
REMARK 500 SER T 5 -16.15
REMARK 500 ARG U 46 10.10
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 G A 752 -23.2 D D OUTSIDE RANGE
REMARK 500 C A1129 -12.4 D D OUTSIDE RANGE
REMARK 500 A A1261 -46.7 D D OUTSIDE RANGE
REMARK 500 GLU B 139 20.9 L L OUTSIDE RANGE
REMARK 500 LEU B 140 22.9 L L OUTSIDE RANGE
REMARK 500 ILE B 199 45.6 L L OUTSIDE RANGE
REMARK 500 ASN B 202 24.8 L L OUTSIDE RANGE
REMARK 500 THR B 210 23.9 L L OUTSIDE RANGE
REMARK 500 LYS C 3 24.3 L L OUTSIDE RANGE
REMARK 500 VAL C 4 45.6 L L OUTSIDE RANGE
REMARK 500 LEU C 114 23.1 L L OUTSIDE RANGE
REMARK 500 THR C 164 24.0 L L OUTSIDE RANGE
REMARK 500 LYS D 7 22.6 L L OUTSIDE RANGE
REMARK 500 ASP D 49 23.3 L L OUTSIDE RANGE
REMARK 500 ASP D 98 24.0 L L OUTSIDE RANGE
REMARK 500 VAL D 128 20.6 L L OUTSIDE RANGE
REMARK 500 GLU D 146 23.4 L L OUTSIDE RANGE
REMARK 500 LYS D 147 24.3 L L OUTSIDE RANGE
REMARK 500 THR E 23 20.0 L L OUTSIDE RANGE
REMARK 500 ALA E 34 22.3 L L OUTSIDE RANGE
REMARK 500 ALA E 52 24.9 L L OUTSIDE RANGE
REMARK 500 ILE E 59 24.6 L L OUTSIDE RANGE
REMARK 500 SER E 129 24.1 L L OUTSIDE RANGE
REMARK 500 VAL E 135 22.4 L L OUTSIDE RANGE
REMARK 500 ARG F 38 24.3 L L OUTSIDE RANGE
REMARK 500 VAL F 70 22.3 L L OUTSIDE RANGE
REMARK 500 LYS G 10 24.6 L L OUTSIDE RANGE
REMARK 500 MET G 30 24.3 L L OUTSIDE RANGE
REMARK 500 LYS G 34 23.8 L L OUTSIDE RANGE
REMARK 500 ARG G 78 22.1 L L OUTSIDE RANGE
REMARK 500 GLN H 17 25.0 L L OUTSIDE RANGE
REMARK 500 CYS H 126 23.6 L L OUTSIDE RANGE
REMARK 500 LEU I 97 23.9 L L OUTSIDE RANGE
REMARK 500 ARG I 123 24.2 L L OUTSIDE RANGE
REMARK 500 GLN I 125 46.8 L L OUTSIDE RANGE
REMARK 500 GLN J 35 23.2 L L OUTSIDE RANGE
REMARK 500 LYS J 46 24.3 L L OUTSIDE RANGE
REMARK 500 ARG J 62 23.8 L L OUTSIDE RANGE
REMARK 500 GLU J 78 24.0 L L OUTSIDE RANGE
REMARK 500 CYS K 120 23.8 L L OUTSIDE RANGE
REMARK 500 ARG L 11 20.7 L L OUTSIDE RANGE
REMARK 500 ALA L 12 22.5 L L OUTSIDE RANGE
REMARK 500 SER L 18 23.9 L L OUTSIDE RANGE
REMARK 500 PRO L 41 45.1 L L OUTSIDE RANGE
REMARK 500 LEU L 101 21.9 L L OUTSIDE RANGE
REMARK 500 ILE M 3 23.2 L L OUTSIDE RANGE
REMARK 500 LYS M 26 45.3 L L OUTSIDE RANGE
REMARK 500 LYS M 43 22.5 L L OUTSIDE RANGE
REMARK 500 GLN M 99 22.7 L L OUTSIDE RANGE
REMARK 500 ARG M 106 23.6 L L OUTSIDE RANGE
REMARK 500
REMARK 500 THIS ENTRY HAS 76 CHIRALITY DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VHP RELATED DB: PDB
REMARK 900 STRUCTURE OF PDF BINDING HELIX IN COMPLEX WITH THE
REMARK 900 RIBOSOME
REMARK 900 RELATED ID: EMD-1884 RELATED DB: EMDB
REMARK 900 RSGA-30S RIBOSOMAL SUBUNIT-GMPPNP COMPLEX
DBREF1 2YKR A 2 1534 GB NC_013008
DBREF2 2YKR A 254791136 3508729 3510261
DBREF 2YKR B 8 225 UNP B7NID0 RS2_ECO7I 9 226
DBREF 2YKR C 1 206 UNP A1AGK2 RS3_ECOK1 2 207
DBREF 2YKR D 1 205 UNP A1AGI7 RS4_ECOK1 2 206
DBREF 2YKR E 9 158 UNP D6JG86 D6JG86_ECOLX 10 159
DBREF 2YKR F 1 100 UNP B6I2A6 RS6_ECOSE 1 100
DBREF 2YKR G 1 151 UNP E3XT25 E3XT25_ECOLX 2 152
DBREF 2YKR H 1 129 UNP B6I220 RS8_ECOSE 2 130
DBREF 2YKR I 3 129 UNP Q0TCN6 RS9_ECOL5 4 130
DBREF 2YKR J 5 102 UNP A7ZSL0 RS10_ECO24 5 102
DBREF 2YKR K 12 128 UNP B7M103 RS11_ECO8A 13 129
DBREF 2YKR L 1 123 UNP P0A7S4 RS12_ECOL6 2 124
DBREF 2YKR M 1 114 UNP A1AGI9 RS13_ECOK1 2 115
DBREF 2YKR N 1 100 UNP B7M1M1 RS14_ECO8A 2 101
DBREF 2YKR O 1 88 UNP B3HGB0 B3HGB0_ECOLX 2 89
DBREF 2YKR P 1 82 UNP B7N6J5 RS16_ECOLU 1 82
DBREF 2YKR Q 3 82 UNP P0AG65 RS17_ECO57 4 83
DBREF 2YKR R 19 73 UNP E3PE70 E3PE70_ECOH1 20 74
DBREF 2YKR S 2 80 UNP B6I230 RS19_ECOSE 3 81
DBREF 2YKR T 2 86 UNP B7L4E5 RS20_ECO55 3 87
DBREF 2YKR U 3 53 UNP B1LF57 RS21_ECOSM 4 54
DBREF 2YKR W 1 350 UNP E3PE32 E3PE32_ECOH1 1 350
SEQADV 2YKR ASP N 39 UNP B7M1M1 GLU 40 CONFLICT
SEQRES 1 A 1533 A A U U G A A G A G U U U
SEQRES 2 A 1533 G A U C A U G G C U C A G
SEQRES 3 A 1533 A U U G A A C G C U G G C
SEQRES 4 A 1533 G G C A G G C C U A A C A
SEQRES 5 A 1533 C A U G C A A G U C G A A
SEQRES 6 A 1533 C G G U A A C A G G A A G
SEQRES 7 A 1533 A A G C U U G C U U C U U
SEQRES 8 A 1533 U G C U G A C G A G U G G
SEQRES 9 A 1533 C G G A C G G G U G A G U
SEQRES 10 A 1533 A A U G U C U G G G A A A
SEQRES 11 A 1533 C U G C C U G A U G G A G
SEQRES 12 A 1533 G G G G A U A A C U A C U
SEQRES 13 A 1533 G G A A A C G G U A G C U
SEQRES 14 A 1533 A A U A C C G C A U A A C
SEQRES 15 A 1533 G U C G C A A G A C C A A
SEQRES 16 A 1533 A G A G G G G G A C C U U
SEQRES 17 A 1533 C G G G C C U C U U G C C
SEQRES 18 A 1533 A U C G G A U G U G C C C
SEQRES 19 A 1533 A G A U G G G A U U A G C
SEQRES 20 A 1533 U A G U A G G U G G G G U
SEQRES 21 A 1533 A A C G G C U C A C C U A
SEQRES 22 A 1533 G G C G A C G A U C C C U
SEQRES 23 A 1533 A G C U G G U C U G A G A
SEQRES 24 A 1533 G G A U G A C C A G C C A
SEQRES 25 A 1533 C A C U G G A A C U G A G
SEQRES 26 A 1533 A C A C G G U C C A G A C
SEQRES 27 A 1533 U C C U A C G G G A G G C
SEQRES 28 A 1533 A G C A G U G G G G A A U
SEQRES 29 A 1533 A U U G C A C A A U G G G
SEQRES 30 A 1533 C G C A A G C C U G A U G
SEQRES 31 A 1533 C A G C C A U G C C G C G
SEQRES 32 A 1533 U G U A U G A A G A A G G
SEQRES 33 A 1533 C C U U C G G G U U G U A
SEQRES 34 A 1533 A A G U A C U U U C A G C
SEQRES 35 A 1533 G G G G A G G A A G G G A
SEQRES 36 A 1533 G U A A A G U U A A U A C
SEQRES 37 A 1533 C U U U G C U C A U U G A
SEQRES 38 A 1533 C G U U A C C C G C A G A
SEQRES 39 A 1533 A G A A G C A C C G G C U
SEQRES 40 A 1533 A A C U C C G U G C C A G
SEQRES 41 A 1533 C A G C C G C G G U A A U
SEQRES 42 A 1533 A C G G A G G G U G C A A
SEQRES 43 A 1533 G C G U U A A U C G G A A
SEQRES 44 A 1533 U U A C U G G G C G U A A
SEQRES 45 A 1533 A G C G C A C G C A G G C
SEQRES 46 A 1533 G G U U U G U U A A G U C
SEQRES 47 A 1533 A G A U G U G A A A U C C
SEQRES 48 A 1533 C C G G G C U C A A C C U
SEQRES 49 A 1533 G G G A A C U G C A U C U
SEQRES 50 A 1533 G A U A C U G G C A A G C
SEQRES 51 A 1533 U U G A G U C U C G U A G
SEQRES 52 A 1533 A G G G G G G U A G A A U
SEQRES 53 A 1533 U C C A G G U G U A G C G
SEQRES 54 A 1533 G U G A A A U G C G U A G
SEQRES 55 A 1533 A G A U C U G G A G G A A
SEQRES 56 A 1533 U A C C G G U G G C G A A
SEQRES 57 A 1533 G G C G G C C C C C U G G
SEQRES 58 A 1533 A C G A A G A C U G A C G
SEQRES 59 A 1533 C U C A G G U G C G A A A
SEQRES 60 A 1533 G C G U G G G G A G C A A
SEQRES 61 A 1533 A C A G G A U U A G A U A
SEQRES 62 A 1533 C C C U G G U A G U C C A
SEQRES 63 A 1533 C G C C G U A A A C G A U
SEQRES 64 A 1533 G U C G A C U U G G A G G
SEQRES 65 A 1533 U U G U G C C C U U G A G
SEQRES 66 A 1533 G C G U G G C U U C C G G
SEQRES 67 A 1533 A G C U A A C G C G U U A
SEQRES 68 A 1533 A G U C G A C C G C C U G
SEQRES 69 A 1533 G G G A G U A C G G C C G
SEQRES 70 A 1533 C A A G G U U A A A A C U
SEQRES 71 A 1533 C A A A U G A A U U G A C
SEQRES 72 A 1533 G G G G G C C C G C A C A
SEQRES 73 A 1533 A G C G G U G G A G C A U
SEQRES 74 A 1533 G U G G U U U A A U U C G
SEQRES 75 A 1533 A U G C A A C G C G A A G
SEQRES 76 A 1533 A A C C U U A C C U G G U
SEQRES 77 A 1533 C U U G A C A U C C A C G
SEQRES 78 A 1533 G A A G U U U U C A G A G
SEQRES 79 A 1533 A U G A G A A U G U G C C
SEQRES 80 A 1533 U U C G G G A A C C G U G
SEQRES 81 A 1533 A G A C A G G U G C U G C
SEQRES 82 A 1533 A U G G C U G U C G U C A
SEQRES 83 A 1533 G C U C G U G U U G U G A
SEQRES 84 A 1533 A A U G U U G G G U U A A
SEQRES 85 A 1533 G U C C C G C A A C G A G
SEQRES 86 A 1533 C G C A A C C C U U A U C
SEQRES 87 A 1533 C U U U G U U G C C A G C
SEQRES 88 A 1533 G G U C C G G C C G G G A
SEQRES 89 A 1533 A C U C A A A G G A G A C
SEQRES 90 A 1533 U G C C A G U G A U A A A
SEQRES 91 A 1533 C U G G A G G A A G G U G
SEQRES 92 A 1533 G G G A U G A C G U C A A
SEQRES 93 A 1533 G U C A U C A U G G C C C
SEQRES 94 A 1533 U U A C G A C C A G G G C
SEQRES 95 A 1533 U A C A C A C G U G C U A
SEQRES 96 A 1533 C A A U G G C G C A U A C
SEQRES 97 A 1533 A A A G A G A A G C G A C
SEQRES 98 A 1533 C U C G C G A G A G C A A
SEQRES 99 A 1533 G C G G A C C U C A U A A
SEQRES 100 A 1533 A G U G C G U C G U A G U
SEQRES 101 A 1533 C C G G A U U G G A G U C
SEQRES 102 A 1533 U G C A A C U C G A C U C
SEQRES 103 A 1533 C A U G A A G U C G G A A
SEQRES 104 A 1533 U C G C U A G U A A U C G
SEQRES 105 A 1533 U G G A U C A G A A U G C
SEQRES 106 A 1533 C A C G G U G A A U A C G
SEQRES 107 A 1533 U U C C C G G G C C U U G
SEQRES 108 A 1533 U A C A C A C C G C C C G
SEQRES 109 A 1533 U C A C A C C A U G G G A
SEQRES 110 A 1533 G U G G G U U G C A A A A
SEQRES 111 A 1533 G A A G U A G G U A G C U
SEQRES 112 A 1533 U A A C C U U C G G G A G
SEQRES 113 A 1533 G G C G C U U A C C A C U
SEQRES 114 A 1533 U U G U G A U U C A U G A
SEQRES 115 A 1533 C U G G G G U G A A G U C
SEQRES 116 A 1533 G U A A C A A G G U A A C
SEQRES 117 A 1533 C G U A G G G G A A C C U
SEQRES 118 A 1533 G C G G U U G G A U C A
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 151 PRO ARG ARG ARG VAL ILE GLY GLN ARG LYS ILE LEU PRO
SEQRES 2 G 151 ASP PRO LYS PHE GLY SER GLU LEU LEU ALA LYS PHE VAL
SEQRES 3 G 151 ASN ILE LEU MET VAL ASP GLY LYS LYS SER THR ALA GLU
SEQRES 4 G 151 SER ILE VAL TYR SER ALA LEU GLU THR LEU ALA GLN ARG
SEQRES 5 G 151 SER GLY LYS SER GLU LEU GLU ALA PHE GLU VAL ALA LEU
SEQRES 6 G 151 GLU ASN VAL ARG PRO THR VAL GLU VAL LYS SER ARG ARG
SEQRES 7 G 151 VAL GLY GLY SER THR TYR GLN VAL PRO VAL GLU VAL ARG
SEQRES 8 G 151 PRO VAL ARG ARG ASN ALA LEU ALA MET ARG TRP ILE VAL
SEQRES 9 G 151 GLU ALA ALA ARG LYS ARG GLY ASP LYS SER MET ALA LEU
SEQRES 10 G 151 ARG LEU ALA ASN GLU LEU SER ASP ALA ALA GLU ASN LYS
SEQRES 11 G 151 GLY THR ALA VAL LYS LYS ARG GLU ASP VAL HIS ARG MET
SEQRES 12 G 151 ALA 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 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 114 ALA ARG ILE ALA GLY ILE ASN ILE PRO ASP HIS LYS HIS
SEQRES 2 M 114 ALA VAL ILE ALA LEU THR SER ILE TYR GLY VAL GLY LYS
SEQRES 3 M 114 THR ARG SER LYS ALA ILE LEU ALA ALA ALA GLY ILE ALA
SEQRES 4 M 114 GLU ASP VAL LYS ILE SER GLU LEU SER GLU GLY GLN ILE
SEQRES 5 M 114 ASP THR LEU ARG ASP GLU VAL ALA LYS PHE VAL VAL GLU
SEQRES 6 M 114 GLY ASP LEU ARG ARG GLU ILE SER MET SER ILE LYS ARG
SEQRES 7 M 114 LEU MET ASP LEU GLY CYS TYR ARG GLY LEU ARG HIS ARG
SEQRES 8 M 114 ARG GLY LEU PRO VAL ARG GLY GLN ARG THR LYS THR ASN
SEQRES 9 M 114 ALA ARG THR ARG LYS GLY PRO ARG LYS PRO
SEQRES 1 N 100 ALA LYS GLN SER MET LYS ALA ARG GLU VAL LYS ARG VAL
SEQRES 2 N 100 ALA LEU ALA ASP LYS TYR PHE ALA LYS ARG ALA GLU LEU
SEQRES 3 N 100 LYS ALA ILE ILE SER ASP VAL ASN ALA SER ASP GLU ASP
SEQRES 4 N 100 ARG TRP ASN ALA VAL LEU LYS LEU GLN THR LEU PRO ARG
SEQRES 5 N 100 ASP SER SER PRO SER ARG GLN ARG ASN ARG CYS ARG GLN
SEQRES 6 N 100 THR GLY ARG PRO HIS GLY PHE LEU ARG LYS PHE GLY LEU
SEQRES 7 N 100 SER ARG ILE LYS VAL ARG GLU ALA ALA MET ARG GLY GLU
SEQRES 8 N 100 ILE PRO GLY LEU 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 GLN LEU ILE GLU ARG LEU GLY LEU ARG ARG
SEQRES 1 P 82 MET VAL THR ILE ARG LEU ALA ARG HIS GLY ALA LYS LYS
SEQRES 2 P 82 ARG PRO PHE TYR GLN VAL VAL VAL ALA ASP SER ARG ASN
SEQRES 3 P 82 ALA ARG ASN GLY ARG PHE ILE GLU ARG VAL GLY PHE PHE
SEQRES 4 P 82 ASN PRO ILE ALA SER GLU LYS GLU GLU GLY THR ARG LEU
SEQRES 5 P 82 ASP LEU ASP ARG ILE ALA HIS TRP VAL GLY GLN GLY ALA
SEQRES 6 P 82 THR ILE SER ASP ARG VAL ALA ALA LEU ILE LYS GLU VAL
SEQRES 7 P 82 ASN LYS ALA ALA
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 W 350 MET SER LYS ASN LYS LEU SER LYS GLY GLN GLN ARG ARG
SEQRES 2 W 350 VAL ASN ALA ASN HIS GLN ARG ARG LEU LYS THR SER LYS
SEQRES 3 W 350 GLU LYS PRO ASP TYR ASP ASP ASN LEU PHE GLY GLU PRO
SEQRES 4 W 350 ASP GLU GLY ILE VAL ILE SER ARG PHE GLY MET HIS ALA
SEQRES 5 W 350 ASP VAL GLU SER ALA ASP GLY ASP VAL HIS ARG CYS ASN
SEQRES 6 W 350 ILE ARG ARG THR ILE ARG SER LEU VAL THR GLY ASP ARG
SEQRES 7 W 350 VAL VAL TRP ARG PRO GLY LYS PRO ALA ALA GLU GLY VAL
SEQRES 8 W 350 ASN VAL LYS GLY ILE VAL GLU ALA VAL HIS GLU ARG THR
SEQRES 9 W 350 SER VAL LEU THR ARG PRO ASP PHE TYR ASP GLY VAL LYS
SEQRES 10 W 350 PRO ILE ALA ALA ASN ILE ASP GLN ILE VAL ILE VAL SER
SEQRES 11 W 350 ALA ILE LEU PRO GLU LEU SER LEU ASN ILE ILE ASP ARG
SEQRES 12 W 350 TYR LEU VAL ALA CYS GLU THR LEU GLN ILE GLU PRO ILE
SEQRES 13 W 350 ILE VAL LEU ASN LYS ILE ASP LEU LEU ASP ASP GLU GLY
SEQRES 14 W 350 MET ALA PHE VAL ASN GLU GLN MET ASP ILE TYR ARG ASN
SEQRES 15 W 350 ILE GLY TYR ARG VAL LEU MET VAL SER SER HIS THR GLN
SEQRES 16 W 350 ASP GLY LEU LYS PRO LEU GLU GLU ALA LEU THR GLY ARG
SEQRES 17 W 350 ILE SER ILE PHE ALA GLY GLN SER GLY VAL GLY LYS SER
SEQRES 18 W 350 SER LEU LEU ASN ALA LEU LEU GLY LEU GLN LYS GLU ILE
SEQRES 19 W 350 LEU THR ASN ASP VAL SER ASP ASN SER GLY LEU GLY GLN
SEQRES 20 W 350 HIS THR THR THR ALA ALA ARG LEU TYR HIS PHE PRO HIS
SEQRES 21 W 350 GLY GLY ASP VAL ILE ASP SER PRO GLY VAL ARG GLU PHE
SEQRES 22 W 350 GLY LEU TRP HIS LEU GLU PRO GLU GLN ILE THR GLN GLY
SEQRES 23 W 350 PHE VAL GLU PHE HIS ASP TYR LEU GLY LEU CYS LYS TYR
SEQRES 24 W 350 ARG ASP CYS LYS HIS ASP THR ASP PRO GLY CYS ALA ILE
SEQRES 25 W 350 ARG GLU ALA VAL GLU GLU GLY LYS ILE ALA GLU THR ARG
SEQRES 26 W 350 PHE GLU ASN TYR HIS ARG ILE LEU GLU SER MET ALA GLN
SEQRES 27 W 350 VAL LYS THR ARG LYS ASN PHE SER ASP THR ASP ASP
HELIX 1 1 LYS B 44 ILE B 59 1 16
HELIX 2 2 ASN B 102 VAL B 106 5 5
HELIX 3 3 LYS B 114 THR B 118 5 5
HELIX 4 4 GLU B 141 SER B 146 1 6
HELIX 5 5 GLU B 168 ASN B 177 1 10
HELIX 6 6 VAL B 209 ARG B 221 1 13
HELIX 7 7 ASN C 24 LEU C 46 1 23
HELIX 8 8 ARG C 71 GLY C 77 1 7
HELIX 9 9 GLY C 80 ASP C 92 1 13
HELIX 10 10 ASP C 111 GLU C 124 1 14
HELIX 11 11 MET C 128 ARG C 142 1 15
HELIX 12 12 PRO D 6 GLY D 15 1 10
HELIX 13 13 SER D 48 GLY D 65 1 18
HELIX 14 14 LEU D 67 LEU D 81 1 15
HELIX 15 15 ASN D 84 GLY D 95 1 12
HELIX 16 16 ASP D 98 ARG D 103 1 6
HELIX 17 17 THR D 109 HIS D 119 1 11
HELIX 18 18 GLN D 151 GLN D 163 1 13
HELIX 19 19 LEU D 198 TYR D 203 1 6
HELIX 20 20 GLU E 54 ARG E 68 1 15
HELIX 21 21 ALA E 112 GLY E 118 1 7
HELIX 22 22 ASN E 134 ASN E 145 1 12
HELIX 23 23 GLN F 17 ALA F 32 1 16
HELIX 24 24 GLU F 69 ASN F 81 1 13
HELIX 25 25 SER G 19 ILE G 28 1 10
HELIX 26 26 GLU G 39 GLY G 54 1 16
HELIX 27 27 GLU G 57 ARG G 69 1 13
HELIX 28 28 ARG G 91 GLU G 105 1 15
HELIX 29 29 SER G 114 GLU G 128 1 15
HELIX 30 30 GLY G 131 ALA G 144 1 14
HELIX 31 31 ASP H 4 ALA H 19 1 16
HELIX 32 32 SER H 29 GLU H 41 1 13
HELIX 33 33 THR H 111 ALA H 118 1 8
HELIX 34 34 ILE I 29 ARG I 32 5 4
HELIX 35 35 GLY I 70 LEU I 86 1 17
HELIX 36 36 MET I 87 TYR I 89 5 3
HELIX 37 37 ASP J 14 ASP J 19 1 6
HELIX 38 38 ASP J 19 THR J 32 1 14
HELIX 39 39 THR J 80 MET J 88 1 9
HELIX 40 40 THR K 58 ASP K 71 1 14
HELIX 41 41 VAL K 73 GLY K 77 5 5
HELIX 42 42 GLU K 93 ALA K 101 1 9
HELIX 43 43 THR L 2 LYS L 9 1 8
HELIX 44 44 LYS M 26 ALA M 34 1 9
HELIX 45 45 SER M 48 GLN M 51 5 4
HELIX 46 46 ILE M 52 VAL M 59 1 8
HELIX 47 47 VAL M 64 GLY M 83 1 20
HELIX 48 48 TYR M 85 ARG M 91 1 7
HELIX 49 49 LYS N 2 ARG N 8 1 7
HELIX 50 50 GLU N 9 VAL N 13 5 5
HELIX 51 51 ALA N 14 TYR N 19 1 6
HELIX 52 52 SER N 79 MET N 88 1 10
HELIX 53 53 SER O 3 SER O 12 1 10
HELIX 54 54 SER O 23 GLU O 44 1 22
HELIX 55 55 ASP O 48 ASP O 73 1 26
HELIX 56 56 ASP O 73 LEU O 84 1 12
HELIX 57 57 ASP P 53 GLN P 63 1 11
HELIX 58 58 ARG P 70 LYS P 76 1 7
HELIX 59 59 THR R 27 TYR R 31 5 5
HELIX 60 60 ARG R 47 SER R 65 1 19
HELIX 61 61 ASP S 11 SER S 24 1 14
HELIX 62 62 LYS S 69 ALA S 74 1 6
HELIX 63 63 LYS T 7 GLU T 14 1 8
HELIX 64 64 ARG T 17 ALA T 40 1 24
HELIX 65 65 ASP T 42 ARG T 59 1 18
HELIX 66 66 ARG T 59 GLY T 64 1 6
HELIX 67 67 HIS T 67 ILE T 82 1 16
HELIX 68 68 LYS U 24 ALA U 29 1 6
HELIX 69 69 SER W 137 GLN W 152 1 16
HELIX 70 70 ASP W 166 GLY W 184 1 19
HELIX 71 71 GLY W 197 THR W 206 1 10
HELIX 72 72 GLY W 219 GLY W 229 1 11
HELIX 73 73 SER W 267 PHE W 273 1 7
HELIX 74 74 GLU W 279 GLY W 286 1 8
HELIX 75 75 VAL W 288 CYS W 297 1 10
HELIX 76 76 CYS W 310 GLY W 319 1 10
HELIX 77 77 ALA W 322 ALA W 337 1 16
SHEET 1 BA 2 PHE B 31 GLY B 32 0
SHEET 2 BA 2 LYS B 36 VAL B 37 -1 O VAL B 37 N PHE B 31
SHEET 1 BB 5 PHE B 90 VAL B 91 0
SHEET 2 BB 5 PHE B 68 VAL B 69 1 O PHE B 68 N VAL B 91
SHEET 3 BB 5 LEU B 160 VAL B 162 1 O PHE B 161 N VAL B 69
SHEET 4 BB 5 VAL B 182 ILE B 185 1 O PHE B 183 N VAL B 162
SHEET 5 BB 5 VAL B 195 ILE B 199 1 N ASP B 196 O VAL B 182
SHEET 1 CA 3 VAL C 51 GLU C 57 0
SHEET 2 CA 3 ARG C 64 THR C 69 -1 O ARG C 64 N GLU C 57
SHEET 3 CA 3 GLN C 99 GLU C 104 1 O GLN C 99 N VAL C 65
SHEET 1 CB 2 GLU C 165 TRP C 166 0
SHEET 2 CB 2 GLY C 147 VAL C 152 -1 O VAL C 152 N GLU C 165
SHEET 1 CC 2 GLU C 169 GLY C 170 0
SHEET 2 CC 2 GLY C 147 VAL C 152 -1 O ILE C 148 N GLU C 169
SHEET 1 CD 4 ALA C 179 ALA C 188 0
SHEET 2 CD 4 ILE C 195 GLU C 205 -1 O ILE C 195 N ALA C 188
SHEET 3 CD 4 GLY C 147 VAL C 152 -1 O GLY C 147 N PHE C 202
SHEET 4 CD 4 GLU C 165 TRP C 166 -1 O GLU C 165 N VAL C 152
SHEET 1 CE 4 ALA C 179 ALA C 188 0
SHEET 2 CE 4 ILE C 195 GLU C 205 -1 O ILE C 195 N ALA C 188
SHEET 3 CE 4 GLY C 147 VAL C 152 -1 O GLY C 147 N PHE C 202
SHEET 4 CE 4 GLU C 169 GLY C 170 -1 O GLU C 169 N ILE C 148
SHEET 1 DA 2 ASP D 140 VAL D 141 0
SHEET 2 DA 2 THR D 180 PHE D 181 -1 O PHE D 181 N ASP D 140
SHEET 1 EA 3 GLU E 12 VAL E 17 0
SHEET 2 EA 3 ALA E 34 GLY E 41 -1 O LEU E 35 N ALA E 16
SHEET 3 EA 3 ARG E 44 TYR E 49 -1 O ARG E 44 N ASP E 40
SHEET 1 EB 3 VAL E 84 GLY E 86 0
SHEET 2 EB 3 VAL E 93 PRO E 97 -1 O VAL E 93 N GLY E 86
SHEET 3 EB 3 VAL E 122 ALA E 124 -1 O LEU E 123 N GLN E 96
SHEET 1 FA 3 ARG F 2 MET F 9 0
SHEET 2 FA 3 HIS F 58 ALA F 66 -1 O VAL F 60 N PHE F 8
SHEET 3 FA 3 ILE F 36 ARG F 44 -1 N HIS F 37 O ASN F 63
SHEET 1 HA 3 ALA H 23 THR H 25 0
SHEET 2 HA 3 LEU H 58 LEU H 62 -1 O LEU H 60 N VAL H 24
SHEET 3 HA 3 ILE H 45 VAL H 50 -1 N GLU H 46 O THR H 61
SHEET 1 HB 3 VAL H 109 MET H 110 0
SHEET 2 HB 3 VAL H 103 SER H 104 -1 O VAL H 103 N MET H 110
SHEET 3 HB 3 GLU H 123 ILE H 124 -1 N GLU H 123 O SER H 104
SHEET 1 IA 2 ALA I 15 ALA I 16 0
SHEET 2 IA 2 VAL I 66 LYS I 67 -1 O LYS I 67 N ALA I 15
SHEET 1 IB 2 PHE I 19 LYS I 21 0
SHEET 2 IB 2 ASP I 61 TYR I 63 -1 O ASP I 61 N LYS I 21
SHEET 1 JA 2 ARG J 7 LYS J 11 0
SHEET 2 JA 2 ASP J 97 SER J 101 -1 O ASP J 97 N LYS J 11
SHEET 1 JB 2 VAL J 36 ILE J 40 0
SHEET 2 JB 2 VAL J 74 ILE J 76 -1 O VAL J 74 N ILE J 40
SHEET 1 JC 2 PHE J 49 VAL J 51 0
SHEET 2 JC 2 ASP J 63 TYR J 65 -1 O ASP J 63 N VAL J 51
SHEET 1 KA 5 GLY K 42 ALA K 44 0
SHEET 2 KA 5 ILE K 30 ASP K 35 -1 O VAL K 31 N ALA K 44
SHEET 3 KA 5 ASP K 17 HIS K 23 -1 O VAL K 19 N THR K 34
SHEET 4 KA 5 ASN K 80 LYS K 86 1 O ASN K 80 N GLY K 18
SHEET 5 KA 5 ARG K 105 ASP K 111 1 O ARG K 105 N LEU K 81
SHEET 1 LA 2 VAL L 32 ARG L 35 0
SHEET 2 LA 2 ARG L 49 ARG L 55 -1 O ARG L 53 N ARG L 35
SHEET 1 LB 2 THR L 38 THR L 39 0
SHEET 2 LB 2 ARG L 49 ARG L 55 -1 O ARG L 49 N THR L 39
SHEET 1 LC 2 VAL L 62 TYR L 65 0
SHEET 2 LC 2 ARG L 49 ARG L 55 1 O CYS L 52 N SER L 64
SHEET 1 PA 4 GLU P 34 ARG P 35 0
SHEET 2 PA 4 GLN P 18 ASP P 23 -1 O VAL P 21 N GLU P 34
SHEET 3 PA 4 VAL P 2 ALA P 7 -1 O THR P 3 N ALA P 22
SHEET 4 PA 4 ALA P 65 THR P 66 1 O THR P 66 N ILE P 4
SHEET 1 QA 3 THR Q 6 GLN Q 8 0
SHEET 2 QA 3 ASP Q 56 SER Q 67 -1 O ILE Q 60 N LEU Q 7
SHEET 3 QA 3 LYS Q 70 LYS Q 80 -1 O LYS Q 70 N LEU Q 66
SHEET 1 QB 2 VAL Q 21 GLU Q 25 0
SHEET 2 QB 2 THR Q 40 HIS Q 44 -1 O THR Q 41 N ILE Q 24
SHEET 1 QC 2 VAL Q 28 LYS Q 29 0
SHEET 2 QC 2 PHE Q 36 ILE Q 37 -1 O ILE Q 37 N VAL Q 28
SHEET 1 SA 3 ARG S 31 THR S 32 0
SHEET 2 SA 3 ILE S 48 HIS S 51 1 O ALA S 49 N THR S 32
SHEET 3 SA 3 HIS S 56 VAL S 59 -1 O VAL S 57 N VAL S 50
SHEET 1 WA 5 VAL W 61 CYS W 64 0
SHEET 2 WA 5 ALA W 52 SER W 56 -1 O ALA W 52 N CYS W 64
SHEET 3 WA 5 ASP W 40 SER W 46 -1 O ILE W 43 N GLU W 55
SHEET 4 WA 5 ARG W 78 PRO W 83 -1 O VAL W 79 N GLY W 42
SHEET 5 WA 5 GLY W 95 VAL W 97 -1 O ILE W 96 N ARG W 82
SHEET 1 WB 6 VAL W 187 MET W 189 0
SHEET 2 WB 6 GLU W 154 LEU W 159 1 O ILE W 157 N LEU W 188
SHEET 3 WB 6 GLN W 125 SER W 130 1 O ILE W 126 N ILE W 156
SHEET 4 WB 6 ILE W 209 ALA W 213 1 O ILE W 211 N VAL W 127
SHEET 5 WB 6 ASP W 263 ASP W 266 1 O ASP W 263 N SER W 210
SHEET 6 WB 6 ARG W 254 HIS W 257 -1 O ARG W 254 N ASP W 266
CISPEP 1 LEU W 133 PRO W 134 0 -6.75
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
