HEADER TRANSLATION 17-JUN-15 3JAM
TITLE CRYOEM STRUCTURE OF 40S-EIF1A-EIF1 COMPLEX FROM YEAST
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 18S RRNA;
COMPND 3 CHAIN: 2;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: US2;
COMPND 6 CHAIN: A;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: ES1;
COMPND 9 CHAIN: B;
COMPND 10 MOL_ID: 4;
COMPND 11 MOLECULE: US5;
COMPND 12 CHAIN: C;
COMPND 13 MOL_ID: 5;
COMPND 14 MOLECULE: US3;
COMPND 15 CHAIN: D;
COMPND 16 MOL_ID: 6;
COMPND 17 MOLECULE: ES4;
COMPND 18 CHAIN: E;
COMPND 19 MOL_ID: 7;
COMPND 20 MOLECULE: US7;
COMPND 21 CHAIN: F;
COMPND 22 MOL_ID: 8;
COMPND 23 MOLECULE: ES6;
COMPND 24 CHAIN: G;
COMPND 25 MOL_ID: 9;
COMPND 26 MOLECULE: ES7;
COMPND 27 CHAIN: H;
COMPND 28 MOL_ID: 10;
COMPND 29 MOLECULE: ES8;
COMPND 30 CHAIN: I;
COMPND 31 MOL_ID: 11;
COMPND 32 MOLECULE: US4;
COMPND 33 CHAIN: J;
COMPND 34 MOL_ID: 12;
COMPND 35 MOLECULE: ES10;
COMPND 36 CHAIN: K;
COMPND 37 MOL_ID: 13;
COMPND 38 MOLECULE: US17;
COMPND 39 CHAIN: L;
COMPND 40 MOL_ID: 14;
COMPND 41 MOLECULE: ES12;
COMPND 42 CHAIN: M;
COMPND 43 MOL_ID: 15;
COMPND 44 MOLECULE: US15;
COMPND 45 CHAIN: N;
COMPND 46 MOL_ID: 16;
COMPND 47 MOLECULE: US11;
COMPND 48 CHAIN: O;
COMPND 49 MOL_ID: 17;
COMPND 50 MOLECULE: US19;
COMPND 51 CHAIN: P;
COMPND 52 MOL_ID: 18;
COMPND 53 MOLECULE: US9;
COMPND 54 CHAIN: Q;
COMPND 55 MOL_ID: 19;
COMPND 56 MOLECULE: ES17;
COMPND 57 CHAIN: R;
COMPND 58 MOL_ID: 20;
COMPND 59 MOLECULE: US13;
COMPND 60 CHAIN: S;
COMPND 61 MOL_ID: 21;
COMPND 62 MOLECULE: ES19;
COMPND 63 CHAIN: T;
COMPND 64 MOL_ID: 22;
COMPND 65 MOLECULE: US10;
COMPND 66 CHAIN: U;
COMPND 67 MOL_ID: 23;
COMPND 68 MOLECULE: ES21;
COMPND 69 CHAIN: V;
COMPND 70 MOL_ID: 24;
COMPND 71 MOLECULE: US8;
COMPND 72 CHAIN: W;
COMPND 73 MOL_ID: 25;
COMPND 74 MOLECULE: US12;
COMPND 75 CHAIN: X;
COMPND 76 MOL_ID: 26;
COMPND 77 MOLECULE: ES24;
COMPND 78 CHAIN: Y;
COMPND 79 MOL_ID: 27;
COMPND 80 MOLECULE: ES25;
COMPND 81 CHAIN: Z;
COMPND 82 MOL_ID: 28;
COMPND 83 MOLECULE: ES26;
COMPND 84 CHAIN: a;
COMPND 85 MOL_ID: 29;
COMPND 86 MOLECULE: ES27;
COMPND 87 CHAIN: b;
COMPND 88 MOL_ID: 30;
COMPND 89 MOLECULE: ES28;
COMPND 90 CHAIN: c;
COMPND 91 MOL_ID: 31;
COMPND 92 MOLECULE: US14;
COMPND 93 CHAIN: d;
COMPND 94 MOL_ID: 32;
COMPND 95 MOLECULE: ES30;
COMPND 96 CHAIN: e;
COMPND 97 MOL_ID: 33;
COMPND 98 MOLECULE: ES31;
COMPND 99 CHAIN: f;
COMPND 100 MOL_ID: 34;
COMPND 101 MOLECULE: RACK1;
COMPND 102 CHAIN: g;
COMPND 103 MOL_ID: 35;
COMPND 104 MOLECULE: EL41;
COMPND 105 CHAIN: h;
COMPND 106 MOL_ID: 36;
COMPND 107 MOLECULE: EIF1A;
COMPND 108 CHAIN: i;
COMPND 109 ENGINEERED: YES;
COMPND 110 MOL_ID: 37;
COMPND 111 MOLECULE: EIF1;
COMPND 112 CHAIN: j;
COMPND 113 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 3 ORGANISM_TAXID: 28985;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 6 ORGANISM_TAXID: 28985;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 9 ORGANISM_TAXID: 28985;
SOURCE 10 MOL_ID: 4;
SOURCE 11 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 12 ORGANISM_TAXID: 28985;
SOURCE 13 MOL_ID: 5;
SOURCE 14 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 15 ORGANISM_TAXID: 28985;
SOURCE 16 MOL_ID: 6;
SOURCE 17 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 18 ORGANISM_TAXID: 28985;
SOURCE 19 MOL_ID: 7;
SOURCE 20 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 21 ORGANISM_TAXID: 28985;
SOURCE 22 MOL_ID: 8;
SOURCE 23 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 24 ORGANISM_TAXID: 28985;
SOURCE 25 MOL_ID: 9;
SOURCE 26 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 27 ORGANISM_TAXID: 28985;
SOURCE 28 MOL_ID: 10;
SOURCE 29 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 30 ORGANISM_TAXID: 28985;
SOURCE 31 MOL_ID: 11;
SOURCE 32 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 33 ORGANISM_TAXID: 28985;
SOURCE 34 MOL_ID: 12;
SOURCE 35 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 36 ORGANISM_TAXID: 28985;
SOURCE 37 MOL_ID: 13;
SOURCE 38 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 39 ORGANISM_TAXID: 28985;
SOURCE 40 MOL_ID: 14;
SOURCE 41 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 42 ORGANISM_TAXID: 28985;
SOURCE 43 MOL_ID: 15;
SOURCE 44 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 45 ORGANISM_TAXID: 28985;
SOURCE 46 MOL_ID: 16;
SOURCE 47 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 48 ORGANISM_TAXID: 28985;
SOURCE 49 MOL_ID: 17;
SOURCE 50 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 51 ORGANISM_TAXID: 28985;
SOURCE 52 MOL_ID: 18;
SOURCE 53 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 54 ORGANISM_TAXID: 28985;
SOURCE 55 MOL_ID: 19;
SOURCE 56 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 57 ORGANISM_TAXID: 28985;
SOURCE 58 MOL_ID: 20;
SOURCE 59 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 60 ORGANISM_TAXID: 28985;
SOURCE 61 MOL_ID: 21;
SOURCE 62 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 63 ORGANISM_TAXID: 28985;
SOURCE 64 MOL_ID: 22;
SOURCE 65 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 66 ORGANISM_TAXID: 28985;
SOURCE 67 MOL_ID: 23;
SOURCE 68 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 69 ORGANISM_TAXID: 28985;
SOURCE 70 MOL_ID: 24;
SOURCE 71 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 72 ORGANISM_TAXID: 28985;
SOURCE 73 MOL_ID: 25;
SOURCE 74 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 75 ORGANISM_TAXID: 28985;
SOURCE 76 MOL_ID: 26;
SOURCE 77 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 78 ORGANISM_TAXID: 28985;
SOURCE 79 MOL_ID: 27;
SOURCE 80 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 81 ORGANISM_TAXID: 28985;
SOURCE 82 MOL_ID: 28;
SOURCE 83 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 84 ORGANISM_TAXID: 28985;
SOURCE 85 MOL_ID: 29;
SOURCE 86 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 87 ORGANISM_TAXID: 28985;
SOURCE 88 MOL_ID: 30;
SOURCE 89 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 90 ORGANISM_TAXID: 28985;
SOURCE 91 MOL_ID: 31;
SOURCE 92 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 93 ORGANISM_TAXID: 28985;
SOURCE 94 MOL_ID: 32;
SOURCE 95 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 96 ORGANISM_TAXID: 28985;
SOURCE 97 MOL_ID: 33;
SOURCE 98 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 99 ORGANISM_TAXID: 28985;
SOURCE 100 MOL_ID: 34;
SOURCE 101 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 102 ORGANISM_TAXID: 28985;
SOURCE 103 MOL_ID: 35;
SOURCE 104 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;
SOURCE 105 ORGANISM_TAXID: 28985;
SOURCE 106 MOL_ID: 36;
SOURCE 107 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 108 ORGANISM_TAXID: 4932;
SOURCE 109 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 110 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 111 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 112 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 113 EXPRESSION_SYSTEM_PLASMID: PTYB2;
SOURCE 114 MOL_ID: 37;
SOURCE 115 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 116 ORGANISM_TAXID: 4932;
SOURCE 117 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 118 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 119 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 120 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 121 EXPRESSION_SYSTEM_PLASMID: PTYB2
KEYWDS EUKARYOTIC TRANSLATION INITIATION, 48S, SMALL RIBOSOME SUBUNIT, 40S,
KEYWDS 2 43S, TRANSLATION
EXPDTA ELECTRON MICROSCOPY
AUTHOR J.L.LLACER,T.HUSSAIN,V.RAMAKRISHNAN
REVDAT 2 02-SEP-15 3JAM 1 JRNL
REVDAT 1 12-AUG-15 3JAM 0
JRNL AUTH J.L.LLACER,T.HUSSAIN,L.MARLER,C.E.AITKEN,A.THAKUR,
JRNL AUTH 2 J.R.LORSCH,A.G.HINNEBUSCH,V.RAMAKRISHNAN
JRNL TITL CONFORMATIONAL DIFFERENCES BETWEEN OPEN AND CLOSED STATES OF
JRNL TITL 2 THE EUKARYOTIC TRANSLATION INITIATION COMPLEX.
JRNL REF MOL.CELL V. 59 399 2015
JRNL REFN ISSN 1097-2765
JRNL PMID 26212456
JRNL DOI 10.1016/J.MOLCEL.2015.06.033
REMARK 2
REMARK 2 RESOLUTION. 3.46 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : CHIMERA, COOT, REFMAC
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : 3J80
REMARK 3 REFINEMENT SPACE : RECIPROCAL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : R-FACTOR, FSC
REMARK 3 OVERALL ANISOTROPIC B VALUE : 89.000
REMARK 3
REMARK 3 FITTING PROCEDURE : LOCAL REFINEMENT
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : 1.340
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : 1.340
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.460
REMARK 3 NUMBER OF PARTICLES : 86055
REMARK 3 CTF CORRECTION METHOD : NULL
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: GOLD-STANDARD
REMARK 4
REMARK 4 3JAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUL-15.
REMARK 100 THE RCSB ID CODE IS RCSB160460.
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 : INITIATION FACTORS EIF1A AND
REMARK 245 EIF1 BOUND TO THE 40S RIBOSOME
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.17
REMARK 245 SAMPLE SUPPORT DETAILS : QUANTIFOIL R2/2 400 MESH COPPER
REMARK 245 GRIDS WITH 4-5 NM THIN CARBON ON
REMARK 245 TOP
REMARK 245 SAMPLE VITRIFICATION DETAILS : BLOT FOR 2.5 TO 3 SECONDS
REMARK 245 BEFORE PLUNGING INTO LIQUID
REMARK 245 ETHANE (FEI VITROBOT MARK I).
REMARK 245 SAMPLE BUFFER : 20 MM MES-KOH, 40 MM POTASSIUM
REMARK 245 ACETATE, 10 MM AMMONIUM ACETATE,
REMARK 245 8 MM MAGNESIUM ACETATE, 2 MM DTT
REMARK 245 PH : 6.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : 28-APR-14
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 2056
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : FEI FALCON II (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 4000.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.70
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 27.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 78000
REMARK 245 CALIBRATED MAGNIFICATION : 104478
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : COMPLETE DATASET WAS
REMARK 245 COLLECTED OVER TWO NON-CONSECUTIVE DAYS.
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: 37-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 2, A, B, C, D, E, F, G, H,
REMARK 350 AND CHAINS: I, J, K, L, M, N, O, P, Q,
REMARK 350 AND CHAINS: R, S, T, U, V, W, X, Y, Z,
REMARK 350 AND CHAINS: a, b, c, d, e, f, g, h, i, j
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 C 2 657A
REMARK 465 G 2 657B
REMARK 465 A 2 657C
REMARK 465 C 2 657D
REMARK 465 U 2 657E
REMARK 465 U 2 657F
REMARK 465 U 2 657G
REMARK 465 A 2 657H
REMARK 465 U 2 657I
REMARK 465 G 2 657J
REMARK 465 U 2 657K
REMARK 465 C 2 657L
REMARK 465 G 2 657M
REMARK 465 C 2 657N
REMARK 465 G 2 657O
REMARK 465 C 2 657P
REMARK 465 A 2 657Q
REMARK 465 C 2 657R
REMARK 465 U 2 657S
REMARK 465 MET A 1
REMARK 465 ILE A 210
REMARK 465 GLU A 211
REMARK 465 GLN A 212
REMARK 465 GLN A 213
REMARK 465 THR A 214
REMARK 465 ALA A 215
REMARK 465 GLU A 216
REMARK 465 GLU A 217
REMARK 465 GLU A 218
REMARK 465 ALA A 219
REMARK 465 VAL A 220
REMARK 465 ALA A 221
REMARK 465 SER A 222
REMARK 465 GLY A 223
REMARK 465 GLU A 224
REMARK 465 GLN A 225
REMARK 465 THR A 226
REMARK 465 GLU A 227
REMARK 465 GLU A 228
REMARK 465 ALA A 229
REMARK 465 VAL A 230
REMARK 465 ASP A 231
REMARK 465 ALA A 232
REMARK 465 THR A 233
REMARK 465 GLU A 234
REMARK 465 GLU A 235
REMARK 465 GLN A 236
REMARK 465 THR A 237
REMARK 465 GLU A 238
REMARK 465 ALA A 239
REMARK 465 ALA A 240
REMARK 465 GLU A 241
REMARK 465 TRP A 242
REMARK 465 ALA A 243
REMARK 465 GLU A 244
REMARK 465 GLU A 245
REMARK 465 GLY A 246
REMARK 465 GLN A 247
REMARK 465 ALA A 248
REMARK 465 GLN A 249
REMARK 465 GLU A 250
REMARK 465 GLU A 251
REMARK 465 GLU A 252
REMARK 465 TRP A 253
REMARK 465 ASN A 254
REMARK 465 MET B 1
REMARK 465 SER B 10
REMARK 465 LYS B 11
REMARK 465 GLY B 12
REMARK 465 LYS B 13
REMARK 465 LYS B 14
REMARK 465 GLY B 15
REMARK 465 LEU B 16
REMARK 465 LYS B 17
REMARK 465 LYS B 18
REMARK 465 GLU B 234
REMARK 465 ALA B 235
REMARK 465 SER B 236
REMARK 465 ALA B 237
REMARK 465 GLU B 238
REMARK 465 GLU B 239
REMARK 465 LYS B 240
REMARK 465 GLY B 241
REMARK 465 LYS B 242
REMARK 465 LYS B 243
REMARK 465 VAL B 244
REMARK 465 ALA B 245
REMARK 465 GLY B 246
REMARK 465 PHE B 247
REMARK 465 LYS B 248
REMARK 465 ASP B 249
REMARK 465 GLU B 250
REMARK 465 ILE B 251
REMARK 465 LEU B 252
REMARK 465 GLU B 253
REMARK 465 THR B 254
REMARK 465 VAL B 255
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 ALA C 3
REMARK 465 PRO C 4
REMARK 465 GLN C 5
REMARK 465 ALA C 6
REMARK 465 GLN C 7
REMARK 465 GLY C 8
REMARK 465 GLN C 9
REMARK 465 GLN C 10
REMARK 465 ALA C 11
REMARK 465 PRO C 12
REMARK 465 ARG C 13
REMARK 465 ARG C 14
REMARK 465 GLY C 15
REMARK 465 GLY C 16
REMARK 465 PHE C 17
REMARK 465 GLY C 18
REMARK 465 GLY C 19
REMARK 465 ALA C 20
REMARK 465 ASN C 21
REMARK 465 ARG C 22
REMARK 465 GLY C 23
REMARK 465 GLY C 24
REMARK 465 ARG C 25
REMARK 465 GLY C 26
REMARK 465 GLY C 27
REMARK 465 ARG C 28
REMARK 465 ARG C 29
REMARK 465 GLY C 30
REMARK 465 GLY C 31
REMARK 465 ARG C 32
REMARK 465 ARG C 33
REMARK 465 ASP C 34
REMARK 465 GLN C 35
REMARK 465 GLU C 36
REMARK 465 GLU C 37
REMARK 465 LYS C 38
REMARK 465 LYS C 256
REMARK 465 LYS C 257
REMARK 465 LYS C 258
REMARK 465 LEU C 259
REMARK 465 MET D 1
REMARK 465 VAL D 2
REMARK 465 ARG D 226
REMARK 465 PRO D 227
REMARK 465 THR D 228
REMARK 465 GLU D 229
REMARK 465 PRO D 230
REMARK 465 VAL D 231
REMARK 465 GLU D 232
REMARK 465 ALA D 233
REMARK 465 ALA D 234
REMARK 465 GLU D 235
REMARK 465 SER D 236
REMARK 465 ALA D 237
REMARK 465 MET E 1
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 GLU F 3
REMARK 465 HIS F 4
REMARK 465 GLU F 5
REMARK 465 ALA F 6
REMARK 465 GLN F 7
REMARK 465 VAL F 8
REMARK 465 GLU F 9
REMARK 465 VAL F 10
REMARK 465 GLU F 11
REMARK 465 VAL F 12
REMARK 465 GLN F 13
REMARK 465 GLU F 14
REMARK 465 ASP F 15
REMARK 465 PHE F 16
REMARK 465 GLU F 17
REMARK 465 VAL F 18
REMARK 465 VAL F 19
REMARK 465 GLN F 20
REMARK 465 GLU F 21
REMARK 465 ARG G 227
REMARK 465 LYS G 228
REMARK 465 ARG G 229
REMARK 465 ARG G 230
REMARK 465 ALA G 231
REMARK 465 SER G 232
REMARK 465 SER G 233
REMARK 465 LEU G 234
REMARK 465 LYS G 235
REMARK 465 ALA G 236
REMARK 465 MET H 1
REMARK 465 SER H 2
REMARK 465 ASP H 3
REMARK 465 GLU H 188
REMARK 465 THR H 189
REMARK 465 HIS H 190
REMARK 465 MET I 1
REMARK 465 LYS I 124
REMARK 465 LYS I 125
REMARK 465 ASN I 126
REMARK 465 THR I 127
REMARK 465 LYS I 128
REMARK 465 ALA I 129
REMARK 465 GLU I 130
REMARK 465 GLU I 131
REMARK 465 GLU I 132
REMARK 465 THR I 133
REMARK 465 ALA I 134
REMARK 465 THR I 135
REMARK 465 MET J 1
REMARK 465 GLU J 184
REMARK 465 ALA J 185
REMARK 465 ASP J 186
REMARK 465 GLU J 187
REMARK 465 GLU J 188
REMARK 465 GLY K 97
REMARK 465 ASP K 98
REMARK 465 GLN K 99
REMARK 465 ARG K 100
REMARK 465 PRO K 101
REMARK 465 GLN K 102
REMARK 465 GLY K 103
REMARK 465 LYS K 104
REMARK 465 LYS K 105
REMARK 465 TYR K 106
REMARK 465 MET L 1
REMARK 465 MET M 1
REMARK 465 SER M 2
REMARK 465 ASP M 3
REMARK 465 VAL M 4
REMARK 465 GLU M 5
REMARK 465 GLU M 6
REMARK 465 VAL M 7
REMARK 465 GLN M 8
REMARK 465 GLN M 9
REMARK 465 VAL M 10
REMARK 465 PRO M 11
REMARK 465 VAL M 12
REMARK 465 MET N 1
REMARK 465 MET O 1
REMARK 465 ALA O 2
REMARK 465 ASN O 3
REMARK 465 VAL O 4
REMARK 465 VAL O 5
REMARK 465 GLN O 6
REMARK 465 ALA O 7
REMARK 465 LYS O 8
REMARK 465 ASP O 9
REMARK 465 ASN O 10
REMARK 465 MET P 1
REMARK 465 SER P 2
REMARK 465 GLU P 3
REMARK 465 ALA P 4
REMARK 465 ALA P 5
REMARK 465 ALA P 6
REMARK 465 PRO P 7
REMARK 465 ALA P 131
REMARK 465 GLY P 132
REMARK 465 ALA P 133
REMARK 465 THR P 134
REMARK 465 THR P 135
REMARK 465 SER P 136
REMARK 465 ARG P 137
REMARK 465 PHE P 138
REMARK 465 ILE P 139
REMARK 465 PRO P 140
REMARK 465 LEU P 141
REMARK 465 ARG P 142
REMARK 465 MET Q 1
REMARK 465 SER Q 2
REMARK 465 MET R 1
REMARK 465 VAL R 127
REMARK 465 ARG R 128
REMARK 465 ASP R 129
REMARK 465 ARG R 130
REMARK 465 ARG R 131
REMARK 465 PHE R 132
REMARK 465 ARG R 133
REMARK 465 LYS R 134
REMARK 465 ARG R 135
REMARK 465 ASN R 136
REMARK 465 MET S 1
REMARK 465 MET T 1
REMARK 465 MET U 4
REMARK 465 SER U 5
REMARK 465 GLN U 6
REMARK 465 VAL U 7
REMARK 465 GLU U 8
REMARK 465 LYS U 9
REMARK 465 LYS U 10
REMARK 465 SER U 11
REMARK 465 GLU U 12
REMARK 465 GLN U 13
REMARK 465 GLN U 14
REMARK 465 MET W 1
REMARK 465 MET X 1
REMARK 465 MET Y 1
REMARK 465 MET Z 1
REMARK 465 PRO Z 2
REMARK 465 PRO Z 3
REMARK 465 LYS Z 4
REMARK 465 GLN Z 5
REMARK 465 GLN Z 6
REMARK 465 LEU Z 7
REMARK 465 SER Z 8
REMARK 465 LYS Z 9
REMARK 465 ALA Z 10
REMARK 465 ALA Z 11
REMARK 465 LYS Z 12
REMARK 465 ALA Z 13
REMARK 465 ALA Z 14
REMARK 465 ALA Z 15
REMARK 465 ALA Z 16
REMARK 465 MET Z 17
REMARK 465 ALA Z 18
REMARK 465 GLY Z 19
REMARK 465 GLY Z 20
REMARK 465 LYS Z 21
REMARK 465 LYS Z 22
REMARK 465 SER Z 23
REMARK 465 LYS Z 24
REMARK 465 LYS Z 25
REMARK 465 LYS Z 26
REMARK 465 TRP Z 27
REMARK 465 SER Z 28
REMARK 465 LYS Z 29
REMARK 465 LYS Z 30
REMARK 465 SER Z 31
REMARK 465 HIS Z 32
REMARK 465 LYS Z 33
REMARK 465 ASP Z 34
REMARK 465 LYS Z 35
REMARK 465 ALA Z 106
REMARK 465 SER Z 107
REMARK 465 GLU Z 108
REMARK 465 MET a 1
REMARK 465 ARG a 100
REMARK 465 PRO a 101
REMARK 465 ARG a 102
REMARK 465 PHE a 103
REMARK 465 ASN a 104
REMARK 465 ARG a 105
REMARK 465 ASP a 106
REMARK 465 ASN a 107
REMARK 465 LYS a 108
REMARK 465 VAL a 109
REMARK 465 SER a 110
REMARK 465 PRO a 111
REMARK 465 ALA a 112
REMARK 465 ASP a 113
REMARK 465 ALA a 114
REMARK 465 ALA a 115
REMARK 465 LYS a 116
REMARK 465 LYS a 117
REMARK 465 ALA a 118
REMARK 465 LEU a 119
REMARK 465 MET b 1
REMARK 465 MET c 1
REMARK 465 ASP c 2
REMARK 465 THR c 3
REMARK 465 LYS c 4
REMARK 465 MET d 1
REMARK 465 ALA d 2
REMARK 465 HIS d 3
REMARK 465 MET e 1
REMARK 465 GLY e 2
REMARK 465 LYS e 3
REMARK 465 VAL e 4
REMARK 465 HIS e 5
REMARK 465 GLY e 6
REMARK 465 SER e 7
REMARK 465 LEU e 8
REMARK 465 SER e 62
REMARK 465 GLN e 63
REMARK 465 MET f 1
REMARK 465 GLN f 2
REMARK 465 ILE f 3
REMARK 465 PHE f 4
REMARK 465 VAL f 5
REMARK 465 LYS f 6
REMARK 465 THR f 7
REMARK 465 LEU f 8
REMARK 465 THR f 9
REMARK 465 GLY f 10
REMARK 465 LYS f 11
REMARK 465 THR f 12
REMARK 465 ILE f 13
REMARK 465 THR f 14
REMARK 465 LEU f 15
REMARK 465 GLU f 16
REMARK 465 VAL f 17
REMARK 465 GLU f 18
REMARK 465 SER f 19
REMARK 465 SER f 20
REMARK 465 ASP f 21
REMARK 465 THR f 22
REMARK 465 ILE f 23
REMARK 465 ASP f 24
REMARK 465 ASN f 25
REMARK 465 VAL f 26
REMARK 465 LYS f 27
REMARK 465 SER f 28
REMARK 465 LYS f 29
REMARK 465 ILE f 30
REMARK 465 GLN f 31
REMARK 465 ASP f 32
REMARK 465 LYS f 33
REMARK 465 GLU f 34
REMARK 465 GLY f 35
REMARK 465 ILE f 36
REMARK 465 PRO f 37
REMARK 465 PRO f 38
REMARK 465 ASP f 39
REMARK 465 GLN f 40
REMARK 465 GLN f 41
REMARK 465 ARG f 42
REMARK 465 LEU f 43
REMARK 465 ILE f 44
REMARK 465 PHE f 45
REMARK 465 ALA f 46
REMARK 465 GLY f 47
REMARK 465 LYS f 48
REMARK 465 GLN f 49
REMARK 465 LEU f 50
REMARK 465 GLU f 51
REMARK 465 ASP f 52
REMARK 465 GLY f 53
REMARK 465 ARG f 54
REMARK 465 THR f 55
REMARK 465 LEU f 56
REMARK 465 SER f 57
REMARK 465 ASP f 58
REMARK 465 TYR f 59
REMARK 465 ASN f 60
REMARK 465 ILE f 61
REMARK 465 GLN f 62
REMARK 465 LYS f 63
REMARK 465 GLU f 64
REMARK 465 SER f 65
REMARK 465 THR f 66
REMARK 465 LEU f 67
REMARK 465 HIS f 68
REMARK 465 LEU f 69
REMARK 465 VAL f 70
REMARK 465 LEU f 71
REMARK 465 ARG f 72
REMARK 465 LEU f 73
REMARK 465 ARG f 74
REMARK 465 GLY f 75
REMARK 465 GLY f 76
REMARK 465 GLY f 77
REMARK 465 LYS f 78
REMARK 465 LYS f 79
REMARK 465 ARG f 80
REMARK 465 LYS f 81
REMARK 465 MET g 1
REMARK 465 SER g 2
REMARK 465 GLU g 163
REMARK 465 ASP g 164
REMARK 465 GLY g 165
REMARK 465 GLU g 166
REMARK 465 GLU g 190
REMARK 465 ASP g 191
REMARK 465 MET i 1
REMARK 465 GLY i 2
REMARK 465 LYS i 3
REMARK 465 LYS i 4
REMARK 465 ASN i 5
REMARK 465 THR i 6
REMARK 465 LYS i 7
REMARK 465 GLY i 8
REMARK 465 GLY i 9
REMARK 465 LYS i 10
REMARK 465 LYS i 11
REMARK 465 GLY i 12
REMARK 465 ARG i 13
REMARK 465 ARG i 14
REMARK 465 GLY i 15
REMARK 465 LYS i 16
REMARK 465 ASN i 17
REMARK 465 ASP i 18
REMARK 465 SER i 19
REMARK 465 ASP i 20
REMARK 465 GLY i 21
REMARK 465 THR i 118
REMARK 465 ASP i 119
REMARK 465 ASN i 120
REMARK 465 PHE i 121
REMARK 465 GLY i 122
REMARK 465 PHE i 123
REMARK 465 GLU i 124
REMARK 465 SER i 125
REMARK 465 ASP i 126
REMARK 465 GLU i 127
REMARK 465 ASP i 128
REMARK 465 VAL i 129
REMARK 465 ASN i 130
REMARK 465 PHE i 131
REMARK 465 GLU i 132
REMARK 465 PHE i 133
REMARK 465 GLY i 134
REMARK 465 ASN i 135
REMARK 465 ALA i 136
REMARK 465 ASP i 137
REMARK 465 GLU i 138
REMARK 465 ASP i 139
REMARK 465 ASP i 140
REMARK 465 GLU i 141
REMARK 465 GLU i 142
REMARK 465 GLY i 143
REMARK 465 GLU i 144
REMARK 465 ASP i 145
REMARK 465 GLU i 146
REMARK 465 GLU i 147
REMARK 465 LEU i 148
REMARK 465 ASP i 149
REMARK 465 ILE i 150
REMARK 465 ASP i 151
REMARK 465 ASP i 152
REMARK 465 ILE i 153
REMARK 465 MET j 1
REMARK 465 SER j 2
REMARK 465 ILE j 3
REMARK 465 GLU j 4
REMARK 465 ASN j 5
REMARK 465 LEU j 6
REMARK 465 LYS j 7
REMARK 465 SER j 8
REMARK 465 PHE j 9
REMARK 465 ASP j 10
REMARK 465 PRO j 11
REMARK 465 PHE j 12
REMARK 465 ALA j 13
REMARK 465 ASP j 14
REMARK 465 THR j 15
REMARK 465 GLY j 16
REMARK 465 ASP j 17
REMARK 465 ASP j 18
REMARK 465 GLU j 19
REMARK 465 THR j 20
REMARK 465 ALA j 21
REMARK 465 THR j 22
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 A 21692 N9 C8 N7 C5 C6 N6 N1
REMARK 470 A 21692 C2 N3 C4
REMARK 470 G 21693 N9 C8 N7 C5 C6 O6 N1
REMARK 470 G 21693 C2 N2 N3 C4
REMARK 470 G 21694 N9 C8 N7 C5 C6 O6 N1
REMARK 470 G 21694 C2 N2 N3 C4
REMARK 470 G 21695 N9 C8 N7 C5 C6 O6 N1
REMARK 470 G 21695 C2 N2 N3 C4
REMARK 470 G 21696 N9 C8 N7 C5 C6 O6 N1
REMARK 470 G 21696 C2 N2 N3 C4
REMARK 470 G 21697 N9 C8 N7 C5 C6 O6 N1
REMARK 470 G 21697 C2 N2 N3 C4
REMARK 470 C 21698 N1 C2 O2 N3 C4 N4 C5
REMARK 470 C 21698 C6
REMARK 470 A 21699 N9 C8 N7 C5 C6 N6 N1
REMARK 470 A 21699 C2 N3 C4
REMARK 470 A 21700 N9 C8 N7 C5 C6 N6 N1
REMARK 470 A 21700 C2 N3 C4
REMARK 470 C 21701 N1 C2 O2 N3 C4 N4 C5
REMARK 470 C 21701 C6
REMARK 470 U 21702 N1 C2 O2 N3 C4 O4 C5
REMARK 470 U 21702 C6
REMARK 470 C 21703 N1 C2 O2 N3 C4 N4 C5
REMARK 470 C 21703 C6
REMARK 470 C 21704 N1 C2 O2 N3 C4 N4 C5
REMARK 470 C 21704 C6
REMARK 470 A 21705 N9 C8 N7 C5 C6 N6 N1
REMARK 470 A 21705 C2 N3 C4
REMARK 470 LYS A 27 CG CD CE NZ
REMARK 470 GLU A 209 CG CD OE1 OE2
REMARK 470 LYS B 5 CG CD CE NZ
REMARK 470 ASN B 6 CG OD1 ND2
REMARK 470 LYS B 7 CG CD CE NZ
REMARK 470 LEU B 9 CG CD1 CD2
REMARK 470 ARG B 19 CG CD NE CZ NH1 NH2
REMARK 470 LYS I 123 CG CD CE NZ
REMARK 470 ARG P 130 CG CD NE CZ NH1 NH2
REMARK 470 ASN R 97 CG OD1 ND2
REMARK 470 GLN f 149 CG CD OE1 NE2
REMARK 470 LYS f 150 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 N1 A 2 991 O4 U 2 1011 1.40
REMARK 500 N1 A 2 480 O4 U 2 506 1.62
REMARK 500 O4 U 2 1079 N1 A 2 1090 1.66
REMARK 500 N3 U 2 628 N6 A 2 969 1.77
REMARK 500 N1 A 2 864 O4 U 2 964 1.83
REMARK 500 N6 A 2 51 N3 U 2 439 1.83
REMARK 500 O4 U 2 1292 N1 A 2 1321 1.86
REMARK 500 N1 A 2 51 O4 U 2 439 1.87
REMARK 500 N3 U 2 1593 N6 A 2 1598 1.90
REMARK 500 O4 U 2 1593 N1 A 2 1598 1.90
REMARK 500 O4 U 2 1037 N1 A 2 1091 1.98
REMARK 500 O2' U 2 1319 OP1 A 2 1321 2.04
REMARK 500 N1 A 2 480 C4 U 2 506 2.13
REMARK 500 C2 A 2 991 O4 U 2 1011 2.14
REMARK 500 C2 A 2 480 O4 U 2 506 2.16
REMARK 500 N3 U 2 8 N6 A 2 1138 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 G 21315 C2' - C3' - O3' ANGL. DEV. = 11.4 DEGREES
REMARK 500 G 21534 C2' - C3' - O3' ANGL. DEV. = 9.8 DEGREES
REMARK 500 LEU B 181 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500 PRO D 220 C - N - CA ANGL. DEV. = 10.4 DEGREES
REMARK 500 LEU H 118 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 LEU I 29 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 LEU I 190 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 PRO K 88 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 LEU S 105 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 PRO X 64 C - N - CD ANGL. DEV. = -14.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 5 -27.77 61.16
REMARK 500 LEU A 9 88.23 -69.63
REMARK 500 ARG A 21 47.00 78.45
REMARK 500 LYS A 27 158.24 66.80
REMARK 500 LYS A 39 176.25 58.93
REMARK 500 PRO A 42 -19.98 -46.32
REMARK 500 TYR A 81 2.21 -64.19
REMARK 500 THR A 93 -175.19 -66.07
REMARK 500 ALA A 95 125.02 46.34
REMARK 500 THR A 103 102.73 67.84
REMARK 500 ASN A 109 87.72 61.06
REMARK 500 LEU A 120 135.07 -173.91
REMARK 500 ASP A 129 41.74 -100.29
REMARK 500 LEU A 149 49.58 -83.88
REMARK 500 ASP A 150 -37.85 -156.97
REMARK 500 VAL A 158 106.92 84.36
REMARK 500 LYS A 167 -71.87 68.02
REMARK 500 TRP A 195 133.14 68.17
REMARK 500 TYR A 202 -113.92 -81.69
REMARK 500 PHE A 203 -151.03 55.07
REMARK 500 PRO A 207 107.04 -50.35
REMARK 500 GLU A 208 -34.04 -140.66
REMARK 500 ASP B 22 77.64 63.43
REMARK 500 VAL B 43 -67.79 -94.42
REMARK 500 LEU B 54 104.81 61.02
REMARK 500 LYS B 55 63.88 101.62
REMARK 500 SER B 60 49.46 -89.84
REMARK 500 LEU B 61 -49.86 -138.60
REMARK 500 ASP B 89 -58.82 -124.18
REMARK 500 LYS B 94 -54.87 70.32
REMARK 500 TRP B 117 15.13 82.27
REMARK 500 ASP B 131 -132.90 -86.81
REMARK 500 ALA B 147 83.89 -56.50
REMARK 500 ASN B 148 -25.27 167.05
REMARK 500 THR B 153 -86.75 -119.63
REMARK 500 SER B 154 53.35 82.07
REMARK 500 GLN B 177 -22.86 66.46
REMARK 500 SER B 179 170.47 97.99
REMARK 500 GLU B 191 58.78 39.77
REMARK 500 PRO B 206 -64.12 -24.76
REMARK 500 LEU B 207 145.61 66.99
REMARK 500 LYS B 214 114.23 64.37
REMARK 500 PRO B 221 -124.44 -72.23
REMARK 500 LYS B 222 -113.27 -81.45
REMARK 500 PHE B 223 -51.64 -127.65
REMARK 500 ASP B 224 86.87 52.82
REMARK 500 SER B 230 -8.22 -57.91
REMARK 500 THR C 44 137.97 68.27
REMARK 500 ASN C 80 47.73 -107.33
REMARK 500 ASP C 111 -104.95 -104.45
REMARK 500
REMARK 500 THIS ENTRY HAS 485 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 PHE K 87 PRO K 88 -148.67
REMARK 500 MET P 28 PRO P 29 -149.85
REMARK 500 GLN Q 40 PRO Q 41 138.98
REMARK 500 GLN X 63 PRO X 64 -134.74
REMARK 500 HIS Y 29 PRO Y 30 -147.64
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 VAL C 141 24.6 L L OUTSIDE RANGE
REMARK 500 ILE F 66 24.9 L L OUTSIDE RANGE
REMARK 500 SER H 31 24.9 L L OUTSIDE RANGE
REMARK 500 GLN H 74 23.0 L L OUTSIDE RANGE
REMARK 500 PHE H 131 23.5 L L OUTSIDE RANGE
REMARK 500 THR L 6 24.7 L L OUTSIDE RANGE
REMARK 500 ILE L 54 23.6 L L OUTSIDE RANGE
REMARK 500 VAL Q 39 24.3 L L OUTSIDE RANGE
REMARK 500 GLN Q 40 24.3 L L OUTSIDE RANGE
REMARK 500 PHE R 71 23.9 L L OUTSIDE RANGE
REMARK 500 ILE W 83 23.9 L L OUTSIDE RANGE
REMARK 500 ASN Y 31 24.1 L L OUTSIDE RANGE
REMARK 500 LYS Z 97 24.3 L L OUTSIDE RANGE
REMARK 500 HIS f 143 24.9 L L OUTSIDE RANGE
REMARK 500 GLU j 73 24.9 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21865 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 21427 OP2
REMARK 620 2 C 21273 OP1 113.7
REMARK 620 3 G 21426 OP1 95.3 106.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21826 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 21327 OP2
REMARK 620 2 G 21329 O6 130.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21874 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 2 914 OP2
REMARK 620 2 G 2 894 O6 131.9
REMARK 620 3 U 2 916 O4 131.7 79.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21803 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 2 554 OP2
REMARK 620 2 A 2 555 OP2 87.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21818 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 2 604 OP1
REMARK 620 2 G 2 606 OP1 81.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21812 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 21769 OP1
REMARK 620 2 A 21761 OP1 90.8
REMARK 620 3 G 21765 O3' 161.3 106.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21828 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 2 101 OP2
REMARK 620 2 C 2 360 OP2 160.2
REMARK 620 3 A 2 100 OP2 85.0 81.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21823 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 2 620 OP2
REMARK 620 2 A 2 618 OP2 149.1
REMARK 620 3 A 2 619 OP2 66.5 82.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21835 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 2 267 OP1
REMARK 620 2 GLN G 176 OE1 120.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21834 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 21628 OP1
REMARK 620 2 G 21791 OP1 143.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21864 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U 21520 OP2
REMARK 620 2 U 21518 O2 123.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21869 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C 2 249 OP1
REMARK 620 2 A 2 250 OP2 92.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21836 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 2 459 OP2
REMARK 620 2 G 2 460 OP2 85.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21872 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 2 635 OP2
REMARK 620 2 A 2 634 OP1 75.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21822 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 21761 OP2
REMARK 620 2 A 21760 OP2 93.7
REMARK 620 3 G 21766 OP2 91.3 91.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21816 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 2 377 OP2
REMARK 620 2 U 2 378 OP2 87.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN a 500 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS a 26 SG
REMARK 620 2 CYS a 77 SG 99.4
REMARK 620 3 CYS a 23 SG 129.6 113.4
REMARK 620 4 CYS a 74 SG 110.3 95.9 103.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21866 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A 21201 OP1
REMARK 620 2 C 21597 O2 119.5
REMARK 620 3 A 21202 OP2 62.6 118.5
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21830 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 21109 OP2
REMARK 620 2 G 21108 OP1 73.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG 21862 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G 21426 OP2
REMARK 620 2 C 21273 OP2 69.1
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1809
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1811
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1812
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1814
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1815
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1816
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1817
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1818
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1819
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1820
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1821
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1822
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1823
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1824
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1825
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1826
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1827
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1828
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1830
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1831
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1832
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1833
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1834
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1835
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1836
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1837
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1841
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1842
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1844
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1845
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1846
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1849
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1850
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1852
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1854
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1855
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1856
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1857
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1858
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1859
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1860
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1861
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1862
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1863
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1864
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1865
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1866
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1868
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1869
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1870
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1871
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1872
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1874
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1875
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1876
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1877
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN a 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN b 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG f 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN f 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-3047 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-3048 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-3049 RELATED DB: EMDB
REMARK 900 RELATED ID: 3J80 RELATED DB: PDB
REMARK 900 YEAST 40S-EIF1-EIF1A AT LOWER RESOLUTION, FITTED INTO AN EM
REMARK 900 MAP WITH AN EXTRA COMPONENT NOT FOUND IN EMD-3047
REMARK 900 RELATED ID: 3JAP RELATED DB: PDB
REMARK 900 RELATED ID: 3JAQ RELATED DB: PDB
DBREF1 3JAM 2 1 1798 GB NC_006040.1
DBREF2 3JAM 2 NC_006040.1 1505732 1507530
DBREF 3JAM A 1 254 UNP Q6CN12 RSSA_KLULA 1 254
DBREF 3JAM B 1 255 UNP Q6CWD0 RS3A_KLULA 1 255
DBREF 3JAM C 1 259 UNP Q6CKL3 Q6CKL3_KLULA 1 259
DBREF 3JAM D 1 237 UNP Q6CRK7 Q6CRK7_KLULA 1 237
DBREF 3JAM E 1 261 UNP Q6CWJ2 Q6CWJ2_KLULA 1 261
DBREF 3JAM F 1 227 UNP Q6CRA3 Q6CRA3_KLULA 1 227
DBREF 3JAM G 1 236 UNP Q6CM04 RS6_KLULA 1 236
DBREF 3JAM H 1 190 UNP Q6CTD6 Q6CTD6_KLULA 1 190
DBREF 3JAM I 1 201 UNP Q6CMG3 Q6CMG3_KLULA 1 201
DBREF 3JAM J 1 188 UNP Q6CM18 Q6CM18_KLULA 1 188
DBREF 3JAM K 1 106 UNP Q6CVZ5 Q6CVZ5_KLULA 1 106
DBREF 3JAM L 1 156 UNP Q6CX80 Q6CX80_KLULA 1 156
DBREF 3JAM M 1 134 UNP Q6CLU4 Q6CLU4_KLULA 1 134
DBREF 3JAM N 1 151 UNP Q6CJK0 Q6CJK0_KLULA 1 151
DBREF 3JAM O 1 137 UNP P27069 RS14_KLULA 1 137
DBREF 3JAM P 1 142 UNP Q6CKV4 Q6CKV4_KLULA 1 142
DBREF 3JAM Q 1 143 UNP Q875N2 RS16_KLULA 1 143
DBREF 3JAM R 1 136 UNP Q6CWU3 Q6CWU3_KLULA 1 136
DBREF 3JAM S 1 146 UNP Q6CWT9 Q6CWT9_KLULA 1 146
DBREF 3JAM T 1 144 UNP Q6CXM0 Q6CXM0_KLULA 1 144
DBREF 3JAM U 4 120 UNP Q6CIM1 Q6CIM1_KLULA 1 117
DBREF 3JAM V 1 87 UNP Q6CXT6 RS21_KLULA 1 87
DBREF 3JAM W 1 130 UNP Q6CW21 RS22_KLULA 1 130
DBREF 3JAM X 1 145 UNP F2Z602 F2Z602_KLULA 1 145
DBREF 3JAM Y 1 135 UNP Q6CU44 Q6CU44_KLULA 1 135
DBREF 3JAM Z 1 108 UNP Q6CW78 Q6CW78_KLULA 1 108
DBREF 3JAM a 1 119 UNP Q6CS01 Q6CS01_KLULA 1 119
DBREF 3JAM b 1 82 UNP Q6CNL2 Q6CNL2_KLULA 1 82
DBREF 3JAM c 1 67 UNP P33285 RS28_KLULA 1 67
DBREF 3JAM d 1 56 UNP Q6CPG3 RS29_KLULA 1 56
DBREF 3JAM e 1 63 UNP Q6CUH5 Q6CUH5_KLULA 1 63
DBREF 3JAM f 1 150 UNP P69061 RS27A_KLULA 1 150
DBREF 3JAM g 1 326 UNP Q6CNI7 Q6CNI7_KLULA 1 326
DBREF 3JAM h 1 25 UNP P0CX86 RL41A_YEAST 1 25
DBREF 3JAM i 1 153 UNP P38912 IF1A_YEAST 1 153
DBREF 3JAM j 1 108 UNP P32911 SUI1_YEAST 1 108
SEQRES 1 2 1799 U A U C U G G U U G A U C
SEQRES 2 2 1799 C U G C C A G U A G U C A
SEQRES 3 2 1799 U A U G C U U G U C U C A
SEQRES 4 2 1799 A A G A U U A A G C C A U
SEQRES 5 2 1799 G C A U G U C U A A G U A
SEQRES 6 2 1799 U A A G C A A U U U A U A
SEQRES 7 2 1799 C A G U G A A A C U G C G
SEQRES 8 2 1799 A A U G G C U C A U U A A
SEQRES 9 2 1799 A U C A G U U A U C G U U
SEQRES 10 2 1799 U A U U U G A U A G U U C
SEQRES 11 2 1799 C U U U A C U A C A U G G
SEQRES 12 2 1799 A U A U C U G U G G U A A
SEQRES 13 2 1799 U U C U A G A G C U A A U
SEQRES 14 2 1799 A C A U G C U U A A A A U
SEQRES 15 2 1799 C U C G A C C C U U U G G
SEQRES 16 2 1799 A A G A G A U G U A U U U
SEQRES 17 2 1799 A U U A G A U A A A A A A
SEQRES 18 2 1799 U C A A U G U C U U C G G
SEQRES 19 2 1799 A C U C C U U G A U G A U
SEQRES 20 2 1799 U C A U A A U A A C U U U
SEQRES 21 2 1799 U C G A A U C G C A U G G
SEQRES 22 2 1799 C C U U G U G C U G G C G
SEQRES 23 2 1799 A U G G U U C A U U C A A
SEQRES 24 2 1799 A U U U C U G C C C U A U
SEQRES 25 2 1799 C A A C U U U C G A U G G
SEQRES 26 2 1799 U A G G A U A G U G G C C
SEQRES 27 2 1799 U A C C A U G G U U U C A
SEQRES 28 2 1799 A C G G G U A A C G G G G
SEQRES 29 2 1799 A A U A A G G G U U C G A
SEQRES 30 2 1799 U U C C G G A G A G G G A
SEQRES 31 2 1799 G C C U G A G A A A C G G
SEQRES 32 2 1799 C U A C C A C A U C C A A
SEQRES 33 2 1799 G G A A G G C A G C A G G
SEQRES 34 2 1799 C G C G C A A A U U A C C
SEQRES 35 2 1799 C A A U C C U A A U U C A
SEQRES 36 2 1799 G G G A G G U A G U G A C
SEQRES 37 2 1799 A A U A A A U A A C G A U
SEQRES 38 2 1799 A C A G G G C C C A U U C
SEQRES 39 2 1799 G G G U C U U G U A A U U
SEQRES 40 2 1799 G G A A U G A G U A C A A
SEQRES 41 2 1799 U G U A A A U A C C U U A
SEQRES 42 2 1799 A C G A G G A A C A A C U
SEQRES 43 2 1799 G G A G G G C A A G U C U
SEQRES 44 2 1799 G G U G C C A G C A G C C
SEQRES 45 2 1799 G C G G U A A U U C C A G
SEQRES 46 2 1799 C U C C A G U A G C G U A
SEQRES 47 2 1799 U A U U A A A G U U G U U
SEQRES 48 2 1799 G C A G U U A A A A A G C
SEQRES 49 2 1799 U C G U A G U U G A A C U
SEQRES 50 2 1799 U U G G G U C U G G U U G
SEQRES 51 2 1799 U C C G G U C C G A C U U
SEQRES 52 2 1799 U A U G U C G C G C A C U
SEQRES 53 2 1799 G G U U U U U C A A C C G
SEQRES 54 2 1799 G A U C U U U C C U U C U
SEQRES 55 2 1799 G G C U A A C C U G U A C
SEQRES 56 2 1799 U C C U U G U G G G U G C
SEQRES 57 2 1799 A G G C G A A C C A G G A
SEQRES 58 2 1799 C U U U U A C U U U G A A
SEQRES 59 2 1799 A A A A U U A G A G U G U
SEQRES 60 2 1799 U C A A A G C A G G C G A
SEQRES 61 2 1799 A A G C U C G A A U A U A
SEQRES 62 2 1799 U U A G C A U G G A A U A
SEQRES 63 2 1799 A U G G A A U A G G A C G
SEQRES 64 2 1799 U U U G G U U C U A U U U
SEQRES 65 2 1799 U G U U G G U U U C U A G
SEQRES 66 2 1799 G A C C A U C G U A A U G
SEQRES 67 2 1799 A U U A A U A G G G A C G
SEQRES 68 2 1799 G U C G G G G G C A U C A
SEQRES 69 2 1799 G U A U U C A A U U G U C
SEQRES 70 2 1799 A G A G G U G A A A U U C
SEQRES 71 2 1799 U U G G A U U U A U U G A
SEQRES 72 2 1799 A G A C U A A C U A C U G
SEQRES 73 2 1799 C G A A A G C A U U U G C
SEQRES 74 2 1799 C A A G G A C G U U U U C
SEQRES 75 2 1799 A U U A A U C A A G A A C
SEQRES 76 2 1799 G A A A G U U A G G G G A
SEQRES 77 2 1799 U C G A A G A U G A U C A
SEQRES 78 2 1799 G A U A C C G U C G U A G
SEQRES 79 2 1799 U C U U A A C C A U A A A
SEQRES 80 2 1799 C U A U G C C G A C U A G
SEQRES 81 2 1799 G G A U C G G G U G G U G
SEQRES 82 2 1799 U U U U U C U U A U G A C
SEQRES 83 2 1799 C C A C U C G G C A C C U
SEQRES 84 2 1799 U A C G A G A A A U C A A
SEQRES 85 2 1799 A G U C U U U G G G U U C
SEQRES 86 2 1799 U G G G G G G A G U A U G
SEQRES 87 2 1799 G U C G C A A G G C U G A
SEQRES 88 2 1799 A A C U U A A A G G A A U
SEQRES 89 2 1799 U G A C G G A A G G G C A
SEQRES 90 2 1799 C C A C C A G G A G U G G
SEQRES 91 2 1799 A G C C U G C G G C U U A
SEQRES 92 2 1799 A U U U G A C U C A A C A
SEQRES 93 2 1799 C G G G G A A A C U C A C
SEQRES 94 2 1799 C A G G U C C A G A C A C
SEQRES 95 2 1799 A A U A A G G A U U G A C
SEQRES 96 2 1799 A G A U U G A G A G C U C
SEQRES 97 2 1799 U U U C U U G A U U U U G
SEQRES 98 2 1799 U G G G U G G U G G U G C
SEQRES 99 2 1799 A U G G C C G U U C U U A
SEQRES 100 2 1799 G U U G G U G G A G U G A
SEQRES 101 2 1799 U U U G U C U G C U U A A
SEQRES 102 2 1799 U U G C G A U A A C G A A
SEQRES 103 2 1799 C G A G A C C U U A A C C
SEQRES 104 2 1799 U A C U A A A U A G G G U
SEQRES 105 2 1799 U G C U G G C A C U U G C
SEQRES 106 2 1799 C G G U U G A C U C U U C
SEQRES 107 2 1799 U U A G A G G G A C U A U
SEQRES 108 2 1799 C G G U U U C A A G C C G
SEQRES 109 2 1799 A U G G A A G U U U G A G
SEQRES 110 2 1799 G C A A U A A C A G G U C
SEQRES 111 2 1799 U G U G A U G C C C U U A
SEQRES 112 2 1799 G A C G U U C U G G G C C
SEQRES 113 2 1799 G C A C G C G C G C U A C
SEQRES 114 2 1799 A C U G A C G G A G C C A
SEQRES 115 2 1799 G C G A G U A C A A C C U
SEQRES 116 2 1799 U G G C C G A G A G G U C
SEQRES 117 2 1799 U G G G U A A U C U U G U
SEQRES 118 2 1799 G A A A C U C C G U C G U
SEQRES 119 2 1799 G C U G G G G A U A G A G
SEQRES 120 2 1799 C A U U G U A A U U A U U
SEQRES 121 2 1799 G C U C U U C A A C G A G
SEQRES 122 2 1799 G A A U U C C U A G U A A
SEQRES 123 2 1799 G C G C A A G U C A U C A
SEQRES 124 2 1799 G C U U G C G U U G A U U
SEQRES 125 2 1799 A C G U C C C U G C C C U
SEQRES 126 2 1799 U U G U A C A C A C C G C
SEQRES 127 2 1799 C C G U C G C U A G U A C
SEQRES 128 2 1799 C G A U U G A A U G G C U
SEQRES 129 2 1799 U A G U G A G G C C U C A
SEQRES 130 2 1799 G G A U U U G C U U A G A
SEQRES 131 2 1799 G A A G G G G G C A A C U
SEQRES 132 2 1799 C C A U C U C A G A G C G
SEQRES 133 2 1799 A A G A A U C U G G U C A
SEQRES 134 2 1799 A A C U U G G U C A U U U
SEQRES 135 2 1799 A G A G G A A C U A A A A
SEQRES 136 2 1799 G U C G U A A C A A G G U
SEQRES 137 2 1799 U U C C G U A G G U G A A
SEQRES 138 2 1799 C C U G C G G A A G G A U
SEQRES 139 2 1799 C A U U A
SEQRES 1 A 254 MET SER LEU PRO SER THR PHE ASP LEU THR SER GLU ASP
SEQRES 2 A 254 ALA GLN LEU LEU LEU ALA ALA ARG VAL HIS LEU GLY ALA
SEQRES 3 A 254 LYS ASN VAL GLN VAL HIS GLN GLU PRO TYR VAL TYR LYS
SEQRES 4 A 254 ALA ARG PRO ASP GLY VAL ASN VAL ILE ASN VAL GLY LYS
SEQRES 5 A 254 THR TRP GLU LYS ILE VAL LEU ALA ALA ARG ILE ILE ALA
SEQRES 6 A 254 ALA ILE PRO ASN PRO GLU ASP VAL VAL ALA ILE SER SER
SEQRES 7 A 254 ARG THR TYR GLY GLN ARG ALA VAL LEU LYS TYR ALA ALA
SEQRES 8 A 254 HIS THR GLY ALA THR PRO ILE ALA GLY ARG PHE THR PRO
SEQRES 9 A 254 GLY SER PHE THR ASN TYR ILE THR ARG SER PHE LYS GLU
SEQRES 10 A 254 PRO ARG LEU VAL ILE VAL THR ASP PRO ARG SER ASP ALA
SEQRES 11 A 254 GLN ALA ILE LYS GLU SER SER TYR VAL ASN ILE PRO VAL
SEQRES 12 A 254 ILE ALA LEU THR ASP LEU ASP SER PRO SER GLU TYR VAL
SEQRES 13 A 254 ASP VAL ALA ILE PRO CYS ASN ASN ARG GLY LYS HIS SER
SEQRES 14 A 254 ILE GLY LEU ILE TRP TYR LEU LEU ALA ARG GLU VAL LEU
SEQRES 15 A 254 ARG LEU ARG GLY ALA LEU PRO ASP ARG THR GLN PRO TRP
SEQRES 16 A 254 ALA ILE MET PRO ASP LEU TYR PHE TYR ARG ASN PRO GLU
SEQRES 17 A 254 GLU ILE GLU GLN GLN THR ALA GLU GLU GLU ALA VAL ALA
SEQRES 18 A 254 SER GLY GLU GLN THR GLU GLU ALA VAL ASP ALA THR GLU
SEQRES 19 A 254 GLU GLN THR GLU ALA ALA GLU TRP ALA GLU GLU GLY GLN
SEQRES 20 A 254 ALA GLN GLU GLU GLU TRP ASN
SEQRES 1 B 255 MET ALA VAL GLY LYS ASN LYS ARG LEU SER LYS GLY LYS
SEQRES 2 B 255 LYS GLY LEU LYS LYS ARG VAL VAL ASP PRO PHE THR ARG
SEQRES 3 B 255 LYS GLU TRP TYR ASP ILE LYS ALA PRO SER THR PHE GLU
SEQRES 4 B 255 ASN ARG ASN VAL GLY LYS THR LEU VAL ASN LYS SER VAL
SEQRES 5 B 255 GLY LEU LYS ASN ALA SER ASP SER LEU LYS GLY ARG VAL
SEQRES 6 B 255 VAL GLU VAL CYS LEU ALA ASP LEU GLN GLY SER GLU ASP
SEQRES 7 B 255 HIS SER PHE ARG LYS VAL LYS LEU ARG VAL ASP GLU VAL
SEQRES 8 B 255 GLN GLY LYS ASN LEU LEU THR ASN PHE HIS GLY MET ASP
SEQRES 9 B 255 PHE THR THR ASP LYS LEU ARG SER MET VAL ARG LYS TRP
SEQRES 10 B 255 GLN THR LEU ILE GLU ALA ASN VAL THR VAL LYS THR SER
SEQRES 11 B 255 ASP ASP TYR VAL LEU ARG ILE PHE ALA ILE ALA PHE THR
SEQRES 12 B 255 ARG LYS GLN ALA ASN GLN VAL LYS ARG THR SER TYR ALA
SEQRES 13 B 255 GLN SER SER HIS ILE ARG GLN ILE ARG LYS VAL ILE SER
SEQRES 14 B 255 GLU ILE LEU THR ARG GLU VAL GLN ASN SER THR LEU ALA
SEQRES 15 B 255 GLN LEU THR SER LYS LEU ILE PRO GLU VAL ILE ASN LYS
SEQRES 16 B 255 GLU ILE GLU ASN ALA THR LYS ASP ILE PHE PRO LEU GLN
SEQRES 17 B 255 ASN VAL HIS ILE ARG LYS VAL LYS LEU LEU LYS GLN PRO
SEQRES 18 B 255 LYS PHE ASP LEU GLY SER LEU LEU SER LEU HIS GLY GLU
SEQRES 19 B 255 ALA SER ALA GLU GLU LYS GLY LYS LYS VAL ALA GLY PHE
SEQRES 20 B 255 LYS ASP GLU ILE LEU GLU THR VAL
SEQRES 1 C 259 MET SER ALA PRO GLN ALA GLN GLY GLN GLN ALA PRO ARG
SEQRES 2 C 259 ARG GLY GLY PHE GLY GLY ALA ASN ARG GLY GLY ARG GLY
SEQRES 3 C 259 GLY ARG ARG GLY GLY ARG ARG ASP GLN GLU GLU LYS GLY
SEQRES 4 C 259 TRP VAL PRO VAL THR LYS LEU GLY ARG LEU VAL LYS ALA
SEQRES 5 C 259 GLY LYS ILE SER SER ILE GLU GLU ILE PHE LEU HIS SER
SEQRES 6 C 259 LEU PRO VAL LYS GLU PHE GLN ILE ILE ASP GLN LEU LEU
SEQRES 7 C 259 PRO ASN LEU LYS ASP GLU VAL MET ASN ILE LYS PRO VAL
SEQRES 8 C 259 GLN LYS GLN THR ARG ALA GLY GLN ARG THR ARG PHE LYS
SEQRES 9 C 259 ALA VAL VAL VAL VAL GLY ASP SER ASN GLY HIS VAL GLY
SEQRES 10 C 259 LEU GLY ILE LYS THR ALA LYS GLU VAL ALA GLY ALA ILE
SEQRES 11 C 259 ARG ALA GLY ILE ILE ILE ALA LYS LEU SER VAL ILE PRO
SEQRES 12 C 259 ILE ARG ARG GLY TYR TRP GLY THR ASN LEU GLY GLN PRO
SEQRES 13 C 259 HIS SER LEU ALA THR LYS THR SER GLY LYS CYS GLY SER
SEQRES 14 C 259 VAL SER VAL ARG LEU ILE PRO ALA PRO ARG GLY SER GLY
SEQRES 15 C 259 ILE VAL ALA SER PRO ALA VAL LYS LYS LEU MET GLN LEU
SEQRES 16 C 259 ALA GLY VAL GLU ASP VAL TYR THR SER SER THR GLY SER
SEQRES 17 C 259 THR ARG THR LEU GLU ASN THR LEU LYS ALA ALA PHE VAL
SEQRES 18 C 259 ALA ILE GLY ASN THR TYR GLY PHE LEU THR PRO ASN LEU
SEQRES 19 C 259 TRP GLU VAL GLN ALA LEU THR PRO SER PRO MET ASP VAL
SEQRES 20 C 259 TYR ALA ASP TYR ALA THR ALA SER LYS LYS LYS LEU
SEQRES 1 D 237 MET VAL ALA ILE ILE SER LYS LYS ARG LYS LEU VAL ALA
SEQRES 2 D 237 ASP GLY VAL PHE TYR ALA GLU LEU ASN GLU PHE PHE THR
SEQRES 3 D 237 ARG GLU LEU ALA GLU GLU GLY TYR SER GLY VAL GLU VAL
SEQRES 4 D 237 ARG VAL THR PRO THR LYS THR GLU ILE ILE ILE ARG ALA
SEQRES 5 D 237 THR LYS VAL GLN ASP VAL VAL GLY GLU ASN GLY ARG ARG
SEQRES 6 D 237 ILE ASN GLU LEU THR LEU LEU ILE GLU LYS ARG PHE LYS
SEQRES 7 D 237 TYR LYS ARG GLY THR ILE ALA LEU TYR ALA GLU ARG VAL
SEQRES 8 D 237 HIS ASP ARG GLY LEU SER ALA VAL ALA GLN ALA GLU SER
SEQRES 9 D 237 MET LYS PHE LYS LEU LEU ASN GLY LEU ALA ILE ARG ARG
SEQRES 10 D 237 ALA ALA TYR GLY VAL VAL ARG TYR VAL MET GLU SER GLY
SEQRES 11 D 237 ALA LYS GLY CYS GLU VAL VAL ILE SER GLY LYS LEU ARG
SEQRES 12 D 237 ALA ALA ARG ALA LYS SER MET LYS PHE ALA ASP GLY PHE
SEQRES 13 D 237 LEU ILE HIS SER GLY GLN PRO VAL ASN ASP PHE ILE GLU
SEQRES 14 D 237 THR ALA THR ARG HIS VAL LEU LEU ARG GLN GLY VAL LEU
SEQRES 15 D 237 GLY ILE LYS VAL LYS ILE MET LYS ASP PRO SER ARG ASN
SEQRES 16 D 237 THR SER GLY PRO LYS ALA LEU PRO ASP ALA VAL THR ILE
SEQRES 17 D 237 ILE GLU PRO LYS GLU GLU GLU PRO VAL LEU GLU PRO SER
SEQRES 18 D 237 VAL LYS ASP TYR ARG PRO THR GLU PRO VAL GLU ALA ALA
SEQRES 19 D 237 GLU SER ALA
SEQRES 1 E 261 MET ALA ARG GLY PRO LYS LYS HIS LEU LYS ARG LEU ALA
SEQRES 2 E 261 ALA PRO HIS HIS TRP MET LEU ASP LYS LEU SER GLY CYS
SEQRES 3 E 261 TYR ALA PRO ARG PRO SER ALA GLY PRO HIS LYS LEU ARG
SEQRES 4 E 261 GLU SER LEU PRO LEU ILE VAL PHE LEU ARG ASN ARG LEU
SEQRES 5 E 261 LYS TYR ALA LEU ASN GLY ARG GLU VAL LYS ALA ILE LEU
SEQRES 6 E 261 MET GLN ARG HIS VAL LYS VAL ASP GLY LYS VAL ARG THR
SEQRES 7 E 261 ASP THR THR PHE PRO ALA GLY PHE MET ASP VAL ILE THR
SEQRES 8 E 261 LEU GLU ALA THR ASN GLU ASN PHE ARG LEU VAL TYR ASP
SEQRES 9 E 261 VAL LYS GLY ARG PHE ALA VAL HIS ARG ILE THR ASP GLU
SEQRES 10 E 261 GLU ALA SER TYR LYS LEU ALA LYS VAL LYS LYS VAL GLN
SEQRES 11 E 261 LEU GLY LYS LYS GLY ILE PRO TYR VAL VAL THR HIS ASP
SEQRES 12 E 261 GLY ARG THR ILE ARG TYR PRO ASP PRO ASN ILE LYS VAL
SEQRES 13 E 261 ASN ASP THR VAL LYS VAL ASP LEU ALA THR GLY THR ILE
SEQRES 14 E 261 THR ASP PHE ILE LYS PHE ASP THR GLY LYS LEU VAL TYR
SEQRES 15 E 261 VAL THR GLY GLY ARG ASN LEU GLY ARG VAL GLY THR ILE
SEQRES 16 E 261 VAL HIS ARG GLU ARG HIS GLU GLY GLY PHE ASP LEU VAL
SEQRES 17 E 261 HIS ILE LYS ASP SER LEU GLU ASN THR PHE VAL THR ARG
SEQRES 18 E 261 LEU ASN ASN VAL PHE VAL ILE GLY GLU PRO GLY ARG PRO
SEQRES 19 E 261 TRP ILE SER LEU PRO LYS GLY LYS GLY ILE LYS LEU THR
SEQRES 20 E 261 ILE SER GLU GLU ARG ASP ARG ARG ARG ALA GLN HIS GLY
SEQRES 21 E 261 LEU
SEQRES 1 F 227 MET SER GLU HIS GLU ALA GLN VAL GLU VAL GLU VAL GLN
SEQRES 2 F 227 GLU ASP PHE GLU VAL VAL GLN GLU PHE VAL PRO VAL GLU
SEQRES 3 F 227 LEU ALA THR THR ILE PRO VAL GLU ILE GLN GLN ALA GLN
SEQRES 4 F 227 GLN GLU ILE LYS LEU PHE ASN LYS TRP SER PHE GLU ASP
SEQRES 5 F 227 VAL GLU VAL LYS ASP ALA SER LEU VAL ASP TYR ILE GLN
SEQRES 6 F 227 ILE SER LYS PRO ILE TYR VAL ALA HIS THR ALA GLY ARG
SEQRES 7 F 227 TYR ALA ASN LYS ARG PHE ARG LYS ALA GLN CYS PRO ILE
SEQRES 8 F 227 VAL GLU ARG LEU THR ASN SER LEU MET MET ASN GLY ARG
SEQRES 9 F 227 ASN ASN GLY LYS LYS LEU LYS ALA VAL ARG ILE VAL LYS
SEQRES 10 F 227 HIS THR LEU GLU ILE ILE ASN VAL LEU THR ASP GLN ASN
SEQRES 11 F 227 PRO LEU GLN VAL VAL VAL ASP ALA ILE ILE ASN SER GLY
SEQRES 12 F 227 PRO ARG GLU ASP THR THR ARG VAL GLY GLY GLY GLY ALA
SEQRES 13 F 227 ALA ARG ARG GLN ALA VAL ASP VAL SER PRO LEU ARG ARG
SEQRES 14 F 227 VAL ASN GLN SER ILE ALA LEU LEU THR ILE GLY ALA ARG
SEQRES 15 F 227 GLU ALA ALA PHE ARG ASN ILE LYS THR ILE ALA GLU THR
SEQRES 16 F 227 LEU ALA GLU GLU LEU ILE ASN ALA ALA LYS GLY SER SER
SEQRES 17 F 227 THR SER TYR ALA ILE LYS LYS LYS ASP GLU LEU GLU ARG
SEQRES 18 F 227 VAL ALA LYS SER ASN ARG
SEQRES 1 G 236 MET LYS LEU ASN ILE SER TYR PRO ILE ASN GLY THR GLN
SEQRES 2 G 236 LYS CYS ILE GLU ILE ASP ASP GLU HIS ARG VAL ARG VAL
SEQRES 3 G 236 PHE TYR ASP LYS ARG ILE GLY GLN GLU VAL ASP GLY GLU
SEQRES 4 G 236 SER VAL GLY ASP GLU PHE LYS GLY TYR VAL PHE LYS ILE
SEQRES 5 G 236 ALA GLY GLY ASN ASP LYS GLN GLY PHE PRO MET LYS GLN
SEQRES 6 G 236 GLY VAL LEU LEU PRO THR ARG VAL LYS LEU LEU LEU ALA
SEQRES 7 G 236 LYS GLY HIS SER CYS TYR ARG PRO ARG ARG ASN GLY GLU
SEQRES 8 G 236 ARG LYS ARG LYS SER VAL ARG GLY ALA ILE VAL GLY PRO
SEQRES 9 G 236 ASP LEU ALA VAL LEU ALA LEU ILE ILE THR LYS LYS GLY
SEQRES 10 G 236 GLU GLN GLU ILE GLU GLY ILE THR ASN ASP THR VAL PRO
SEQRES 11 G 236 LYS ARG LEU GLY PRO LYS ARG ALA ASN ASN ILE ARG LYS
SEQRES 12 G 236 PHE PHE GLY LEU THR LYS GLU ASP ASP VAL ARG ASP TYR
SEQRES 13 G 236 VAL ILE ARG ARG GLU VAL THR LYS GLY ASP LYS SER TYR
SEQRES 14 G 236 THR LYS ALA PRO LYS ILE GLN ARG LEU VAL THR PRO GLN
SEQRES 15 G 236 ARG LEU GLN ARG LYS ARG GLN GLN LYS SER LEU LYS ILE
SEQRES 16 G 236 LYS ASN ALA GLN ALA GLN ARG GLU ALA ALA ALA GLU TYR
SEQRES 17 G 236 ALA GLN LEU LEU ALA LYS ARG LEU SER GLU ARG LYS ALA
SEQRES 18 G 236 GLU LYS ALA GLU VAL ARG LYS ARG ARG ALA SER SER LEU
SEQRES 19 G 236 LYS ALA
SEQRES 1 H 190 MET SER ASP PRO GLN ALA LYS ILE LEU SER GLN ALA PRO
SEQRES 2 H 190 THR GLU LEU GLU LEU GLN VAL ALA GLN ALA PHE ILE ASP
SEQRES 3 H 190 LEU GLU ASN ASN SER PRO GLU LEU LYS ALA ASP LEU ARG
SEQRES 4 H 190 ALA LEU GLN PHE LYS SER ILE ARG GLU ILE GLU VAL ALA
SEQRES 5 H 190 GLY GLY LYS LYS ALA LEU ALA VAL PHE VAL PRO VAL PRO
SEQRES 6 H 190 SER LEU ALA ALA TYR HIS LYS VAL GLN ILE LYS LEU THR
SEQRES 7 H 190 ARG GLU LEU GLU LYS LYS PHE GLN ASP ARG HIS VAL ILE
SEQRES 8 H 190 PHE LEU ALA GLU ARG ARG ILE LEU PRO LYS PRO SER ARG
SEQRES 9 H 190 LYS SER ARG GLN THR GLN LYS ARG PRO ARG SER ARG THR
SEQRES 10 H 190 LEU THR ALA VAL HIS ASP LYS ILE LEU GLU ASP LEU VAL
SEQRES 11 H 190 PHE PRO THR GLU ILE VAL GLY LYS ARG VAL ARG TYR LEU
SEQRES 12 H 190 VAL GLY GLY ASN LYS ILE GLN LYS ILE LEU LEU ASN SER
SEQRES 13 H 190 LYS ASP VAL GLN HIS ILE ASP ASN LYS LEU GLU SER PHE
SEQRES 14 H 190 GLN ALA VAL TYR ASN LYS LEU THR GLY LYS GLN ILE VAL
SEQRES 15 H 190 PHE GLU ILE PRO SER GLU THR HIS
SEQRES 1 I 201 MET GLY ILE SER ARG ASP SER ARG HIS LYS ARG ALA ALA
SEQRES 2 I 201 THR GLY ALA LYS ARG ALA GLN PHE ARG LYS LYS ARG LYS
SEQRES 3 I 201 PHE GLU LEU GLY ARG GLN ALA ALA ASN THR LYS ILE GLY
SEQRES 4 I 201 THR LYS ARG ILE HIS PRO VAL ARG THR ARG GLY GLY ASN
SEQRES 5 I 201 GLN LYS PHE ARG ALA LEU ARG ILE GLU THR GLY ASN PHE
SEQRES 6 I 201 SER TRP ALA SER GLU GLY VAL ALA ARG LYS THR ARG ILE
SEQRES 7 I 201 THR GLY VAL VAL TYR HIS PRO SER ASN ASN GLU LEU VAL
SEQRES 8 I 201 ARG THR ASN THR LEU THR LYS ALA ALA ILE VAL GLN ILE
SEQRES 9 I 201 ASP ALA THR PRO PHE ARG GLN TRP TYR GLU SER HIS TYR
SEQRES 10 I 201 GLY GLN SER LEU GLY LYS LYS LYS ASN THR LYS ALA GLU
SEQRES 11 I 201 GLU GLU THR ALA THR THR SER LYS ASN THR GLU ARG LYS
SEQRES 12 I 201 TRP ALA ALA ARG ALA ALA GLU ALA LYS ILE GLU HIS ALA
SEQRES 13 I 201 VAL ASP SER GLN PHE GLY ALA GLY ARG LEU TYR ALA ALA
SEQRES 14 I 201 ILE SER SER ARG PRO GLY GLN SER GLY ARG CYS ASP GLY
SEQRES 15 I 201 TYR ILE LEU GLU GLY GLU GLU LEU ALA PHE TYR LEU ARG
SEQRES 16 I 201 ARG LEU THR ALA LYS LYS
SEQRES 1 J 188 MET PRO ARG ALA PRO ARG THR TYR SER LYS THR TYR SER
SEQRES 2 J 188 THR PRO LYS ARG PRO TYR GLU SER ALA ARG LEU ASP ALA
SEQRES 3 J 188 GLU LEU LYS LEU ALA GLY GLU TYR GLY LEU LYS ASN LYS
SEQRES 4 J 188 ARG GLU ILE TYR ARG ILE SER PHE GLN LEU SER LYS ILE
SEQRES 5 J 188 ARG ARG ALA ALA ARG ASP LEU LEU THR ARG ASP GLU LYS
SEQRES 6 J 188 ASP PRO LYS ARG LEU PHE GLU GLY ASN ALA LEU ILE ARG
SEQRES 7 J 188 ARG LEU VAL ARG ILE GLY VAL LEU SER GLU ASP LYS LYS
SEQRES 8 J 188 LYS LEU ASP TYR VAL LEU ALA LEU LYS VAL GLU ASP PHE
SEQRES 9 J 188 LEU GLU ARG ARG LEU GLN THR GLN VAL TYR LYS LEU GLY
SEQRES 10 J 188 LEU ALA LYS SER VAL HIS HIS ALA ARG VAL LEU ILE SER
SEQRES 11 J 188 GLN ARG HIS ILE ALA VAL GLY LYS GLN ILE VAL ASN ILE
SEQRES 12 J 188 PRO SER PHE MET VAL ARG LEU GLU SER GLU LYS HIS ILE
SEQRES 13 J 188 ASP PHE ALA ARG THR SER PRO PHE GLY GLY ALA ARG PRO
SEQRES 14 J 188 GLY ARG VAL ALA ARG LYS ARG ALA ALA ALA ALA GLY GLY
SEQRES 15 J 188 GLU GLU ALA ASP GLU GLU
SEQRES 1 K 106 MET LEU ILE PRO LYS GLU ASP ARG LYS LYS ILE TYR GLN
SEQRES 2 K 106 HIS LEU PHE GLN GLU GLY VAL LEU VAL ALA LYS LYS ASP
SEQRES 3 K 106 PHE ASN GLN PRO LYS HIS GLU GLU ILE ASP THR LYS ASN
SEQRES 4 K 106 LEU PHE VAL ILE LYS ALA LEU GLN SER LEU THR SER LYS
SEQRES 5 K 106 GLY PHE VAL LYS THR GLN PHE SER TRP GLN TYR TYR TYR
SEQRES 6 K 106 TYR THR LEU THR GLU GLU GLY VAL VAL TYR LEU ARG GLU
SEQRES 7 K 106 TYR LEU ASN LEU PRO GLU HIS ILE PHE PRO ALA THR TYR
SEQRES 8 K 106 LEU ALA GLY GLN SER GLY ASP GLN ARG PRO GLN GLY LYS
SEQRES 9 K 106 LYS TYR
SEQRES 1 L 156 MET SER THR GLU LEU THR VAL GLN SER GLU ARG ALA PHE
SEQRES 2 L 156 GLN LYS GLN PRO HIS ILE PHE THR ASN PRO LYS ALA LYS
SEQRES 3 L 156 ALA ASN ARG LYS THR LYS ARG TRP TYR LYS ASN VAL GLY
SEQRES 4 L 156 LEU GLY PHE LYS THR PRO LYS THR ALA ILE GLU GLY SER
SEQRES 5 L 156 TYR ILE ASP LYS LYS CYS PRO PHE THR GLY LEU VAL SER
SEQRES 6 L 156 ILE ARG GLY LYS ILE LEU THR GLY THR VAL VAL SER THR
SEQRES 7 L 156 ARG MET HIS ARG THR ILE VAL ILE ARG ARG ASP TYR LEU
SEQRES 8 L 156 HIS TYR VAL PRO LYS TYR ASN ARG TYR GLU LYS ARG HIS
SEQRES 9 L 156 LYS ASN VAL PRO ALA HIS VAL SER PRO ALA PHE ARG VAL
SEQRES 10 L 156 GLN VAL GLY ASP ILE VAL THR VAL GLY GLN CYS ARG PRO
SEQRES 11 L 156 ILE SER LYS THR VAL ARG PHE ASN VAL LEU LYS VAL ALA
SEQRES 12 L 156 SER ALA THR GLY LYS ALA ASN LYS GLN PHE ALA LYS PHE
SEQRES 1 M 134 MET SER ASP VAL GLU GLU VAL GLN GLN VAL PRO VAL ALA
SEQRES 2 M 134 GLU LEU THR ILE GLU ASP ALA LEU LYS VAL VAL LEU ARG
SEQRES 3 M 134 THR SER LEU VAL HIS ASP GLY LEU ALA ARG GLY LEU ARG
SEQRES 4 M 134 GLU SER ALA LYS ALA LEU THR ARG GLY GLU GLY GLN LEU
SEQRES 5 M 134 ALA VAL LEU VAL GLU SER VAL THR GLU GLU ALA ILE SER
SEQRES 6 M 134 LYS LEU VAL GLN GLY LEU ALA THR GLU ASN ASN VAL PRO
SEQRES 7 M 134 LEU ILE LYS VAL ALA ASP ALA LYS GLN LEU GLY GLU TRP
SEQRES 8 M 134 ALA GLY LEU GLY LYS ILE ASP ARG ASP GLY ASN ALA ARG
SEQRES 9 M 134 LYS VAL VAL GLY ALA SER VAL VAL VAL VAL LYS ASN TRP
SEQRES 10 M 134 GLY ALA ASP THR GLN GLU ARG GLU ILE LEU LEU GLU HIS
SEQRES 11 M 134 PHE SER GLN GLN
SEQRES 1 N 151 MET GLY ARG MET HIS SER LYS GLY LYS GLY MET SER SER
SEQRES 2 N 151 SER ALA ILE PRO TYR SER ARG ASN ALA PRO ALA TRP PHE
SEQRES 3 N 151 LYS GLY SER SER ASP GLY VAL VAL GLU GLN ILE ILE LYS
SEQRES 4 N 151 TYR ALA ARG LYS GLY LEU THR PRO SER GLN ILE GLY VAL
SEQRES 5 N 151 LEU LEU ARG ASP ALA HIS GLY VAL THR GLN ALA LYS VAL
SEQRES 6 N 151 ILE THR GLY ASN LYS ILE LEU ARG ILE LEU LYS SER ASN
SEQRES 7 N 151 GLY LEU ALA PRO GLU ILE PRO GLU ASP LEU TYR PHE LEU
SEQRES 8 N 151 ILE LYS LYS ALA VAL SER VAL ARG LYS HIS LEU GLU ARG
SEQRES 9 N 151 ASN ARG LYS ASP LYS ASP ALA LYS PHE ARG LEU ILE LEU
SEQRES 10 N 151 ILE GLU SER ARG ILE HIS ARG LEU ALA ARG TYR TYR ARG
SEQRES 11 N 151 THR VAL SER VAL LEU PRO PRO ASN TRP LYS TYR GLU SER
SEQRES 12 N 151 ALA THR ALA SER ALA LEU VAL ASN
SEQRES 1 O 137 MET ALA ASN VAL VAL GLN ALA LYS ASP ASN SER GLN VAL
SEQRES 2 O 137 PHE GLY VAL ALA ARG ILE PHE ALA SER PHE ASN ASP THR
SEQRES 3 O 137 PHE VAL HIS VAL THR ASP LEU SER GLY ARG GLU THR ILE
SEQRES 4 O 137 ALA ARG VAL THR GLY GLY MET LYS VAL LYS ALA ASP ARG
SEQRES 5 O 137 ASP GLU SER SER PRO TYR ALA ALA MET LEU ALA ALA GLN
SEQRES 6 O 137 ASP VAL ALA ALA LYS CYS LYS GLU VAL GLY ILE THR ALA
SEQRES 7 O 137 VAL HIS ILE LYS ILE ARG ALA THR GLY GLY THR ARG SER
SEQRES 8 O 137 LYS THR PRO GLY PRO GLY GLY GLN ALA ALA LEU ARG ALA
SEQRES 9 O 137 LEU ALA ARG SER GLY LEU ARG ILE GLY ARG ILE GLU ASP
SEQRES 10 O 137 VAL THR PRO VAL PRO SER ASP SER THR ARG LYS LYS GLY
SEQRES 11 O 137 GLY ARG ARG GLY ARG ARG LEU
SEQRES 1 P 142 MET SER GLU ALA ALA ALA PRO ARG LYS ARG SER PHE LYS
SEQRES 2 P 142 THR TYR SER TYR LYS GLY VAL ASP LEU GLU LYS LEU LEU
SEQRES 3 P 142 GLU MET PRO THR GLU ASP PHE VAL LYS LEU ALA PRO ALA
SEQRES 4 P 142 ARG VAL ARG ARG LYS PHE ALA ARG GLY LEU SER GLU LYS
SEQRES 5 P 142 PRO ALA GLY LEU MET LYS LYS LEU ARG ALA ALA LYS LEU
SEQRES 6 P 142 SER ALA PRO GLU ASN GLU LYS PRO ALA VAL VAL ARG THR
SEQRES 7 P 142 HIS LEU ARG ASN MET ILE ILE VAL PRO GLU MET ILE GLY
SEQRES 8 P 142 SER VAL VAL GLY VAL TYR ASN GLY LYS VAL PHE ASN GLN
SEQRES 9 P 142 VAL GLU ILE ARG PRO GLU MET VAL GLY HIS TYR LEU GLY
SEQRES 10 P 142 GLU PHE SER ILE THR TYR THR PRO VAL ARG HIS GLY ARG
SEQRES 11 P 142 ALA GLY ALA THR THR SER ARG PHE ILE PRO LEU ARG
SEQRES 1 Q 143 MET SER THR VAL PRO SER VAL GLN THR PHE GLY LYS LYS
SEQRES 2 Q 143 LYS SER ALA THR ALA VAL ALA HIS VAL LYS ALA GLY LYS
SEQRES 3 Q 143 GLY LEU ILE LYS VAL ASN GLY SER PRO ILE THR LEU VAL
SEQRES 4 Q 143 GLN PRO GLU ILE LEU ARG PHE LYS VAL TYR GLU PRO LEU
SEQRES 5 Q 143 LEU LEU VAL GLY LEU ASP LYS PHE ALA ASN ILE ASP ILE
SEQRES 6 Q 143 ARG VAL LYS VAL THR GLY GLY GLY HIS VAL SER GLN VAL
SEQRES 7 Q 143 TYR ALA ILE ARG GLN ALA ILE ALA LYS GLY LEU VAL ALA
SEQRES 8 Q 143 TYR HIS GLN LYS PHE VAL ASP GLU GLN SER LYS ASN GLU
SEQRES 9 Q 143 LEU LYS LYS ALA PHE THR SER TYR ASP ARG THR LEU LEU
SEQRES 10 Q 143 ILE ALA ASP SER ARG ARG PRO GLU PRO LYS LYS PHE GLY
SEQRES 11 Q 143 GLY ARG GLY ALA ARG SER ARG PHE GLN LYS SER TYR ARG
SEQRES 1 R 136 MET GLY ARG VAL ARG THR LYS THR VAL LYS ARG ALA SER
SEQRES 2 R 136 LYS ALA LEU ILE GLU LYS TYR TYR PRO LYS LEU THR MET
SEQRES 3 R 136 ASP PHE GLN THR ASN LYS ARG LEU CYS ASP GLU ILE ALA
SEQRES 4 R 136 THR ILE GLN SER LYS ARG LEU ARG ASN LYS ILE ALA GLY
SEQRES 5 R 136 TYR THR THR HIS LEU MET LYS ARG ILE GLN LYS GLY PRO
SEQRES 6 R 136 VAL ARG GLY ILE SER PHE LYS LEU GLN GLU GLU GLU ARG
SEQRES 7 R 136 GLU ARG LYS ASP GLN TYR VAL PRO ASP VAL SER ALA LEU
SEQRES 8 R 136 ASP LEU SER HIS SER ASN ASP VAL LEU ASN VAL ASP THR
SEQRES 9 R 136 GLN THR ALA GLU LEU VAL ASN SER LEU GLY LEU LYS LEU
SEQRES 10 R 136 PRO LEU SER VAL SER SER VAL SER ALA VAL ARG ASP ARG
SEQRES 11 R 136 ARG PHE ARG LYS ARG ASN
SEQRES 1 S 146 MET SER LEU VAL VAL GLN GLU GLN GLY SER PHE GLN HIS
SEQRES 2 S 146 ILE LEU ARG LEU LEU ASN THR ASN VAL ASP GLY ASN ILE
SEQRES 3 S 146 ASN VAL VAL TYR ALA LEU THR THR ILE ARG GLY VAL GLY
SEQRES 4 S 146 ARG ARG TYR ALA ASN LEU VAL CYS LYS LYS ALA ASP VAL
SEQRES 5 S 146 ASP LEU HIS LYS ARG ALA GLY GLU LEU THR GLN GLU GLU
SEQRES 6 S 146 LEU GLU ARG ILE VAL GLN ILE MET GLN ASN PRO THR HIS
SEQRES 7 S 146 TYR LYS ILE PRO ALA TRP PHE LEU ASN ARG GLN LYS ASP
SEQRES 8 S 146 VAL ASN ASP GLY LYS ASP TYR HIS SER LEU ALA ASN ASN
SEQRES 9 S 146 LEU GLU SER LYS LEU ARG ASP ASP LEU GLU ARG LEU LYS
SEQRES 10 S 146 LYS ILE ARG SER HIS ARG GLY ILE ARG HIS PHE TRP GLY
SEQRES 11 S 146 LEU ARG VAL ARG GLY GLN HIS THR LYS THR THR GLY ARG
SEQRES 12 S 146 ARG ARG ALA
SEQRES 1 T 144 MET PRO GLY VAL SER VAL ARG ASP VAL PRO ALA GLN ASP
SEQRES 2 T 144 PHE ILE ASN ASN TYR ALA SER PHE LEU GLN ARG GLN GLY
SEQRES 3 T 144 LYS LEU GLU VAL PRO GLY TYR VAL ASP ILE VAL LYS THR
SEQRES 4 T 144 SER ALA GLY ASN GLU LEU PRO PRO GLN ASP SER GLU GLY
SEQRES 5 T 144 TRP PHE TYR LYS ARG ALA ALA SER VAL ALA ARG HIS ILE
SEQRES 6 T 144 TYR LEU ARG LYS GLN VAL GLY VAL GLY LYS LEU ASN LYS
SEQRES 7 T 144 LEU TYR GLY GLY ALA LYS ASN ARG GLY VAL ARG PRO HIS
SEQRES 8 T 144 LYS HIS VAL ASP ALA SER GLY SER ILE ASN ARG LYS VAL
SEQRES 9 T 144 LEU GLN SER LEU GLU LYS LEU GLY VAL VAL GLU ILE SER
SEQRES 10 T 144 PRO LYS GLY GLY ARG ARG ILE SER ASP ASN GLY LEU ARG
SEQRES 11 T 144 ASP LEU ASP ARG ILE ALA ALA ALA THR LEU GLU ASP GLU
SEQRES 12 T 144 GLU
SEQRES 1 U 117 MET SER GLN VAL GLU LYS LYS SER GLU GLN GLN GLN GLU
SEQRES 2 U 117 VAL VAL ILE HIS LYS ILE ARG ILE ASN LEU THR SER THR
SEQRES 3 U 117 LYS VAL LYS GLN LEU GLU ASN VAL SER ALA ASN ILE ILE
SEQRES 4 U 117 LYS ASN ALA GLU THR PHE LYS LEU VAL LYS LYS GLY PRO
SEQRES 5 U 117 VAL ARG LEU PRO THR LYS VAL LEU LYS ILE SER THR ARG
SEQRES 6 U 117 LYS THR PRO ASN GLY GLU GLY SER LYS THR TRP ASP THR
SEQRES 7 U 117 TYR GLU MET ARG ILE HIS LYS ARG TYR ILE ASP LEU GLU
SEQRES 8 U 117 ALA PRO ALA HIS ILE VAL LYS ARG ILE THR GLN ILE THR
SEQRES 9 U 117 ILE GLU PRO GLY VAL ASP VAL GLU VAL ILE ILE ALA ALA
SEQRES 1 V 87 MET GLU ASN ASP LYS GLY GLN LEU VAL GLU LEU TYR VAL
SEQRES 2 V 87 PRO ARG LYS CYS SER ALA THR ASN ARG ILE ILE LYS ALA
SEQRES 3 V 87 LYS ASP HIS SER SER VAL GLN ILE ASN ILE ALA GLN VAL
SEQRES 4 V 87 ASP GLU GLU GLY ARG ALA ILE PRO GLY GLU TYR VAL THR
SEQRES 5 V 87 TYR ALA LEU SER GLY TYR ILE ARG ALA ARG GLY GLU ALA
SEQRES 6 V 87 ASP ASP SER LEU ASN ARG LEU ALA GLN GLN ASP GLY LEU
SEQRES 7 V 87 LEU LYS ASN VAL TRP SER TYR SER ARG
SEQRES 1 W 130 MET THR ARG THR SER VAL LEU ALA ASP ALA LEU ASN ALA
SEQRES 2 W 130 ILE ASN ASN ALA GLU LYS THR GLY LYS ARG GLN VAL LEU
SEQRES 3 W 130 ILE ARG PRO SER SER LYS VAL ILE ILE LYS PHE LEU GLN
SEQRES 4 W 130 VAL MET GLN LYS HIS GLY TYR ILE GLY GLU PHE GLU TYR
SEQRES 5 W 130 ILE ASP ASP HIS ARG SER GLY LYS ILE VAL VAL GLN LEU
SEQRES 6 W 130 ASN GLY ARG LEU ASN LYS CYS GLY VAL ILE SER PRO ARG
SEQRES 7 W 130 PHE ASN VAL LYS ILE ALA ASP VAL GLU LYS TRP THR ALA
SEQRES 8 W 130 ASN LEU LEU PRO ALA ARG GLN PHE GLY TYR VAL ILE LEU
SEQRES 9 W 130 THR THR SER ALA GLY ILE MET ASP HIS GLU GLU ALA HIS
SEQRES 10 W 130 ARG LYS HIS VAL SER GLY LYS ILE LEU GLY PHE VAL TYR
SEQRES 1 X 145 MET GLY LYS GLY LYS PRO ARG GLY LEU ASN SER ALA ARG
SEQRES 2 X 145 LYS LEU ARG VAL HIS ARG ARG ASN ASN ARG TRP ALA GLU
SEQRES 3 X 145 THR THR TYR LYS LYS ARG LEU LEU GLY THR ALA PHE LYS
SEQRES 4 X 145 SER SER PRO PHE GLY GLY SER SER HIS ALA LYS GLY ILE
SEQRES 5 X 145 VAL LEU GLU LYS ILE GLY ILE GLU SER LYS GLN PRO ASN
SEQRES 6 X 145 SER ALA ILE ARG LYS CYS VAL ARG VAL GLN LEU ILE LYS
SEQRES 7 X 145 ASN GLY LYS LYS VAL THR ALA PHE VAL PRO ASN ASP GLY
SEQRES 8 X 145 CYS LEU ASN PHE VAL ASP GLU ASN ASP GLU VAL LEU LEU
SEQRES 9 X 145 ALA GLY PHE GLY ARG LYS GLY LYS ALA LYS GLY ASP ILE
SEQRES 10 X 145 PRO GLY VAL ARG PHE LYS VAL VAL LYS VAL SER GLY VAL
SEQRES 11 X 145 SER LEU LEU ALA LEU TRP LYS GLU LYS LYS GLU LYS PRO
SEQRES 12 X 145 ARG SER
SEQRES 1 Y 135 MET SER ASP ALA ILE THR ILE ARG THR ARG LYS VAL ILE
SEQRES 2 Y 135 SER ASN PRO LEU LEU ALA ARG LYS GLN PHE VAL VAL ASP
SEQRES 3 Y 135 VAL LEU HIS PRO ASN ARG ALA ASN VAL SER LYS ASP GLU
SEQRES 4 Y 135 LEU ARG GLU LYS LEU ALA GLU ALA TYR LYS ALA GLU LYS
SEQRES 5 Y 135 ASP ALA VAL SER VAL PHE GLY PHE ARG THR GLN TYR GLY
SEQRES 6 Y 135 GLY GLY LYS SER THR GLY PHE GLY LEU VAL TYR ASN SER
SEQRES 7 Y 135 VAL ALA ASP ALA LYS LYS PHE GLU PRO ALA TYR ARG LEU
SEQRES 8 Y 135 VAL ARG TYR GLY LEU ALA GLU LYS VAL GLU LYS ALA SER
SEQRES 9 Y 135 ARG GLN GLN ARG LYS GLN ARG LYS ASN ARG GLY LYS LYS
SEQRES 10 Y 135 ILE PHE GLY THR GLY LYS SER ILE ALA LYS LYS ALA ALA
SEQRES 11 Y 135 ARG ARG ASN ALA ASP
SEQRES 1 Z 108 MET PRO PRO LYS GLN GLN LEU SER LYS ALA ALA LYS ALA
SEQRES 2 Z 108 ALA ALA ALA MET ALA GLY GLY LYS LYS SER LYS LYS LYS
SEQRES 3 Z 108 TRP SER LYS LYS SER HIS LYS ASP LYS ALA LYS HIS ALA
SEQRES 4 Z 108 VAL VAL LEU ASP GLN ASP LYS PHE ASP ARG ILE MET LYS
SEQRES 5 Z 108 GLU ALA PRO THR TYR ARG TYR VAL SER VAL SER VAL LEU
SEQRES 6 Z 108 VAL ASP ARG PHE LYS LEU GLY GLY SER LEU ALA ARG VAL
SEQRES 7 Z 108 ALA LEU ARG HIS LEU GLU ASN GLU GLY ILE ILE LYS PRO
SEQRES 8 Z 108 VAL SER LYS HIS SER LYS GLN ALA ILE TYR THR ARG ALA
SEQRES 9 Z 108 THR ALA SER GLU
SEQRES 1 a 119 MET PRO LYS LYS ARG ALA SER ASN GLY ARG ASN LYS LYS
SEQRES 2 a 119 GLY ARG GLY HIS VAL LYS PRO VAL ARG CYS VAL ASN CYS
SEQRES 3 a 119 SER ARG SER VAL PRO LYS ASP LYS ALA ILE LYS ARG MET
SEQRES 4 a 119 ALA ILE ARG ASN ILE VAL GLU ALA ALA ALA ILE ARG ASP
SEQRES 5 a 119 LEU SER GLU ALA SER VAL TYR ALA GLU TYR ALA LEU PRO
SEQRES 6 a 119 LYS THR TYR ASN LYS LEU HIS TYR CYS ILE SER CYS ALA
SEQRES 7 a 119 ILE HIS ALA ARG ILE VAL ARG VAL ARG SER ARG THR ASP
SEQRES 8 a 119 ARG ARG ILE ARG ALA PRO PRO GLN ARG PRO ARG PHE ASN
SEQRES 9 a 119 ARG ASP ASN LYS VAL SER PRO ALA ASP ALA ALA LYS LYS
SEQRES 10 a 119 ALA LEU
SEQRES 1 b 82 MET VAL LEU VAL GLN ASP LEU LEU HIS PRO THR ALA ALA
SEQRES 2 b 82 SER GLU ALA ARG LYS HIS LYS LEU LYS THR LEU VAL GLN
SEQRES 3 b 82 SER PRO ARG SER HIS PHE LEU ASP VAL LYS CYS PRO GLY
SEQRES 4 b 82 CYS LEU ASN ILE THR THR VAL PHE SER HIS ALA GLN THR
SEQRES 5 b 82 ALA VAL THR CYS GLU SER CYS SER THR VAL LEU CYS THR
SEQRES 6 b 82 PRO THR GLY GLY LYS ALA LYS LEU SER GLU GLY THR SER
SEQRES 7 b 82 PHE ARG ARG LYS
SEQRES 1 c 67 MET ASP THR LYS THR PRO VAL THR LEU ALA LYS VAL ILE
SEQRES 2 c 67 LYS VAL LEU GLY ARG THR GLY SER ARG GLY GLY VAL THR
SEQRES 3 c 67 GLN VAL ARG VAL GLU PHE LEU GLU ASP THR THR ARG THR
SEQRES 4 c 67 ILE VAL ARG ASN VAL LYS GLY PRO VAL ARG GLU GLY ASP
SEQRES 5 c 67 ILE LEU VAL LEU MET GLU SER GLU ARG GLU ALA ARG ARG
SEQRES 6 c 67 LEU ARG
SEQRES 1 d 56 MET ALA HIS GLU ASN VAL TRP TYR SER HIS PRO ARG LYS
SEQRES 2 d 56 PHE GLY LYS GLY SER ARG GLN CYS ARG ILE SER GLY SER
SEQRES 3 d 56 HIS SER GLY LEU ILE ARG LYS TYR GLY LEU ASN ILE ASP
SEQRES 4 d 56 ARG GLN SER PHE ARG GLU LYS ALA ASN ASP ILE GLY PHE
SEQRES 5 d 56 TYR LYS TYR ARG
SEQRES 1 e 63 MET GLY LYS VAL HIS GLY SER LEU ALA ARG ALA GLY LYS
SEQRES 2 e 63 VAL LYS SER GLN THR PRO LYS VAL GLU LYS GLN GLU LYS
SEQRES 3 e 63 PRO LYS GLN PRO LYS GLY ARG ALA TYR LYS ARG LEU LEU
SEQRES 4 e 63 TYR THR ARG ARG PHE VAL ASN VAL THR LEU THR ASN GLY
SEQRES 5 e 63 LYS ARG LYS MET ASN PRO SER PRO SER SER GLN
SEQRES 1 f 150 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 f 150 THR LEU GLU VAL GLU SER SER ASP THR ILE ASP ASN VAL
SEQRES 3 f 150 LYS SER LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 f 150 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 f 150 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 f 150 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY GLY LYS
SEQRES 7 f 150 LYS ARG LYS LYS LYS VAL TYR THR THR PRO LYS LYS ILE
SEQRES 8 f 150 ARG HIS LYS HIS LYS LYS VAL LYS LEU ALA VAL LEU ASN
SEQRES 9 f 150 TYR TYR LYS VAL ASP ASP GLU GLY LYS VAL ALA LYS LEU
SEQRES 10 f 150 ARG LYS GLU CYS PRO ASN CYS GLY PRO GLY ILE PHE LEU
SEQRES 11 f 150 ALA ASN HIS GLY ASP ARG PHE TYR CYS GLY LYS CYS HIS
SEQRES 12 f 150 SER THR PHE ALA THR GLN LYS
SEQRES 1 g 326 MET SER SER SER ASN ILE MET LEU VAL LEU ARG GLY THR
SEQRES 2 g 326 LEU GLU GLY HIS ASN GLY TRP VAL THR SER LEU SER THR
SEQRES 3 g 326 SER ALA ALA GLN PRO ASN LEU LEU VAL SER GLY SER ARG
SEQRES 4 g 326 ASP LYS THR LEU ILE SER TRP ARG LEU THR GLU ASN GLU
SEQRES 5 g 326 GLN GLN PHE GLY VAL PRO VAL ARG SER TYR LYS GLY HIS
SEQRES 6 g 326 SER HIS ILE VAL GLN ASP VAL VAL VAL SER ALA ASP GLY
SEQRES 7 g 326 ASN TYR ALA VAL SER ALA SER TRP ASP LYS THR LEU ARG
SEQRES 8 g 326 LEU TRP ASN LEU ALA THR GLY ASN SER GLU ALA ARG PHE
SEQRES 9 g 326 VAL GLY HIS THR GLY ASP VAL LEU SER VAL ALA ILE ASP
SEQRES 10 g 326 ALA ASN SER SER LYS ILE ILE SER ALA SER ARG ASP LYS
SEQRES 11 g 326 THR ILE ARG VAL TRP ASN THR VAL GLY ASP CYS ALA TYR
SEQRES 12 g 326 VAL LEU LEU GLY HIS THR ASP TRP VAL THR LYS VAL ARG
SEQRES 13 g 326 VAL ALA PRO LYS ASN LEU GLU ASP GLY GLU VAL ASP ASP
SEQRES 14 g 326 GLY ARG ILE THR PHE VAL SER ALA GLY MET ASP LYS ILE
SEQRES 15 g 326 VAL ARG SER TRP SER LEU ASN GLU ASP SER TYR ARG ILE
SEQRES 16 g 326 GLU ALA ASP PHE ILE GLY HIS ASN ASN TYR ILE ASN VAL
SEQRES 17 g 326 VAL GLN PRO SER PRO ASP GLY SER LEU ALA ALA SER ALA
SEQRES 18 g 326 GLY LYS ASP GLY GLN ILE TYR VAL TRP ASN LEU LYS HIS
SEQRES 19 g 326 LYS SER ALA PHE MET ASN PHE ASP ALA LYS ASP GLU VAL
SEQRES 20 g 326 PHE ALA LEU ALA PHE SER PRO SER ARG PHE TRP LEU THR
SEQRES 21 g 326 ALA ALA THR ALA SER GLY ILE LYS ILE TYR ASP LEU GLU
SEQRES 22 g 326 ASN GLU VAL LEU ILE ASP GLU LEU LYS PRO GLU PHE ALA
SEQRES 23 g 326 GLY TYR THR LYS ALA GLN ASP PRO HIS ALA VAL SER LEU
SEQRES 24 g 326 ALA TRP SER ALA ASP GLY GLN THR LEU PHE ALA GLY TYR
SEQRES 25 g 326 THR ASP ASN VAL ILE ARG VAL TRP GLN VAL MET THR ALA
SEQRES 26 g 326 ASN
SEQRES 1 h 25 MET ARG ALA LYS TRP ARG LYS LYS ARG THR ARG ARG LEU
SEQRES 2 h 25 LYS ARG LYS ARG ARG LYS VAL ARG ALA ARG SER LYS
SEQRES 1 i 153 MET GLY LYS LYS ASN THR LYS GLY GLY LYS LYS GLY ARG
SEQRES 2 i 153 ARG GLY LYS ASN ASP SER ASP GLY PRO LYS ARG GLU LEU
SEQRES 3 i 153 ILE TYR LYS GLU GLU GLY GLN GLU TYR ALA GLN ILE THR
SEQRES 4 i 153 LYS MET LEU GLY ASN GLY ARG VAL GLU ALA SER CYS PHE
SEQRES 5 i 153 ASP GLY ASN LYS ARG MET ALA HIS ILE ARG GLY LYS LEU
SEQRES 6 i 153 ARG LYS LYS VAL TRP MET GLY GLN GLY ASP ILE ILE LEU
SEQRES 7 i 153 VAL SER LEU ARG ASP PHE GLN ASP ASP GLN CYS ASP VAL
SEQRES 8 i 153 VAL HIS LYS TYR ASN LEU ASP GLU ALA ARG THR LEU LYS
SEQRES 9 i 153 ASN GLN GLY GLU LEU PRO GLU ASN ALA LYS ILE ASN GLU
SEQRES 10 i 153 THR ASP ASN PHE GLY PHE GLU SER ASP GLU ASP VAL ASN
SEQRES 11 i 153 PHE GLU PHE GLY ASN ALA ASP GLU ASP ASP GLU GLU GLY
SEQRES 12 i 153 GLU ASP GLU GLU LEU ASP ILE ASP ASP ILE
SEQRES 1 j 108 MET SER ILE GLU ASN LEU LYS SER PHE ASP PRO PHE ALA
SEQRES 2 j 108 ASP THR GLY ASP ASP GLU THR ALA THR SER ASN TYR ILE
SEQRES 3 j 108 HIS ILE ARG ILE GLN GLN ARG ASN GLY ARG LYS THR LEU
SEQRES 4 j 108 THR THR VAL GLN GLY VAL PRO GLU GLU TYR ASP LEU LYS
SEQRES 5 j 108 ARG ILE LEU LYS VAL LEU LYS LYS ASP PHE ALA CYS ASN
SEQRES 6 j 108 GLY ASN ILE VAL LYS ASP PRO GLU MET GLY GLU ILE ILE
SEQRES 7 j 108 GLN LEU GLN GLY ASP GLN ARG ALA LYS VAL CYS GLU PHE
SEQRES 8 j 108 MET ILE SER GLN LEU GLY LEU GLN LYS LYS ASN ILE LYS
SEQRES 9 j 108 ILE HIS GLY PHE
HET MG 21801 1
HET MG 21802 1
HET MG 21803 1
HET MG 21804 1
HET MG 21805 1
HET MG 21806 1
HET MG 21807 1
HET MG 21808 1
HET MG 21809 1
HET MG 21810 1
HET MG 21811 1
HET MG 21812 1
HET MG 21813 1
HET MG 21814 1
HET MG 21815 1
HET MG 21816 1
HET MG 21817 1
HET MG 21818 1
HET MG 21819 1
HET MG 21820 1
HET MG 21821 1
HET MG 21822 1
HET MG 21823 1
HET MG 21824 1
HET MG 21825 1
HET MG 21826 1
HET MG 21827 1
HET MG 21828 1
HET MG 21829 1
HET MG 21830 1
HET MG 21831 1
HET MG 21832 1
HET MG 21833 1
HET MG 21834 1
HET MG 21835 1
HET MG 21836 1
HET MG 21837 1
HET MG 21838 1
HET MG 21839 1
HET MG 21840 1
HET MG 21841 1
HET MG 21842 1
HET MG 21843 1
HET MG 21844 1
HET MG 21845 1
HET MG 21846 1
HET MG 21847 1
HET MG 21848 1
HET MG 21849 1
HET MG 21850 1
HET MG 21851 1
HET MG 21852 1
HET MG 21853 1
HET MG 21854 1
HET MG 21855 1
HET MG 21856 1
HET MG 21857 1
HET MG 21858 1
HET MG 21859 1
HET MG 21860 1
HET MG 21861 1
HET MG 21862 1
HET MG 21863 1
HET MG 21864 1
HET MG 21865 1
HET MG 21866 1
HET MG 21867 1
HET MG 21868 1
HET MG 21869 1
HET MG 21870 1
HET MG 21871 1
HET MG 21872 1
HET MG 21873 1
HET MG 21874 1
HET MG 21875 1
HET MG 21876 1
HET MG 21877 1
HET MG 21878 1
HET MG J 201 1
HET ZN a 500 1
HET ZN b 101 1
HET MG f 201 1
HET ZN f 202 1
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
FORMUL 38 MG 80(MG 2+)
FORMUL 17 ZN 3(ZN 2+)
HELIX 1 1 THR A 10 ARG A 21 1 12
HELIX 2 2 ASN A 49 ILE A 67 1 19
HELIX 3 3 ASN A 69 GLU A 71 5 3
HELIX 4 4 ARG A 79 THR A 93 1 15
HELIX 5 5 ASP A 129 TYR A 138 1 10
HELIX 6 6 LYS A 167 GLY A 186 1 20
HELIX 7 7 ASP B 22 THR B 25 5 4
HELIX 8 8 LEU B 70 GLY B 75 1 6
HELIX 9 9 SER B 76 SER B 80 5 5
HELIX 10 10 THR B 106 VAL B 114 1 9
HELIX 11 11 GLN B 157 VAL B 176 1 20
HELIX 12 12 THR B 180 ILE B 189 1 10
HELIX 13 13 GLU B 191 LYS B 202 1 12
HELIX 14 14 ASP B 224 SER B 230 1 7
HELIX 15 15 THR C 44 GLY C 53 1 10
HELIX 16 16 SER C 57 HIS C 64 1 8
HELIX 17 17 GLU C 70 LEU C 78 1 9
HELIX 18 18 GLU C 125 VAL C 141 1 17
HELIX 19 19 SER C 186 GLY C 197 1 12
HELIX 20 20 THR C 211 THR C 226 1 16
HELIX 21 21 THR C 231 TRP C 235 5 5
HELIX 22 22 SER C 243 TYR C 248 1 6
HELIX 23 23 SER D 6 LEU D 29 1 24
HELIX 24 24 LYS D 54 GLY D 60 1 7
HELIX 25 25 ARG D 64 LYS D 78 1 15
HELIX 26 26 SER D 97 GLY D 112 1 16
HELIX 27 27 ALA D 114 GLY D 130 1 17
HELIX 28 28 GLN D 162 PHE D 167 1 6
HELIX 29 29 PRO E 15 MET E 19 5 5
HELIX 30 30 LYS E 37 SER E 41 5 5
HELIX 31 31 PRO E 43 ARG E 51 1 9
HELIX 32 32 ASN E 57 GLN E 67 1 11
HELIX 33 33 THR E 115 SER E 120 1 6
HELIX 34 34 LYS E 133 GLY E 135 5 3
HELIX 35 35 THR E 247 GLN E 258 1 12
HELIX 36 36 PRO F 32 ALA F 38 1 7
HELIX 37 37 PRO F 90 MET F 100 1 11
HELIX 38 38 LYS F 108 LEU F 126 1 19
HELIX 39 39 ASN F 130 ASN F 141 1 12
HELIX 40 40 SER F 165 PHE F 186 1 22
HELIX 41 41 THR F 191 LYS F 205 1 15
HELIX 42 42 SER F 210 ARG F 227 1 18
HELIX 43 43 ASP G 20 ARG G 25 1 6
HELIX 44 44 VAL G 26 TYR G 28 5 3
HELIX 45 45 ARG G 137 GLY G 146 1 10
HELIX 46 46 VAL G 153 VAL G 157 5 5
HELIX 47 47 THR G 180 LYS G 223 1 44
HELIX 48 48 GLU H 15 LEU H 27 1 13
HELIX 49 49 GLU H 28 LYS H 35 5 8
HELIX 50 50 SER H 66 GLN H 74 1 9
HELIX 51 51 GLN H 74 PHE H 85 1 12
HELIX 52 52 THR H 117 VAL H 130 1 14
HELIX 53 53 ASP H 158 ASP H 163 1 6
HELIX 54 54 LYS H 165 THR H 177 1 13
HELIX 55 55 ASN I 87 ASN I 94 1 8
HELIX 56 56 ALA I 106 TYR I 117 1 12
HELIX 57 57 SER I 137 ARG I 147 1 11
HELIX 58 58 GLU I 154 GLY I 164 1 11
HELIX 59 59 ARG I 173 GLY I 178 1 6
HELIX 60 60 GLU I 186 LYS I 201 1 16
HELIX 61 61 GLU J 20 GLY J 35 1 16
HELIX 62 62 ASN J 38 ARG J 62 1 25
HELIX 63 63 ASP J 66 GLY J 84 1 19
HELIX 64 64 SER J 87 LYS J 91 5 5
HELIX 65 65 ASP J 94 LYS J 100 5 7
HELIX 66 66 VAL J 101 GLU J 106 1 6
HELIX 67 67 ARG J 108 LEU J 116 1 9
HELIX 68 68 SER J 121 GLN J 131 1 11
HELIX 69 69 ARG J 171 GLY J 182 1 12
HELIX 70 70 PRO K 4 GLY K 19 1 16
HELIX 71 71 LYS K 38 LYS K 52 1 15
HELIX 72 72 THR K 69 ASN K 81 1 13
HELIX 73 73 PRO L 45 GLY L 51 1 7
HELIX 74 74 GLU M 18 ASP M 32 1 15
HELIX 75 75 GLY M 37 ARG M 47 1 11
HELIX 76 76 GLU M 62 ASN M 75 1 14
HELIX 77 77 ALA M 85 GLY M 93 1 9
HELIX 78 78 GLU M 125 GLN M 133 1 9
HELIX 79 79 SER N 29 GLY N 44 1 16
HELIX 80 80 THR N 46 HIS N 58 1 13
HELIX 81 81 GLN N 62 THR N 67 1 6
HELIX 82 82 LYS N 70 GLY N 79 1 10
HELIX 83 83 PRO N 85 ASN N 105 1 21
HELIX 84 84 ASP N 108 SER N 133 1 26
HELIX 85 85 SER N 143 ASN N 151 1 9
HELIX 86 86 THR O 43 VAL O 48 1 6
HELIX 87 87 ASP O 51 SER O 55 5 5
HELIX 88 88 SER O 56 GLY O 75 1 20
HELIX 89 89 GLY O 98 ARG O 107 1 10
HELIX 90 90 ASP P 21 LEU P 26 1 6
HELIX 91 91 MET P 28 ALA P 37 1 10
HELIX 92 92 PRO P 38 ARG P 47 1 10
HELIX 93 93 PRO P 53 SER P 66 1 14
HELIX 94 94 LEU P 116 ILE P 121 1 6
HELIX 95 95 LEU Q 44 LEU Q 54 1 11
HELIX 96 96 GLY Q 56 PHE Q 60 5 5
HELIX 97 97 HIS Q 74 VAL Q 97 1 24
HELIX 98 98 ASP Q 98 TYR Q 112 1 15
HELIX 99 99 THR R 6 TYR R 21 1 16
HELIX 100 100 ASP R 27 ALA R 39 1 13
HELIX 101 101 SER R 43 GLN R 62 1 20
HELIX 102 102 PHE R 71 GLN R 83 1 13
HELIX 103 103 ASP R 103 GLY R 114 1 12
HELIX 104 104 ALA S 31 ILE S 35 5 5
HELIX 105 105 ARG S 40 ASP S 51 1 12
HELIX 106 106 THR S 62 ASN S 75 1 14
HELIX 107 107 ASN S 104 ARG S 120 1 17
HELIX 108 108 SER S 121 GLY S 130 1 10
HELIX 109 109 SER T 5 VAL T 9 5 5
HELIX 110 110 PRO T 10 GLY T 26 1 17
HELIX 111 111 TRP T 53 ARG T 68 1 16
HELIX 112 112 GLY T 72 GLY T 81 1 10
HELIX 113 113 SER T 97 GLY T 112 1 16
HELIX 114 114 SER T 125 GLU T 144 1 20
HELIX 115 115 LYS U 30 LYS U 49 1 20
HELIX 116 116 PRO U 96 ILE U 106 1 11
HELIX 117 117 SER V 56 GLY V 63 1 8
HELIX 118 118 GLU V 64 GLN V 74 1 11
HELIX 119 119 SER W 5 THR W 20 1 16
HELIX 120 120 SER W 31 GLY W 45 1 15
HELIX 121 121 LYS W 82 ALA W 84 5 3
HELIX 122 122 ASP W 85 LEU W 94 1 10
HELIX 123 123 HIS W 113 HIS W 120 1 8
HELIX 124 124 ALA X 12 TRP X 24 1 13
HELIX 125 125 GLU X 26 GLY X 35 1 10
HELIX 126 126 GLY X 35 SER X 40 1 6
HELIX 127 127 CYS X 92 VAL X 96 5 5
HELIX 128 128 LEU X 132 LYS X 137 1 6
HELIX 129 129 SER Y 36 LYS Y 49 1 14
HELIX 130 130 GLU Y 51 ASP Y 53 5 3
HELIX 131 131 SER Y 78 GLU Y 86 1 9
HELIX 132 132 PRO Y 87 GLY Y 95 1 9
HELIX 133 133 SER Y 104 LYS Y 117 1 14
HELIX 134 134 GLY Y 122 ASP Y 135 1 14
HELIX 135 135 GLN Z 44 LYS Z 52 1 9
HELIX 136 136 SER Z 61 ARG Z 68 1 8
HELIX 137 137 LEU Z 75 ASN Z 85 1 11
HELIX 138 138 ALA a 49 SER a 57 1 9
HELIX 139 139 CYS a 74 ALA a 81 1 8
HELIX 140 140 THR b 11 LYS b 18 1 8
HELIX 141 141 ARG d 32 LEU d 36 5 5
HELIX 142 142 ARG d 40 LYS d 46 1 7
HELIX 143 143 LYS d 46 GLY d 51 1 6
HELIX 144 144 GLY e 12 THR e 18 1 7
HELIX 145 145 GLY e 32 PHE e 44 1 13
HELIX 146 146 ARG h 2 LYS h 25 1 24
HELIX 147 147 GLY i 63 ARG i 66 5 4
HELIX 148 148 LEU i 97 GLY i 107 1 11
HELIX 149 149 ASP j 50 ALA j 63 1 14
HELIX 150 150 ARG j 85 GLN j 95 1 11
SHEET 1 A 2 VAL A 37 ALA A 40 0
SHEET 2 A 2 ASN A 46 ILE A 48 -1 O VAL A 47 N TYR A 38
SHEET 1 B 4 THR A 96 ALA A 99 0
SHEET 2 B 4 VAL A 73 SER A 77 1 N VAL A 73 O THR A 96
SHEET 3 B 4 LEU A 120 VAL A 123 1 O ILE A 122 N ILE A 76
SHEET 4 B 4 VAL A 143 ALA A 145 1 O ILE A 144 N VAL A 121
SHEET 1 C 6 ASN B 42 ASN B 49 0
SHEET 2 C 6 LYS B 27 LYS B 33 -1 N GLU B 28 O VAL B 48
SHEET 3 C 6 ASN B 95 PHE B 105 1 O LEU B 96 N LYS B 33
SHEET 4 C 6 VAL B 215 LYS B 219 -1 O VAL B 215 N MET B 103
SHEET 5 C 6 VAL B 134 PHE B 142 -1 N ARG B 136 O LYS B 216
SHEET 6 C 6 LEU B 120 LYS B 128 -1 N ILE B 121 O ALA B 141
SHEET 1 D 6 VAL B 65 CYS B 69 0
SHEET 2 D 6 ARG B 82 VAL B 91 -1 O VAL B 84 N VAL B 68
SHEET 3 D 6 ASN B 95 PHE B 105 -1 O GLY B 102 N LYS B 85
SHEET 4 D 6 VAL B 215 LYS B 219 -1 O VAL B 215 N MET B 103
SHEET 5 D 6 VAL B 134 PHE B 142 -1 N ARG B 136 O LYS B 216
SHEET 6 D 6 GLN B 208 HIS B 211 -1 O HIS B 211 N ILE B 140
SHEET 1 E 4 LYS C 82 GLN C 94 0
SHEET 2 E 4 GLN C 99 GLY C 110 -1 O VAL C 108 N GLU C 84
SHEET 3 E 4 HIS C 115 ALA C 123 -1 O LYS C 121 N ALA C 105
SHEET 4 E 4 ILE C 142 PRO C 143 -1 O ILE C 142 N VAL C 116
SHEET 1 F 2 ARG C 146 GLY C 147 0
SHEET 2 F 2 SER C 158 LEU C 159 -1 O SER C 158 N GLY C 147
SHEET 1 G 4 THR C 163 CYS C 167 0
SHEET 2 G 4 VAL C 170 PRO C 176 -1 O LEU C 174 N THR C 163
SHEET 3 G 4 VAL C 201 THR C 206 -1 O TYR C 202 N ILE C 175
SHEET 4 G 4 ILE C 183 VAL C 184 1 N VAL C 184 O VAL C 201
SHEET 1 H 3 TYR D 34 VAL D 41 0
SHEET 2 H 3 THR D 46 ALA D 52 -1 O ARG D 51 N SER D 35
SHEET 3 H 3 ILE D 84 GLU D 89 1 O TYR D 87 N ILE D 50
SHEET 1 I 4 MET D 150 GLY D 155 0
SHEET 2 I 4 GLY D 133 SER D 139 -1 N VAL D 136 O PHE D 152
SHEET 3 I 4 GLY D 180 MET D 189 -1 O LYS D 185 N VAL D 137
SHEET 4 I 4 ILE D 168 LEU D 177 -1 N VAL D 175 O LEU D 182
SHEET 1 J 5 LYS D 223 ASP D 224 0
SHEET 2 J 5 ILE g 195 ILE g 200 -1 O ASP g 198 N LYS D 223
SHEET 3 J 5 ILE g 182 LEU g 188 -1 N SER g 185 O ALA g 197
SHEET 4 J 5 ILE g 172 GLY g 178 -1 N PHE g 174 O TRP g 186
SHEET 5 J 5 VAL g 152 VAL g 157 -1 N LYS g 154 O ALA g 177
SHEET 1 K 4 VAL E 70 VAL E 72 0
SHEET 2 K 4 VAL E 89 LEU E 92 -1 O THR E 91 N LYS E 71
SHEET 3 K 4 ASN E 98 ARG E 100 -1 O PHE E 99 N ILE E 90
SHEET 4 K 4 ARG E 113 ILE E 114 -1 O ILE E 114 N ASN E 98
SHEET 1 L 2 VAL E 102 TYR E 103 0
SHEET 2 L 2 PHE E 109 ALA E 110 -1 O ALA E 110 N VAL E 102
SHEET 1 M 5 THR E 146 ARG E 148 0
SHEET 2 M 5 PRO E 137 THR E 141 -1 N VAL E 139 O ILE E 147
SHEET 3 M 5 LYS E 122 LEU E 131 -1 N GLN E 130 O TYR E 138
SHEET 4 M 5 THR E 159 VAL E 162 -1 O VAL E 162 N LYS E 122
SHEET 5 M 5 ILE E 169 ILE E 173 -1 O THR E 170 N LYS E 161
SHEET 1 N 4 VAL E 192 GLY E 193 0
SHEET 2 N 4 LEU E 180 VAL E 183 -1 N VAL E 181 O GLY E 193
SHEET 3 N 4 VAL E 225 GLU E 230 -1 O PHE E 226 N TYR E 182
SHEET 4 N 4 ARG E 233 PRO E 234 -1 O ARG E 233 N GLU E 230
SHEET 1 O 3 HIS E 197 ARG E 198 0
SHEET 2 O 3 LEU E 207 ILE E 210 -1 O HIS E 209 N HIS E 197
SHEET 3 O 3 PHE E 218 ARG E 221 -1 O PHE E 218 N ILE E 210
SHEET 1 P 6 GLU F 146 THR F 149 0
SHEET 2 P 6 GLN F 160 VAL F 164 -1 O VAL F 162 N ASP F 147
SHEET 3 P 6 VAL c 41 LYS c 45 1 O LYS c 45 N ASP F 163
SHEET 4 P 6 VAL c 25 PHE c 32 -1 N THR c 26 O VAL c 44
SHEET 5 P 6 THR c 8 THR c 19 -1 N LYS c 14 O ARG c 29
SHEET 6 P 6 ILE c 53 LEU c 56 -1 O LEU c 54 N ALA c 10
SHEET 1 Q 5 THR G 12 GLU G 17 0
SHEET 2 Q 5 LYS G 2 TYR G 7 -1 N ILE G 5 O LYS G 14
SHEET 3 Q 5 LEU G 106 LYS G 115 1 O ALA G 107 N LYS G 2
SHEET 4 Q 5 VAL G 49 ASP G 57 -1 N ALA G 53 O ALA G 110
SHEET 5 Q 5 GLN G 34 ASP G 37 -1 N VAL G 36 O PHE G 50
SHEET 1 R 2 VAL G 73 LEU G 77 0
SHEET 2 R 2 LYS G 93 VAL G 97 -1 O LYS G 93 N LEU G 77
SHEET 1 S 2 ARG G 160 THR G 163 0
SHEET 2 S 2 SER G 168 LYS G 171 -1 O TYR G 169 N VAL G 162
SHEET 1 T 3 ILE H 46 GLU H 50 0
SHEET 2 T 3 LYS H 56 VAL H 60 -1 O ALA H 59 N ARG H 47
SHEET 3 T 3 VAL H 90 ILE H 91 1 O ILE H 91 N VAL H 60
SHEET 1 U 6 GLN H 180 GLU H 184 0
SHEET 2 U 6 LYS H 148 LEU H 154 1 N ILE H 152 O VAL H 182
SHEET 3 U 6 ILE H 135 TYR H 142 -1 N ARG H 139 O LYS H 151
SHEET 4 U 6 PHE W 50 ILE W 53 -1 O PHE W 50 N TYR H 142
SHEET 5 U 6 LYS W 60 GLN W 64 -1 O VAL W 62 N GLU W 51
SHEET 6 U 6 GLN W 24 ILE W 27 -1 N ILE W 27 O ILE W 61
SHEET 1 V 2 HIS I 44 THR I 48 0
SHEET 2 V 2 GLY I 51 ARG I 56 -1 O LYS I 54 N VAL I 46
SHEET 1 W 6 THR I 62 TRP I 67 0
SHEET 2 W 6 VAL I 72 TYR I 83 -1 O VAL I 72 N TRP I 67
SHEET 3 W 6 ILE I 101 ILE I 104 -1 O GLN I 103 N THR I 79
SHEET 4 W 6 LEU I 166 ILE I 170 -1 O ALA I 168 N VAL I 102
SHEET 5 W 6 ASP I 181 ILE I 184 -1 O TYR I 183 N ALA I 169
SHEET 6 W 6 THR I 62 TRP I 67 1 N SER I 66 O ILE I 184
SHEET 1 X 3 VAL K 20 LYS K 24 0
SHEET 2 X 3 TYR K 63 LEU K 68 -1 O TYR K 66 N LEU K 21
SHEET 3 X 3 VAL K 55 GLN K 58 -1 N LYS K 56 O THR K 67
SHEET 1 Y 6 ILE L 70 SER L 77 0
SHEET 2 Y 6 THR L 83 ARG L 87 -1 O VAL L 85 N VAL L 76
SHEET 3 Y 6 ASN L 106 HIS L 110 -1 O VAL L 107 N ILE L 86
SHEET 4 Y 6 PHE L 137 VAL L 142 1 O VAL L 139 N HIS L 110
SHEET 5 Y 6 ILE L 122 GLN L 127 -1 N GLY L 126 O ASN L 138
SHEET 6 Y 6 ILE L 70 SER L 77 -1 N GLY L 73 O VAL L 123
SHEET 1 Z 2 TYR L 90 VAL L 94 0
SHEET 2 Z 2 ARG L 99 ARG L 103 -1 O ARG L 103 N TYR L 90
SHEET 1 AA 2 LEU M 34 ARG M 36 0
SHEET 2 AA 2 VAL M 112 VAL M 114 -1 O VAL M 113 N ALA M 35
SHEET 1 AB 2 ALA M 53 VAL M 54 0
SHEET 2 AB 2 LEU M 79 ILE M 80 1 O ILE M 80 N ALA M 53
SHEET 1 AC 5 THR O 26 PHE O 27 0
SHEET 2 AC 5 ILE O 19 ALA O 21 -1 N PHE O 20 O PHE O 27
SHEET 3 AC 5 ALA O 78 ARG O 84 1 O ARG O 84 N ALA O 21
SHEET 4 AC 5 PHE O 14 VAL O 16 1 N GLY O 15 O HIS O 80
SHEET 5 AC 5 THR O 31 ASP O 32 -1 O THR O 31 N VAL O 16
SHEET 1 AD 4 THR O 26 PHE O 27 0
SHEET 2 AD 4 ILE O 19 ALA O 21 -1 N PHE O 20 O PHE O 27
SHEET 3 AD 4 ALA O 78 ARG O 84 1 O ARG O 84 N ALA O 21
SHEET 4 AD 4 ARG O 111 ASP O 117 1 O GLU O 116 N ILE O 83
SHEET 1 AE 3 VAL P 76 THR P 78 0
SHEET 2 AE 3 VAL P 94 VAL P 96 1 O GLY P 95 N THR P 78
SHEET 3 AE 3 ASN P 103 VAL P 105 -1 O ASN P 103 N VAL P 96
SHEET 1 AF 5 SER Q 6 LYS Q 13 0
SHEET 2 AF 5 ALA Q 16 ALA Q 24 -1 O VAL Q 22 N VAL Q 7
SHEET 3 AF 5 ILE Q 63 THR Q 70 -1 O THR Q 70 N THR Q 17
SHEET 4 AF 5 ILE Q 29 VAL Q 31 1 N LYS Q 30 O VAL Q 67
SHEET 5 AF 5 SER Q 34 PRO Q 35 -1 O SER Q 34 N VAL Q 31
SHEET 1 AG 2 LEU R 100 VAL R 102 0
SHEET 2 AG 2 LEU R 119 VAL R 121 1 O SER R 120 N VAL R 102
SHEET 1 AH 2 LEU S 15 ARG S 16 0
SHEET 2 AH 2 ASN S 21 VAL S 22 -1 O VAL S 22 N LEU S 15
SHEET 1 AI 2 ALA T 83 LYS T 84 0
SHEET 2 AI 2 LYS T 92 HIS T 93 -1 O LYS T 92 N LYS T 84
SHEET 1 AJ 2 VAL T 114 ILE T 116 0
SHEET 2 AJ 2 ARG T 122 ILE T 124 -1 O ARG T 123 N GLU T 115
SHEET 1 AK 4 ASP U 113 VAL U 116 0
SHEET 2 AK 4 ILE U 22 SER U 28 -1 N THR U 27 O ASP U 113
SHEET 3 AK 4 TRP U 79 GLU U 94 -1 O HIS U 87 N SER U 28
SHEET 4 AK 4 VAL U 51 ARG U 57 -1 N VAL U 56 O TYR U 90
SHEET 1 AL 3 VAL U 51 ARG U 57 0
SHEET 2 AL 3 TRP U 79 GLU U 94 -1 O TYR U 90 N VAL U 56
SHEET 3 AL 3 LYS U 61 LEU U 63 -1 N LEU U 63 O MET U 84
SHEET 1 AM 3 LYS U 61 LEU U 63 0
SHEET 2 AM 3 TRP U 79 GLU U 94 -1 O MET U 84 N LEU U 63
SHEET 3 AM 3 SER U 66 ARG U 68 -1 N THR U 67 O ASP U 80
SHEET 1 AN 3 SER U 66 ARG U 68 0
SHEET 2 AN 3 TRP U 79 GLU U 94 -1 O ASP U 80 N THR U 67
SHEET 3 AN 3 TYR d 53 LYS d 54 -1 O TYR d 53 N GLU U 83
SHEET 1 AO 4 TYR d 53 LYS d 54 0
SHEET 2 AO 4 TRP U 79 GLU U 94 -1 N GLU U 83 O TYR d 53
SHEET 3 AO 4 ILE U 22 SER U 28 -1 N SER U 28 O HIS U 87
SHEET 4 AO 4 ASP U 113 VAL U 116 -1 O ASP U 113 N THR U 27
SHEET 1 AP 2 VAL V 32 ALA V 37 0
SHEET 2 AP 2 TYR V 50 LEU V 55 -1 O VAL V 51 N ILE V 36
SHEET 1 AQ 3 GLY W 109 ASP W 112 0
SHEET 2 AQ 3 TYR W 101 THR W 106 -1 N LEU W 104 O MET W 111
SHEET 3 AQ 3 LYS W 124 VAL W 129 -1 O VAL W 129 N TYR W 101
SHEET 1 AR 7 PHE X 122 LYS X 123 0
SHEET 2 AR 7 LYS X 82 PHE X 86 1 N PHE X 86 O PHE X 122
SHEET 3 AR 7 CYS X 71 LEU X 76 -1 N VAL X 74 O VAL X 83
SHEET 4 AR 7 HIS X 48 ILE X 57 -1 N ILE X 52 O GLN X 75
SHEET 5 AR 7 GLU X 101 ALA X 105 -1 O LEU X 104 N ALA X 49
SHEET 6 AR 7 LYS X 126 VAL X 127 -1 O LYS X 126 N LEU X 103
SHEET 7 AR 7 VAL X 130 SER X 131 -1 O VAL X 130 N VAL X 127
SHEET 1 AS 4 ILE Y 7 ASN Y 15 0
SHEET 2 AS 4 ARG Y 20 LEU Y 28 -1 O GLN Y 22 N ILE Y 13
SHEET 3 AS 4 LYS Y 68 TYR Y 76 -1 O GLY Y 73 N PHE Y 23
SHEET 4 AS 4 VAL Y 55 THR Y 62 -1 N PHE Y 58 O PHE Y 72
SHEET 1 AT 2 ILE Z 89 HIS Z 95 0
SHEET 2 AT 2 GLN Z 98 ARG Z 103 -1 O THR Z 102 N LYS Z 90
SHEET 1 AU 2 PRO a 20 VAL a 21 0
SHEET 2 AU 2 VAL a 30 PRO a 31 -1 O VAL a 30 N VAL a 21
SHEET 1 AV 2 LYS a 37 ASN a 43 0
SHEET 2 AV 2 LYS a 66 HIS a 72 -1 O LEU a 71 N ARG a 38
SHEET 1 AW 3 ILE b 43 PHE b 47 0
SHEET 2 AW 3 PHE b 32 LYS b 36 -1 N VAL b 35 O THR b 44
SHEET 3 AW 3 SER b 78 ARG b 81 -1 O ARG b 80 N ASP b 34
SHEET 1 AX 2 CYS b 64 THR b 65 0
SHEET 2 AX 2 LYS b 72 LEU b 73 -1 O LYS b 72 N THR b 65
SHEET 1 AY 2 LEU d 30 ILE d 31 0
SHEET 2 AY 2 ILE d 38 ASP d 39 -1 O ILE d 38 N ILE d 31
SHEET 1 AZ 2 TYR f 106 LYS f 107 0
SHEET 2 AZ 2 ALA f 115 LYS f 116 -1 O ALA f 115 N LYS f 107
SHEET 1 BA 4 VAL g 9 LEU g 14 0
SHEET 2 BA 4 ILE g 317 GLN g 321 -1 O VAL g 319 N ARG g 11
SHEET 3 BA 4 THR g 307 TYR g 312 -1 N LEU g 308 O TRP g 320
SHEET 4 BA 4 ALA g 296 TRP g 301 -1 N SER g 298 O GLY g 311
SHEET 1 BB 4 SER g 23 SER g 25 0
SHEET 2 BB 4 LEU g 33 GLY g 37 -1 O GLY g 37 N SER g 23
SHEET 3 BB 4 LEU g 43 LEU g 48 -1 O ILE g 44 N SER g 36
SHEET 4 BB 4 GLY g 56 SER g 61 -1 O VAL g 59 N SER g 45
SHEET 1 BC 4 VAL g 69 VAL g 74 0
SHEET 2 BC 4 TYR g 80 SER g 85 -1 O VAL g 82 N VAL g 73
SHEET 3 BC 4 LEU g 90 ASN g 94 -1 O TRP g 93 N ALA g 81
SHEET 4 BC 4 ASN g 99 PHE g 104 -1 O PHE g 104 N LEU g 90
SHEET 1 BD 4 VAL g 111 ILE g 116 0
SHEET 2 BD 4 LYS g 122 SER g 127 -1 O ALA g 126 N SER g 113
SHEET 3 BD 4 ILE g 132 ASN g 136 -1 O ARG g 133 N SER g 125
SHEET 4 BD 4 CYS g 141 LEU g 145 -1 O ALA g 142 N VAL g 134
SHEET 1 BE 4 ILE g 206 PRO g 211 0
SHEET 2 BE 4 LEU g 217 GLY g 222 -1 O ALA g 221 N VAL g 208
SHEET 3 BE 4 GLN g 226 ASN g 231 -1 O TRP g 230 N ALA g 218
SHEET 4 BE 4 ASN g 240 ASP g 242 -1 O PHE g 241 N ILE g 227
SHEET 1 BF 4 ALA g 249 PHE g 252 0
SHEET 2 BF 4 TRP g 258 ALA g 262 -1 O ALA g 262 N ALA g 249
SHEET 3 BF 4 ILE g 267 ASP g 271 -1 O LYS g 268 N ALA g 261
SHEET 4 BF 4 LEU g 277 LEU g 281 -1 O ASP g 279 N ILE g 269
SHEET 1 BG 6 GLN i 33 GLY i 43 0
SHEET 2 BG 6 ARG i 46 CYS i 51 -1 O GLU i 48 N THR i 39
SHEET 3 BG 6 LYS i 56 ILE i 61 -1 O ARG i 57 N ALA i 49
SHEET 4 BG 6 GLN i 88 LYS i 94 1 O CYS i 89 N HIS i 60
SHEET 5 BG 6 ILE i 76 LEU i 81 -1 N LEU i 78 O VAL i 92
SHEET 6 BG 6 GLN i 33 GLY i 43 -1 N ALA i 36 O ILE i 77
SHEET 1 BH 5 ASN j 67 VAL j 69 0
SHEET 2 BH 5 ILE j 77 GLN j 81 -1 O ILE j 77 N VAL j 69
SHEET 3 BH 5 THR j 38 GLN j 43 -1 N THR j 40 O LEU j 80
SHEET 4 BH 5 ILE j 26 GLN j 32 -1 N GLN j 31 O LEU j 39
SHEET 5 BH 5 ILE j 103 ILE j 105 1 O LYS j 104 N ILE j 26
LINK OP2 G 21427 MG MG 21865 1555 1555 1.89
LINK OP1 A 2 618 MG MG 21825 1555 1555 1.89
LINK OP2 G 21327 MG MG 21826 1555 1555 1.93
LINK OP2 A 2 914 MG MG 21874 1555 1555 1.94
LINK OP1 C 21273 MG MG 21865 1555 1555 1.96
LINK OP2 A 2 554 MG MG 21803 1555 1555 1.96
LINK OP2 A 2 47 MG MG 21821 1555 1555 1.98
LINK OP2 C 2 423 MG MG 21870 1555 1555 1.99
LINK OP1 G 2 361 MG MG 21801 1555 1555 1.99
LINK OP1 A 2 604 MG MG 21818 1555 1555 2.02
LINK OP1 U 21769 MG MG 21812 1555 1555 2.02
LINK OP2 U 2 101 MG MG 21828 1555 1555 2.04
LINK OP2 A 21024 MG MG 21805 1555 1555 2.06
LINK OP2 A 2 400 MG MG 21814 1555 1555 2.06
LINK OP2 A 2 620 MG MG 21823 1555 1555 2.09
LINK OP1 G 21426 MG MG 21865 1555 1555 2.11
LINK OP1 C 2 267 MG MG 21835 1555 1555 2.11
LINK OP1 A 21761 MG MG 21812 1555 1555 2.11
LINK OP1 G 2 402 MG MG 21802 1555 1555 2.14
LINK OP1 U 21628 MG MG 21834 1555 1555 2.14
LINK OP2 U 21768 MG MG 21831 1555 1555 2.15
LINK OP2 C 2 360 MG MG 21828 1555 1555 2.16
LINK OP2 A 2 978 MG MG 21842 1555 1555 2.17
LINK OP2 A 2 928 MG MG 21811 1555 1555 2.17
LINK OP2 U 21520 MG MG 21864 1555 1555 2.17
LINK OP2 A 2 618 MG MG 21823 1555 1555 2.20
LINK O6 G 2 894 MG MG 21874 1555 1555 2.23
LINK OP1 C 2 249 MG MG 21869 1555 1555 2.24
LINK OP2 U 2 967 MG MG 21876 1555 1555 2.25
LINK OP2 A 2 250 MG MG 21869 1555 1555 2.25
LINK OP1 G 21791 MG MG 21834 1555 1555 2.26
LINK OP2 A 2 100 MG MG 21828 1555 1555 2.26
LINK OP2 A 2 514 MG MG 21846 1555 1555 2.27
LINK OP2 G 21329 MG MG 21809 1555 1555 2.27
LINK OP1 A 2 28 MG MG 21817 1555 1555 2.28
LINK OP2 A 2 459 MG MG 21836 1555 1555 2.28
LINK OP2 A 2 635 MG MG 21872 1555 1555 2.28
LINK OP1 G 2 16 MG MG 21815 1555 1555 2.29
LINK OP1 A 2 634 MG MG 21872 1555 1555 2.30
LINK OP2 G 2 95 MG MG 21832 1555 1555 2.31
LINK OP2 A 21761 MG MG 21822 1555 1555 2.32
LINK OP2 G 2 460 MG MG 21836 1555 1555 2.32
LINK OP2 A 2 377 MG MG 21816 1555 1555 2.33
LINK O6 G 21329 MG MG 21826 1555 1555 2.33
LINK SG CYS a 26 ZN ZN a 500 1555 1555 2.33
LINK SG CYS a 77 ZN ZN a 500 1555 1555 2.34
LINK OP1 A 2 100 MG MG 21804 1555 1555 2.34
LINK O4 U 2 916 MG MG 21874 1555 1555 2.35
LINK OP2 C 2 49 MG MG 21807 1555 1555 2.37
LINK OP2 U 2 378 MG MG 21816 1555 1555 2.39
LINK OP2 A 2 970 MG MG 21877 1555 1555 2.39
LINK OP1 U 2 988 MG MG 21849 1555 1555 2.42
LINK OP2 A 2 555 MG MG 21803 1555 1555 2.44
LINK OP2 U 21302 MG MG 21841 1555 1555 2.44
LINK OP2 A 2 603 MG MG 21871 1555 1555 2.46
LINK OP2 A 21760 MG MG 21822 1555 1555 2.46
LINK SG CYS a 23 ZN ZN a 500 1555 1555 2.49
LINK OP1 U 21282 MG MG 21855 1555 1555 2.49
LINK OP2 A 2 760 MG MG 21844 1555 1555 2.51
LINK OP2 G 21766 MG MG 21822 1555 1555 2.52
LINK OP1 A 21201 MG MG 21866 1555 1555 2.52
LINK OP2 G 21109 MG MG 21830 1555 1555 2.56
LINK O2 U 21518 MG MG 21864 1555 1555 2.58
LINK OP1 U 2 118 MG MG 21868 1555 1555 2.59
LINK OP2 G 21426 MG MG 21862 1555 1555 2.62
LINK OE1 GLN G 176 MG MG 21835 1555 1555 2.62
LINK O3' G 21765 MG MG 21812 1555 1555 2.63
LINK OP1 C 21455 MG MG 21857 1555 1555 2.67
LINK SG CYS a 74 ZN ZN a 500 1555 1555 2.67
LINK OP2 C 21273 MG MG 21862 1555 1555 2.71
LINK OP2 A 2 619 MG MG 21823 1555 1555 2.80
LINK OP2 G 2 466 MG MG 21837 1555 1555 2.86
LINK O2 C 21597 MG MG 21866 1555 1555 2.87
LINK OP1 G 21108 MG MG 21830 1555 1555 2.90
LINK OP1 A 2 622 MG MG 21827 1555 1555 2.96
LINK OP2 A 21202 MG MG 21866 1555 1555 2.96
LINK OP2 U 21003 MG MG 21819 1555 1555 2.96
LINK OP1 A 21467 MG MG 21856 1555 1555 2.98
LINK OP1 G 2 606 MG MG 21818 1555 1555 3.00
SITE 1 AC1 1 G 2 361
SITE 1 AC2 2 G 2 95 G 2 402
SITE 1 AC3 3 G 2 551 A 2 554 A 2 555
SITE 1 AC4 1 A 2 100
SITE 1 AC5 1 A 21024
SITE 1 AC6 2 C 2 49 A 2 424
SITE 1 AC7 1 G 21329
SITE 1 AC8 1 A 2 928
SITE 1 AC9 5 A 21761 G 21765 G 21766 U 21768
SITE 2 AC9 5 U 21769
SITE 1 BC1 2 A 2 386 A 2 400
SITE 1 BC2 1 G 2 16
SITE 1 BC3 2 A 2 377 U 2 378
SITE 1 BC4 1 A 2 28
SITE 1 BC5 3 G 2 370 A 2 604 G 2 606
SITE 1 BC6 1 U 21003
SITE 1 BC7 1 C 2 426
SITE 1 BC8 2 U 2 44 A 2 47
SITE 1 BC9 5 U 21759 A 21760 A 21761 G 21765
SITE 2 BC9 5 G 21766
SITE 1 CC1 4 U 2 617 A 2 618 A 2 619 A 2 620
SITE 1 CC2 2 U 2 562 A 2 579
SITE 1 CC3 1 A 2 618
SITE 1 CC4 2 G 21327 G 21329
SITE 1 CC5 1 A 2 622
SITE 1 CC6 4 A 2 100 U 2 101 U 2 102 C 2 360
SITE 1 CC7 2 G 21108 G 21109
SITE 1 CC8 1 U 21768
SITE 1 CC9 1 G 2 95
SITE 1 DC1 4 G 21670 G 21671 G 21725 U 21726
SITE 1 DC2 2 U 21628 G 21791
SITE 1 DC3 4 U 2 169 U 2 266 C 2 267 GLN G 176
SITE 1 DC4 2 A 2 459 G 2 460
SITE 1 DC5 1 G 2 466
SITE 1 DC6 1 U 21302
SITE 1 DC7 1 A 2 978
SITE 1 DC8 1 A 2 760
SITE 1 DC9 2 U 2 8 G 21139
SITE 1 EC1 2 A 2 514 C 2 530
SITE 1 EC2 2 U 2 988 C 2 989
SITE 1 EC3 1 A 2 212
SITE 1 EC4 1 U 2 934
SITE 1 EC5 1 G 21392
SITE 1 EC6 2 C 21158 U 21282
SITE 1 EC7 2 A 21467 ASN T 85
SITE 1 EC8 2 A 21201 C 21455
SITE 1 EC9 3 G 21200 A 21598 C 21600
SITE 1 FC1 1 C 21429
SITE 1 FC2 3 A 21195 C 21196 LYS U 77
SITE 1 FC3 2 G 21267 U 21268
SITE 1 FC4 3 G 21272 C 21273 G 21426
SITE 1 FC5 2 G 21539 C 21566
SITE 1 FC6 2 U 21518 U 21520
SITE 1 FC7 3 C 21273 G 21426 G 21427
SITE 1 FC8 3 A 21201 A 21202 C 21597
SITE 1 FC9 2 U 2 118 ASN I 52
SITE 1 GC1 2 C 2 249 A 2 250
SITE 1 GC2 1 C 2 423
SITE 1 GC3 1 A 2 603
SITE 1 GC4 2 A 2 634 A 2 635
SITE 1 GC5 3 G 2 894 A 2 914 U 2 916
SITE 1 GC6 2 G 2 941 GLY a 16
SITE 1 GC7 1 U 2 967
SITE 1 GC8 1 A 2 970
SITE 1 GC9 4 CYS a 23 CYS a 26 CYS a 74 CYS a 77
SITE 1 HC1 4 CYS b 37 GLY b 39 CYS b 40 CYS b 59
SITE 1 HC2 2 TYR f 85 THR f 87
SITE 1 HC3 5 CYS f 121 ILE f 128 CYS f 139 LYS f 141
SITE 2 HC3 5 CYS f 142
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
