HEADER RNA BINDING PROTEIN/RNA 23-OCT-18 6MUU
TITLE CRYO-EM STRUCTURE OF CSM-CRRNA BINARY COMPLEX IN TYPE III-A CRISPR-CAS
TITLE 2 SYSTEM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN CSM1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: UNCHARACTERIZED PROTEIN CSM2;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: UNCHARACTERIZED PROTEIN CSM3;
COMPND 11 CHAIN: C, D;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: UNCHARACTERIZED PROTEIN CSM4;
COMPND 15 CHAIN: E;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 5;
COMPND 18 MOLECULE: UNCHARACTERIZED PROTEIN CSM5;
COMPND 19 CHAIN: F;
COMPND 20 ENGINEERED: YES;
COMPND 21 MOL_ID: 6;
COMPND 22 MOLECULE: RNA (25-MER);
COMPND 23 CHAIN: G;
COMPND 24 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOCOCCUS ONNURINEUS;
SOURCE 3 ORGANISM_TAXID: 342948;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: THERMOCOCCUS ONNURINEUS;
SOURCE 8 ORGANISM_TAXID: 342948;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: THERMOCOCCUS ONNURINEUS;
SOURCE 13 ORGANISM_TAXID: 342948;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: THERMOCOCCUS ONNURINEUS;
SOURCE 18 ORGANISM_TAXID: 342948;
SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 21 MOL_ID: 5;
SOURCE 22 ORGANISM_SCIENTIFIC: THERMOCOCCUS ONNURINEUS;
SOURCE 23 ORGANISM_TAXID: 342948;
SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 26 MOL_ID: 6;
SOURCE 27 SYNTHETIC: YES;
SOURCE 28 ORGANISM_SCIENTIFIC: THERMOCOCCUS ONNURINEUS;
SOURCE 29 ORGANISM_TAXID: 342948
KEYWDS CRYO-EM STRUCTURE, CSM-CRRNA BINARY COMPLEX, TYPE III CRISPR-CAS
KEYWDS 2 SYSTEM, RNA BINDING PROTEIN-RNA COMPLEX
EXPDTA ELECTRON MICROSCOPY
AUTHOR N.JIA,C.WANG,E.T.ENG,D.J.PATEL
REVDAT 3 13-MAR-24 6MUU 1 REMARK
REVDAT 2 30-JAN-19 6MUU 1 JRNL
REVDAT 1 19-DEC-18 6MUU 0
JRNL AUTH N.JIA,C.Y.MO,C.WANG,E.T.ENG,L.A.MARRAFFINI,D.J.PATEL
JRNL TITL TYPE III-A CRISPR-CAS CSM COMPLEXES: ASSEMBLY, PERIODIC RNA
JRNL TITL 2 CLEAVAGE, DNASE ACTIVITY REGULATION, AND AUTOIMMUNITY.
JRNL REF MOL. CELL V. 73 264 2019
JRNL REFN ISSN 1097-4164
JRNL PMID 30503773
JRNL DOI 10.1016/J.MOLCEL.2018.11.007
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : RELION
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.000
REMARK 3 NUMBER OF PARTICLES : 129536
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6MUU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237640.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : CSM-CRRNA BINARY COMPLEX
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.50
REMARK 245 SAMPLE SUPPORT DETAILS : UNSPECIFIED
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.80
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 135.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
REMARK 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: HEPTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G
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 MET A -13
REMARK 465 GLY A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 SER A -3
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 TYR B 3
REMARK 465 HIS B 4
REMARK 465 GLN B 5
REMARK 465 LYS B 6
REMARK 465 HIS B 7
REMARK 465 GLY B 8
REMARK 465 GLY B 9
REMARK 465 TYR B 10
REMARK 465 GLY B 11
REMARK 465 ARG B 12
REMARK 465 GLY B 13
REMARK 465 GLY B 14
REMARK 465 TYR B 15
REMARK 465 GLY B 16
REMARK 465 ARG B 17
REMARK 465 GLN B 18
REMARK 465 ASP B 19
REMARK 465 ARG B 20
REMARK 465 PRO B 21
REMARK 465 GLN B 22
REMARK 465 VAL B 23
REMARK 465 ASP B 24
REMARK 465 ALA B 25
REMARK 465 SER B 26
REMARK 465 ARG B 27
REMARK 465 LEU B 28
REMARK 465 PHE B 29
REMARK 465 GLY B 30
REMARK 465 GLU B 31
REMARK 465 SER B 32
REMARK 465 PRO B 33
REMARK 465 ASP B 34
REMARK 465 LYS B 45
REMARK 465 GLY B 46
REMARK 465 LYS B 47
REMARK 465 GLU B 113
REMARK 465 GLY B 114
REMARK 465 ASP B 115
REMARK 465 ILE B 116
REMARK 465 ALA B 134
REMARK 465 THR B 135
REMARK 465 GLY B 136
REMARK 465 GLN B 137
REMARK 465 SER B 138
REMARK 465 LYS B 139
REMARK 465 GLY B 184
REMARK 465 GLY B 185
REMARK 465 ASP B 186
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 ASP C 2
REMARK 465 ARG C 3
REMARK 465 ARG C 27
REMARK 465 ASP C 28
REMARK 465 ILE C 29
REMARK 465 SER C 30
REMARK 465 GLU C 31
REMARK 465 ILE C 32
REMARK 465 GLY C 33
REMARK 465 GLY C 34
REMARK 465 GLU C 288
REMARK 465 ALA C 289
REMARK 465 GLY C 290
REMARK 465 SER D 0
REMARK 465 ARG D 27
REMARK 465 ASP D 28
REMARK 465 ILE D 29
REMARK 465 SER D 30
REMARK 465 GLU D 288
REMARK 465 ALA D 289
REMARK 465 GLY D 290
REMARK 465 MET E 1
REMARK 465 GLY E 287
REMARK 465 LEU E 288
REMARK 465 GLU E 289
REMARK 465 VAL F 49
REMARK 465 GLY F 63
REMARK 465 ASP F 64
REMARK 465 LEU F 77
REMARK 465 ASP F 78
REMARK 465 LYS F 88
REMARK 465 ILE F 89
REMARK 465 HIS F 90
REMARK 465 GLY F 91
REMARK 465 LYS F 92
REMARK 465 ILE F 93
REMARK 465 GLY F 94
REMARK 465 ARG F 95
REMARK 465 GLY F 134
REMARK 465 ASP F 135
REMARK 465 ALA F 136
REMARK 465 GLY F 148
REMARK 465 ASP F 149
REMARK 465 VAL F 150
REMARK 465 ALA F 151
REMARK 465 ARG F 152
REMARK 465 ASP F 153
REMARK 465 ILE F 154
REMARK 465 GLY F 155
REMARK 465 ARG F 156
REMARK 465 SER F 157
REMARK 465 GLU F 158
REMARK 465 ARG F 170
REMARK 465 ALA F 171
REMARK 465 ARG F 172
REMARK 465 ILE F 173
REMARK 465 ASP F 174
REMARK 465 ASP F 192
REMARK 465 ARG F 193
REMARK 465 GLY F 231
REMARK 465 ASN F 232
REMARK 465 PRO F 233
REMARK 465 GLN F 234
REMARK 465 PRO F 235
REMARK 465 ILE F 236
REMARK 465 PRO F 237
REMARK 465 GLU F 307
REMARK 465 VAL F 308
REMARK 465 GLN F 309
REMARK 465 LYS F 310
REMARK 465 PHE F 311
REMARK 465 GLY F 312
REMARK 465 ARG F 313
REMARK 465 TYR F 314
REMARK 465 THR F 315
REMARK 465 LEU F 325
REMARK 465 GLU F 326
REMARK 465 ASP F 327
REMARK 465 HIS F 328
REMARK 465 SER F 329
REMARK 465 VAL F 351
REMARK 465 GLU F 352
REMARK 465 LYS F 353
REMARK 465 GLY F 354
REMARK 465 TYR F 355
REMARK 465 GLY F 365
REMARK 465 LEU F 366
REMARK 465 GLY F 367
REMARK 465 LYS F 368
REMARK 465 LYS F 369
REMARK 465 PRO F 370
REMARK 465 GLY F 371
REMARK 465 GLY F 372
REMARK 465 SER F 373
REMARK 465 GLY F 374
REMARK 465 PHE F 375
REMARK 465 SER F 376
REMARK 465 ARG F 377
REMARK 465 GLU F 378
REMARK 465 HIS F 398
REMARK 465 HIS F 399
REMARK 465 HIS F 400
REMARK 465 HIS F 401
REMARK 465 HIS F 402
REMARK 465 HIS F 403
REMARK 465 G G 26
REMARK 465 C G 27
REMARK 465 G G 28
REMARK 465 U G 29
REMARK 465 A G 30
REMARK 465 U G 31
REMARK 465 U G 32
REMARK 465 G G 33
REMARK 465 G G 34
REMARK 465 G G 35
REMARK 465 C G 36
REMARK 465 G G 37
REMARK 465 C G 38
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 107 CG CD OE1 OE2
REMARK 470 ARG A 108 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 109 CG CD OE1 OE2
REMARK 470 GLU A 110 CG CD OE1 OE2
REMARK 470 GLN A 112 CG CD OE1 NE2
REMARK 470 PRO A 113 CG CD
REMARK 470 GLN A 114 CG CD OE1 NE2
REMARK 470 VAL B 35 CG1 CG2
REMARK 470 VAL B 36 CG1 CG2
REMARK 470 ILE B 38 CG1 CG2 CD1
REMARK 470 LYS B 39 CG CD CE NZ
REMARK 470 LYS B 40 CG CD CE NZ
REMARK 470 MET B 41 CG SD CE
REMARK 470 LEU B 42 CG CD1 CD2
REMARK 470 GLU B 43 CG CD OE1 OE2
REMARK 470 GLN B 48 CG CD OE1 NE2
REMARK 470 TRP B 49 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 49 CZ3 CH2
REMARK 470 GLU B 50 CG CD OE1 OE2
REMARK 470 ILE B 52 CG1 CG2 CD1
REMARK 470 GLN B 53 CG CD OE1 NE2
REMARK 470 PRO B 54 CG CD
REMARK 470 TYR B 55 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 PHE B 56 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP B 57 CG OD1 OD2
REMARK 470 ASN B 58 CG OD1 ND2
REMARK 470 VAL B 59 CG1 CG2
REMARK 470 VAL B 60 CG1 CG2
REMARK 470 ARG B 61 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 62 CG CD OE1 OE2
REMARK 470 LYS B 64 CG CD CE NZ
REMARK 470 ASN B 65 CG OD1 ND2
REMARK 470 PHE B 66 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU B 67 CG CD1 CD2
REMARK 470 GLU B 68 CG CD OE1 OE2
REMARK 470 TRP B 69 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 69 CZ3 CH2
REMARK 470 SER B 70 OG
REMARK 470 PRO B 71 CG CD
REMARK 470 LYS B 117 CG CD CE NZ
REMARK 470 ASP B 118 CG OD1 OD2
REMARK 470 ASP B 119 CG OD1 OD2
REMARK 470 LEU B 120 CG CD1 CD2
REMARK 470 VAL B 121 CG1 CG2
REMARK 470 LYS B 122 CG CD CE NZ
REMARK 470 MET B 123 CG SD CE
REMARK 470 ARG B 124 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 125 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 126 CG CD1 CD2
REMARK 470 LEU B 127 CG CD1 CD2
REMARK 470 TYR B 129 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR B 130 OG1 CG2
REMARK 470 VAL B 131 CG1 CG2
REMARK 470 LYS B 133 CG CD CE NZ
REMARK 470 LEU F 40 CG CD1 CD2
REMARK 470 VAL F 41 CG1 CG2
REMARK 470 ASN F 42 CG OD1 ND2
REMARK 470 ASP F 43 CG OD1 OD2
REMARK 470 LEU F 44 CG CD1 CD2
REMARK 470 MET F 45 CG SD CE
REMARK 470 ASN F 46 CG OD1 ND2
REMARK 470 LEU F 47 CG CD1 CD2
REMARK 470 GLU F 50 CG CD OE1 OE2
REMARK 470 LEU F 51 CG CD1 CD2
REMARK 470 ASN F 52 CG OD1 ND2
REMARK 470 GLU F 53 CG CD OE1 OE2
REMARK 470 ILE F 54 CG1 CG2 CD1
REMARK 470 LEU F 55 CG CD1 CD2
REMARK 470 LEU F 57 CG CD1 CD2
REMARK 470 LEU F 58 CG CD1 CD2
REMARK 470 LYS F 59 CG CD CE NZ
REMARK 470 ASN F 60 CG OD1 ND2
REMARK 470 PRO F 61 CG CD
REMARK 470 PRO F 62 CG CD
REMARK 470 TYR F 66 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE F 67 CG1 CG2 CD1
REMARK 470 TRP F 68 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP F 68 CZ3 CH2
REMARK 470 LYS F 69 CG CD CE NZ
REMARK 470 TYR F 71 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE F 72 CG1 CG2 CD1
REMARK 470 GLU F 73 CG CD OE1 OE2
REMARK 470 GLU F 74 CG CD OE1 OE2
REMARK 470 PHE F 75 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 HIS F 76 CG ND1 CD2 CE1 NE2
REMARK 470 PRO F 79 CG CD
REMARK 470 SER F 80 OG
REMARK 470 ASP F 81 CG OD1 OD2
REMARK 470 TYR F 82 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER F 83 OG
REMARK 470 ILE F 84 CG1 CG2 CD1
REMARK 470 TYR F 85 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR F 86 OG1 CG2
REMARK 470 LEU F 87 CG CD1 CD2
REMARK 470 ARG F 137 CG CD NE CZ NH1 NH2
REMARK 470 VAL F 139 CG1 CG2
REMARK 470 MET F 140 CG SD CE
REMARK 470 ARG F 141 CG CD NE CZ NH1 NH2
REMARK 470 VAL F 142 CG1 CG2
REMARK 470 VAL F 143 CG1 CG2
REMARK 470 SER F 144 OG
REMARK 470 LYS F 145 CG CD CE NZ
REMARK 470 VAL F 146 CG1 CG2
REMARK 470 ASN F 147 CG OD1 ND2
REMARK 470 ASP F 159 CG OD1 OD2
REMARK 470 VAL F 160 CG1 CG2
REMARK 470 LEU F 161 CG CD1 CD2
REMARK 470 ASP F 162 CG OD1 OD2
REMARK 470 TYR F 163 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR F 164 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET F 165 CG SD CE
REMARK 470 SER F 166 OG
REMARK 470 PHE F 167 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU F 168 CG CD1 CD2
REMARK 470 SER F 169 OG
REMARK 470 ARG F 175 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 176 CG CD CE NZ
REMARK 470 ARG F 177 CG CD NE CZ NH1 NH2
REMARK 470 ASP F 179 CG OD1 OD2
REMARK 470 ASP F 180 CG OD1 OD2
REMARK 470 LEU F 181 CG CD1 CD2
REMARK 470 LEU F 182 CG CD1 CD2
REMARK 470 GLU F 183 CG CD OE1 OE2
REMARK 470 ILE F 185 CG1 CG2 CD1
REMARK 470 VAL F 186 CG1 CG2
REMARK 470 PHE F 187 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET F 189 CG SD CE
REMARK 470 GLU F 190 CG CD OE1 OE2
REMARK 470 PRO F 191 CG CD
REMARK 470 ARG F 194 CG CD NE CZ NH1 NH2
REMARK 470 SER F 195 OG
REMARK 470 LYS F 196 CG CD CE NZ
REMARK 470 LYS F 356 CG CD CE NZ
REMARK 470 TRP F 357 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP F 357 CZ3 CH2
REMARK 470 GLU F 358 CG CD OE1 OE2
REMARK 470 ASN F 359 CG OD1 ND2
REMARK 470 VAL F 360 CG1 CG2
REMARK 470 ARG F 361 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 362 CG CD CE NZ
REMARK 470 LYS F 363 CG CD CE NZ
REMARK 470 LEU F 364 CG CD1 CD2
REMARK 470 PHE F 379 CG CD1 CD2 CE1 CE2 CZ
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 O VAL F 34 CB ASP F 81 1.88
REMARK 500 CB GLN A 114 NE ARG A 117 1.99
REMARK 500 O SER F 339 OP1 U G 23 2.15
REMARK 500 CB TRP F 341 OP1 U G 24 2.17
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 PRO F 61 N - CA - CB ANGL. DEV. = 7.5 DEGREES
REMARK 500 PRO F 62 N - CA - CB ANGL. DEV. = 7.3 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 LYS A 66 54.30 -93.55
REMARK 500 ASN A 67 -53.54 -121.86
REMARK 500 SER A 116 49.42 -157.64
REMARK 500 LYS A 138 -8.72 73.16
REMARK 500 PHE A 185 31.20 -94.43
REMARK 500 THR A 218 -169.30 -103.19
REMARK 500 TYR A 248 43.28 -106.06
REMARK 500 GLU A 326 91.60 -69.58
REMARK 500 GLU A 373 51.69 -94.39
REMARK 500 LYS A 375 -4.17 72.17
REMARK 500 ALA A 585 86.21 -153.68
REMARK 500 ARG A 630 48.26 -82.30
REMARK 500 ARG A 652 -9.44 73.02
REMARK 500 PRO A 720 -169.53 -74.19
REMARK 500 ARG A 724 -13.38 -140.44
REMARK 500 PHE A 742 70.15 63.08
REMARK 500 GLU C 95 -160.73 -77.52
REMARK 500 ASN C 96 108.53 -55.32
REMARK 500 ASN C 106 -53.36 -123.97
REMARK 500 ARG C 107 -1.98 -140.76
REMARK 500 GLU C 134 -9.10 73.37
REMARK 500 ARG C 246 74.80 52.83
REMARK 500 SER C 274 3.89 59.48
REMARK 500 SER C 278 -60.64 -93.08
REMARK 500 PHE C 280 33.53 -88.36
REMARK 500 ASP D 2 67.64 61.25
REMARK 500 ILE D 23 -62.67 -108.46
REMARK 500 ILE D 105 -66.91 -92.72
REMARK 500 SER D 131 70.25 54.39
REMARK 500 ASN D 136 70.01 46.31
REMARK 500 HIS E 36 -62.65 -94.28
REMARK 500 LEU E 81 37.84 -99.01
REMARK 500 GLN E 139 76.57 -69.20
REMARK 500 ARG E 152 -168.99 -79.85
REMARK 500 LYS E 187 83.52 -68.04
REMARK 500 LEU E 219 74.16 49.24
REMARK 500 TYR E 274 -70.73 -61.60
REMARK 500 PHE E 278 78.74 -154.53
REMARK 500 THR F 16 -179.31 76.96
REMARK 500 GLU F 29 -167.62 -118.93
REMARK 500 ASP F 81 -122.17 -160.22
REMARK 500 TYR F 199 70.04 60.19
REMARK 500 TRP F 337 -11.09 72.49
REMARK 500 PRO F 380 48.45 -88.22
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 ZN A 801 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 389 SG
REMARK 620 2 CYS A 392 SG 120.3
REMARK 620 3 CYS A 413 SG 117.2 122.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 111 NE2
REMARK 620 2 CYS C 113 SG 104.3
REMARK 620 3 CYS C 122 SG 111.0 123.4
REMARK 620 4 CYS C 125 SG 97.7 93.2 123.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 111 NE2
REMARK 620 2 CYS D 113 SG 93.5
REMARK 620 3 CYS D 125 SG 101.2 83.0
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-9253 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9254 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-9255 RELATED DB: EMDB
REMARK 900 RELATED ID: 6MUR RELATED DB: PDB
REMARK 900 RELATED ID: 6MUS RELATED DB: PDB
REMARK 900 RELATED ID: 6MUT RELATED DB: PDB
REMARK 900 RELATED ID: 6MUA RELATED DB: PDB
REMARK 900 RELATED ID: EMD-9256 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF CSM-CRRNA BINARY COMPLEX IN TYPE III-A CRISPR-
REMARK 900 CAS SYSTEM
DBREF 6MUU A 1 777 UNP B6YWB8 B6YWB8_THEON 1 777
DBREF 6MUU B 1 186 UNP B6YWB9 B6YWB9_THEON 1 186
DBREF 6MUU C 1 290 UNP B6YWC0 B6YWC0_THEON 1 290
DBREF 6MUU D 1 290 UNP B6YWC0 B6YWC0_THEON 1 290
DBREF 6MUU E 1 289 UNP B6YWC1 B6YWC1_THEON 1 289
DBREF 6MUU F 1 397 UNP B6YWC2 B6YWC2_THEON 1 397
DBREF 6MUU G 1 38 PDB 6MUU 6MUU 1 38
SEQADV 6MUU MET A -13 UNP B6YWB8 INITIATING METHIONINE
SEQADV 6MUU GLY A -12 UNP B6YWB8 EXPRESSION TAG
SEQADV 6MUU SER A -11 UNP B6YWB8 EXPRESSION TAG
SEQADV 6MUU SER A -10 UNP B6YWB8 EXPRESSION TAG
SEQADV 6MUU HIS A -9 UNP B6YWB8 EXPRESSION TAG
SEQADV 6MUU HIS A -8 UNP B6YWB8 EXPRESSION TAG
SEQADV 6MUU HIS A -7 UNP B6YWB8 EXPRESSION TAG
SEQADV 6MUU HIS A -6 UNP B6YWB8 EXPRESSION TAG
SEQADV 6MUU HIS A -5 UNP B6YWB8 EXPRESSION TAG
SEQADV 6MUU HIS A -4 UNP B6YWB8 EXPRESSION TAG
SEQADV 6MUU SER A -3 UNP B6YWB8 EXPRESSION TAG
SEQADV 6MUU GLN A -2 UNP B6YWB8 EXPRESSION TAG
SEQADV 6MUU ASP A -1 UNP B6YWB8 EXPRESSION TAG
SEQADV 6MUU PRO A 0 UNP B6YWB8 EXPRESSION TAG
SEQADV 6MUU SER B 0 UNP B6YWB9 EXPRESSION TAG
SEQADV 6MUU SER C 0 UNP B6YWC0 EXPRESSION TAG
SEQADV 6MUU SER D 0 UNP B6YWC0 EXPRESSION TAG
SEQADV 6MUU HIS F 398 UNP B6YWC2 EXPRESSION TAG
SEQADV 6MUU HIS F 399 UNP B6YWC2 EXPRESSION TAG
SEQADV 6MUU HIS F 400 UNP B6YWC2 EXPRESSION TAG
SEQADV 6MUU HIS F 401 UNP B6YWC2 EXPRESSION TAG
SEQADV 6MUU HIS F 402 UNP B6YWC2 EXPRESSION TAG
SEQADV 6MUU HIS F 403 UNP B6YWC2 EXPRESSION TAG
SEQRES 1 A 791 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 A 791 PRO MET GLU ILE ASP GLU LEU THR ALA LEU GLY GLY LEU
SEQRES 3 A 791 LEU HIS ASP ILE GLY LYS PRO VAL GLN ARG ALA GLY LEU
SEQRES 4 A 791 TYR SER GLY ASP HIS SER THR GLN GLY ALA ARG PHE LEU
SEQRES 5 A 791 ARG ASP LEU ALA GLU ASN THR GLY ARG ALA GLU TYR GLU
SEQRES 6 A 791 LEU LEU SER LEU PHE SER GLU PHE HIS HIS LYS GLY HIS
SEQRES 7 A 791 MET LYS ASN ASP GLU LEU MET ILE ARG ARG ILE LYS GLU
SEQRES 8 A 791 LEU SER PRO GLU ARG PHE GLY LEU THR MET GLU ASP VAL
SEQRES 9 A 791 LEU ASN ALA LEU TRP ILE VAL TYR GLU ALA ASP ASN LEU
SEQRES 10 A 791 ALA SER GLY GLU ARG GLU GLU GLY GLN PRO GLN ALA SER
SEQRES 11 A 791 ARG PRO LEU TYR SER VAL PHE ASN PRO GLY LYS ALA TYR
SEQRES 12 A 791 PRO TRP ALA GLU LEU ASP PHE GLU LYS GLU LEU PRO VAL
SEQRES 13 A 791 PRO GLY ASP VAL PHE SER ILE ARG SER GLN ASP TYR ARG
SEQRES 14 A 791 GLU LEU VAL LYS ARG LEU TRP GLU GLU LEU SER LYS ALA
SEQRES 15 A 791 LYS LEU ARG SER ASP ARG LEU LEU PRO VAL LEU GLU LYS
SEQRES 16 A 791 TYR LEU THR PHE VAL SER SER VAL THR SER GLU GLY ASN
SEQRES 17 A 791 ILE ILE SER LEU TYR ASP HIS MET ARG MET THR SER ALA
SEQRES 18 A 791 ILE ALA LEU ALA MET LEU ARG ALA GLY CYS THR ALA GLU
SEQRES 19 A 791 ASP VAL ARG SER GLY ARG CYS ARG LYS GLU LYS ARG PHE
SEQRES 20 A 791 LEU LEU ILE GLU GLY ASP PHE SER GLY ILE GLN ASP PHE
SEQRES 21 A 791 ILE TYR ARG VAL SER GLY LYS GLY THR LEU LYS TYR LEU
SEQRES 22 A 791 ARG ALA ARG SER ALA TYR LEU GLU LEU ILE GLY TRP ASP
SEQRES 23 A 791 VAL VAL LEU GLU ILE LEU SER ARG LEU GLY LEU THR ARG
SEQRES 24 A 791 ALA ASN VAL VAL PHE ASN ALA GLY GLY HIS PHE MET ILE
SEQRES 25 A 791 ILE ALA GLN ASN THR PRO ASP ALA VAL LYS GLU LEU GLU
SEQRES 26 A 791 GLU ILE ARG ALA LYS ALA VAL GLU TRP LEU TYR ARG GLU
SEQRES 27 A 791 PHE GLU SER ASP LEU TYR LEU ALA ILE GLU TRP GLU PRO
SEQRES 28 A 791 VAL SER GLY ARG GLU PHE GLY ARG GLU GLY GLY LYS ASN
SEQRES 29 A 791 LEU PHE ALA GLU ALA ARG LYS ARG LEU LYS HIS LYS LEU
SEQRES 30 A 791 THR VAL ARG LYS LEU LYS ARG PHE GLY GLU ILE LYS GLY
SEQRES 31 A 791 LEU PHE GLU HIS GLY HIS THR GLU ARG LEU ALA GLU CYS
SEQRES 32 A 791 PRO VAL CYS GLY ARG GLU LEU PRO GLU GLY LYS LEU GLU
SEQRES 33 A 791 PRO SER ALA SER ASP PRO GLU THR LYS VAL CYS PRO THR
SEQRES 34 A 791 CYS ASN ARG LEU VAL SER LEU GLY GLY ASN LEU PRO LYS
SEQRES 35 A 791 LEU LEU GLY PHE GLY ARG THR ALA LYS ASN ASP ALA GLY
SEQRES 36 A 791 VAL LEU VAL GLU GLY PRO PHE SER GLY PHE VAL PRO TYR
SEQRES 37 A 791 LEU GLN GLY GLY ARG PRO VAL GLY GLU GLN ILE LEU VAL
SEQRES 38 A 791 LYS ASN THR LEU ASN PRO GLY GLU ILE PRO GLU SER ALA
SEQRES 39 A 791 GLN PHE VAL PRO TYR PHE VAL ALA ASP TYR PHE LYS LYS
SEQRES 40 A 791 ASP PRO LYS GLY GLY VAL ALA THR PHE GLU GLU LEU SER
SEQRES 41 A 791 MET ALA SER THR GLY THR ARG ARG LEU GLY VAL MET LYS
SEQRES 42 A 791 GLY ASP VAL ASP ARG LEU GLY GLU PHE PHE SER SER MET
SEQRES 43 A 791 ASP SER PRO SER LYS LEU ALA THR ALA SER ARG PHE MET
SEQRES 44 A 791 ASP TYR PHE PHE LYS GLY TYR ILE GLY ALA ILE ILE GLU
SEQRES 45 A 791 GLY LYS PHE GLY TYR ILE ILE GLY ASP VAL PRO SER LEU
SEQRES 46 A 791 ARG ASP TRP PRO GLU GLU PRO ASP ILE VAL VAL VAL TYR
SEQRES 47 A 791 ALA GLY GLY ASP ASP PHE PHE ILE VAL GLY ALA TRP ASP
SEQRES 48 A 791 GLN ILE PHE GLU LEU ALA PHE ARG VAL ARG ARG ALA PHE
SEQRES 49 A 791 ASN ALA TYR THR GLY GLY LYS LEU THR LEU SER VAL GLY
SEQRES 50 A 791 LEU GLY TYR PHE ASP GLU ARG THR PRO ILE TYR ARG MET
SEQRES 51 A 791 ALA ASP VAL VAL SER GLU ARG LEU ASP THR ALA LYS ASP
SEQRES 52 A 791 GLU GLY ARG ASN ARG VAL PHE VAL VAL GLY ARG SER ARG
SEQRES 53 A 791 PRO LEU ASP GLY LYS HIS LYS LEU SER TYR GLU TRP ASN
SEQRES 54 A 791 HIS TYR GLU GLU LEU TRP ARG THR TYR ALA PRO ARG ILE
SEQRES 55 A 791 TYR ALA GLY ASN GLY ARG LEU LYS GLY LYS LEU GLU SER
SEQRES 56 A 791 LYS LYS GLY LEU LEU TRP LYS LEU LEU GLU ILE ARG GLU
SEQRES 57 A 791 LEU TYR VAL ARG ASP PRO ASN ASP VAL ARG TRP ALA TYR
SEQRES 58 A 791 LEU THR ALA TYR LEU LEU GLY ARG HIS GLY LEU SER ASP
SEQRES 59 A 791 LEU PHE PRO GLU LEU VAL GLY ILE ASP THR LYS ALA VAL
SEQRES 60 A 791 GLU ARG LYS GLU PRO GLN PRO VAL TYR TRP VAL ASP GLY
SEQRES 61 A 791 VAL LEU LYS ILE VAL LEU MET ALA VAL ARG ARG
SEQRES 1 B 187 SER MET ALA TYR HIS GLN LYS HIS GLY GLY TYR GLY ARG
SEQRES 2 B 187 GLY GLY TYR GLY ARG GLN ASP ARG PRO GLN VAL ASP ALA
SEQRES 3 B 187 SER ARG LEU PHE GLY GLU SER PRO ASP VAL VAL GLY ILE
SEQRES 4 B 187 LYS LYS MET LEU GLU GLY LYS GLY LYS GLN TRP GLU ALA
SEQRES 5 B 187 ILE GLN PRO TYR PHE ASP ASN VAL VAL ARG GLU ALA LYS
SEQRES 6 B 187 ASN PHE LEU GLU TRP SER PRO ASN LYS ARG LEU ALA ASN
SEQRES 7 B 187 ALA VAL THR VAL ALA ALA TYR LEU THR SER GLN GLY LEU
SEQRES 8 B 187 LYS THR ASN GLN VAL ARG LYS ILE LEU ASP MET ALA ARG
SEQRES 9 B 187 THR THR GLU LEU LYS VAL LYS ARG GLY GLU GLY ASP ILE
SEQRES 10 B 187 LYS ASP ASP LEU VAL LYS MET ARG TYR LEU LEU ALA TYR
SEQRES 11 B 187 THR VAL GLY LYS ALA THR GLY GLN SER LYS TYR SER LEU
SEQRES 12 B 187 ASP ALA PHE HIS ARG ILE LEU ASP PRO MET LEU GLU VAL
SEQRES 13 B 187 LEU MET GLY SER PRO LYS LYS GLU ASN PHE GLU LYS PHE
SEQRES 14 B 187 TYR ASP PHE LEU GLN ALA VAL VAL ALA TYR HIS LYS PHE
SEQRES 15 B 187 PHE GLY GLY GLY ASP
SEQRES 1 C 291 SER MET ASP ARG ARG PHE TYR GLY LYS ILE VAL ILE LYS
SEQRES 2 C 291 GLY LYS ILE LYS ALA VAL THR GLY LEU HIS ILE GLY SER
SEQRES 3 C 291 GLN ARG ASP ILE SER GLU ILE GLY GLY ILE ASP ASN PRO
SEQRES 4 C 291 VAL ILE LYS ASP PRO HIS THR GLY LEU PRO TYR ILE PRO
SEQRES 5 C 291 GLY SER SER LEU LYS GLY ARG LEU ARG SER LEU PHE GLU
SEQRES 6 C 291 ILE LEU VAL ASN SER ARG LEU GLY GLU TRP ARG GLU LYS
SEQRES 7 C 291 TYR PRO SER LEU ALA ASN TYR SER PRO GLY SER CYS ARG
SEQRES 8 C 291 PRO ASP ASN GLN GLU ASN CYS GLY LYS PHE PHE ASN ARG
SEQRES 9 C 291 LYS ILE ASN ARG GLY TRP ILE HIS VAL CYS PRO ASP TYR
SEQRES 10 C 291 GLU THR ALA LEU ALA CYS PRO VAL CYS ARG LEU PHE GLY
SEQRES 11 C 291 ALA SER GLY LYS GLU SER ASN PHE PRO SER ARG ILE ILE
SEQRES 12 C 291 VAL ARG ASP ALA PHE LEU THR LYS GLU TRP GLU GLU LYS
SEQRES 13 C 291 TRP ARG ALA GLY GLU ALA ILE THR GLU ALA LYS ILE GLU
SEQRES 14 C 291 VAL GLY ILE ASP ARG VAL THR SER GLN ALA ASN PRO ARG
SEQRES 15 C 291 THR ASN GLU ARG VAL VAL ALA GLY ALA GLU PHE GLU PHE
SEQRES 16 C 291 GLU ILE ILE TYR ASN VAL GLU ASN THR THR HIS TRP ARG
SEQRES 17 C 291 ASP ASP ILE LYS ASN LEU LEU THR ALA MET ALA LEU LEU
SEQRES 18 C 291 GLU ASP SER TYR LEU GLY GLY SER GLY SER ARG GLY TYR
SEQRES 19 C 291 GLY LYS VAL LYS PHE ILE PHE ASP SER PHE GLU PHE ARG
SEQRES 20 C 291 PRO LEU ASP TYR TYR ARG THR GLY LYS ASP GLU ASP ILE
SEQRES 21 C 291 VAL SER ILE ASP ALA ARG GLU LYS SER VAL SER ASP ILE
SEQRES 22 C 291 LEU SER GLY PHE ASP SER LEU PHE SER GLU VAL GLU GLY
SEQRES 23 C 291 LYS LEU GLU ALA GLY
SEQRES 1 D 291 SER MET ASP ARG ARG PHE TYR GLY LYS ILE VAL ILE LYS
SEQRES 2 D 291 GLY LYS ILE LYS ALA VAL THR GLY LEU HIS ILE GLY SER
SEQRES 3 D 291 GLN ARG ASP ILE SER GLU ILE GLY GLY ILE ASP ASN PRO
SEQRES 4 D 291 VAL ILE LYS ASP PRO HIS THR GLY LEU PRO TYR ILE PRO
SEQRES 5 D 291 GLY SER SER LEU LYS GLY ARG LEU ARG SER LEU PHE GLU
SEQRES 6 D 291 ILE LEU VAL ASN SER ARG LEU GLY GLU TRP ARG GLU LYS
SEQRES 7 D 291 TYR PRO SER LEU ALA ASN TYR SER PRO GLY SER CYS ARG
SEQRES 8 D 291 PRO ASP ASN GLN GLU ASN CYS GLY LYS PHE PHE ASN ARG
SEQRES 9 D 291 LYS ILE ASN ARG GLY TRP ILE HIS VAL CYS PRO ASP TYR
SEQRES 10 D 291 GLU THR ALA LEU ALA CYS PRO VAL CYS ARG LEU PHE GLY
SEQRES 11 D 291 ALA SER GLY LYS GLU SER ASN PHE PRO SER ARG ILE ILE
SEQRES 12 D 291 VAL ARG ASP ALA PHE LEU THR LYS GLU TRP GLU GLU LYS
SEQRES 13 D 291 TRP ARG ALA GLY GLU ALA ILE THR GLU ALA LYS ILE GLU
SEQRES 14 D 291 VAL GLY ILE ASP ARG VAL THR SER GLN ALA ASN PRO ARG
SEQRES 15 D 291 THR ASN GLU ARG VAL VAL ALA GLY ALA GLU PHE GLU PHE
SEQRES 16 D 291 GLU ILE ILE TYR ASN VAL GLU ASN THR THR HIS TRP ARG
SEQRES 17 D 291 ASP ASP ILE LYS ASN LEU LEU THR ALA MET ALA LEU LEU
SEQRES 18 D 291 GLU ASP SER TYR LEU GLY GLY SER GLY SER ARG GLY TYR
SEQRES 19 D 291 GLY LYS VAL LYS PHE ILE PHE ASP SER PHE GLU PHE ARG
SEQRES 20 D 291 PRO LEU ASP TYR TYR ARG THR GLY LYS ASP GLU ASP ILE
SEQRES 21 D 291 VAL SER ILE ASP ALA ARG GLU LYS SER VAL SER ASP ILE
SEQRES 22 D 291 LEU SER GLY PHE ASP SER LEU PHE SER GLU VAL GLU GLY
SEQRES 23 D 291 LYS LEU GLU ALA GLY
SEQRES 1 E 289 MET PRO LYS PHE ILE ALA VAL LYS LEU ILE PRO LYS GLY
SEQRES 2 E 289 PRO PHE ARG ASP ILE PRO ARG ALA ASP THR LEU PHE GLY
SEQRES 3 E 289 ALA ILE GLY ASN ALA ILE SER ALA ILE HIS GLY GLN SER
SEQRES 4 E 289 ALA VAL GLU GLU LEU VAL ASP ALA PHE VAL GLY GLY ALA
SEQRES 5 E 289 ARG ILE SER SER ALA PHE PRO TYR SER GLY ASP THR TYR
SEQRES 6 E 289 TYR LEU PRO LYS PRO LEU SER VAL GLU PRO ALA LEU GLU
SEQRES 7 E 289 GLY ILE LEU THR GLY LEU ASP GLU GLU GLU ARG TYR THR
SEQRES 8 E 289 THR ALA LYS ARG LEU ARG LYS ALA LYS TYR LEU ASP LEU
SEQRES 9 E 289 LYS ASN PHE GLU LEU ALA LEU ARG LEU ARG PRO PHE THR
SEQRES 10 E 289 ILE PRO GLU GLU ILE PRO TYR ALA ARG VAL ASP VAL PRO
SEQRES 11 E 289 ARG VAL VAL LEU ASP ARG VAL THR GLN ASP SER SER ILE
SEQRES 12 E 289 TYR PHE TRP GLU GLU ILE ARG PHE ARG GLU LYS SER GLY
SEQRES 13 E 289 VAL TYR PHE LEU TYR SER GLY PRO ARG GLU VAL PHE ASP
SEQRES 14 E 289 GLY TYR ILE ALA PRO ALA MET ARG PHE LEU GLY ASP THR
SEQRES 15 E 289 GLY ILE GLY GLY LYS SER THR TRP GLY ALA GLY LEU PHE
SEQRES 16 E 289 GLU VAL GLU PHE HIS GLU MET LYS ILE ASP ALA PRO GLY
SEQRES 17 E 289 SER GLU TYR SER VAL THR LEU SER ASN ALA LEU PRO THR
SEQRES 18 E 289 LYS THR PRO VAL LEU TRP ARG LEU LEU ARG LYS GLY GLY
SEQRES 19 E 289 TRP SER PHE GLY ARG ARG LYS PRO ARG MET THR PHE ILE
SEQRES 20 E 289 ALA GLU GLY SER ILE VAL LYS ASN ASP PRO GLY GLY MET
SEQRES 21 E 289 GLU ARG LEU GLU LEU GLY LEU SER HIS GLU VAL TYR VAL
SEQRES 22 E 289 TYR GLY LEU THR PHE PRO LEU GLY VAL GLU LEU PRO GLU
SEQRES 23 E 289 GLY LEU GLU
SEQRES 1 F 403 MET THR GLU ARG THR LEU LYS VAL LEU SER PRO LEU HIS
SEQRES 2 F 403 ILE GLY THR GLY ASN GLU LEU THR PRO VAL ASP ILE TYR
SEQRES 3 F 403 PRO ARG GLU ASN ILE ILE HIS VAL LEU ASP THR GLU ARG
SEQRES 4 F 403 LEU VAL ASN ASP LEU MET ASN LEU GLY VAL GLU LEU ASN
SEQRES 5 F 403 GLU ILE LEU ALA LEU LEU LYS ASN PRO PRO GLY ASP ALA
SEQRES 6 F 403 TYR ILE TRP LYS GLY TYR ILE GLU GLU PHE HIS LEU ASP
SEQRES 7 F 403 PRO SER ASP TYR SER ILE TYR THR LEU LYS ILE HIS GLY
SEQRES 8 F 403 LYS ILE GLY ARG LYS SER MET GLN ILE LYS GLU PHE ILE
SEQRES 9 F 403 LYS LEU ASN GLY ARG PRO TYR ILE PRO GLY SER SER LEU
SEQRES 10 F 403 LYS GLY ALA ILE ARG THR ALA VAL LEU TYR LYS ALA LEU
SEQRES 11 F 403 LYS GLU CYS GLY ASP ALA ARG ALA VAL MET ARG VAL VAL
SEQRES 12 F 403 SER LYS VAL ASN GLY ASP VAL ALA ARG ASP ILE GLY ARG
SEQRES 13 F 403 SER GLU ASP VAL LEU ASP TYR TYR MET SER PHE LEU SER
SEQRES 14 F 403 ARG ALA ARG ILE ASP ARG LYS ARG ALA ASP ASP LEU LEU
SEQRES 15 F 403 GLU ALA ILE VAL PHE GLY MET GLU PRO ASP ARG ARG SER
SEQRES 16 F 403 LYS ILE ARG TYR GLU PRO LYS ARG ASP PRO MET LYS ALA
SEQRES 17 F 403 LEU ILE VAL ARG ASP SER LYS PRO VAL GLY ARG LYS HIS
SEQRES 18 F 403 LEU ALA VAL TYR HIS VAL GLU VAL ILE GLY ASN PRO GLN
SEQRES 19 F 403 PRO ILE PRO ILE TRP VAL GLU ALA ILE GLU PRO GLY ALA
SEQRES 20 F 403 ALA THR ASP VAL GLU ILE HIS VAL ASP THR GLU ALA LEU
SEQRES 21 F 403 ARG LEU ASN ALA ASP TYR PHE ASN GLY LEU LEU TRP GLU
SEQRES 22 F 403 CYS LEU LYS GLU ARG GLY GLU PRO GLY GLU VAL PHE GLU
SEQRES 23 F 403 ASP PHE LEU TRP GLU ALA VAL ASP GLU PHE TYR THR ALA
SEQRES 24 F 403 VAL MET LYS TYR GLU THR ILE GLU VAL GLN LYS PHE GLY
SEQRES 25 F 403 ARG TYR THR SER GLN VAL ARG SER PHE TYR ALA SER LEU
SEQRES 26 F 403 GLU ASP HIS SER GLY HIS VAL LEU ARG LEU GLY TRP GLY
SEQRES 27 F 403 SER GLY TRP LEU ALA MET THR ILE GLY LEU LEU LEU VAL
SEQRES 28 F 403 GLU LYS GLY TYR LYS TRP GLU ASN VAL ARG LYS LYS LEU
SEQRES 29 F 403 GLY LEU GLY LYS LYS PRO GLY GLY SER GLY PHE SER ARG
SEQRES 30 F 403 GLU PHE PRO LYS THR ARG ARG LEU ALA ASP GLY MET PRO
SEQRES 31 F 403 MET GLY TRP VAL VAL LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 G 38 G U G G A A A G G C G G G
SEQRES 2 G 38 C A G A G G C G G U U U G
SEQRES 3 G 38 C G U A U U G G G C G C
HET ZN A 801 1
HET ZN C 301 1
HET ZN D 301 1
HETNAM ZN ZINC ION
FORMUL 8 ZN 3(ZN 2+)
HELIX 1 AA1 GLU A 2 LEU A 13 1 12
HELIX 2 AA2 ILE A 16 ALA A 23 1 8
HELIX 3 AA3 ASP A 29 ASN A 44 1 16
HELIX 4 AA4 GLU A 49 PHE A 59 1 11
HELIX 5 AA5 HIS A 61 LYS A 66 1 6
HELIX 6 AA6 GLU A 69 LEU A 78 1 10
HELIX 7 AA7 SER A 79 PHE A 83 5 5
HELIX 8 AA8 THR A 86 ALA A 104 1 19
HELIX 9 AA9 GLN A 152 ALA A 168 1 17
HELIX 10 AB1 ARG A 171 LEU A 183 1 13
HELIX 11 AB2 SER A 197 GLY A 216 1 20
HELIX 12 AB3 ALA A 219 SER A 224 1 6
HELIX 13 AB4 ILE A 243 TYR A 248 1 6
HELIX 14 AB5 THR A 255 LEU A 281 1 27
HELIX 15 AB6 THR A 303 PHE A 325 1 23
HELIX 16 AB7 LEU A 351 LEU A 368 1 18
HELIX 17 AB8 CYS A 413 LEU A 426 1 14
HELIX 18 AB9 THR A 501 MET A 507 1 7
HELIX 19 AC1 ARG A 524 PHE A 529 1 6
HELIX 20 AC2 SER A 530 MET A 532 5 3
HELIX 21 AC3 SER A 534 GLY A 551 1 18
HELIX 22 AC4 TYR A 552 GLU A 558 1 7
HELIX 23 AC5 PHE A 561 GLY A 566 1 6
HELIX 24 AC6 TRP A 596 THR A 614 1 19
HELIX 25 AC7 PRO A 632 ASP A 645 1 14
HELIX 26 AC8 ASP A 645 GLU A 650 1 6
HELIX 27 AC9 TRP A 674 ILE A 688 1 15
HELIX 28 AD1 LYS A 702 ASP A 719 1 18
HELIX 29 AD2 ARG A 724 HIS A 736 1 13
HELIX 30 AD3 PHE A 742 VAL A 746 5 5
HELIX 31 AD4 ASP A 749 ARG A 755 1 7
HELIX 32 AD5 VAL A 764 VAL A 775 1 12
HELIX 33 AD6 GLY B 37 GLY B 44 1 8
HELIX 34 AD7 TRP B 49 GLN B 53 1 5
HELIX 35 AD8 GLN B 53 ALA B 63 1 11
HELIX 36 AD9 SER B 70 GLN B 88 1 19
HELIX 37 AE1 THR B 92 LYS B 110 1 19
HELIX 38 AE2 ASP B 118 ALA B 128 1 11
HELIX 39 AE3 SER B 141 GLY B 158 1 18
HELIX 40 AE4 PRO B 160 GLY B 183 1 24
HELIX 41 AE5 PRO C 51 SER C 69 1 19
HELIX 42 AE6 TYR C 78 TYR C 84 5 7
HELIX 43 AE7 ASP C 115 LEU C 120 1 6
HELIX 44 AE8 VAL C 124 GLY C 129 1 6
HELIX 45 AE9 GLU C 153 GLY C 159 1 7
HELIX 46 AF1 HIS C 205 LEU C 220 1 16
HELIX 47 AF2 PRO C 247 GLY C 254 1 8
HELIX 48 AF3 SER C 274 PHE C 280 1 7
HELIX 49 AF4 GLU C 282 LEU C 287 1 6
HELIX 50 AF5 PRO D 51 SER D 69 1 19
HELIX 51 AF6 ASP D 115 LEU D 120 1 6
HELIX 52 AF7 CYS D 122 GLY D 129 1 8
HELIX 53 AF8 THR D 149 GLY D 159 1 11
HELIX 54 AF9 HIS D 205 GLU D 221 1 17
HELIX 55 AG1 LEU D 248 GLY D 254 1 7
HELIX 56 AG2 LYS D 267 LEU D 273 1 7
HELIX 57 AG3 GLY D 275 PHE D 280 1 6
HELIX 58 AG4 GLU D 282 LEU D 287 1 6
HELIX 59 AG5 ARG E 20 HIS E 36 1 17
HELIX 60 AG6 GLY E 37 GLY E 50 1 14
HELIX 61 AG7 PRO E 70 GLU E 74 5 5
HELIX 62 AG8 ALA E 76 LEU E 81 1 6
HELIX 63 AG9 GLU E 88 LYS E 98 1 11
HELIX 64 AH1 LEU E 104 ARG E 112 1 9
HELIX 65 AH2 PRO E 164 TYR E 171 1 8
HELIX 66 AH3 TYR E 171 THR E 182 1 12
HELIX 67 AH4 LYS E 187 GLY E 191 5 5
HELIX 68 AH5 ASP F 36 ASN F 46 1 11
HELIX 69 AH6 LEU F 51 ASN F 60 1 10
HELIX 70 AH7 LYS F 69 GLU F 74 1 6
HELIX 71 AH8 PRO F 113 CYS F 133 1 21
HELIX 72 AH9 ALA F 138 VAL F 142 1 5
HELIX 73 AI1 VAL F 160 SER F 169 1 10
HELIX 74 AI2 ALA F 178 GLU F 183 1 6
HELIX 75 AI3 GLU F 200 ASP F 204 5 5
HELIX 76 AI4 THR F 257 ASN F 263 1 7
HELIX 77 AI5 GLY F 269 GLU F 277 1 9
HELIX 78 AI6 GLU F 280 THR F 305 1 26
HELIX 79 AI7 GLN F 317 SER F 324 1 8
HELIX 80 AI8 GLY F 340 THR F 345 1 6
HELIX 81 AI9 ILE F 346 LEU F 349 5 4
HELIX 82 AJ1 TRP F 357 LEU F 364 1 8
SHEET 1 AA1 2 LEU A 119 TYR A 120 0
SHEET 2 AA1 2 ALA A 128 TYR A 129 -1 O TYR A 129 N LEU A 119
SHEET 1 AA2 4 VAL A 288 ASN A 291 0
SHEET 2 AA2 4 HIS A 295 GLN A 301 -1 O MET A 297 N VAL A 289
SHEET 3 AA2 4 PHE A 233 SER A 241 -1 N ILE A 236 O ILE A 298
SHEET 4 AA2 4 TYR A 330 VAL A 338 -1 O TYR A 330 N SER A 241
SHEET 1 AA3 2 ARG A 345 GLU A 346 0
SHEET 2 AA3 2 LYS A 349 ASN A 350 -1 O LYS A 349 N GLU A 346
SHEET 1 AA4 2 LEU A 386 GLU A 388 0
SHEET 2 AA4 2 GLU A 395 PRO A 397 -1 O LEU A 396 N ALA A 387
SHEET 1 AA5 2 GLU A 402 PRO A 403 0
SHEET 2 AA5 2 LYS A 411 VAL A 412 -1 O VAL A 412 N GLU A 402
SHEET 1 AA6 5 VAL A 444 GLU A 445 0
SHEET 2 AA6 5 GLY A 450 TYR A 454 -1 O PHE A 451 N VAL A 444
SHEET 3 AA6 5 GLY A 431 THR A 435 -1 N THR A 435 O GLY A 450
SHEET 4 AA6 5 GLN A 464 LYS A 468 -1 O LEU A 466 N PHE A 432
SHEET 5 AA6 5 VAL A 483 TYR A 485 1 O TYR A 485 N VAL A 467
SHEET 1 AA7 6 ILE A 580 TYR A 584 0
SHEET 2 AA7 6 ASP A 589 ALA A 595 -1 O VAL A 593 N VAL A 581
SHEET 3 AA7 6 LEU A 515 VAL A 522 -1 N GLY A 516 O GLY A 594
SHEET 4 AA7 6 LEU A 620 PHE A 627 -1 O GLY A 623 N LYS A 519
SHEET 5 AA7 6 ARG A 654 PHE A 656 1 O PHE A 656 N VAL A 622
SHEET 6 AA7 6 TYR A 672 GLU A 673 -1 O TYR A 672 N VAL A 655
SHEET 1 AA8 2 TYR A 689 GLY A 691 0
SHEET 2 AA8 2 ARG A 694 LEU A 695 -1 O ARG A 694 N ALA A 690
SHEET 1 AA9 3 ILE C 141 VAL C 143 0
SHEET 2 AA9 3 GLU C 191 VAL C 200 -1 O ILE C 197 N ILE C 142
SHEET 3 AA9 3 PHE C 147 LEU C 148 -1 N PHE C 147 O GLU C 193
SHEET 1 AB1 5 ILE C 141 VAL C 143 0
SHEET 2 AB1 5 GLU C 191 VAL C 200 -1 O ILE C 197 N ILE C 142
SHEET 3 AB1 5 GLY C 7 ALA C 17 -1 N ILE C 15 O PHE C 192
SHEET 4 AB1 5 VAL C 236 GLU C 244 -1 O GLU C 244 N VAL C 10
SHEET 5 AB1 5 VAL C 260 ILE C 262 -1 O SER C 261 N PHE C 243
SHEET 1 AB2 2 SER C 85 SER C 88 0
SHEET 2 AB2 2 LYS C 99 PHE C 101 1 O PHE C 101 N GLY C 87
SHEET 1 AB3 2 ARG C 103 LYS C 104 0
SHEET 2 AB3 2 TRP C 109 ILE C 110 -1 O ILE C 110 N ARG C 103
SHEET 1 AB4 2 THR C 163 GLU C 168 0
SHEET 2 AB4 2 ARG C 181 VAL C 186 -1 O ARG C 185 N GLU C 164
SHEET 1 AB5 3 ILE D 141 VAL D 143 0
SHEET 2 AB5 3 GLU D 191 ASN D 199 -1 O ILE D 197 N ILE D 142
SHEET 3 AB5 3 PHE D 147 LEU D 148 -1 N PHE D 147 O GLU D 193
SHEET 1 AB6 5 ILE D 141 VAL D 143 0
SHEET 2 AB6 5 GLU D 191 ASN D 199 -1 O ILE D 197 N ILE D 142
SHEET 3 AB6 5 GLY D 7 ALA D 17 -1 N ILE D 11 O ILE D 196
SHEET 4 AB6 5 VAL D 236 PRO D 247 -1 O ILE D 239 N LYS D 14
SHEET 5 AB6 5 ILE D 259 SER D 261 -1 O ILE D 259 N PHE D 245
SHEET 1 AB7 2 SER D 85 SER D 88 0
SHEET 2 AB7 2 LYS D 99 PHE D 101 1 O PHE D 101 N GLY D 87
SHEET 1 AB8 2 ARG D 103 LYS D 104 0
SHEET 2 AB8 2 TRP D 109 ILE D 110 -1 O ILE D 110 N ARG D 103
SHEET 1 AB9 2 THR D 163 ILE D 171 0
SHEET 2 AB9 2 ALA D 178 VAL D 186 -1 O ASN D 183 N LYS D 166
SHEET 1 AC1 4 ARG E 53 SER E 61 0
SHEET 2 AC1 4 SER E 155 SER E 162 -1 O TYR E 158 N PHE E 58
SHEET 3 AC1 4 LYS E 3 PRO E 11 -1 N LEU E 9 O VAL E 157
SHEET 4 AC1 4 PHE E 195 LYS E 203 -1 O GLU E 196 N ILE E 10
SHEET 1 AC2 2 TYR E 66 PRO E 68 0
SHEET 2 AC2 2 TYR E 101 ASP E 103 -1 O LEU E 102 N LEU E 67
SHEET 1 AC3 2 TYR E 124 ARG E 131 0
SHEET 2 AC3 2 TYR E 144 PHE E 151 -1 O GLU E 148 N VAL E 127
SHEET 1 AC4 3 ILE E 252 LYS E 254 0
SHEET 2 AC4 3 TYR E 211 THR E 214 -1 N SER E 212 O VAL E 253
SHEET 3 AC4 3 PRO E 279 GLY E 281 -1 O LEU E 280 N VAL E 213
SHEET 1 AC5 2 LEU E 229 SER E 236 0
SHEET 2 AC5 2 ARG E 239 ILE E 247 -1 O ARG E 239 N SER E 236
SHEET 1 AC6 2 GLU E 261 LEU E 263 0
SHEET 2 AC6 2 VAL E 271 VAL E 273 -1 O VAL E 271 N LEU E 263
SHEET 1 AC7 4 ALA F 248 VAL F 251 0
SHEET 2 AC7 4 ARG F 4 VAL F 8 -1 N LEU F 6 O THR F 249
SHEET 3 AC7 4 VAL F 394 LEU F 396 -1 O VAL F 395 N LYS F 7
SHEET 4 AC7 4 HIS F 331 LEU F 333 -1 N LEU F 333 O VAL F 394
SHEET 1 AC8 2 GLU F 19 LEU F 20 0
SHEET 2 AC8 2 ILE F 100 LYS F 101 -1 O ILE F 100 N LEU F 20
SHEET 1 AC9 2 LEU F 209 ILE F 210 0
SHEET 2 AC9 2 HIS F 254 VAL F 255 -1 O HIS F 254 N ILE F 210
SHEET 1 AD1 2 ALA F 223 HIS F 226 0
SHEET 2 AD1 2 TRP F 239 ALA F 242 -1 O VAL F 240 N TYR F 225
LINK SG CYS A 389 ZN ZN A 801 1555 1555 2.44
LINK SG CYS A 392 ZN ZN A 801 1555 1555 2.47
LINK SG CYS A 413 ZN ZN A 801 1555 1555 2.43
LINK NE2 HIS C 111 ZN ZN C 301 1555 1555 1.79
LINK SG CYS C 113 ZN ZN C 301 1555 1555 2.50
LINK SG CYS C 122 ZN ZN C 301 1555 1555 1.95
LINK SG CYS C 125 ZN ZN C 301 1555 1555 2.51
LINK NE2 HIS D 111 ZN ZN D 301 1555 1555 2.49
LINK SG CYS D 113 ZN ZN D 301 1555 1555 2.82
LINK SG CYS D 125 ZN ZN D 301 1555 1555 2.66
SITE 1 AC1 4 CYS A 389 CYS A 392 CYS A 413 CYS A 416
SITE 1 AC2 4 HIS C 111 CYS C 113 CYS C 122 CYS C 125
SITE 1 AC3 4 HIS D 111 CYS D 113 CYS D 122 CYS D 125
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
