HEADER STRUCTURAL PROTEIN/HYDROLASE/DNA 08-JAN-18 5Z3L
TITLE STRUCTURE OF SNF2-NUCLEOSOME COMPLEX IN APO STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H3.2;
COMPND 3 CHAIN: A, E;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: HISTONE H4;
COMPND 7 CHAIN: B, F;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: HISTONE H2A;
COMPND 11 CHAIN: C, G;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 4;
COMPND 14 MOLECULE: HISTONE H2B 1.1;
COMPND 15 CHAIN: D, H;
COMPND 16 SYNONYM: H2B1.1;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 5;
COMPND 19 MOLECULE: DNA (167-MER);
COMPND 20 CHAIN: I;
COMPND 21 ENGINEERED: YES;
COMPND 22 MOL_ID: 6;
COMPND 23 MOLECULE: DNA (167-MER);
COMPND 24 CHAIN: J;
COMPND 25 ENGINEERED: YES;
COMPND 26 MOL_ID: 7;
COMPND 27 MOLECULE: TRANSCRIPTION REGULATORY PROTEIN SNF2;
COMPND 28 CHAIN: O;
COMPND 29 SYNONYM: ATP-DEPENDENT HELICASE SNF2,REGULATORY PROTEIN GAM1,
COMPND 30 REGULATORY PROTEIN SWI2,SWI/SNF COMPLEX COMPONENT SNF2,TRANSCRIPTION
COMPND 31 FACTOR TYE3;
COMPND 32 EC: 3.6.4.-;
COMPND 33 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 3 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 4 ORGANISM_TAXID: 8355;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 9 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 10 ORGANISM_TAXID: 8355;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 15 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 16 ORGANISM_TAXID: 8355;
SOURCE 17 GENE: HIST1H2AJ, LOC494591;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 20 MOL_ID: 4;
SOURCE 21 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS;
SOURCE 22 ORGANISM_COMMON: AFRICAN CLAWED FROG;
SOURCE 23 ORGANISM_TAXID: 8355;
SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 25 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 26 MOL_ID: 5;
SOURCE 27 SYNTHETIC: YES;
SOURCE 28 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 29 ORGANISM_TAXID: 32630;
SOURCE 30 MOL_ID: 6;
SOURCE 31 SYNTHETIC: YES;
SOURCE 32 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 33 ORGANISM_TAXID: 32630;
SOURCE 34 MOL_ID: 7;
SOURCE 35 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 36 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 37 ORGANISM_TAXID: 559292;
SOURCE 38 STRAIN: ATCC 204508 / S288C;
SOURCE 39 GENE: SNF2, GAM1, RIC1, SWI2, TYE3, YOR290C;
SOURCE 40 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 41 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COMPLEX, NUCLEOSOME, CHROMATIN REMODELING, GENE REGULATION,
KEYWDS 2 STRUCTURAL PROTEIN-HYDROLASE-DNA COMPLEX
EXPDTA ELECTRON MICROSCOPY
AUTHOR M.LI,X.XIA,X.LIU,X.LI,Z.CHEN
REVDAT 2 27-MAR-24 5Z3L 1 REMARK
REVDAT 1 03-APR-19 5Z3L 0
JRNL AUTH M.LI,X.XIA,Y.TIAN,Q.JIA,X.LIU,Y.LU,M.LI,X.LI,Z.CHEN
JRNL TITL MECHANISM OF DNA TRANSLOCATION UNDERLYING CHROMATIN
JRNL TITL 2 REMODELLING BY SNF2.
JRNL REF NATURE V. 567 409 2019
JRNL REFN ESSN 1476-4687
JRNL PMID 30867599
JRNL DOI 10.1038/S41586-019-1029-2
REMARK 2
REMARK 2 RESOLUTION. 4.31 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : UCSFIMAGE4, GCTF, RELION
REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE
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) : 4.310
REMARK 3 NUMBER OF PARTICLES : 42383
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 5Z3L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1300006314.
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 : COMPLEX OF SNF2 AND NUCLEOSOME
REMARK 245 IN APO STATE
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.30
REMARK 245 SAMPLE SUPPORT DETAILS : NO CARBON COATED
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 4023
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) : 1800.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 3200.00
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) : 5000.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 22500
REMARK 245 CALIBRATED MAGNIFICATION : 22500
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: UNDECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: O
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 ALA A 1
REMARK 465 ARG A 2
REMARK 465 THR A 3
REMARK 465 LYS A 4
REMARK 465 GLN A 5
REMARK 465 THR A 6
REMARK 465 ALA A 7
REMARK 465 ARG A 8
REMARK 465 LYS A 9
REMARK 465 SER A 10
REMARK 465 THR A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 LYS A 14
REMARK 465 ALA A 15
REMARK 465 PRO A 16
REMARK 465 ARG A 17
REMARK 465 LYS A 18
REMARK 465 GLN A 19
REMARK 465 LEU A 20
REMARK 465 ALA A 21
REMARK 465 THR A 22
REMARK 465 LYS A 23
REMARK 465 ALA A 24
REMARK 465 ALA A 25
REMARK 465 ARG A 26
REMARK 465 LYS A 27
REMARK 465 SER A 28
REMARK 465 ALA A 29
REMARK 465 PRO A 30
REMARK 465 ALA A 31
REMARK 465 THR A 32
REMARK 465 GLY A 33
REMARK 465 GLY A 34
REMARK 465 VAL A 35
REMARK 465 LYS A 36
REMARK 465 ALA A 135
REMARK 465 SER B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 GLY B 4
REMARK 465 LYS B 5
REMARK 465 GLY B 6
REMARK 465 GLY B 7
REMARK 465 LYS B 8
REMARK 465 GLY B 9
REMARK 465 LEU B 10
REMARK 465 GLY B 11
REMARK 465 LYS B 12
REMARK 465 GLY B 13
REMARK 465 GLY B 14
REMARK 465 GLY B 102
REMARK 465 SER C 1
REMARK 465 GLY C 2
REMARK 465 ARG C 3
REMARK 465 GLY C 4
REMARK 465 LYS C 5
REMARK 465 GLN C 6
REMARK 465 GLY C 7
REMARK 465 GLY C 8
REMARK 465 LYS C 9
REMARK 465 THR C 10
REMARK 465 ARG C 11
REMARK 465 LYS C 119
REMARK 465 THR C 120
REMARK 465 GLU C 121
REMARK 465 SER C 122
REMARK 465 SER C 123
REMARK 465 LYS C 124
REMARK 465 SER C 125
REMARK 465 ALA C 126
REMARK 465 LYS C 127
REMARK 465 SER C 128
REMARK 465 LYS C 129
REMARK 465 ALA D 1
REMARK 465 LYS D 2
REMARK 465 SER D 3
REMARK 465 ALA D 4
REMARK 465 PRO D 5
REMARK 465 ALA D 6
REMARK 465 PRO D 7
REMARK 465 LYS D 8
REMARK 465 LYS D 9
REMARK 465 GLY D 10
REMARK 465 SER D 11
REMARK 465 LYS D 12
REMARK 465 LYS D 13
REMARK 465 ALA D 14
REMARK 465 VAL D 15
REMARK 465 THR D 16
REMARK 465 LYS D 17
REMARK 465 THR D 18
REMARK 465 GLN D 19
REMARK 465 LYS D 20
REMARK 465 LYS D 21
REMARK 465 ASP D 22
REMARK 465 GLY D 23
REMARK 465 LYS D 24
REMARK 465 LYS D 25
REMARK 465 ARG D 26
REMARK 465 ARG D 27
REMARK 465 LYS D 28
REMARK 465 LYS D 122
REMARK 465 ALA E 1
REMARK 465 ARG E 2
REMARK 465 THR E 3
REMARK 465 LYS E 4
REMARK 465 GLN E 5
REMARK 465 THR E 6
REMARK 465 ALA E 7
REMARK 465 ARG E 8
REMARK 465 LYS E 9
REMARK 465 SER E 10
REMARK 465 THR E 11
REMARK 465 GLY E 12
REMARK 465 GLY E 13
REMARK 465 LYS E 14
REMARK 465 ALA E 15
REMARK 465 PRO E 16
REMARK 465 ARG E 17
REMARK 465 LYS E 18
REMARK 465 GLN E 19
REMARK 465 LEU E 20
REMARK 465 ALA E 21
REMARK 465 THR E 22
REMARK 465 LYS E 23
REMARK 465 ALA E 24
REMARK 465 ALA E 25
REMARK 465 ARG E 26
REMARK 465 LYS E 27
REMARK 465 SER E 28
REMARK 465 ALA E 29
REMARK 465 PRO E 30
REMARK 465 ALA E 31
REMARK 465 THR E 32
REMARK 465 GLY E 33
REMARK 465 GLY E 34
REMARK 465 VAL E 35
REMARK 465 LYS E 36
REMARK 465 LYS E 37
REMARK 465 PRO E 38
REMARK 465 HIS E 39
REMARK 465 ALA E 135
REMARK 465 SER F 1
REMARK 465 GLY F 2
REMARK 465 ARG F 3
REMARK 465 GLY F 4
REMARK 465 LYS F 5
REMARK 465 GLY F 6
REMARK 465 GLY F 7
REMARK 465 LYS F 8
REMARK 465 GLY F 9
REMARK 465 LEU F 10
REMARK 465 GLY F 11
REMARK 465 LYS F 12
REMARK 465 GLY F 13
REMARK 465 GLY F 14
REMARK 465 ALA F 15
REMARK 465 LYS F 16
REMARK 465 SER G 1
REMARK 465 GLY G 2
REMARK 465 ARG G 3
REMARK 465 GLY G 4
REMARK 465 LYS G 5
REMARK 465 GLN G 6
REMARK 465 GLY G 7
REMARK 465 GLY G 8
REMARK 465 LYS G 9
REMARK 465 THR G 10
REMARK 465 ARG G 11
REMARK 465 LYS G 119
REMARK 465 THR G 120
REMARK 465 GLU G 121
REMARK 465 SER G 122
REMARK 465 SER G 123
REMARK 465 LYS G 124
REMARK 465 SER G 125
REMARK 465 ALA G 126
REMARK 465 LYS G 127
REMARK 465 SER G 128
REMARK 465 LYS G 129
REMARK 465 ALA H 1
REMARK 465 LYS H 2
REMARK 465 SER H 3
REMARK 465 ALA H 4
REMARK 465 PRO H 5
REMARK 465 ALA H 6
REMARK 465 PRO H 7
REMARK 465 LYS H 8
REMARK 465 LYS H 9
REMARK 465 GLY H 10
REMARK 465 SER H 11
REMARK 465 LYS H 12
REMARK 465 LYS H 13
REMARK 465 ALA H 14
REMARK 465 VAL H 15
REMARK 465 THR H 16
REMARK 465 LYS H 17
REMARK 465 THR H 18
REMARK 465 GLN H 19
REMARK 465 LYS H 20
REMARK 465 LYS H 21
REMARK 465 ASP H 22
REMARK 465 GLY H 23
REMARK 465 LYS H 24
REMARK 465 LYS H 25
REMARK 465 ARG H 26
REMARK 465 ARG H 27
REMARK 465 LYS H 28
REMARK 465 LYS H 122
REMARK 465 DA I 1
REMARK 465 DA I 148
REMARK 465 DG I 149
REMARK 465 DC I 150
REMARK 465 DT I 151
REMARK 465 DT I 152
REMARK 465 DG I 153
REMARK 465 DT I 154
REMARK 465 DC I 155
REMARK 465 DG I 156
REMARK 465 DA I 157
REMARK 465 DG I 158
REMARK 465 DA I 159
REMARK 465 DA I 160
REMARK 465 DG I 161
REMARK 465 DT I 162
REMARK 465 DA I 163
REMARK 465 DC I 164
REMARK 465 DG I 165
REMARK 465 DA I 166
REMARK 465 DT I 167
REMARK 465 DA J -19
REMARK 465 DT J -18
REMARK 465 DC J -17
REMARK 465 DG J -16
REMARK 465 DT J -15
REMARK 465 DA J -14
REMARK 465 DC J -13
REMARK 465 DT J -12
REMARK 465 DT J -11
REMARK 465 DC J -10
REMARK 465 DT J -9
REMARK 465 DC J -8
REMARK 465 DG J -7
REMARK 465 DA J -6
REMARK 465 DC J -5
REMARK 465 DA J -4
REMARK 465 DA J -3
REMARK 465 DG J -2
REMARK 465 DC J -1
REMARK 465 DT J 0
REMARK 465 DT J 147
REMARK 465 ALA O 666
REMARK 465 TYR O 667
REMARK 465 ILE O 668
REMARK 465 LYS O 669
REMARK 465 ASP O 691
REMARK 465 SER O 692
REMARK 465 LEU O 693
REMARK 465 THR O 694
REMARK 465 ARG O 695
REMARK 465 ALA O 696
REMARK 465 VAL O 697
REMARK 465 LYS O 698
REMARK 465 ASP O 699
REMARK 465 GLN O 700
REMARK 465 GLN O 701
REMARK 465 LYS O 702
REMARK 465 TYR O 703
REMARK 465 THR O 704
REMARK 465 LYS O 705
REMARK 465 GLU O 706
REMARK 465 MET O 707
REMARK 465 ILE O 708
REMARK 465 ASP O 709
REMARK 465 SER O 710
REMARK 465 HIS O 711
REMARK 465 ILE O 712
REMARK 465 LYS O 713
REMARK 465 GLU O 714
REMARK 465 ALA O 715
REMARK 465 SER O 716
REMARK 465 GLU O 717
REMARK 465 GLU O 718
REMARK 465 VAL O 719
REMARK 465 ASP O 720
REMARK 465 ASP O 721
REMARK 465 LEU O 722
REMARK 465 SER O 723
REMARK 465 MET O 724
REMARK 465 VAL O 725
REMARK 465 PRO O 726
REMARK 465 LYS O 727
REMARK 465 MET O 728
REMARK 465 LYS O 729
REMARK 465 ASP O 730
REMARK 465 GLU O 731
REMARK 465 GLU O 732
REMARK 465 TYR O 733
REMARK 465 ASP O 734
REMARK 465 ASP O 735
REMARK 465 ASP O 736
REMARK 465 ASP O 737
REMARK 465 ASP O 738
REMARK 465 ASN O 739
REMARK 465 SER O 740
REMARK 465 ASN O 741
REMARK 465 VAL O 742
REMARK 465 ALA O 961
REMARK 465 ASN O 962
REMARK 465 THR O 963
REMARK 465 GLY O 964
REMARK 465 GLY O 965
REMARK 465 GLN O 966
REMARK 465 PHE O 1033
REMARK 465 ILE O 1034
REMARK 465 GLY O 1035
REMARK 465 ASP O 1036
REMARK 465 GLN O 1037
REMARK 465 ASN O 1038
REMARK 465 ASN O 1039
REMARK 465 LYS O 1040
REMARK 465 LYS O 1041
REMARK 465 MET O 1042
REMARK 465 VAL O 1043
REMARK 465 GLY O 1044
REMARK 465 LEU O 1045
REMARK 465 ARG O 1046
REMARK 465 SER O 1270
REMARK 465 GLY O 1271
REMARK 465 VAL O 1272
REMARK 465 GLU O 1273
REMARK 465 GLU O 1274
REMARK 465 GLU O 1275
REMARK 465 GLU O 1276
REMARK 465 GLU O 1310
REMARK 465 LEU O 1311
REMARK 465 GLY O 1312
REMARK 465 VAL O 1313
REMARK 465 SER O 1321
REMARK 465 GLU O 1322
REMARK 465 LEU O 1323
REMARK 465 PRO O 1324
REMARK 465 ASP O 1325
REMARK 465 ILE O 1326
REMARK 465 TYR O 1327
REMARK 465 SER O 1328
REMARK 465 ARG O 1329
REMARK 465 ASP O 1330
REMARK 465 ILE O 1331
REMARK 465 GLY O 1332
REMARK 465 ALA O 1333
REMARK 465 GLU O 1334
REMARK 465 LEU O 1335
REMARK 465 ARG O 1349
REMARK 465 GLY O 1350
REMARK 465 ALA O 1351
REMARK 465 ARG O 1352
REMARK 465 GLU O 1353
REMARK 465 ARG O 1354
REMARK 465 LYS O 1355
REMARK 465 THR O 1356
REMARK 465 ALA O 1357
REMARK 465 THR O 1358
REMARK 465 TYR O 1359
REMARK 465 ASN O 1360
REMARK 465 ASP O 1361
REMARK 465 ASN O 1362
REMARK 465 MET O 1363
REMARK 465 SER O 1364
REMARK 465 GLU O 1365
REMARK 465 GLU O 1366
REMARK 465 GLN O 1367
REMARK 465 TRP O 1368
REMARK 465 LEU O 1369
REMARK 465 ARG O 1370
REMARK 465 GLN O 1371
REMARK 465 PHE O 1372
REMARK 465 GLU O 1373
REMARK 465 VAL O 1374
REMARK 465 SER O 1375
REMARK 465 ASP O 1376
REMARK 465 ASP O 1377
REMARK 465 GLU O 1378
REMARK 465 LYS O 1379
REMARK 465 ASN O 1380
REMARK 465 ASP O 1381
REMARK 465 LYS O 1382
REMARK 465 GLN O 1383
REMARK 465 ALA O 1384
REMARK 465 ARG O 1385
REMARK 465 LYS O 1386
REMARK 465 GLN O 1387
REMARK 465 ARG O 1388
REMARK 465 THR O 1389
REMARK 465 LYS O 1390
REMARK 465 LYS O 1391
REMARK 465 GLU O 1392
REMARK 465 ASP O 1393
REMARK 465 LYS O 1394
REMARK 465 SER O 1395
REMARK 465 GLU O 1396
REMARK 465 ALA O 1397
REMARK 465 ILE O 1398
REMARK 465 ASP O 1399
REMARK 465 GLY O 1400
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 LYS A 37 CG CD CE NZ
REMARK 470 ARG A 134 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 13 CG CD CE NZ
REMARK 470 LYS C 36 CG CD CE NZ
REMARK 470 LYS C 118 CG CD CE NZ
REMARK 470 LYS D 31 CG CD CE NZ
REMARK 470 LYS D 54 CG CD CE NZ
REMARK 470 ARG E 134 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 17 CG CD NE CZ NH1 NH2
REMARK 470 ARG F 19 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 20 CG CD CE NZ
REMARK 470 ARG F 23 CG CD NE CZ NH1 NH2
REMARK 470 LYS G 74 CG CD CE NZ
REMARK 470 LYS G 118 CG CD CE NZ
REMARK 470 VAL O 889 CG1
REMARK 470 ASN O 957 CG OD1 ND2
REMARK 470 THR O 958 OG1 CG2
REMARK 470 PRO O 959 CG CD
REMARK 470 PHE O 960 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN O1243 CG OD1 ND2
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 DC I 66 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DG I 83 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC I 95 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DC I 123 C3' - C2' - C1' ANGL. DEV. = -4.9 DEGREES
REMARK 500 DC I 123 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DG I 128 C3' - C2' - C1' ANGL. DEV. = -5.1 DEGREES
REMARK 500 DG I 128 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DA I 135 O4' - C1' - N9 ANGL. DEV. = 3.1 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 LEU A 61 -64.65 -109.21
REMARK 500 ASP A 81 65.88 38.37
REMARK 500 LYS A 115 -4.24 72.67
REMARK 500 GLU A 133 -65.54 -94.44
REMARK 500 LEU B 22 164.39 176.36
REMARK 500 LYS B 44 -74.59 -102.72
REMARK 500 LYS B 77 -4.39 68.72
REMARK 500 GLN C 24 -62.25 -107.66
REMARK 500 ALA C 45 -64.93 -101.25
REMARK 500 GLN C 104 -3.08 68.18
REMARK 500 ALA D 35 -113.49 56.23
REMARK 500 VAL D 45 -64.80 -103.21
REMARK 500 LEU E 61 -64.64 -109.18
REMARK 500 ASP E 81 65.82 38.43
REMARK 500 LYS E 115 -4.30 72.73
REMARK 500 GLU E 133 -65.48 -94.48
REMARK 500 ILE F 26 -61.82 -124.40
REMARK 500 LYS F 44 -65.13 -90.49
REMARK 500 GLN G 24 -62.26 -107.67
REMARK 500 ALA G 45 -64.90 -101.30
REMARK 500 GLN G 104 -3.07 68.18
REMARK 500 ALA H 35 -113.47 56.23
REMARK 500 VAL H 45 -64.79 -103.23
REMARK 500 GLU O 811 -61.86 -106.65
REMARK 500 ARG O 816 -4.50 61.62
REMARK 500 PHE O 866 158.72 179.59
REMARK 500 ASP O 867 -65.63 -131.59
REMARK 500 TYR O 914 -132.79 64.67
REMARK 500 ASN O 929 -120.20 63.20
REMARK 500 ASN O 930 -167.10 -75.19
REMARK 500 ALA O 936 -71.29 -109.11
REMARK 500 ASN O 939 -66.92 -134.61
REMARK 500 PHE O 946 -73.14 -55.34
REMARK 500 LYS O 968 -66.27 -127.19
REMARK 500 LEU O 971 -73.12 -82.92
REMARK 500 GLU O 973 -61.86 -122.17
REMARK 500 GLU O 974 -73.72 -56.15
REMARK 500 VAL O 999 -67.40 -129.49
REMARK 500 GLN O1020 -167.21 -74.26
REMARK 500 ARG O1031 -69.26 -132.14
REMARK 500 ASN O1049 70.69 54.70
REMARK 500 LEU O1055 -70.07 -125.16
REMARK 500 ASN O1060 -71.19 -81.44
REMARK 500 PHE O1065 -5.01 61.36
REMARK 500 GLU O1066 -4.09 69.48
REMARK 500 MET O1112 74.73 50.49
REMARK 500 ASN O1127 66.18 60.36
REMARK 500 LEU O1133 158.92 179.98
REMARK 500 SER O1139 -5.36 66.44
REMARK 500 LEU O1157 -74.67 -112.86
REMARK 500
REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-6879 RELATED DB: EMDB
REMARK 900 STRUCTURE OF SNF2-NUCLEOSOME COMPLEX IN APO STATE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS STATE THAT THE SAMPLE SEQUENCE OF CHAIN D/H IS CONFORMED BY
REMARK 999 DNA SEQUENCING AND CONSISTENTS WITH THE LITERATURE (PDB CODE 3MVD)
DBREF 5Z3L A 1 135 UNP P84233 H32_XENLA 2 136
DBREF 5Z3L B 1 102 UNP P62799 H4_XENLA 2 103
DBREF 5Z3L C 1 129 UNP Q6AZJ8 Q6AZJ8_XENLA 2 130
DBREF 5Z3L D 1 122 UNP P02281 H2B11_XENLA 5 126
DBREF 5Z3L E 1 135 UNP P84233 H32_XENLA 2 136
DBREF 5Z3L F 1 102 UNP P62799 H4_XENLA 2 103
DBREF 5Z3L G 1 129 UNP Q6AZJ8 Q6AZJ8_XENLA 2 130
DBREF 5Z3L H 1 122 UNP P02281 H2B11_XENLA 5 126
DBREF 5Z3L I 1 167 PDB 5Z3L 5Z3L 1 167
DBREF 5Z3L J -19 147 PDB 5Z3L 5Z3L -19 147
DBREF 5Z3L O 666 1400 UNP P22082 SNF2_YEAST 666 1400
SEQADV 5Z3L ALA A 102 UNP P84233 GLY 103 SEE SEQUENCE DETAILS
SEQADV 5Z3L THR D 29 UNP P02281 SER 33 SEE SEQUENCE DETAILS
SEQADV 5Z3L ALA E 102 UNP P84233 GLY 103 SEE SEQUENCE DETAILS
SEQADV 5Z3L THR H 29 UNP P02281 SER 33 SEE SEQUENCE DETAILS
SEQRES 1 A 135 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY
SEQRES 2 A 135 LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG
SEQRES 3 A 135 LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS
SEQRES 4 A 135 ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG
SEQRES 5 A 135 ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU
SEQRES 6 A 135 PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE
SEQRES 7 A 135 LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA
SEQRES 8 A 135 LEU GLN GLU ALA SER GLU ALA TYR LEU VAL ALA LEU PHE
SEQRES 9 A 135 GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL
SEQRES 10 A 135 THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE
SEQRES 11 A 135 ARG GLY GLU ARG ALA
SEQRES 1 B 102 SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY
SEQRES 2 B 102 GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE
SEQRES 3 B 102 GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG
SEQRES 4 B 102 ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU
SEQRES 5 B 102 GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL
SEQRES 6 B 102 ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG
SEQRES 7 B 102 LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS
SEQRES 8 B 102 ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 C 129 SER GLY ARG GLY LYS GLN GLY GLY LYS THR ARG ALA LYS
SEQRES 2 C 129 ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE PRO
SEQRES 3 C 129 VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN TYR
SEQRES 4 C 129 ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA
SEQRES 5 C 129 ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU LEU
SEQRES 6 C 129 ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE
SEQRES 7 C 129 ILE PRO ARG HIS LEU GLN LEU ALA VAL ARG ASN ASP GLU
SEQRES 8 C 129 GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA GLN
SEQRES 9 C 129 GLY GLY VAL LEU PRO ASN ILE GLN SER VAL LEU LEU PRO
SEQRES 10 C 129 LYS LYS THR GLU SER SER LYS SER ALA LYS SER LYS
SEQRES 1 D 122 ALA LYS SER ALA PRO ALA PRO LYS LYS GLY SER LYS LYS
SEQRES 2 D 122 ALA VAL THR LYS THR GLN LYS LYS ASP GLY LYS LYS ARG
SEQRES 3 D 122 ARG LYS THR ARG LYS GLU SER TYR ALA ILE TYR VAL TYR
SEQRES 4 D 122 LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER
SEQRES 5 D 122 SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP
SEQRES 6 D 122 VAL PHE GLU ARG ILE ALA GLY GLU ALA SER ARG LEU ALA
SEQRES 7 D 122 HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE
SEQRES 8 D 122 GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA
SEQRES 9 D 122 LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS
SEQRES 10 D 122 TYR THR SER ALA LYS
SEQRES 1 E 135 ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY GLY
SEQRES 2 E 135 LYS ALA PRO ARG LYS GLN LEU ALA THR LYS ALA ALA ARG
SEQRES 3 E 135 LYS SER ALA PRO ALA THR GLY GLY VAL LYS LYS PRO HIS
SEQRES 4 E 135 ARG TYR ARG PRO GLY THR VAL ALA LEU ARG GLU ILE ARG
SEQRES 5 E 135 ARG TYR GLN LYS SER THR GLU LEU LEU ILE ARG LYS LEU
SEQRES 6 E 135 PRO PHE GLN ARG LEU VAL ARG GLU ILE ALA GLN ASP PHE
SEQRES 7 E 135 LYS THR ASP LEU ARG PHE GLN SER SER ALA VAL MET ALA
SEQRES 8 E 135 LEU GLN GLU ALA SER GLU ALA TYR LEU VAL ALA LEU PHE
SEQRES 9 E 135 GLU ASP THR ASN LEU CYS ALA ILE HIS ALA LYS ARG VAL
SEQRES 10 E 135 THR ILE MET PRO LYS ASP ILE GLN LEU ALA ARG ARG ILE
SEQRES 11 E 135 ARG GLY GLU ARG ALA
SEQRES 1 F 102 SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY LYS GLY
SEQRES 2 F 102 GLY ALA LYS ARG HIS ARG LYS VAL LEU ARG ASP ASN ILE
SEQRES 3 F 102 GLN GLY ILE THR LYS PRO ALA ILE ARG ARG LEU ALA ARG
SEQRES 4 F 102 ARG GLY GLY VAL LYS ARG ILE SER GLY LEU ILE TYR GLU
SEQRES 5 F 102 GLU THR ARG GLY VAL LEU LYS VAL PHE LEU GLU ASN VAL
SEQRES 6 F 102 ILE ARG ASP ALA VAL THR TYR THR GLU HIS ALA LYS ARG
SEQRES 7 F 102 LYS THR VAL THR ALA MET ASP VAL VAL TYR ALA LEU LYS
SEQRES 8 F 102 ARG GLN GLY ARG THR LEU TYR GLY PHE GLY GLY
SEQRES 1 G 129 SER GLY ARG GLY LYS GLN GLY GLY LYS THR ARG ALA LYS
SEQRES 2 G 129 ALA LYS THR ARG SER SER ARG ALA GLY LEU GLN PHE PRO
SEQRES 3 G 129 VAL GLY ARG VAL HIS ARG LEU LEU ARG LYS GLY ASN TYR
SEQRES 4 G 129 ALA GLU ARG VAL GLY ALA GLY ALA PRO VAL TYR LEU ALA
SEQRES 5 G 129 ALA VAL LEU GLU TYR LEU THR ALA GLU ILE LEU GLU LEU
SEQRES 6 G 129 ALA GLY ASN ALA ALA ARG ASP ASN LYS LYS THR ARG ILE
SEQRES 7 G 129 ILE PRO ARG HIS LEU GLN LEU ALA VAL ARG ASN ASP GLU
SEQRES 8 G 129 GLU LEU ASN LYS LEU LEU GLY ARG VAL THR ILE ALA GLN
SEQRES 9 G 129 GLY GLY VAL LEU PRO ASN ILE GLN SER VAL LEU LEU PRO
SEQRES 10 G 129 LYS LYS THR GLU SER SER LYS SER ALA LYS SER LYS
SEQRES 1 H 122 ALA LYS SER ALA PRO ALA PRO LYS LYS GLY SER LYS LYS
SEQRES 2 H 122 ALA VAL THR LYS THR GLN LYS LYS ASP GLY LYS LYS ARG
SEQRES 3 H 122 ARG LYS THR ARG LYS GLU SER TYR ALA ILE TYR VAL TYR
SEQRES 4 H 122 LYS VAL LEU LYS GLN VAL HIS PRO ASP THR GLY ILE SER
SEQRES 5 H 122 SER LYS ALA MET SER ILE MET ASN SER PHE VAL ASN ASP
SEQRES 6 H 122 VAL PHE GLU ARG ILE ALA GLY GLU ALA SER ARG LEU ALA
SEQRES 7 H 122 HIS TYR ASN LYS ARG SER THR ILE THR SER ARG GLU ILE
SEQRES 8 H 122 GLN THR ALA VAL ARG LEU LEU LEU PRO GLY GLU LEU ALA
SEQRES 9 H 122 LYS HIS ALA VAL SER GLU GLY THR LYS ALA VAL THR LYS
SEQRES 10 H 122 TYR THR SER ALA LYS
SEQRES 1 I 167 DA DT DC DG DA DG DA DA DT DC DC DC DG
SEQRES 2 I 167 DG DT DG DC DC DG DA DG DG DC DC DG DC
SEQRES 3 I 167 DT DC DA DA DT DT DG DG DT DC DG DT DA
SEQRES 4 I 167 DG DA DC DA DG DC DT DC DT DA DG DC DA
SEQRES 5 I 167 DC DC DG DC DT DT DA DA DA DC DG DC DA
SEQRES 6 I 167 DC DG DT DA DC DG DC DG DC DT DG DT DC
SEQRES 7 I 167 DC DC DC DC DG DC DG DT DT DT DT DA DA
SEQRES 8 I 167 DC DC DG DC DC DA DA DG DG DG DG DA DT
SEQRES 9 I 167 DT DA DC DT DC DC DC DT DA DG DT DC DT
SEQRES 10 I 167 DC DC DA DG DG DC DA DC DG DT DG DT DC
SEQRES 11 I 167 DA DG DA DT DA DT DA DT DA DC DA DT DC
SEQRES 12 I 167 DC DT DG DA DA DG DC DT DT DG DT DC DG
SEQRES 13 I 167 DA DG DA DA DG DT DA DC DG DA DT
SEQRES 1 J 167 DA DT DC DG DT DA DC DT DT DC DT DC DG
SEQRES 2 J 167 DA DC DA DA DG DC DT DT DC DA DG DG DA
SEQRES 3 J 167 DT DG DT DA DT DA DT DA DT DC DT DG DA
SEQRES 4 J 167 DC DA DC DG DT DG DC DC DT DG DG DA DG
SEQRES 5 J 167 DA DC DT DA DG DG DG DA DG DT DA DA DT
SEQRES 6 J 167 DC DC DC DC DT DT DG DG DC DG DG DT DT
SEQRES 7 J 167 DA DA DA DA DC DG DC DG DG DG DG DG DA
SEQRES 8 J 167 DC DA DG DC DG DC DG DT DA DC DG DT DG
SEQRES 9 J 167 DC DG DT DT DT DA DA DG DC DG DG DT DG
SEQRES 10 J 167 DC DT DA DG DA DG DC DT DG DT DC DT DA
SEQRES 11 J 167 DC DG DA DC DC DA DA DT DT DG DA DG DC
SEQRES 12 J 167 DG DG DC DC DT DC DG DG DC DA DC DC DG
SEQRES 13 J 167 DG DG DA DT DT DC DT DC DG DA DT
SEQRES 1 O 735 ALA TYR ILE LYS LEU LEU ASP GLN THR LYS ASP THR ARG
SEQRES 2 O 735 ILE THR HIS LEU LEU ARG GLN THR ASN ALA PHE LEU ASP
SEQRES 3 O 735 SER LEU THR ARG ALA VAL LYS ASP GLN GLN LYS TYR THR
SEQRES 4 O 735 LYS GLU MET ILE ASP SER HIS ILE LYS GLU ALA SER GLU
SEQRES 5 O 735 GLU VAL ASP ASP LEU SER MET VAL PRO LYS MET LYS ASP
SEQRES 6 O 735 GLU GLU TYR ASP ASP ASP ASP ASP ASN SER ASN VAL ASP
SEQRES 7 O 735 TYR TYR ASN VAL ALA HIS ARG ILE LYS GLU ASP ILE LYS
SEQRES 8 O 735 LYS GLN PRO SER ILE LEU VAL GLY GLY THR LEU LYS ASP
SEQRES 9 O 735 TYR GLN ILE LYS GLY LEU GLN TRP MET VAL SER LEU PHE
SEQRES 10 O 735 ASN ASN HIS LEU ASN GLY ILE LEU ALA ASP GLU MET GLY
SEQRES 11 O 735 LEU GLY LYS THR ILE GLN THR ILE SER LEU LEU THR TYR
SEQRES 12 O 735 LEU TYR GLU MET LYS ASN ILE ARG GLY PRO TYR LEU VAL
SEQRES 13 O 735 ILE VAL PRO LEU SER THR LEU SER ASN TRP SER SER GLU
SEQRES 14 O 735 PHE ALA LYS TRP ALA PRO THR LEU ARG THR ILE SER PHE
SEQRES 15 O 735 LYS GLY SER PRO ASN GLU ARG LYS ALA LYS GLN ALA LYS
SEQRES 16 O 735 ILE ARG ALA GLY GLU PHE ASP VAL VAL LEU THR THR PHE
SEQRES 17 O 735 GLU TYR ILE ILE LYS GLU ARG ALA LEU LEU SER LYS VAL
SEQRES 18 O 735 LYS TRP VAL HIS MET ILE ILE ASP GLU GLY HIS ARG MET
SEQRES 19 O 735 LYS ASN ALA GLN SER LYS LEU SER LEU THR LEU ASN THR
SEQRES 20 O 735 HIS TYR HIS ALA ASP TYR ARG LEU ILE LEU THR GLY THR
SEQRES 21 O 735 PRO LEU GLN ASN ASN LEU PRO GLU LEU TRP ALA LEU LEU
SEQRES 22 O 735 ASN PHE VAL LEU PRO LYS ILE PHE ASN SER VAL LYS SER
SEQRES 23 O 735 PHE ASP GLU TRP PHE ASN THR PRO PHE ALA ASN THR GLY
SEQRES 24 O 735 GLY GLN ASP LYS ILE GLU LEU SER GLU GLU GLU THR LEU
SEQRES 25 O 735 LEU VAL ILE ARG ARG LEU HIS LYS VAL LEU ARG PRO PHE
SEQRES 26 O 735 LEU LEU ARG ARG LEU LYS LYS ASP VAL GLU LYS GLU LEU
SEQRES 27 O 735 PRO ASP LYS VAL GLU LYS VAL VAL LYS CYS LYS MET SER
SEQRES 28 O 735 ALA LEU GLN GLN ILE MET TYR GLN GLN MET LEU LYS TYR
SEQRES 29 O 735 ARG ARG LEU PHE ILE GLY ASP GLN ASN ASN LYS LYS MET
SEQRES 30 O 735 VAL GLY LEU ARG GLY PHE ASN ASN GLN ILE MET GLN LEU
SEQRES 31 O 735 LYS LYS ILE CYS ASN HIS PRO PHE VAL PHE GLU GLU VAL
SEQRES 32 O 735 GLU ASP GLN ILE ASN PRO THR ARG GLU THR ASN ASP ASP
SEQRES 33 O 735 ILE TRP ARG VAL ALA GLY LYS PHE GLU LEU LEU ASP ARG
SEQRES 34 O 735 ILE LEU PRO LYS LEU LYS ALA THR GLY HIS ARG VAL LEU
SEQRES 35 O 735 ILE PHE PHE GLN MET THR GLN ILE MET ASP ILE MET GLU
SEQRES 36 O 735 ASP PHE LEU ARG TYR ILE ASN ILE LYS TYR LEU ARG LEU
SEQRES 37 O 735 ASP GLY HIS THR LYS SER ASP GLU ARG SER GLU LEU LEU
SEQRES 38 O 735 ARG LEU PHE ASN ALA PRO ASP SER GLU TYR LEU CYS PHE
SEQRES 39 O 735 ILE LEU SER THR ARG ALA GLY GLY LEU GLY LEU ASN LEU
SEQRES 40 O 735 GLN THR ALA ASP THR VAL ILE ILE PHE ASP THR ASP TRP
SEQRES 41 O 735 ASN PRO HIS GLN ASP LEU GLN ALA GLN ASP ARG ALA HIS
SEQRES 42 O 735 ARG ILE GLY GLN LYS ASN GLU VAL ARG ILE LEU ARG LEU
SEQRES 43 O 735 ILE THR THR ASN SER VAL GLU GLU VAL ILE LEU GLU ARG
SEQRES 44 O 735 ALA TYR LYS LYS LEU ASP ILE ASP GLY LYS VAL ILE GLN
SEQRES 45 O 735 ALA GLY LYS PHE ASP ASN LYS SER THR SER GLU GLU GLN
SEQRES 46 O 735 GLU ALA LEU LEU ARG SER LEU LEU ASP ALA GLU GLU GLU
SEQRES 47 O 735 ARG ARG LYS LYS ARG GLU SER GLY VAL GLU GLU GLU GLU
SEQRES 48 O 735 GLU LEU LYS ASP SER GLU ILE ASN GLU ILE LEU ALA ARG
SEQRES 49 O 735 ASN ASP GLU GLU MET ALA VAL LEU THR ARG MET ASP GLU
SEQRES 50 O 735 ASP ARG SER LYS LYS GLU GLU GLU LEU GLY VAL LYS SER
SEQRES 51 O 735 ARG LEU LEU GLU LYS SER GLU LEU PRO ASP ILE TYR SER
SEQRES 52 O 735 ARG ASP ILE GLY ALA GLU LEU LYS ARG GLU GLU SER GLU
SEQRES 53 O 735 SER ALA ALA VAL TYR ASN GLY ARG GLY ALA ARG GLU ARG
SEQRES 54 O 735 LYS THR ALA THR TYR ASN ASP ASN MET SER GLU GLU GLN
SEQRES 55 O 735 TRP LEU ARG GLN PHE GLU VAL SER ASP ASP GLU LYS ASN
SEQRES 56 O 735 ASP LYS GLN ALA ARG LYS GLN ARG THR LYS LYS GLU ASP
SEQRES 57 O 735 LYS SER GLU ALA ILE ASP GLY
HELIX 1 AA1 GLY A 44 SER A 57 1 14
HELIX 2 AA2 ARG A 63 LYS A 79 1 17
HELIX 3 AA3 GLN A 85 ALA A 114 1 30
HELIX 4 AA4 MET A 120 ARG A 131 1 12
HELIX 5 AA5 ASP B 24 ILE B 29 5 6
HELIX 6 AA6 THR B 30 GLY B 42 1 13
HELIX 7 AA7 GLY B 48 ALA B 76 1 29
HELIX 8 AA8 THR B 82 GLY B 94 1 13
HELIX 9 AA9 THR C 16 ALA C 21 1 6
HELIX 10 AB1 PRO C 26 GLY C 37 1 12
HELIX 11 AB2 GLY C 46 ASN C 73 1 28
HELIX 12 AB3 ILE C 79 ASP C 90 1 12
HELIX 13 AB4 ASP C 90 GLY C 98 1 9
HELIX 14 AB5 ALA D 35 HIS D 46 1 12
HELIX 15 AB6 SER D 52 ASN D 81 1 30
HELIX 16 AB7 THR D 87 LEU D 99 1 13
HELIX 17 AB8 GLU D 102 SER D 120 1 19
HELIX 18 AB9 GLY E 44 SER E 57 1 14
HELIX 19 AC1 ARG E 63 LYS E 79 1 17
HELIX 20 AC2 GLN E 85 ALA E 114 1 30
HELIX 21 AC3 MET E 120 ARG E 131 1 12
HELIX 22 AC4 THR F 30 GLY F 41 1 12
HELIX 23 AC5 LEU F 49 ALA F 76 1 28
HELIX 24 AC6 THR F 82 GLY F 94 1 13
HELIX 25 AC7 THR G 16 ALA G 21 1 6
HELIX 26 AC8 PRO G 26 GLY G 37 1 12
HELIX 27 AC9 GLY G 46 ASN G 73 1 28
HELIX 28 AD1 ILE G 79 ASP G 90 1 12
HELIX 29 AD2 ASP G 90 GLY G 98 1 9
HELIX 30 AD3 ALA H 35 HIS H 46 1 12
HELIX 31 AD4 SER H 52 ASN H 81 1 30
HELIX 32 AD5 THR H 87 LEU H 99 1 13
HELIX 33 AD6 GLU H 102 SER H 120 1 19
HELIX 34 AD7 THR O 674 LEU O 683 1 10
HELIX 35 AD8 LEU O 683 PHE O 689 1 7
HELIX 36 AD9 TYR O 744 ARG O 750 1 7
HELIX 37 AE1 LYS O 768 HIS O 785 1 18
HELIX 38 AE2 GLY O 797 TYR O 810 1 14
HELIX 39 AE3 THR O 827 TRP O 838 1 12
HELIX 40 AE4 SER O 850 ALA O 863 1 14
HELIX 41 AE5 GLU O 879 VAL O 886 1 8
HELIX 42 AE6 SER O 904 HIS O 913 1 10
HELIX 43 AE7 LYS O 944 THR O 958 1 15
HELIX 44 AE8 LYS O 968 GLU O 973 1 6
HELIX 45 AE9 GLU O 975 LEU O 987 1 13
HELIX 46 AF1 LEU O 995 VAL O 999 5 5
HELIX 47 AF2 GLN O 1020 ARG O 1031 1 12
HELIX 48 AF3 LEU O 1055 HIS O 1061 1 7
HELIX 49 AF4 VAL O 1068 ASN O 1073 1 6
HELIX 50 AF5 ILE O 1082 VAL O 1085 5 4
HELIX 51 AF6 ALA O 1086 LEU O 1091 1 6
HELIX 52 AF7 LEU O 1091 GLY O 1103 1 13
HELIX 53 AF8 THR O 1113 ASN O 1127 1 15
HELIX 54 AF9 ASP O 1134 LYS O 1138 5 5
HELIX 55 AG1 SER O 1139 ASN O 1150 1 12
HELIX 56 AG2 PRO O 1187 HIS O 1198 1 12
HELIX 57 AG3 VAL O 1217 TYR O 1226 1 10
HELIX 58 AG4 LEU O 1229 ILE O 1231 5 3
HELIX 59 AG5 ASP O 1232 ASN O 1243 1 12
HELIX 60 AG6 THR O 1246 GLN O 1250 5 5
HELIX 61 AG7 LEU O 1253 ASP O 1259 1 7
HELIX 62 AG8 GLU O 1261 GLU O 1269 1 9
HELIX 63 AG9 LYS O 1279 LEU O 1287 1 9
HELIX 64 AH1 ASN O 1290 LYS O 1307 1 18
HELIX 65 AH2 GLU O 1338 ALA O 1343 1 6
HELIX 66 AH3 ALA O 1344 ASN O 1347 5 4
SHEET 1 AA1 2 ARG A 83 PHE A 84 0
SHEET 2 AA1 2 THR B 80 VAL B 81 1 O VAL B 81 N ARG A 83
SHEET 1 AA2 2 THR E 118 ILE E 119 0
SHEET 2 AA2 2 ARG F 45 ILE F 46 1 O ARG F 45 N ILE E 119
SHEET 1 AA3 6 ILE O 789 LEU O 790 0
SHEET 2 AA3 6 TYR O 918 LEU O 922 1 O ILE O 921 N LEU O 790
SHEET 3 AA3 6 HIS O 890 ILE O 892 1 N MET O 891 O TYR O 918
SHEET 4 AA3 6 TYR O 819 VAL O 821 1 N LEU O 820 O ILE O 892
SHEET 5 AA3 6 VAL O 868 VAL O 869 1 O VAL O 869 N VAL O 821
SHEET 6 AA3 6 THR O 844 ILE O 845 1 N ILE O 845 O VAL O 868
SHEET 1 AA4 5 TYR O1130 LEU O1131 0
SHEET 2 AA4 5 CYS O1158 SER O1162 1 O ILE O1160 N LEU O1131
SHEET 3 AA4 5 VAL O1106 PHE O1110 1 N ILE O1108 O PHE O1159
SHEET 4 AA4 5 THR O1177 ILE O1180 1 O THR O1177 N LEU O1107
SHEET 5 AA4 5 ARG O1207 ARG O1210 1 O LEU O1209 N ILE O1180
CISPEP 1 GLY O 817 PRO O 818 0 -3.63
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 0.004735 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004735 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004735 0.00000
(ATOM LINES ARE NOT SHOWN.)
END