HEADER MEMBRANE PROTEIN 05-AUG-19 6SGZ
TITLE STRUCTURE OF PROTOMER 2 OF THE ESX-3 CORE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESX-3 SECRETION SYSTEM PROTEIN ECCD3;
COMPND 3 CHAIN: E, H;
COMPND 4 SYNONYM: ESX CONSERVED COMPONENT D3,TYPE VII SECRETION SYSTEM PROTEIN
COMPND 5 ECCD3,T7SS PROTEIN ECCD3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ESX-3 SECRETION SYSTEM ATPASE ECCB3;
COMPND 9 CHAIN: I;
COMPND 10 SYNONYM: ESX CONSERVED COMPONENT B3,TYPE VII SECRETION SYSTEM PROTEIN
COMPND 11 ECCB3,T7SS PROTEIN ECCB3;
COMPND 12 EC: 3.6.-.-;
COMPND 13 ENGINEERED: YES;
COMPND 14 MOL_ID: 3;
COMPND 15 MOLECULE: ESX-3 SECRETION SYSTEM PROTEIN ECCC3;
COMPND 16 CHAIN: J;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: ESX-3 SECRETION SYSTEM PROTEIN ECCE3;
COMPND 20 CHAIN: D;
COMPND 21 SYNONYM: ESX CONSERVED COMPONENT E3,TYPE VII SECRETION SYSTEM PROTEIN
COMPND 22 ECCE3,T7SS PROTEIN ECCE3;
COMPND 23 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS (STRAIN ATCC 700084 /
SOURCE 3 MC(2)155);
SOURCE 4 ORGANISM_TAXID: 246196;
SOURCE 5 STRAIN: ATCC 700084 / MC(2)155;
SOURCE 6 GENE: ECCD3, SNM, MSMEG_0623, MSMEI_0607;
SOURCE 7 EXPRESSION_SYSTEM: MYCOLICIBACTERIUM SMEGMATIS MC2 155;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 246196;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS (STRAIN ATCC 700084 /
SOURCE 11 MC(2)155);
SOURCE 12 ORGANISM_TAXID: 246196;
SOURCE 13 STRAIN: ATCC 700084 / MC(2)155;
SOURCE 14 GENE: ECCB3, MSMEG_0616, MSMEI_0600;
SOURCE 15 EXPRESSION_SYSTEM: MYCOLICIBACTERIUM SMEGMATIS MC2 155;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 246196;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS (STRAIN ATCC 700084 /
SOURCE 19 MC(2)155);
SOURCE 20 ORGANISM_TAXID: 246196;
SOURCE 21 GENE: ECCC3, MSMEG_0617, MSMEI_0601;
SOURCE 22 EXPRESSION_SYSTEM: MYCOLICIBACTERIUM SMEGMATIS MC2 155;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 246196;
SOURCE 24 MOL_ID: 4;
SOURCE 25 ORGANISM_SCIENTIFIC: MYCOBACTERIUM SMEGMATIS (STRAIN ATCC 700084 /
SOURCE 26 MC(2)155);
SOURCE 27 ORGANISM_TAXID: 246196;
SOURCE 28 STRAIN: ATCC 700084 / MC(2)155;
SOURCE 29 GENE: ECCE3, MSMEG_0626, MSMEI_0609;
SOURCE 30 EXPRESSION_SYSTEM: MYCOLICIBACTERIUM SMEGMATIS MC2 155;
SOURCE 31 EXPRESSION_SYSTEM_TAXID: 246196
KEYWDS TYPE VII SECRETION SYSTEM ESX-3 SECRETION SYSTEM T7SS ESX-3
KEYWDS 2 MYCOBACTERIUM SMEGMATIS, MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR N.FAMELIS,A.RIVERA-CALZADA,O.LLORCA,S.GEIBEL
REVDAT 3 25-DEC-19 6SGZ 1 JRNL
REVDAT 2 23-OCT-19 6SGZ 1 JRNL
REVDAT 1 09-OCT-19 6SGZ 0
JRNL AUTH N.FAMELIS,A.RIVERA-CALZADA,G.DEGLIESPOSTI,M.WINGENDER,
JRNL AUTH 2 N.MIETRACH,J.M.SKEHEL,R.FERNANDEZ-LEIRO,B.BOTTCHER,
JRNL AUTH 3 A.SCHLOSSER,O.LLORCA,S.GEIBEL
JRNL TITL ARCHITECTURE OF THE MYCOBACTERIAL TYPE VII SECRETION SYSTEM.
JRNL REF NATURE V. 576 321 2019
JRNL REFN ESSN 1476-4687
JRNL PMID 31597161
JRNL DOI 10.1038/S41586-019-1633-1
REMARK 2
REMARK 2 RESOLUTION. 3.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : EPU, GCTF, PHENIX, RELION, RELION,
REMARK 3 RELION, 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 : REAL
REMARK 3 REFINEMENT PROTOCOL : AB INITIO MODEL
REMARK 3 REFINEMENT TARGET : MAP CORRELATION COEFFICIENT
REMARK 3 OVERALL ANISOTROPIC B VALUE : 29.400
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) : 3.900
REMARK 3 NUMBER OF PARTICLES : 160062
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: IN ORDER TO GET THE BEST POSSIBLE RESOLUTION FOR
REMARK 3 PROTOMER 2, THE EXTRA DENSITY NOT CORRESPONDING TO THIS PROTOMER
REMARK 3 WAS MASKED OUT DURING THE REFINEMENT.
REMARK 4
REMARK 4 6SGZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-AUG-19.
REMARK 100 THE DEPOSITION ID IS D_1292103705.
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 : PROTOMER2 OF THE ESX-3 CORE
REMARK 245 COMPLEX; ESX-3 SECRETION SYSTEM
REMARK 245 PROTEIN ECCD3; ESX-3 SECRETION
REMARK 245 SYSTEM PROTEIN ECCB3; ESX-3
REMARK 245 SECRETION SYSTEM PROTEIN ECCC3;
REMARK 245 ESX-3 SECRETION SYSTEM PROTEIN
REMARK 245 ECCD3
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.30
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : BLOTTING TIME: 3S BLOTTING
REMARK 245 FORCE: -10
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
REMARK 245 SAMPLE DETAILS : ESX-3 CORE COMPLEX THE SAMPLE
REMARK 245 CONSISTS OF FOUR PROTEIN COMPONENTS, ECCB3:ECCC3:ECCD3:ECCE3 IN
REMARK 245 A 1:1:2:1 STOICHIOMETRY MOLECULAR WEIGHT OF THE COMPLEX WITHOUT
REMARK 245 THE AMPHIPOL MICELLE: 0.65 MDA
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 11903
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : FEI FALCON III (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : 1600.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 2600.00
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) : 50.00
REMARK 245 ILLUMINATION MODE : SPOT SCAN
REMARK 245 NOMINAL MAGNIFICATION : 75000
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 71850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -144.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, H, I, J, D
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 PRO E 48
REMARK 465 ALA E 49
REMARK 465 ARG E 50
REMARK 465 GLU E 51
REMARK 465 ASN E 52
REMARK 465 ASP E 53
REMARK 465 GLY E 54
REMARK 465 ALA E 55
REMARK 465 ALA E 56
REMARK 465 ASP E 57
REMARK 465 PRO E 58
REMARK 465 ALA E 59
REMARK 465 ALA E 60
REMARK 465 ALA E 61
REMARK 465 PRO E 62
REMARK 465 ASN E 63
REMARK 465 VAL E 300
REMARK 465 ILE E 301
REMARK 465 PRO E 302
REMARK 465 ALA E 303
REMARK 465 PRO E 304
REMARK 465 GLY E 305
REMARK 465 ASP E 306
REMARK 465 PRO E 307
REMARK 465 THR E 308
REMARK 465 PRO E 309
REMARK 465 ALA E 310
REMARK 465 ALA E 311
REMARK 465 ARG E 312
REMARK 465 PRO E 313
REMARK 465 LEU E 314
REMARK 465 VAL E 472
REMARK 465 VAL H 6
REMARK 465 MET H 7
REMARK 465 ALA H 17
REMARK 465 GLY H 18
REMARK 465 ASP H 19
REMARK 465 ASP H 20
REMARK 465 PRO H 48
REMARK 465 ALA H 49
REMARK 465 ARG H 50
REMARK 465 GLU H 51
REMARK 465 ASN H 52
REMARK 465 ASP H 53
REMARK 465 GLY H 54
REMARK 465 ALA H 55
REMARK 465 ALA H 56
REMARK 465 ASP H 57
REMARK 465 PRO H 58
REMARK 465 ALA H 59
REMARK 465 ALA H 60
REMARK 465 ALA H 61
REMARK 465 PRO H 62
REMARK 465 ASN H 63
REMARK 465 PRO H 64
REMARK 465 PHE H 212
REMARK 465 GLY H 213
REMARK 465 PRO J 301
REMARK 465 LEU J 302
REMARK 465 PHE J 303
REMARK 465 PRO J 304
REMARK 465 ALA J 305
REMARK 465 GLU J 306
REMARK 465 SER J 307
REMARK 465 GLY J 308
REMARK 465 ALA J 309
REMARK 465 ALA J 310
REMARK 465 LYS J 331
REMARK 465 PRO J 332
REMARK 465 GLY J 333
REMARK 465 GLY J 373
REMARK 465 GLY J 374
REMARK 465 ALA D 42
REMARK 465 TRP D 43
REMARK 465 TRP D 44
REMARK 465 LYS D 45
REMARK 465 GLY D 46
REMARK 465 ALA D 65
REMARK 465 GLU D 66
REMARK 465 ASP D 67
REMARK 465 THR D 68
REMARK 465 VAL D 69
REMARK 465 GLU D 70
REMARK 465 THR D 71
REMARK 465 SER D 179
REMARK 465 GLY D 180
REMARK 465 LYS D 181
REMARK 465 GLU D 182
REMARK 465 THR D 183
REMARK 465 TRP D 184
REMARK 465 ARG D 185
REMARK 465 GLY D 186
REMARK 465 VAL D 187
REMARK 465 ALA D 188
REMARK 465 ASP D 189
REMARK 465 ASP D 190
REMARK 465 ALA D 191
REMARK 465 GLY D 192
REMARK 465 VAL D 193
REMARK 465 ASP D 202
REMARK 465 ASP D 203
REMARK 465 ARG D 204
REMARK 465 LEU D 205
REMARK 465 GLY D 213
REMARK 465 HIS D 214
REMARK 465 LEU D 215
REMARK 465 THR D 243
REMARK 465 SER D 244
REMARK 465 ASP D 245
REMARK 465 ARG D 246
REMARK 465 PRO D 247
REMARK 465 ALA D 248
REMARK 465 ALA D 249
REMARK 465 LYS D 250
REMARK 465 ALA D 251
REMARK 465 ARG D 262
REMARK 465 HIS D 263
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 ALA E 105 71.36 57.79
REMARK 500 PRO E 129 45.38 -84.09
REMARK 500 ALA E 186 -4.00 66.35
REMARK 500 VAL E 208 73.90 52.61
REMARK 500 PHE E 212 -12.04 73.36
REMARK 500 ARG E 239 -158.90 -159.24
REMARK 500 ASP E 319 47.73 -91.46
REMARK 500 ASN E 354 15.12 54.56
REMARK 500 ASP E 378 10.46 57.48
REMARK 500 PRO E 431 73.32 -69.89
REMARK 500 LEU H 33 145.74 -170.21
REMARK 500 ALA H 105 76.15 55.07
REMARK 500 PRO H 106 4.98 -63.27
REMARK 500 GLN H 126 -167.54 -79.59
REMARK 500 ILE H 157 -62.79 -96.43
REMARK 500 VAL H 187 -51.53 -125.09
REMARK 500 ARG H 239 -7.65 71.70
REMARK 500 ALA H 242 -36.20 -35.24
REMARK 500 GLN H 285 52.85 -94.03
REMARK 500 ASP H 306 66.39 -156.09
REMARK 500 TYR H 407 -3.65 67.83
REMARK 500 PRO H 431 47.99 -74.51
REMARK 500 LYS J 19 50.89 -91.86
REMARK 500 PRO J 28 -177.71 -66.54
REMARK 500 LEU J 30 75.11 53.68
REMARK 500 PRO J 133 43.24 -77.30
REMARK 500 GLN J 145 -67.43 -95.66
REMARK 500 HIS J 163 -164.69 -161.13
REMARK 500 LEU J 167 74.68 59.91
REMARK 500 ASP J 168 -35.68 -34.91
REMARK 500 ALA J 170 -60.05 -92.25
REMARK 500 ASP J 175 97.93 -69.09
REMARK 500 ASP J 178 -172.88 -69.03
REMARK 500 ARG J 201 -168.23 -75.66
REMARK 500 ALA J 213 -6.32 68.04
REMARK 500 ARG J 214 136.36 -170.52
REMARK 500 SER J 255 31.87 -140.27
REMARK 500 ASP J 257 -150.30 -77.34
REMARK 500 TRP J 258 -7.02 -41.48
REMARK 500 ASN J 271 65.72 60.03
REMARK 500 ASP J 274 24.58 49.68
REMARK 500 ALA J 279 -50.50 -122.44
REMARK 500 ALA J 298 88.19 -150.67
REMARK 500 ASP J 299 -1.72 -142.24
REMARK 500 ASP J 324 77.87 44.91
REMARK 500 PRO J 325 -178.94 -67.56
REMARK 500 ASN J 348 -61.88 -92.65
REMARK 500 TYR J 352 73.35 53.36
REMARK 500 ALA J 363 -168.26 -78.92
REMARK 500 GLN J 376 73.32 51.63
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-10191 RELATED DB: EMDB
REMARK 900 STRUCTURE OF PROTOMER 2 OF THE ESX-3 CORE COMPLEX
DBREF 6SGZ E 6 472 UNP A0QQ46 ECCD3_MYCS2 6 472
DBREF 6SGZ H 6 472 UNP A0QQ46 ECCD3_MYCS2 6 472
DBREF 6SGZ I 33 91 UNP A0QQ39 ECCB3_MYCS2 33 91
DBREF 6SGZ J 1 403 PDB 6SGZ 6SGZ 1 403
DBREF 6SGZ D 2 287 UNP A0QQ48 ECCE3_MYCS2 2 287
SEQRES 1 E 467 VAL MET PRO ILE VAL ARG VAL ALA VAL LEU ALA ALA GLY
SEQRES 2 E 467 ASP ASP GLY GLY ARG LEU THR GLU MET ALA LEU PRO SER
SEQRES 3 E 467 GLU LEU PRO LEU ARG GLU ILE LEU PRO ALA VAL GLN ARG
SEQRES 4 E 467 ILE VAL GLN PRO ALA ARG GLU ASN ASP GLY ALA ALA ASP
SEQRES 5 E 467 PRO ALA ALA ALA PRO ASN PRO VAL ARG LEU SER LEU ALA
SEQRES 6 E 467 PRO ILE GLY GLY ALA PRO PHE SER LEU ASP ALA THR LEU
SEQRES 7 E 467 ASP THR VAL GLY VAL VAL ASP GLY ASP LEU LEU ALA LEU
SEQRES 8 E 467 GLN ALA VAL PRO SER GLY PRO PRO ALA PRO ARG ILE VAL
SEQRES 9 E 467 GLU ASP ILE ALA ASP ALA ALA VAL ILE PHE SER GLU ALA
SEQRES 10 E 467 ARG ARG ARG GLN TRP GLY PRO THR HIS ILE ALA ARG GLY
SEQRES 11 E 467 ALA ALA LEU ALA LEU ILE GLY LEU ILE LEU VAL GLY THR
SEQRES 12 E 467 GLY LEU SER VAL ALA HIS ARG VAL ILE THR GLY ASP LEU
SEQRES 13 E 467 LEU GLY GLN PHE ILE VAL SER GLY ILE ALA LEU ALA THR
SEQRES 14 E 467 VAL ILE ALA ALA LEU ALA VAL ARG ASN ARG SER ALA VAL
SEQRES 15 E 467 LEU ALA THR SER LEU ALA VAL THR ALA LEU VAL PRO VAL
SEQRES 16 E 467 ALA ALA ALA PHE ALA LEU GLY VAL PRO GLY ASP PHE GLY
SEQRES 17 E 467 ALA PRO ASN VAL LEU LEU ALA ALA ALA GLY VAL ALA ALA
SEQRES 18 E 467 TRP SER LEU ILE SER MET ALA GLY SER PRO ASP ASP ARG
SEQRES 19 E 467 GLY ILE ALA VAL PHE THR ALA THR ALA VAL THR GLY VAL
SEQRES 20 E 467 GLY VAL LEU LEU VAL ALA GLY ALA ALA SER LEU TRP VAL
SEQRES 21 E 467 ILE SER SER ASP VAL ILE GLY CYS ALA LEU VAL LEU LEU
SEQRES 22 E 467 GLY LEU ILE VAL THR VAL GLN ALA ALA GLN LEU SER ALA
SEQRES 23 E 467 MET TRP ALA ARG PHE PRO LEU PRO VAL ILE PRO ALA PRO
SEQRES 24 E 467 GLY ASP PRO THR PRO ALA ALA ARG PRO LEU SER VAL LEU
SEQRES 25 E 467 ALA ASP LEU PRO ARG ARG VAL ARG VAL SER GLN ALA HIS
SEQRES 26 E 467 GLN THR GLY VAL ILE ALA ALA GLY VAL LEU LEU GLY VAL
SEQRES 27 E 467 ALA GLY SER VAL ALA LEU VAL SER SER ALA ASN ALA SER
SEQRES 28 E 467 PRO TRP ALA TRP TYR ILE VAL VAL ALA ALA ALA ALA GLY
SEQRES 29 E 467 ALA ALA LEU ARG ALA ARG VAL TRP ASP SER ALA ALA CYS
SEQRES 30 E 467 LYS ALA TRP LEU LEU GLY HIS SER TYR LEU LEU ALA VAL
SEQRES 31 E 467 ALA LEU LEU VAL ALA PHE VAL ILE GLY ASP ARG TYR GLN
SEQRES 32 E 467 ALA ALA LEU TRP ALA LEU ALA ALA LEU ALA VAL LEU VAL
SEQRES 33 E 467 LEU VAL TRP ILE VAL ALA ALA LEU ASN PRO LYS ILE ALA
SEQRES 34 E 467 SER PRO ASP THR TYR SER LEU PRO MET ARG ARG MET VAL
SEQRES 35 E 467 GLY PHE LEU ALA THR GLY LEU ASP ALA SER LEU ILE PRO
SEQRES 36 E 467 VAL MET ALA LEU LEU VAL GLY LEU PHE SER LEU VAL
SEQRES 1 H 467 VAL MET PRO ILE VAL ARG VAL ALA VAL LEU ALA ALA GLY
SEQRES 2 H 467 ASP ASP GLY GLY ARG LEU THR GLU MET ALA LEU PRO SER
SEQRES 3 H 467 GLU LEU PRO LEU ARG GLU ILE LEU PRO ALA VAL GLN ARG
SEQRES 4 H 467 ILE VAL GLN PRO ALA ARG GLU ASN ASP GLY ALA ALA ASP
SEQRES 5 H 467 PRO ALA ALA ALA PRO ASN PRO VAL ARG LEU SER LEU ALA
SEQRES 6 H 467 PRO ILE GLY GLY ALA PRO PHE SER LEU ASP ALA THR LEU
SEQRES 7 H 467 ASP THR VAL GLY VAL VAL ASP GLY ASP LEU LEU ALA LEU
SEQRES 8 H 467 GLN ALA VAL PRO SER GLY PRO PRO ALA PRO ARG ILE VAL
SEQRES 9 H 467 GLU ASP ILE ALA ASP ALA ALA VAL ILE PHE SER GLU ALA
SEQRES 10 H 467 ARG ARG ARG GLN TRP GLY PRO THR HIS ILE ALA ARG GLY
SEQRES 11 H 467 ALA ALA LEU ALA LEU ILE GLY LEU ILE LEU VAL GLY THR
SEQRES 12 H 467 GLY LEU SER VAL ALA HIS ARG VAL ILE THR GLY ASP LEU
SEQRES 13 H 467 LEU GLY GLN PHE ILE VAL SER GLY ILE ALA LEU ALA THR
SEQRES 14 H 467 VAL ILE ALA ALA LEU ALA VAL ARG ASN ARG SER ALA VAL
SEQRES 15 H 467 LEU ALA THR SER LEU ALA VAL THR ALA LEU VAL PRO VAL
SEQRES 16 H 467 ALA ALA ALA PHE ALA LEU GLY VAL PRO GLY ASP PHE GLY
SEQRES 17 H 467 ALA PRO ASN VAL LEU LEU ALA ALA ALA GLY VAL ALA ALA
SEQRES 18 H 467 TRP SER LEU ILE SER MET ALA GLY SER PRO ASP ASP ARG
SEQRES 19 H 467 GLY ILE ALA VAL PHE THR ALA THR ALA VAL THR GLY VAL
SEQRES 20 H 467 GLY VAL LEU LEU VAL ALA GLY ALA ALA SER LEU TRP VAL
SEQRES 21 H 467 ILE SER SER ASP VAL ILE GLY CYS ALA LEU VAL LEU LEU
SEQRES 22 H 467 GLY LEU ILE VAL THR VAL GLN ALA ALA GLN LEU SER ALA
SEQRES 23 H 467 MET TRP ALA ARG PHE PRO LEU PRO VAL ILE PRO ALA PRO
SEQRES 24 H 467 GLY ASP PRO THR PRO ALA ALA ARG PRO LEU SER VAL LEU
SEQRES 25 H 467 ALA ASP LEU PRO ARG ARG VAL ARG VAL SER GLN ALA HIS
SEQRES 26 H 467 GLN THR GLY VAL ILE ALA ALA GLY VAL LEU LEU GLY VAL
SEQRES 27 H 467 ALA GLY SER VAL ALA LEU VAL SER SER ALA ASN ALA SER
SEQRES 28 H 467 PRO TRP ALA TRP TYR ILE VAL VAL ALA ALA ALA ALA GLY
SEQRES 29 H 467 ALA ALA LEU ARG ALA ARG VAL TRP ASP SER ALA ALA CYS
SEQRES 30 H 467 LYS ALA TRP LEU LEU GLY HIS SER TYR LEU LEU ALA VAL
SEQRES 31 H 467 ALA LEU LEU VAL ALA PHE VAL ILE GLY ASP ARG TYR GLN
SEQRES 32 H 467 ALA ALA LEU TRP ALA LEU ALA ALA LEU ALA VAL LEU VAL
SEQRES 33 H 467 LEU VAL TRP ILE VAL ALA ALA LEU ASN PRO LYS ILE ALA
SEQRES 34 H 467 SER PRO ASP THR TYR SER LEU PRO MET ARG ARG MET VAL
SEQRES 35 H 467 GLY PHE LEU ALA THR GLY LEU ASP ALA SER LEU ILE PRO
SEQRES 36 H 467 VAL MET ALA LEU LEU VAL GLY LEU PHE SER LEU VAL
SEQRES 1 I 59 VAL THR ARG HIS GLN VAL SER GLY TRP ARG PHE VAL MET
SEQRES 2 I 59 ARG ARG ILE ALA SER GLY VAL ALA LEU HIS ASP THR ARG
SEQRES 3 I 59 MET LEU VAL ASP PRO LEU ARG THR GLN SER ARG ALA VAL
SEQRES 4 I 59 LEU THR GLY ALA LEU ILE LEU VAL THR GLY LEU VAL GLY
SEQRES 5 I 59 CYS PHE ILE PHE SER LEU PHE
SEQRES 1 J 343 MET SER ARG LEU ILE PHE GLU HIS GLN ARG ARG LEU THR
SEQRES 2 J 343 PRO PRO THR THR ARG LYS GLY THR ILE THR ILE GLU PRO
SEQRES 3 J 343 PRO PRO GLN LEU PRO MET ARG THR GLU GLU VAL ASP ALA
SEQRES 4 J 343 GLU ARG ALA ASP TYR LEU ARG TYR LEU SER VAL VAL ARG
SEQRES 5 J 343 ASP ASN VAL ARG ALA HIS ALA ALA GLU GLN ARG ALA ALA
SEQRES 6 J 343 LEU GLU TRP SER HIS PRO GLU PRO GLU VAL LEU ALA THR
SEQRES 7 J 343 ILE PRO GLY THR ARG ARG GLN TRP GLU ARG ASP PRO ARG
SEQRES 8 J 343 ASP ARG ASP PHE LEU VAL LEU ARG ALA GLY ARG HIS ASP
SEQRES 9 J 343 VAL PRO LEU ASP ALA ALA LEU LYS VAL LYS ASP THR ALA
SEQRES 10 J 343 ASP GLU ILE ASP LEU GLU PRO VAL ALA HIS SER ALA LEU
SEQRES 11 J 343 ARG GLY LEU LEU ASP VAL GLN ARG THR VAL ARG ASP ALA
SEQRES 12 J 343 PRO THR GLY LEU ASP VAL ALA LYS LEU ALA ARG ILE THR
SEQRES 13 J 343 VAL ILE GLY GLU ALA ASP GLU ALA ARG ALA ALA ILE ARG
SEQRES 14 J 343 ALA TRP ILE ALA GLN ALA VAL THR TRP HIS ASP PRO THR
SEQRES 15 J 343 MET LEU GLY VAL ALA LEU ALA ALA PRO ASP LEU GLU SER
SEQRES 16 J 343 GLY ASP TRP SER TRP LEU LYS TRP LEU PRO HIS VAL ASP
SEQRES 17 J 343 VAL PRO ASN GLU ALA ASP GLY VAL GLY PRO ALA ARG TYR
SEQRES 18 J 343 LEU THR THR SER THR ALA GLU LEU ARG GLU ARG LEU ALA
SEQRES 19 J 343 PRO ALA LEU ALA ASP ARG PRO LEU PHE PRO ALA GLU SER
SEQRES 20 J 343 GLY ALA ALA LEU LYS HIS LEU LEU VAL VAL LEU ASP ASP
SEQRES 21 J 343 PRO ASP ALA ASP PRO ASP ASP ILE ALA ARG LYS PRO GLY
SEQRES 22 J 343 LEU THR GLY VAL THR VAL ILE HIS ARG THR THR GLU LEU
SEQRES 23 J 343 PRO ASN ARG GLU GLN TYR PRO ASP PRO GLU ARG PRO ILE
SEQRES 24 J 343 LEU ARG VAL ALA ASP GLY ARG ILE GLU ARG TRP GLN VAL
SEQRES 25 J 343 GLY GLY TRP GLN PRO CYS VAL ASP VAL ALA ASP ALA MET
SEQRES 26 J 343 SER ALA ALA GLU ALA ALA HIS ILE ALA ARG ARG LEU SER
SEQRES 27 J 343 ARG TRP ASP SER ASN
SEQRES 1 D 286 THR ALA ARG ILE ALA LEU ALA SER LEU PHE VAL VAL ALA
SEQRES 2 D 286 ALA VAL LEU ALA GLN PRO TRP GLN THR THR THR GLN ARG
SEQRES 3 D 286 TRP VAL LEU GLY VAL SER ILE ALA ALA VAL ILE VAL LEU
SEQRES 4 D 286 LEU ALA TRP TRP LYS GLY MET PHE LEU THR THR ARG ILE
SEQRES 5 D 286 GLY ARG ALA LEU ALA MET VAL ARG ARG ASN ARG ALA GLU
SEQRES 6 D 286 ASP THR VAL GLU THR ASP ALA HIS ARG ALA THR VAL VAL
SEQRES 7 D 286 LEU ARG VAL ASP PRO ALA ALA PRO ALA GLN LEU PRO VAL
SEQRES 8 D 286 VAL VAL GLY TYR LEU ASP ARG TYR GLY ILE THR CYS ASP
SEQRES 9 D 286 LYS VAL ARG ILE THR HIS ARG ASP ALA GLY GLY THR ARG
SEQRES 10 D 286 ARG SER TRP ILE SER LEU THR VAL ASP ALA VAL ASP ASN
SEQRES 11 D 286 LEU ALA ALA LEU GLN ALA ARG SER ALA ARG ILE PRO LEU
SEQRES 12 D 286 GLN ASP THR THR GLU VAL VAL GLY ARG ARG LEU ALA ASP
SEQRES 13 D 286 HIS LEU ARG GLU GLN GLY TRP THR VAL THR VAL VAL GLU
SEQRES 14 D 286 GLY VAL ASP THR PRO LEU PRO VAL SER GLY LYS GLU THR
SEQRES 15 D 286 TRP ARG GLY VAL ALA ASP ASP ALA GLY VAL VAL ALA ALA
SEQRES 16 D 286 TYR ARG VAL LYS VAL ASP ASP ARG LEU ASP GLU VAL LEU
SEQRES 17 D 286 ALA GLU ILE GLY HIS LEU PRO ALA GLU GLU THR TRP THR
SEQRES 18 D 286 ALA LEU GLU PHE THR GLY SER PRO ALA GLU PRO LEU LEU
SEQRES 19 D 286 THR VAL CYS ALA ALA VAL ARG THR SER ASP ARG PRO ALA
SEQRES 20 D 286 ALA LYS ALA PRO LEU ALA GLY LEU THR PRO ALA ARG GLY
SEQRES 21 D 286 ARG HIS ARG PRO ALA LEU ALA ALA LEU ASN PRO LEU SER
SEQRES 22 D 286 THR GLU ARG LEU ASP GLY THR ALA VAL PRO LEU PRO ALA
HELIX 1 AA1 PRO E 34 GLN E 47 1 14
HELIX 2 AA2 THR E 82 GLY E 87 1 6
HELIX 3 AA3 ASP E 111 PHE E 119 1 9
HELIX 4 AA4 TRP E 127 THR E 158 1 32
HELIX 5 AA5 ASP E 160 VAL E 181 1 22
HELIX 6 AA6 VAL E 187 ALA E 196 1 10
HELIX 7 AA7 ALA E 196 PHE E 204 1 9
HELIX 8 AA8 ALA E 214 ALA E 233 1 20
HELIX 9 AA9 GLY E 240 TRP E 264 1 25
HELIX 10 AB1 ASP E 269 GLN E 285 1 17
HELIX 11 AB2 ALA E 286 TRP E 293 1 8
HELIX 12 AB3 ALA E 294 PHE E 296 5 3
HELIX 13 AB4 ASP E 319 VAL E 350 1 32
HELIX 14 AB5 SER E 356 ARG E 373 1 18
HELIX 15 AB6 ARG E 373 ASP E 378 1 6
HELIX 16 AB7 SER E 379 GLY E 404 1 26
HELIX 17 AB8 ALA E 409 ASN E 430 1 22
HELIX 18 AB9 SER E 440 ALA E 456 1 17
HELIX 19 AC1 SER E 457 GLY E 467 1 11
HELIX 20 AC2 PRO H 34 GLU H 37 5 4
HELIX 21 AC3 ILE H 38 GLN H 47 1 10
HELIX 22 AC4 THR H 82 GLY H 87 1 6
HELIX 23 AC5 ALA H 115 ARG H 124 1 10
HELIX 24 AC6 PRO H 129 GLY H 159 1 31
HELIX 25 AC7 ASP H 160 LEU H 179 1 20
HELIX 26 AC8 VAL H 187 LEU H 206 1 20
HELIX 27 AC9 PRO H 215 GLY H 234 1 20
HELIX 28 AD1 ILE H 241 TRP H 264 1 24
HELIX 29 AD2 SER H 267 GLN H 285 1 19
HELIX 30 AD3 ALA H 287 ALA H 294 1 8
HELIX 31 AD4 PRO H 313 GLY H 345 1 33
HELIX 32 AD5 GLY H 345 VAL H 350 1 6
HELIX 33 AD6 SER H 356 ARG H 373 1 18
HELIX 34 AD7 ALA H 374 VAL H 376 5 3
HELIX 35 AD8 SER H 379 GLY H 404 1 26
HELIX 36 AD9 GLN H 408 LEU H 429 1 22
HELIX 37 AE1 SER H 435 TYR H 439 5 5
HELIX 38 AE2 SER H 440 GLY H 467 1 28
HELIX 39 AE3 LEU H 468 LEU H 471 5 4
HELIX 40 AE4 THR I 34 HIS I 55 1 22
HELIX 41 AE5 ASP I 62 LEU I 90 1 29
HELIX 42 AE6 ARG J 93 HIS J 130 1 38
HELIX 43 AE7 GLU J 134 ILE J 139 5 6
HELIX 44 AE8 GLU J 183 GLN J 197 1 15
HELIX 45 AE9 ALA J 210 LEU J 212 5 3
HELIX 46 AF1 GLU J 220 THR J 237 1 18
HELIX 47 AF2 ASP J 257 TRP J 263 5 7
HELIX 48 AF3 SER J 285 ALA J 294 1 10
HELIX 49 AF4 PRO J 295 LEU J 297 5 3
HELIX 50 AF5 SER J 386 ARG J 399 1 14
HELIX 51 AF6 ALA D 3 LEU D 17 1 15
HELIX 52 AF7 ARG D 27 ILE D 38 1 12
HELIX 53 AF8 LEU D 49 ARG D 62 1 14
HELIX 54 AF9 ALA D 86 ALA D 88 5 3
HELIX 55 AG1 GLN D 89 GLY D 95 1 7
HELIX 56 AG2 TYR D 96 ASP D 98 5 3
HELIX 57 AG3 ASN D 131 ALA D 140 1 10
HELIX 58 AG4 PRO D 143 GLY D 163 1 21
HELIX 59 AG5 GLU D 207 ILE D 212 1 6
HELIX 60 AG6 PRO D 265 LEU D 270 1 6
SHEET 1 AA1 5 LEU E 67 PRO E 71 0
SHEET 2 AA1 5 LEU E 93 ALA E 98 -1 O ALA E 95 N ALA E 70
SHEET 3 AA1 5 ILE E 9 ALA E 16 1 N LEU E 15 O LEU E 96
SHEET 4 AA1 5 ARG E 23 PRO E 30 -1 O LEU E 29 N VAL E 10
SHEET 5 AA1 5 GLU H 110 ASP H 111 -1 O GLU H 110 N LEU E 24
SHEET 1 AA2 4 LEU H 24 PRO H 30 0
SHEET 2 AA2 4 ILE H 9 LEU H 15 -1 N VAL H 10 O LEU H 29
SHEET 3 AA2 4 LEU H 93 ALA H 98 1 O LEU H 96 N LEU H 15
SHEET 4 AA2 4 LEU H 67 PRO H 71 -1 N ALA H 70 O ALA H 95
SHEET 1 AA3 2 THR J 23 ILE J 24 0
SHEET 2 AA3 2 LYS J 172 VAL J 173 1 O LYS J 172 N ILE J 24
SHEET 1 AA4 2 VAL J 157 VAL J 165 0
SHEET 2 AA4 2 VAL J 200 ASP J 208 -1 O LEU J 207 N LEU J 158
SHEET 1 AA5 6 LEU J 244 ALA J 249 0
SHEET 2 AA5 6 HIS J 313 LEU J 318 1 O LEU J 315 N GLY J 245
SHEET 3 AA5 6 VAL J 337 THR J 343 1 O ILE J 340 N VAL J 316
SHEET 4 AA5 6 ARG J 214 ILE J 218 1 N VAL J 217 O HIS J 341
SHEET 5 AA5 6 ILE J 359 VAL J 362 1 O LEU J 360 N THR J 216
SHEET 6 AA5 6 ILE J 367 ARG J 369 -1 O GLU J 368 N ARG J 361
SHEET 1 AA6 7 THR D 167 VAL D 168 0
SHEET 2 AA6 7 ARG D 75 ARG D 81 -1 N ARG D 81 O THR D 167
SHEET 3 AA6 7 SER D 120 ASP D 127 -1 O VAL D 126 N ALA D 76
SHEET 4 AA6 7 LYS D 106 HIS D 111 -1 N THR D 110 O TRP D 121
SHEET 5 AA6 7 TRP D 221 GLY D 228 -1 O THR D 222 N HIS D 111
SHEET 6 AA6 7 PRO D 233 VAL D 241 -1 O CYS D 238 N ALA D 223
SHEET 7 AA6 7 ALA D 195 TYR D 197 -1 N TYR D 197 O ALA D 239
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 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
