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7puy.pdb
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HEADER VIRAL PROTEIN 01-OCT-21 7PUY
TITLE STRUCTURE OF THE MEMBRANE SOLUBLE SPIKE COMPLEX FROM THE LASSA VIRUS
TITLE 2 IN A C3-SYMMETRIC MAP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOPROTEIN G2;
COMPND 3 CHAIN: a, b, c;
COMPND 4 SYNONYM: GP2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PRE-GLYCOPROTEIN POLYPROTEIN GP COMPLEX;
COMPND 8 CHAIN: A, B, C;
COMPND 9 SYNONYM: PRE-GP-C;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LASSA VIRUS (STRAIN MOUSE/SIERRA
SOURCE 3 LEONE/JOSIAH/1976);
SOURCE 4 ORGANISM_COMMON: LASV;
SOURCE 5 ORGANISM_TAXID: 11622;
SOURCE 6 STRAIN: MOUSE/SIERRA LEONE/JOSIAH/1976;
SOURCE 7 GENE: GPC, GP-C;
SOURCE 8 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: LASSA VIRUS (STRAIN MOUSE/SIERRA
SOURCE 12 LEONE/JOSIAH/1976);
SOURCE 13 ORGANISM_COMMON: LASV;
SOURCE 14 ORGANISM_TAXID: 11622;
SOURCE 15 STRAIN: MOUSE/SIERRA LEONE/JOSIAH/1976;
SOURCE 16 GENE: GPC, GP-C;
SOURCE 17 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS SPIKE COMPLEX, GLYCOPROTEIN, VIRAL PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR R.DISKIN,M.KATZ
REVDAT 3 16-MAR-22 7PUY 1 JRNL
REVDAT 2 02-MAR-22 7PUY 1 JRNL
REVDAT 1 29-DEC-21 7PUY 0
JRNL AUTH M.KATZ,J.WEINSTEIN,M.EILON-ASHKENAZY,K.GEHRING,
JRNL AUTH 2 H.COHEN-DVASHI,N.ELAD,S.J.FLEISHMAN,R.DISKIN
JRNL TITL STRUCTURE AND RECEPTOR RECOGNITION BY THE LASSA VIRUS SPIKE
JRNL TITL 2 COMPLEX.
JRNL REF NATURE V. 603 174 2022
JRNL REFN ESSN 1476-4687
JRNL PMID 35173332
JRNL DOI 10.1038/S41586-022-04429-2
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
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) : 3.300
REMARK 3 NUMBER OF PARTICLES : 91903
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: GLOBAL LOW-PASS FILTERING BASED ON MAP-MODEL FSC
REMARK 4
REMARK 4 7PUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-OCT-21.
REMARK 100 THE DEPOSITION ID IS D_1292118286.
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 : THE COMPLETE SPIKE COMPLEX
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.40
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 K3 (6K 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) : 7300.00
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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: a, b, c, A, B, C, D, E, F, G,
REMARK 350 AND CHAINS: H, I, J, K, L, M, N, 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 LEU a 449
REMARK 465 VAL a 450
REMARK 465 LYS a 451
REMARK 465 ILE a 452
REMARK 465 PRO a 453
REMARK 465 THR a 454
REMARK 465 HIS a 455
REMARK 465 ARG a 456
REMARK 465 HIS a 457
REMARK 465 ILE a 458
REMARK 465 VAL a 459
REMARK 465 GLY a 460
REMARK 465 LYS a 461
REMARK 465 SER a 462
REMARK 465 CYS a 463
REMARK 465 PRO a 464
REMARK 465 LYS a 465
REMARK 465 PRO a 466
REMARK 465 HIS a 467
REMARK 465 ARG a 468
REMARK 465 LEU a 469
REMARK 465 ASN a 470
REMARK 465 HIS a 471
REMARK 465 MET a 472
REMARK 465 GLY a 473
REMARK 465 ILE a 474
REMARK 465 CYS a 475
REMARK 465 SER a 476
REMARK 465 CYS a 477
REMARK 465 GLY a 478
REMARK 465 LEU a 479
REMARK 465 TYR a 480
REMARK 465 LYS a 481
REMARK 465 GLN a 482
REMARK 465 PRO a 483
REMARK 465 GLY a 484
REMARK 465 VAL a 485
REMARK 465 PRO a 486
REMARK 465 VAL a 487
REMARK 465 LYS a 488
REMARK 465 TRP a 489
REMARK 465 LYS a 490
REMARK 465 ARG a 491
REMARK 465 GLY a 492
REMARK 465 GLY a 493
REMARK 465 GLY a 494
REMARK 465 SER a 495
REMARK 465 ASP a 496
REMARK 465 TYR a 497
REMARK 465 LYS a 498
REMARK 465 ASP a 499
REMARK 465 ASP a 500
REMARK 465 ASP a 501
REMARK 465 ASP a 502
REMARK 465 LYS a 503
REMARK 465 LEU b 449
REMARK 465 VAL b 450
REMARK 465 LYS b 451
REMARK 465 ILE b 452
REMARK 465 PRO b 453
REMARK 465 THR b 454
REMARK 465 HIS b 455
REMARK 465 ARG b 456
REMARK 465 HIS b 457
REMARK 465 ILE b 458
REMARK 465 VAL b 459
REMARK 465 GLY b 460
REMARK 465 LYS b 461
REMARK 465 SER b 462
REMARK 465 CYS b 463
REMARK 465 PRO b 464
REMARK 465 LYS b 465
REMARK 465 PRO b 466
REMARK 465 HIS b 467
REMARK 465 ARG b 468
REMARK 465 LEU b 469
REMARK 465 ASN b 470
REMARK 465 HIS b 471
REMARK 465 MET b 472
REMARK 465 GLY b 473
REMARK 465 ILE b 474
REMARK 465 CYS b 475
REMARK 465 SER b 476
REMARK 465 CYS b 477
REMARK 465 GLY b 478
REMARK 465 LEU b 479
REMARK 465 TYR b 480
REMARK 465 LYS b 481
REMARK 465 GLN b 482
REMARK 465 PRO b 483
REMARK 465 GLY b 484
REMARK 465 VAL b 485
REMARK 465 PRO b 486
REMARK 465 VAL b 487
REMARK 465 LYS b 488
REMARK 465 TRP b 489
REMARK 465 LYS b 490
REMARK 465 ARG b 491
REMARK 465 GLY b 492
REMARK 465 GLY b 493
REMARK 465 GLY b 494
REMARK 465 SER b 495
REMARK 465 ASP b 496
REMARK 465 TYR b 497
REMARK 465 LYS b 498
REMARK 465 ASP b 499
REMARK 465 ASP b 500
REMARK 465 ASP b 501
REMARK 465 ASP b 502
REMARK 465 LYS b 503
REMARK 465 LEU c 449
REMARK 465 VAL c 450
REMARK 465 LYS c 451
REMARK 465 ILE c 452
REMARK 465 PRO c 453
REMARK 465 THR c 454
REMARK 465 HIS c 455
REMARK 465 ARG c 456
REMARK 465 HIS c 457
REMARK 465 ILE c 458
REMARK 465 VAL c 459
REMARK 465 GLY c 460
REMARK 465 LYS c 461
REMARK 465 SER c 462
REMARK 465 CYS c 463
REMARK 465 PRO c 464
REMARK 465 LYS c 465
REMARK 465 PRO c 466
REMARK 465 HIS c 467
REMARK 465 ARG c 468
REMARK 465 LEU c 469
REMARK 465 ASN c 470
REMARK 465 HIS c 471
REMARK 465 MET c 472
REMARK 465 GLY c 473
REMARK 465 ILE c 474
REMARK 465 CYS c 475
REMARK 465 SER c 476
REMARK 465 CYS c 477
REMARK 465 GLY c 478
REMARK 465 LEU c 479
REMARK 465 TYR c 480
REMARK 465 LYS c 481
REMARK 465 GLN c 482
REMARK 465 PRO c 483
REMARK 465 GLY c 484
REMARK 465 VAL c 485
REMARK 465 PRO c 486
REMARK 465 VAL c 487
REMARK 465 LYS c 488
REMARK 465 TRP c 489
REMARK 465 LYS c 490
REMARK 465 ARG c 491
REMARK 465 GLY c 492
REMARK 465 GLY c 493
REMARK 465 GLY c 494
REMARK 465 SER c 495
REMARK 465 ASP c 496
REMARK 465 TYR c 497
REMARK 465 LYS c 498
REMARK 465 ASP c 499
REMARK 465 ASP c 500
REMARK 465 ASP c 501
REMARK 465 ASP c 502
REMARK 465 LYS c 503
REMARK 465 MET A 1
REMARK 465 TYR A 36
REMARK 465 ASN A 37
REMARK 465 PHE A 38
REMARK 465 ALA A 39
REMARK 465 THR A 40
REMARK 465 CYS A 41
REMARK 465 GLY A 42
REMARK 465 LEU A 43
REMARK 465 VAL A 44
REMARK 465 GLY A 45
REMARK 465 LEU A 46
REMARK 465 VAL A 47
REMARK 465 THR A 48
REMARK 465 PHE A 49
REMARK 465 LEU A 50
REMARK 465 LEU A 51
REMARK 465 LEU A 52
REMARK 465 CYS A 53
REMARK 465 GLY A 54
REMARK 465 ARG A 55
REMARK 465 SER A 56
REMARK 465 CYS A 57
REMARK 465 THR A 58
REMARK 465 SER A 171
REMARK 465 TYR A 172
REMARK 465 ALA A 173
REMARK 465 GLY A 174
REMARK 465 ASP A 175
REMARK 465 ALA A 176
REMARK 465 ALA A 177
REMARK 465 ASN A 178
REMARK 465 SER A 199
REMARK 465 TYR A 200
REMARK 465 ILE A 201
REMARK 465 ALA A 202
REMARK 465 LEU A 203
REMARK 465 ASP A 204
REMARK 465 SER A 205
REMARK 465 GLY A 206
REMARK 465 MET B 1
REMARK 465 TYR B 36
REMARK 465 ASN B 37
REMARK 465 PHE B 38
REMARK 465 ALA B 39
REMARK 465 THR B 40
REMARK 465 CYS B 41
REMARK 465 GLY B 42
REMARK 465 LEU B 43
REMARK 465 VAL B 44
REMARK 465 GLY B 45
REMARK 465 LEU B 46
REMARK 465 VAL B 47
REMARK 465 THR B 48
REMARK 465 PHE B 49
REMARK 465 LEU B 50
REMARK 465 LEU B 51
REMARK 465 LEU B 52
REMARK 465 CYS B 53
REMARK 465 GLY B 54
REMARK 465 ARG B 55
REMARK 465 SER B 56
REMARK 465 CYS B 57
REMARK 465 THR B 58
REMARK 465 SER B 171
REMARK 465 TYR B 172
REMARK 465 ALA B 173
REMARK 465 GLY B 174
REMARK 465 ASP B 175
REMARK 465 ALA B 176
REMARK 465 ALA B 177
REMARK 465 ASN B 178
REMARK 465 SER B 199
REMARK 465 TYR B 200
REMARK 465 ILE B 201
REMARK 465 ALA B 202
REMARK 465 LEU B 203
REMARK 465 ASP B 204
REMARK 465 SER B 205
REMARK 465 GLY B 206
REMARK 465 MET C 1
REMARK 465 TYR C 36
REMARK 465 ASN C 37
REMARK 465 PHE C 38
REMARK 465 ALA C 39
REMARK 465 THR C 40
REMARK 465 CYS C 41
REMARK 465 GLY C 42
REMARK 465 LEU C 43
REMARK 465 VAL C 44
REMARK 465 GLY C 45
REMARK 465 LEU C 46
REMARK 465 VAL C 47
REMARK 465 THR C 48
REMARK 465 PHE C 49
REMARK 465 LEU C 50
REMARK 465 LEU C 51
REMARK 465 LEU C 52
REMARK 465 CYS C 53
REMARK 465 GLY C 54
REMARK 465 ARG C 55
REMARK 465 SER C 56
REMARK 465 CYS C 57
REMARK 465 THR C 58
REMARK 465 SER C 171
REMARK 465 TYR C 172
REMARK 465 ALA C 173
REMARK 465 GLY C 174
REMARK 465 ASP C 175
REMARK 465 ALA C 176
REMARK 465 ALA C 177
REMARK 465 ASN C 178
REMARK 465 SER C 199
REMARK 465 TYR C 200
REMARK 465 ILE C 201
REMARK 465 ALA C 202
REMARK 465 LEU C 203
REMARK 465 ASP C 204
REMARK 465 SER C 205
REMARK 465 GLY C 206
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 PHE C 233 O4 NAG c 601 2.07
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 ALA a 288 17.65 -142.56
REMARK 500 GLU a 289 -137.27 60.91
REMARK 500 CYS a 301 31.95 -93.89
REMARK 500 LEU a 326 -167.59 -126.59
REMARK 500 GLU a 329 -2.02 68.01
REMARK 500 ALA a 330 -1.45 71.53
REMARK 500 ALA b 288 17.66 -142.56
REMARK 500 GLU b 289 -137.21 60.89
REMARK 500 CYS b 301 31.97 -93.92
REMARK 500 LEU b 326 -167.60 -126.59
REMARK 500 GLU b 329 -2.02 67.97
REMARK 500 ALA b 330 -1.48 71.58
REMARK 500 ALA c 288 17.59 -142.54
REMARK 500 GLU c 289 -137.24 60.90
REMARK 500 CYS c 301 31.96 -93.90
REMARK 500 LEU c 326 -167.60 -126.57
REMARK 500 GLU c 329 -2.02 68.00
REMARK 500 ALA c 330 -1.52 71.59
REMARK 500 LYS A 63 -116.26 53.54
REMARK 500 ASN A 90 -2.86 68.62
REMARK 500 CYS A 180 -169.80 -126.54
REMARK 500 HIS A 230 50.61 -90.66
REMARK 500 LYS B 63 -116.32 53.54
REMARK 500 ASN B 90 -2.82 68.57
REMARK 500 CYS B 180 -169.77 -126.57
REMARK 500 HIS B 230 50.60 -90.65
REMARK 500 LYS C 63 -116.25 53.56
REMARK 500 ASN C 90 -2.87 68.66
REMARK 500 CYS C 180 -169.73 -126.55
REMARK 500 HIS C 230 50.59 -90.60
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-13662 RELATED DB: EMDB
REMARK 900 STRUCTURE OF THE MEMBRANE SOLUBLE SPIKE COMPLEX FROM THE LASSA
REMARK 900 VIRUS IN A C3-SYMMETRIC MAP
DBREF 7PUY a 260 491 UNP P08669 GLYC_LASSJ 260 491
DBREF 7PUY b 260 491 UNP P08669 GLYC_LASSJ 260 491
DBREF 7PUY c 260 491 UNP P08669 GLYC_LASSJ 260 491
DBREF 7PUY A 1 259 UNP P08669 GLYC_LASSJ 1 259
DBREF 7PUY B 1 259 UNP P08669 GLYC_LASSJ 1 259
DBREF 7PUY C 1 259 UNP P08669 GLYC_LASSJ 1 259
SEQADV 7PUY GLY a 492 UNP P08669 EXPRESSION TAG
SEQADV 7PUY GLY a 493 UNP P08669 EXPRESSION TAG
SEQADV 7PUY GLY a 494 UNP P08669 EXPRESSION TAG
SEQADV 7PUY SER a 495 UNP P08669 EXPRESSION TAG
SEQADV 7PUY ASP a 496 UNP P08669 EXPRESSION TAG
SEQADV 7PUY TYR a 497 UNP P08669 EXPRESSION TAG
SEQADV 7PUY LYS a 498 UNP P08669 EXPRESSION TAG
SEQADV 7PUY ASP a 499 UNP P08669 EXPRESSION TAG
SEQADV 7PUY ASP a 500 UNP P08669 EXPRESSION TAG
SEQADV 7PUY ASP a 501 UNP P08669 EXPRESSION TAG
SEQADV 7PUY ASP a 502 UNP P08669 EXPRESSION TAG
SEQADV 7PUY LYS a 503 UNP P08669 EXPRESSION TAG
SEQADV 7PUY GLY b 492 UNP P08669 EXPRESSION TAG
SEQADV 7PUY GLY b 493 UNP P08669 EXPRESSION TAG
SEQADV 7PUY GLY b 494 UNP P08669 EXPRESSION TAG
SEQADV 7PUY SER b 495 UNP P08669 EXPRESSION TAG
SEQADV 7PUY ASP b 496 UNP P08669 EXPRESSION TAG
SEQADV 7PUY TYR b 497 UNP P08669 EXPRESSION TAG
SEQADV 7PUY LYS b 498 UNP P08669 EXPRESSION TAG
SEQADV 7PUY ASP b 499 UNP P08669 EXPRESSION TAG
SEQADV 7PUY ASP b 500 UNP P08669 EXPRESSION TAG
SEQADV 7PUY ASP b 501 UNP P08669 EXPRESSION TAG
SEQADV 7PUY ASP b 502 UNP P08669 EXPRESSION TAG
SEQADV 7PUY LYS b 503 UNP P08669 EXPRESSION TAG
SEQADV 7PUY GLY c 492 UNP P08669 EXPRESSION TAG
SEQADV 7PUY GLY c 493 UNP P08669 EXPRESSION TAG
SEQADV 7PUY GLY c 494 UNP P08669 EXPRESSION TAG
SEQADV 7PUY SER c 495 UNP P08669 EXPRESSION TAG
SEQADV 7PUY ASP c 496 UNP P08669 EXPRESSION TAG
SEQADV 7PUY TYR c 497 UNP P08669 EXPRESSION TAG
SEQADV 7PUY LYS c 498 UNP P08669 EXPRESSION TAG
SEQADV 7PUY ASP c 499 UNP P08669 EXPRESSION TAG
SEQADV 7PUY ASP c 500 UNP P08669 EXPRESSION TAG
SEQADV 7PUY ASP c 501 UNP P08669 EXPRESSION TAG
SEQADV 7PUY ASP c 502 UNP P08669 EXPRESSION TAG
SEQADV 7PUY LYS c 503 UNP P08669 EXPRESSION TAG
SEQRES 1 a 244 GLY THR PHE THR TRP THR LEU SER ASP SER GLU GLY LYS
SEQRES 2 a 244 ASP THR PRO GLY GLY TYR CYS LEU THR ARG TRP MET LEU
SEQRES 3 a 244 ILE GLU ALA GLU LEU LYS CYS PHE GLY ASN THR ALA VAL
SEQRES 4 a 244 ALA LYS CYS ASN GLU LYS HIS ASP GLU GLU PHE CYS ASP
SEQRES 5 a 244 MET LEU ARG LEU PHE ASP PHE ASN LYS GLN ALA ILE GLN
SEQRES 6 a 244 ARG LEU LYS ALA GLU ALA GLN MET SER ILE GLN LEU ILE
SEQRES 7 a 244 ASN LYS ALA VAL ASN ALA LEU ILE ASN ASP GLN LEU ILE
SEQRES 8 a 244 MET LYS ASN HIS LEU ARG ASP ILE MET GLY ILE PRO TYR
SEQRES 9 a 244 CYS ASN TYR SER LYS TYR TRP TYR LEU ASN HIS THR THR
SEQRES 10 a 244 THR GLY ARG THR SER LEU PRO LYS CYS TRP LEU VAL SER
SEQRES 11 a 244 ASN GLY SER TYR LEU ASN GLU THR HIS PHE SER ASP ASP
SEQRES 12 a 244 ILE GLU GLN GLN ALA ASP ASN MET ILE THR GLU MET LEU
SEQRES 13 a 244 GLN LYS GLU TYR MET GLU ARG GLN GLY LYS THR PRO LEU
SEQRES 14 a 244 GLY LEU VAL ASP LEU PHE VAL PHE SER THR SER PHE TYR
SEQRES 15 a 244 LEU ILE SER ILE PHE LEU HIS LEU VAL LYS ILE PRO THR
SEQRES 16 a 244 HIS ARG HIS ILE VAL GLY LYS SER CYS PRO LYS PRO HIS
SEQRES 17 a 244 ARG LEU ASN HIS MET GLY ILE CYS SER CYS GLY LEU TYR
SEQRES 18 a 244 LYS GLN PRO GLY VAL PRO VAL LYS TRP LYS ARG GLY GLY
SEQRES 19 a 244 GLY SER ASP TYR LYS ASP ASP ASP ASP LYS
SEQRES 1 b 244 GLY THR PHE THR TRP THR LEU SER ASP SER GLU GLY LYS
SEQRES 2 b 244 ASP THR PRO GLY GLY TYR CYS LEU THR ARG TRP MET LEU
SEQRES 3 b 244 ILE GLU ALA GLU LEU LYS CYS PHE GLY ASN THR ALA VAL
SEQRES 4 b 244 ALA LYS CYS ASN GLU LYS HIS ASP GLU GLU PHE CYS ASP
SEQRES 5 b 244 MET LEU ARG LEU PHE ASP PHE ASN LYS GLN ALA ILE GLN
SEQRES 6 b 244 ARG LEU LYS ALA GLU ALA GLN MET SER ILE GLN LEU ILE
SEQRES 7 b 244 ASN LYS ALA VAL ASN ALA LEU ILE ASN ASP GLN LEU ILE
SEQRES 8 b 244 MET LYS ASN HIS LEU ARG ASP ILE MET GLY ILE PRO TYR
SEQRES 9 b 244 CYS ASN TYR SER LYS TYR TRP TYR LEU ASN HIS THR THR
SEQRES 10 b 244 THR GLY ARG THR SER LEU PRO LYS CYS TRP LEU VAL SER
SEQRES 11 b 244 ASN GLY SER TYR LEU ASN GLU THR HIS PHE SER ASP ASP
SEQRES 12 b 244 ILE GLU GLN GLN ALA ASP ASN MET ILE THR GLU MET LEU
SEQRES 13 b 244 GLN LYS GLU TYR MET GLU ARG GLN GLY LYS THR PRO LEU
SEQRES 14 b 244 GLY LEU VAL ASP LEU PHE VAL PHE SER THR SER PHE TYR
SEQRES 15 b 244 LEU ILE SER ILE PHE LEU HIS LEU VAL LYS ILE PRO THR
SEQRES 16 b 244 HIS ARG HIS ILE VAL GLY LYS SER CYS PRO LYS PRO HIS
SEQRES 17 b 244 ARG LEU ASN HIS MET GLY ILE CYS SER CYS GLY LEU TYR
SEQRES 18 b 244 LYS GLN PRO GLY VAL PRO VAL LYS TRP LYS ARG GLY GLY
SEQRES 19 b 244 GLY SER ASP TYR LYS ASP ASP ASP ASP LYS
SEQRES 1 c 244 GLY THR PHE THR TRP THR LEU SER ASP SER GLU GLY LYS
SEQRES 2 c 244 ASP THR PRO GLY GLY TYR CYS LEU THR ARG TRP MET LEU
SEQRES 3 c 244 ILE GLU ALA GLU LEU LYS CYS PHE GLY ASN THR ALA VAL
SEQRES 4 c 244 ALA LYS CYS ASN GLU LYS HIS ASP GLU GLU PHE CYS ASP
SEQRES 5 c 244 MET LEU ARG LEU PHE ASP PHE ASN LYS GLN ALA ILE GLN
SEQRES 6 c 244 ARG LEU LYS ALA GLU ALA GLN MET SER ILE GLN LEU ILE
SEQRES 7 c 244 ASN LYS ALA VAL ASN ALA LEU ILE ASN ASP GLN LEU ILE
SEQRES 8 c 244 MET LYS ASN HIS LEU ARG ASP ILE MET GLY ILE PRO TYR
SEQRES 9 c 244 CYS ASN TYR SER LYS TYR TRP TYR LEU ASN HIS THR THR
SEQRES 10 c 244 THR GLY ARG THR SER LEU PRO LYS CYS TRP LEU VAL SER
SEQRES 11 c 244 ASN GLY SER TYR LEU ASN GLU THR HIS PHE SER ASP ASP
SEQRES 12 c 244 ILE GLU GLN GLN ALA ASP ASN MET ILE THR GLU MET LEU
SEQRES 13 c 244 GLN LYS GLU TYR MET GLU ARG GLN GLY LYS THR PRO LEU
SEQRES 14 c 244 GLY LEU VAL ASP LEU PHE VAL PHE SER THR SER PHE TYR
SEQRES 15 c 244 LEU ILE SER ILE PHE LEU HIS LEU VAL LYS ILE PRO THR
SEQRES 16 c 244 HIS ARG HIS ILE VAL GLY LYS SER CYS PRO LYS PRO HIS
SEQRES 17 c 244 ARG LEU ASN HIS MET GLY ILE CYS SER CYS GLY LEU TYR
SEQRES 18 c 244 LYS GLN PRO GLY VAL PRO VAL LYS TRP LYS ARG GLY GLY
SEQRES 19 c 244 GLY SER ASP TYR LYS ASP ASP ASP ASP LYS
SEQRES 1 A 259 MET GLY GLN ILE VAL THR PHE PHE GLN GLU VAL PRO HIS
SEQRES 2 A 259 VAL ILE GLU GLU VAL MET ASN ILE VAL LEU ILE ALA LEU
SEQRES 3 A 259 SER VAL LEU ALA VAL LEU LYS GLY LEU TYR ASN PHE ALA
SEQRES 4 A 259 THR CYS GLY LEU VAL GLY LEU VAL THR PHE LEU LEU LEU
SEQRES 5 A 259 CYS GLY ARG SER CYS THR THR SER LEU TYR LYS GLY VAL
SEQRES 6 A 259 TYR GLU LEU GLN THR LEU GLU LEU ASN MET GLU THR LEU
SEQRES 7 A 259 ASN MET THR MET PRO LEU SER CYS THR LYS ASN ASN SER
SEQRES 8 A 259 HIS HIS TYR ILE MET VAL GLY ASN GLU THR GLY LEU GLU
SEQRES 9 A 259 LEU THR LEU THR ASN THR SER ILE ILE ASN HIS LYS PHE
SEQRES 10 A 259 CYS ASN LEU SER ASP ALA HIS LYS LYS ASN LEU TYR ASP
SEQRES 11 A 259 HIS ALA LEU MET SER ILE ILE SER THR PHE HIS LEU SER
SEQRES 12 A 259 ILE PRO ASN PHE ASN GLN TYR GLU ALA MET SER CYS ASP
SEQRES 13 A 259 PHE ASN GLY GLY LYS ILE SER VAL GLN TYR ASN LEU SER
SEQRES 14 A 259 HIS SER TYR ALA GLY ASP ALA ALA ASN HIS CYS GLY THR
SEQRES 15 A 259 VAL ALA ASN GLY VAL LEU GLN THR PHE MET ARG MET ALA
SEQRES 16 A 259 TRP GLY GLY SER TYR ILE ALA LEU ASP SER GLY ARG GLY
SEQRES 17 A 259 ASN TRP ASP CYS ILE MET THR SER TYR GLN TYR LEU ILE
SEQRES 18 A 259 ILE GLN ASN THR THR TRP GLU ASP HIS CYS GLN PHE SER
SEQRES 19 A 259 ARG PRO SER PRO ILE GLY TYR LEU GLY LEU LEU SER GLN
SEQRES 20 A 259 ARG THR ARG ASP ILE TYR ILE SER ARG ARG LEU LEU
SEQRES 1 B 259 MET GLY GLN ILE VAL THR PHE PHE GLN GLU VAL PRO HIS
SEQRES 2 B 259 VAL ILE GLU GLU VAL MET ASN ILE VAL LEU ILE ALA LEU
SEQRES 3 B 259 SER VAL LEU ALA VAL LEU LYS GLY LEU TYR ASN PHE ALA
SEQRES 4 B 259 THR CYS GLY LEU VAL GLY LEU VAL THR PHE LEU LEU LEU
SEQRES 5 B 259 CYS GLY ARG SER CYS THR THR SER LEU TYR LYS GLY VAL
SEQRES 6 B 259 TYR GLU LEU GLN THR LEU GLU LEU ASN MET GLU THR LEU
SEQRES 7 B 259 ASN MET THR MET PRO LEU SER CYS THR LYS ASN ASN SER
SEQRES 8 B 259 HIS HIS TYR ILE MET VAL GLY ASN GLU THR GLY LEU GLU
SEQRES 9 B 259 LEU THR LEU THR ASN THR SER ILE ILE ASN HIS LYS PHE
SEQRES 10 B 259 CYS ASN LEU SER ASP ALA HIS LYS LYS ASN LEU TYR ASP
SEQRES 11 B 259 HIS ALA LEU MET SER ILE ILE SER THR PHE HIS LEU SER
SEQRES 12 B 259 ILE PRO ASN PHE ASN GLN TYR GLU ALA MET SER CYS ASP
SEQRES 13 B 259 PHE ASN GLY GLY LYS ILE SER VAL GLN TYR ASN LEU SER
SEQRES 14 B 259 HIS SER TYR ALA GLY ASP ALA ALA ASN HIS CYS GLY THR
SEQRES 15 B 259 VAL ALA ASN GLY VAL LEU GLN THR PHE MET ARG MET ALA
SEQRES 16 B 259 TRP GLY GLY SER TYR ILE ALA LEU ASP SER GLY ARG GLY
SEQRES 17 B 259 ASN TRP ASP CYS ILE MET THR SER TYR GLN TYR LEU ILE
SEQRES 18 B 259 ILE GLN ASN THR THR TRP GLU ASP HIS CYS GLN PHE SER
SEQRES 19 B 259 ARG PRO SER PRO ILE GLY TYR LEU GLY LEU LEU SER GLN
SEQRES 20 B 259 ARG THR ARG ASP ILE TYR ILE SER ARG ARG LEU LEU
SEQRES 1 C 259 MET GLY GLN ILE VAL THR PHE PHE GLN GLU VAL PRO HIS
SEQRES 2 C 259 VAL ILE GLU GLU VAL MET ASN ILE VAL LEU ILE ALA LEU
SEQRES 3 C 259 SER VAL LEU ALA VAL LEU LYS GLY LEU TYR ASN PHE ALA
SEQRES 4 C 259 THR CYS GLY LEU VAL GLY LEU VAL THR PHE LEU LEU LEU
SEQRES 5 C 259 CYS GLY ARG SER CYS THR THR SER LEU TYR LYS GLY VAL
SEQRES 6 C 259 TYR GLU LEU GLN THR LEU GLU LEU ASN MET GLU THR LEU
SEQRES 7 C 259 ASN MET THR MET PRO LEU SER CYS THR LYS ASN ASN SER
SEQRES 8 C 259 HIS HIS TYR ILE MET VAL GLY ASN GLU THR GLY LEU GLU
SEQRES 9 C 259 LEU THR LEU THR ASN THR SER ILE ILE ASN HIS LYS PHE
SEQRES 10 C 259 CYS ASN LEU SER ASP ALA HIS LYS LYS ASN LEU TYR ASP
SEQRES 11 C 259 HIS ALA LEU MET SER ILE ILE SER THR PHE HIS LEU SER
SEQRES 12 C 259 ILE PRO ASN PHE ASN GLN TYR GLU ALA MET SER CYS ASP
SEQRES 13 C 259 PHE ASN GLY GLY LYS ILE SER VAL GLN TYR ASN LEU SER
SEQRES 14 C 259 HIS SER TYR ALA GLY ASP ALA ALA ASN HIS CYS GLY THR
SEQRES 15 C 259 VAL ALA ASN GLY VAL LEU GLN THR PHE MET ARG MET ALA
SEQRES 16 C 259 TRP GLY GLY SER TYR ILE ALA LEU ASP SER GLY ARG GLY
SEQRES 17 C 259 ASN TRP ASP CYS ILE MET THR SER TYR GLN TYR LEU ILE
SEQRES 18 C 259 ILE GLN ASN THR THR TRP GLU ASP HIS CYS GLN PHE SER
SEQRES 19 C 259 ARG PRO SER PRO ILE GLY TYR LEU GLY LEU LEU SER GLN
SEQRES 20 C 259 ARG THR ARG ASP ILE TYR ILE SER ARG ARG LEU LEU
HET NAG D 1 14
HET NAG D 2 14
HET NAG E 1 14
HET NAG E 2 14
HET NAG F 1 14
HET NAG F 2 14
HET XYS G 1 10
HET BDP G 2 12
HET XYS G 3 9
HET NAG H 1 14
HET NAG H 2 14
HET NAG I 1 14
HET NAG I 2 14
HET NAG J 1 14
HET NAG J 2 14
HET XYS K 1 10
HET BDP K 2 12
HET XYS K 3 9
HET NAG L 1 14
HET NAG L 2 14
HET NAG M 1 14
HET NAG M 2 14
HET NAG N 1 14
HET NAG N 2 14
HET XYS O 1 10
HET BDP O 2 12
HET XYS O 3 9
HET NAG a 601 14
HET NAG a 602 14
HET NAG a 603 14
HET NAG b 601 14
HET NAG b 602 14
HET NAG b 603 14
HET NAG c 601 14
HET NAG c 602 14
HET NAG c 603 14
HET NAG A 301 14
HET NAG A 302 14
HET NAG B 301 14
HET NAG B 302 14
HET NAG C 301 14
HET NAG C 302 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM XYS ALPHA-D-XYLOPYRANOSE
HETNAM BDP BETA-D-GLUCOPYRANURONIC ACID
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN XYS ALPHA-D-XYLOSE; D-XYLOSE; XYLOSE; XYLOPYRANOSE
HETSYN BDP BETA-D-GLUCURONIC ACID; D-GLUCURONIC ACID; GLUCURONIC
HETSYN 2 BDP ACID
FORMUL 7 NAG 33(C8 H15 N O6)
FORMUL 10 XYS 6(C5 H10 O5)
FORMUL 10 BDP 3(C6 H10 O7)
HELIX 1 AA1 GLY a 294 LYS a 300 1 7
HELIX 2 AA2 CYS a 301 GLU a 303 5 3
HELIX 3 AA3 GLU a 308 ARG a 325 1 18
HELIX 4 AA4 SER a 333 ILE a 345 1 13
HELIX 5 AA5 GLN a 348 GLY a 360 1 13
HELIX 6 AA6 PHE a 399 THR a 426 1 28
HELIX 7 AA7 PRO a 427 HIS a 448 1 22
HELIX 8 AA8 GLY b 294 LYS b 300 1 7
HELIX 9 AA9 CYS b 301 GLU b 303 5 3
HELIX 10 AB1 GLU b 308 ARG b 325 1 18
HELIX 11 AB2 SER b 333 ILE b 345 1 13
HELIX 12 AB3 GLN b 348 GLY b 360 1 13
HELIX 13 AB4 PHE b 399 THR b 426 1 28
HELIX 14 AB5 PRO b 427 HIS b 448 1 22
HELIX 15 AB6 GLY c 294 LYS c 300 1 7
HELIX 16 AB7 CYS c 301 GLU c 303 5 3
HELIX 17 AB8 GLU c 308 ARG c 325 1 18
HELIX 18 AB9 SER c 333 ILE c 345 1 13
HELIX 19 AC1 GLN c 348 GLY c 360 1 13
HELIX 20 AC2 PHE c 399 THR c 426 1 28
HELIX 21 AC3 PRO c 427 HIS c 448 1 22
HELIX 22 AC4 GLN A 3 VAL A 11 1 9
HELIX 23 AC5 VAL A 14 LEU A 35 1 22
HELIX 24 AC6 ASN A 74 ASN A 79 5 6
HELIX 25 AC7 ASN A 119 LYS A 126 1 8
HELIX 26 AC8 ASP A 130 SER A 143 1 14
HELIX 27 AC9 PHE A 157 LYS A 161 5 5
HELIX 28 AD1 THR A 182 ALA A 195 1 14
HELIX 29 AD2 PRO A 238 ARG A 248 1 11
HELIX 30 AD3 GLN B 3 VAL B 11 1 9
HELIX 31 AD4 VAL B 14 LEU B 35 1 22
HELIX 32 AD5 ASN B 74 ASN B 79 5 6
HELIX 33 AD6 ASN B 119 LYS B 126 1 8
HELIX 34 AD7 ASP B 130 SER B 143 1 14
HELIX 35 AD8 PHE B 157 LYS B 161 5 5
HELIX 36 AD9 THR B 182 ALA B 195 1 14
HELIX 37 AE1 PRO B 238 ARG B 248 1 11
HELIX 38 AE2 GLN C 3 VAL C 11 1 9
HELIX 39 AE3 VAL C 14 LEU C 35 1 22
HELIX 40 AE4 ASN C 74 ASN C 79 5 6
HELIX 41 AE5 ASN C 119 LYS C 126 1 8
HELIX 42 AE6 ASP C 130 SER C 143 1 14
HELIX 43 AE7 PHE C 157 LYS C 161 5 5
HELIX 44 AE8 THR C 182 ALA C 195 1 14
HELIX 45 AE9 PRO C 238 ARG C 248 1 11
SHEET 1 AA1 2 CYS a 279 LEU a 280 0
SHEET 2 AA1 2 LYS a 291 CYS a 292 -1 O LYS a 291 N LEU a 280
SHEET 1 AA2 5 SER a 392 TYR a 393 0
SHEET 2 AA2 5 LYS a 384 SER a 389 -1 N SER a 389 O SER a 392
SHEET 3 AA2 5 TYR a 363 HIS a 374 -1 N TYR a 363 O VAL a 388
SHEET 4 AA2 5 TYR A 66 GLU A 72 -1 O LEU A 71 N TYR a 369
SHEET 5 AA2 5 LEU A 61 TYR A 62 -1 N TYR A 62 O TYR A 66
SHEET 1 AA3 2 CYS b 279 LEU b 280 0
SHEET 2 AA3 2 LYS b 291 CYS b 292 -1 O LYS b 291 N LEU b 280
SHEET 1 AA4 5 SER b 392 TYR b 393 0
SHEET 2 AA4 5 LYS b 384 SER b 389 -1 N SER b 389 O SER b 392
SHEET 3 AA4 5 TYR b 363 HIS b 374 -1 N TYR b 363 O VAL b 388
SHEET 4 AA4 5 TYR B 66 GLU B 72 -1 O LEU B 71 N TYR b 369
SHEET 5 AA4 5 LEU B 61 TYR B 62 -1 N TYR B 62 O TYR B 66
SHEET 1 AA5 2 CYS c 279 LEU c 280 0
SHEET 2 AA5 2 LYS c 291 CYS c 292 -1 O LYS c 291 N LEU c 280
SHEET 1 AA6 5 SER c 392 TYR c 393 0
SHEET 2 AA6 5 LYS c 384 SER c 389 -1 N SER c 389 O SER c 392
SHEET 3 AA6 5 TYR c 363 HIS c 374 -1 N TYR c 363 O VAL c 388
SHEET 4 AA6 5 TYR C 66 GLU C 72 -1 O LEU C 71 N TYR c 369
SHEET 5 AA6 5 LEU C 61 TYR C 62 -1 N TYR C 62 O TYR C 66
SHEET 1 AA7 6 LEU A 84 THR A 87 0
SHEET 2 AA7 6 HIS A 92 VAL A 97 -1 O MET A 96 N LEU A 84
SHEET 3 AA7 6 THR A 101 THR A 108 -1 O LEU A 105 N HIS A 93
SHEET 4 AA7 6 TYR A 219 THR A 225 -1 O GLN A 223 N GLU A 104
SHEET 5 AA7 6 SER A 163 ASN A 167 -1 N TYR A 166 O LEU A 220
SHEET 6 AA7 6 SER A 154 ASP A 156 -1 N ASP A 156 O SER A 163
SHEET 1 AA8 6 LEU B 84 THR B 87 0
SHEET 2 AA8 6 HIS B 92 VAL B 97 -1 O MET B 96 N LEU B 84
SHEET 3 AA8 6 THR B 101 THR B 108 -1 O LEU B 105 N HIS B 93
SHEET 4 AA8 6 TYR B 219 THR B 225 -1 O GLN B 223 N GLU B 104
SHEET 5 AA8 6 SER B 163 ASN B 167 -1 N TYR B 166 O LEU B 220
SHEET 6 AA8 6 SER B 154 ASP B 156 -1 N ASP B 156 O SER B 163
SHEET 1 AA9 6 LEU C 84 THR C 87 0
SHEET 2 AA9 6 HIS C 92 VAL C 97 -1 O MET C 96 N LEU C 84
SHEET 3 AA9 6 THR C 101 THR C 108 -1 O LEU C 105 N HIS C 93
SHEET 4 AA9 6 TYR C 219 THR C 225 -1 O GLN C 223 N GLU C 104
SHEET 5 AA9 6 SER C 163 ASN C 167 -1 N TYR C 166 O LEU C 220
SHEET 6 AA9 6 SER C 154 ASP C 156 -1 N ASP C 156 O SER C 163
SSBOND 1 CYS a 279 CYS a 292 1555 1555 2.03
SSBOND 2 CYS a 301 CYS a 310 1555 1555 2.03
SSBOND 3 CYS a 364 CYS a 385 1555 1555 2.03
SSBOND 4 CYS b 279 CYS b 292 1555 1555 2.03
SSBOND 5 CYS b 301 CYS b 310 1555 1555 2.03
SSBOND 6 CYS b 364 CYS b 385 1555 1555 2.03
SSBOND 7 CYS c 279 CYS c 292 1555 1555 2.03
SSBOND 8 CYS c 301 CYS c 310 1555 1555 2.03
SSBOND 9 CYS c 364 CYS c 385 1555 1555 2.03
SSBOND 10 CYS A 86 CYS A 231 1555 1555 2.03
SSBOND 11 CYS A 118 CYS A 155 1555 1555 2.03
SSBOND 12 CYS A 180 CYS A 212 1555 1555 2.03
SSBOND 13 CYS B 86 CYS B 231 1555 1555 2.03
SSBOND 14 CYS B 118 CYS B 155 1555 1555 2.03
SSBOND 15 CYS B 180 CYS B 212 1555 1555 2.03
SSBOND 16 CYS C 86 CYS C 231 1555 1555 2.03
SSBOND 17 CYS C 118 CYS C 155 1555 1555 2.03
SSBOND 18 CYS C 180 CYS C 212 1555 1555 2.03
LINK ND2 ASN a 365 C1 NAG a 601 1555 1555 1.44
LINK ND2 ASN a 373 C1 NAG a 602 1555 1555 1.44
LINK ND2 ASN a 395 C1 NAG a 603 1555 1555 1.44
LINK ND2 ASN b 365 C1 NAG b 601 1555 1555 1.44
LINK ND2 ASN b 373 C1 NAG b 602 1555 1555 1.44
LINK ND2 ASN b 395 C1 NAG b 603 1555 1555 1.44
LINK ND2 ASN c 365 C1 NAG c 601 1555 1555 1.44
LINK ND2 ASN c 373 C1 NAG c 602 1555 1555 1.44
LINK ND2 ASN c 395 C1 NAG c 603 1555 1555 1.44
LINK ND2 ASN A 79 C1 NAG F 1 1555 1555 1.45
LINK ND2 ASN A 99 C1 NAG A 301 1555 1555 1.44
LINK ND2 ASN A 109 C1 NAG A 302 1555 1555 1.44
LINK ND2 ASN A 119 C1 NAG D 1 1555 1555 1.45
LINK ND2 ASN A 167 C1 NAG E 1 1555 1555 1.44
LINK ND2 ASN B 79 C1 NAG J 1 1555 1555 1.45
LINK ND2 ASN B 99 C1 NAG B 301 1555 1555 1.44
LINK ND2 ASN B 109 C1 NAG B 302 1555 1555 1.44
LINK ND2 ASN B 119 C1 NAG H 1 1555 1555 1.45
LINK ND2 ASN B 167 C1 NAG I 1 1555 1555 1.44
LINK ND2 ASN C 79 C1 NAG N 1 1555 1555 1.45
LINK ND2 ASN C 99 C1 NAG C 301 1555 1555 1.44
LINK ND2 ASN C 109 C1 NAG C 302 1555 1555 1.44
LINK ND2 ASN C 119 C1 NAG L 1 1555 1555 1.45
LINK ND2 ASN C 167 C1 NAG M 1 1555 1555 1.44
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44
LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44
LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44
LINK O3 XYS G 1 C1 BDP G 2 1555 1555 1.45
LINK O3 BDP G 2 C1 XYS G 3 1555 1555 1.44
LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44
LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44
LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44
LINK O3 XYS K 1 C1 BDP K 2 1555 1555 1.45
LINK O3 BDP K 2 C1 XYS K 3 1555 1555 1.44
LINK O4 NAG L 1 C1 NAG L 2 1555 1555 1.44
LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.44
LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.44
LINK O3 XYS O 1 C1 BDP O 2 1555 1555 1.45
LINK O3 BDP O 2 C1 XYS O 3 1555 1555 1.44
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
MTRIX1 1 -0.495545 -0.868581 -0.001462 314.27517 1
MTRIX2 1 0.868581 -0.495540 -0.002558 83.66379 1
MTRIX3 1 0.001497 -0.002538 0.999996 -0.00826 1
MTRIX1 2 -0.503503 0.863993 0.000693 84.85545 1
MTRIX2 2 -0.863989 -0.503503 0.002917 314.00290 1
MTRIX3 2 0.002870 0.000870 0.999996 -0.47468 1
MTRIX1 3 -0.500899 -0.865505 -0.000693 314.54473 1
MTRIX2 3 0.865505 -0.500900 0.000604 84.26124 1
MTRIX3 3 -0.000870 -0.000297 1.000000 -0.04413 1
MTRIX1 4 -0.498615 0.866820 -0.002721 84.36599 1
MTRIX2 4 -0.866821 -0.498619 -0.001042 314.40996 1
MTRIX3 4 -0.002260 0.001839 0.999996 0.11112 1
ATOM 1 N GLY a 260 135.457 132.754 145.581 1.00 28.37 N
ATOM 2 CA GLY a 260 136.092 132.297 144.360 1.00 28.37 C
ATOM 3 C GLY a 260 135.268 131.271 143.606 1.00 28.37 C
ATOM 4 O GLY a 260 134.070 131.123 143.846 1.00 28.37 O
ATOM 5 N THR a 261 135.914 130.561 142.685 1.00 28.52 N
ATOM 6 CA THR a 261 135.279 129.520 141.889 1.00 28.52 C
ATOM 7 C THR a 261 136.126 128.255 141.957 1.00 28.52 C
ATOM 8 O THR a 261 137.188 128.222 142.584 1.00 28.52 O
ATOM 9 CB THR a 261 135.089 129.959 140.430 1.00 28.52 C
ATOM 10 OG1 THR a 261 136.365 130.030 139.784 1.00 28.52 O
ATOM 11 CG2 THR a 261 134.410 131.320 140.353 1.00 28.52 C
ATOM 12 N PHE a 262 135.643 127.205 141.301 1.00 28.44 N
ATOM 13 CA PHE a 262 136.378 125.951 141.237 1.00 28.44 C
ATOM 14 C PHE a 262 137.637 126.105 140.389 1.00 28.44 C
ATOM 15 O PHE a 262 137.669 126.854 139.409 1.00 28.44 O
ATOM 16 CB PHE a 262 135.488 124.848 140.666 1.00 28.44 C
ATOM 17 CG PHE a 262 134.854 125.203 139.350 1.00 28.44 C
ATOM 18 CD1 PHE a 262 135.513 124.958 138.156 1.00 28.44 C
ATOM 19 CD2 PHE a 262 133.597 125.783 139.308 1.00 28.44 C
ATOM 20 CE1 PHE a 262 134.932 125.289 136.949 1.00 28.44 C
ATOM 21 CE2 PHE a 262 133.010 126.115 138.105 1.00 28.44 C
ATOM 22 CZ PHE a 262 133.678 125.868 136.924 1.00 28.44 C
ATOM 23 N THR a 263 138.688 125.384 140.784 1.00 28.35 N
ATOM 24 CA THR a 263 139.940 125.378 140.040 1.00 28.35 C
ATOM 25 C THR a 263 140.488 123.989 139.752 1.00 28.35 C
ATOM 26 O THR a 263 141.475 123.882 139.015 1.00 28.35 O
ATOM 27 CB THR a 263 141.016 126.181 140.787 1.00 28.35 C
ATOM 28 OG1 THR a 263 141.099 125.725 142.144 1.00 28.35 O
ATOM 29 CG2 THR a 263 140.680 127.661 140.775 1.00 28.35 C
ATOM 30 N TRP a 264 139.893 122.932 140.299 1.00 28.07 N
ATOM 31 CA TRP a 264 140.408 121.585 140.092 1.00 28.07 C
ATOM 32 C TRP a 264 140.328 121.190 138.623 1.00 28.07 C
ATOM 33 O TRP a 264 139.402 121.569 137.900 1.00 28.07 O
ATOM 34 CB TRP a 264 139.632 120.588 140.951 1.00 28.07 C
ATOM 35 CG TRP a 264 140.155 119.183 140.900 1.00 28.07 C
ATOM 36 CD1 TRP a 264 139.850 118.230 139.973 1.00 28.07 C
ATOM 37 CD2 TRP a 264 141.073 118.572 141.816 1.00 28.07 C
ATOM 38 NE1 TRP a 264 140.520 117.064 140.254 1.00 28.07 N
ATOM 39 CE2 TRP a 264 141.278 117.248 141.380 1.00 28.07 C
ATOM 40 CE3 TRP a 264 141.741 119.016 142.961 1.00 28.07 C
ATOM 41 CZ2 TRP a 264 142.122 116.364 142.048 1.00 28.07 C
ATOM 42 CZ3 TRP a 264 142.578 118.137 143.622 1.00 28.07 C
ATOM 43 CH2 TRP a 264 142.761 116.826 143.164 1.00 28.07 C
ATOM 44 N THR a 265 141.316 120.414 138.184 1.00 32.55 N
ATOM 45 CA THR a 265 141.405 119.950 136.810 1.00 32.55 C
ATOM 46 C THR a 265 141.316 118.431 136.775 1.00 32.55 C
ATOM 47 O THR a 265 141.767 117.743 137.697 1.00 32.55 O
ATOM 48 CB THR a 265 142.709 120.407 136.145 1.00 32.55 C
ATOM 49 OG1 THR a 265 143.826 119.875 136.867 1.00 32.55 O
ATOM 50 CG2 THR a 265 142.796 121.925 136.132 1.00 32.55 C
ATOM 51 N LEU a 266 140.740 117.913 135.695 1.00 38.00 N
ATOM 52 CA LEU a 266 140.467 116.487 135.590 1.00 38.00 C
ATOM 53 C LEU a 266 141.729 115.717 135.226 1.00 38.00 C
ATOM 54 O LEU a 266 142.431 116.069 134.274 1.00 38.00 O
ATOM 55 CB LEU a 266 139.378 116.238 134.550 1.00 38.00 C
ATOM 56 CG LEU a 266 137.980 116.700 134.956 1.00 38.00 C
ATOM 57 CD1 LEU a 266 136.996 116.401 133.849 1.00 38.00 C
ATOM 58 CD2 LEU a 266 137.550 116.033 136.254 1.00 38.00 C
ATOM 59 N SER a 267 142.013 114.666 135.991 1.00 42.77 N
ATOM 60 CA SER a 267 143.165 113.822 135.717 1.00 42.77 C
ATOM 61 C SER a 267 142.978 113.067 134.406 1.00 42.77 C
ATOM 62 O SER a 267 141.855 112.774 133.986 1.00 42.77 O
ATOM 63 CB SER a 267 143.392 112.836 136.862 1.00 42.77 C
ATOM 64 OG SER a 267 144.489 111.982 136.588 1.00 42.77 O
ATOM 65 N ASP a 268 144.098 112.770 133.750 1.00 52.98 N
ATOM 66 CA ASP a 268 144.070 112.015 132.504 1.00 52.98 C
ATOM 67 C ASP a 268 143.389 110.667 132.707 1.00 52.98 C
ATOM 68 O ASP a 268 143.656 109.961 133.684 1.00 52.98 O
ATOM 69 CB ASP a 268 145.491 111.817 131.977 1.00 52.98 C
ATOM 70 CG ASP a 268 146.420 111.226 133.017 1.00 52.98 C
ATOM 71 OD1 ASP a 268 146.495 111.784 134.133 1.00 52.98 O
ATOM 72 OD2 ASP a 268 147.074 110.204 132.722 1.00 52.98 O
ATOM 73 N SER a 269 142.504 110.314 131.780 1.00 61.65 N
ATOM 74 CA SER a 269 141.698 109.106 131.872 1.00 61.65 C
ATOM 75 C SER a 269 142.164 108.095 130.834 1.00 61.65 C
ATOM 76 O SER a 269 142.417 108.449 129.678 1.00 61.65 O
ATOM 77 CB SER a 269 140.212 109.418 131.670 1.00 61.65 C
ATOM 78 OG SER a 269 139.960 109.860 130.348 1.00 61.65 O
ATOM 79 N GLU a 270 142.277 106.834 131.253 1.00 70.87 N
ATOM 80 CA GLU a 270 142.782 105.768 130.389 1.00 70.87 C
ATOM 81 C GLU a 270 141.660 105.207 129.510 1.00 70.87 C
ATOM 82 O GLU a 270 141.276 104.041 129.593 1.00 70.87 O
ATOM 83 CB GLU a 270 143.430 104.675 131.229 1.00 70.87 C
ATOM 84 CG GLU a 270 144.745 105.085 131.873 1.00 70.87 C
ATOM 85 CD GLU a 270 145.769 105.562 130.861 1.00 70.87 C
ATOM 86 OE1 GLU a 270 145.895 104.927 129.792 1.00 70.87 O
ATOM 87 OE2 GLU a 270 146.449 106.574 131.134 1.00 70.87 O
ATOM 88 N GLY a 271 141.135 106.078 128.653 1.00 70.82 N
ATOM 89 CA GLY a 271 140.155 105.678 127.663 1.00 70.82 C
ATOM 90 C GLY a 271 140.631 105.930 126.248 1.00 70.82 C
ATOM 91 O GLY a 271 140.923 107.073 125.882 1.00 70.82 O
ATOM 92 N LYS a 272 140.727 104.867 125.446 1.00 75.33 N
ATOM 93 CA LYS a 272 141.254 105.011 124.092 1.00 75.33 C
ATOM 94 C LYS a 272 140.355 105.895 123.236 1.00 75.33 C
ATOM 95 O LYS a 272 140.844 106.749 122.486 1.00 75.33 O
ATOM 96 CB LYS a 272 141.431 103.633 123.450 1.00 75.33 C
ATOM 97 CG LYS a 272 140.223 102.718 123.582 1.00 75.33 C
ATOM 98 CD LYS a 272 140.450 101.394 122.871 1.00 75.33 C
ATOM 99 CE LYS a 272 139.239 100.484 123.000 1.00 75.33 C
ATOM 100 NZ LYS a 272 139.487 99.141 122.406 1.00 75.33 N
ATOM 101 N ASP a 273 139.036 105.703 123.329 1.00 70.54 N
ATOM 102 CA ASP a 273 138.116 106.517 122.541 1.00 70.54 C
ATOM 103 C ASP a 273 138.146 107.975 122.984 1.00 70.54 C
ATOM 104 O ASP a 273 138.105 108.885 122.148 1.00 70.54 O
ATOM 105 CB ASP a 273 136.699 105.950 122.635 1.00 70.54 C
ATOM 106 CG ASP a 273 136.184 105.895 124.059 1.00 70.54 C
ATOM 107 OD1 ASP a 273 137.001 105.697 124.983 1.00 70.54 O
ATOM 108 OD2 ASP a 273 134.960 106.051 124.254 1.00 70.54 O
ATOM 109 N THR a 274 138.219 108.217 124.295 1.00 67.10 N
ATOM 110 CA THR a 274 138.167 109.562 124.868 1.00 67.10 C
ATOM 111 C THR a 274 139.472 109.817 125.611 1.00 67.10 C
ATOM 112 O THR a 274 139.606 109.458 126.791 1.00 67.10 O
ATOM 113 CB THR a 274 136.967 109.714 125.800 1.00 67.10 C
ATOM 114 OG1 THR a 274 137.143 108.872 126.946 1.00 67.10 O
ATOM 115 CG2 THR a 274 135.688 109.307 125.082 1.00 67.10 C
ATOM 116 N PRO a 275 140.462 110.433 124.960 1.00 64.99 N
ATOM 117 CA PRO a 275 141.767 110.629 125.608 1.00 64.99 C
ATOM 118 C PRO a 275 141.722 111.576 126.798 1.00 64.99 C
ATOM 119 O PRO a 275 142.292 111.280 127.853 1.00 64.99 O
ATOM 120 CB PRO a 275 142.639 111.199 124.480 1.00 64.99 C
ATOM 121 CG PRO a 275 141.675 111.754 123.483 1.00 64.99 C
ATOM 122 CD PRO a 275 140.455 110.895 123.562 1.00 64.99 C
ATOM 123 N GLY a 276 141.051 112.714 126.643 1.00 56.90 N
ATOM 124 CA GLY a 276 141.085 113.746 127.661 1.00 56.90 C
ATOM 125 C GLY a 276 139.826 113.889 128.492 1.00 56.90 C
ATOM 126 O GLY a 276 139.733 114.799 129.321 1.00 56.90 O
ATOM 127 N GLY a 277 138.852 113.008 128.289 1.00 50.78 N
ATOM 128 CA GLY a 277 137.554 113.118 128.933 1.00 50.78 C
ATOM 129 C GLY a 277 137.361 112.028 129.974 1.00 50.78 C
ATOM 130 O GLY a 277 137.671 110.860 129.729 1.00 50.78 O
ATOM 131 N TYR a 278 136.863 112.437 131.140 1.00 44.16 N
ATOM 132 CA TYR a 278 136.652 111.513 132.248 1.00 44.16 C
ATOM 133 C TYR a 278 135.718 110.383 131.836 1.00 44.16 C
ATOM 134 O TYR a 278 134.564 110.622 131.465 1.00 44.16 O