HEADER MEMBRANE PROTEIN, METAL TRANSPORT 03-JAN-18 6C14
TITLE CRYOEM STRUCTURE OF MOUSE PCDH15-1EC-LHFPL5 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTOCADHERIN-15;
COMPND 3 CHAIN: A, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: LHFPL TETRASPAN SUBFAMILY MEMBER 5 PROTEIN;
COMPND 7 CHAIN: B, D;
COMPND 8 SYNONYM: LIPOMA HMGIC FUSION PARTNER-LIKE 5 PROTEIN,TETRASPAN
COMPND 9 MEMBRANE PROTEIN OF HAIR CELL STEREOCILIA;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PCDH15;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_COMMON: MOUSE;
SOURCE 11 ORGANISM_TAXID: 10090;
SOURCE 12 GENE: LHFPL5, TMHS;
SOURCE 13 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS PCDH15, LHFPL5, PROTOCADHERIN, TIP LINK, HAIR CELL, TMHS, HEARING,
KEYWDS 2 MEMBRANE PROTEIN, METAL TRANSPORT
EXPDTA ELECTRON MICROSCOPY
AUTHOR E.GOUAUX,J.ELFERICH,J.GE
REVDAT 2 18-DEC-19 6C14 1 SCALE
REVDAT 1 15-AUG-18 6C14 0
JRNL AUTH J.GE,J.ELFERICH,A.GOEHRING,J.ZHAO,P.SCHUCK,E.GOUAUX
JRNL TITL STRUCTURE OF MOUSE PROTOCADHERIN 15 OF THE STEREOCILIA TIP
JRNL TITL 2 LINK IN COMPLEX WITH LHFPL5.
JRNL REF ELIFE V. 7 2018
JRNL REFN ESSN 2050-084X
JRNL PMID 30070639
JRNL DOI 10.7554/ELIFE.38770
REMARK 2
REMARK 2 RESOLUTION. 4.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : GAUTOMATCH, GCTF, RELION
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.500
REMARK 3 NUMBER OF PARTICLES : 78792
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 6C14 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1000231914.
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 : MEMBRANE PROTEIN 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 : 8.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 74.00
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 GLY A 1140
REMARK 465 GLN A 1141
REMARK 465 TYR A 1142
REMARK 465 ASP A 1143
REMARK 465 ASP A 1144
REMARK 465 GLN A 1411
REMARK 465 ALA A 1412
REMARK 465 GLU A 1413
REMARK 465 CYS A 1414
REMARK 465 THR A 1415
REMARK 465 LYS A 1416
REMARK 465 THR A 1417
REMARK 465 ALA A 1418
REMARK 465 ARG A 1419
REMARK 465 ILE A 1420
REMARK 465 GLN A 1421
REMARK 465 SER A 1422
REMARK 465 ALA A 1423
REMARK 465 MET A 1424
REMARK 465 PRO A 1425
REMARK 465 ALA A 1426
REMARK 465 ALA A 1427
REMARK 465 LYS A 1428
REMARK 465 PRO A 1429
REMARK 465 ALA A 1430
REMARK 465 ALA A 1431
REMARK 465 PRO A 1432
REMARK 465 VAL A 1433
REMARK 465 PRO A 1434
REMARK 465 ALA A 1435
REMARK 465 ALA A 1436
REMARK 465 PRO A 1437
REMARK 465 ALA A 1438
REMARK 465 PRO A 1439
REMARK 465 PRO A 1440
REMARK 465 PRO A 1441
REMARK 465 PRO A 1442
REMARK 465 PRO A 1443
REMARK 465 PRO A 1444
REMARK 465 PRO A 1445
REMARK 465 PRO A 1446
REMARK 465 PRO A 1447
REMARK 465 PRO A 1448
REMARK 465 GLY A 1449
REMARK 465 ALA A 1450
REMARK 465 HIS A 1451
REMARK 465 LEU A 1452
REMARK 465 TYR A 1453
REMARK 465 GLU A 1454
REMARK 465 GLU A 1455
REMARK 465 LEU A 1456
REMARK 465 GLY A 1457
REMARK 465 GLU A 1458
REMARK 465 SER A 1459
REMARK 465 ALA A 1460
REMARK 465 MET A 1461
REMARK 465 HIS A 1462
REMARK 465 LYS A 1463
REMARK 465 TYR A 1464
REMARK 465 GLU A 1465
REMARK 465 THR A 1466
REMARK 465 ALA A 1467
REMARK 465 LEU A 1468
REMARK 465 PHE A 1469
REMARK 465 GLU A 1470
REMARK 465 SER A 1471
REMARK 465 ARG A 1472
REMARK 465 LEU A 1473
REMARK 465 VAL A 1474
REMARK 465 PRO A 1475
REMARK 465 ARG A 1476
REMARK 465 GLY B -6
REMARK 465 SER B -5
REMARK 465 GLY B -4
REMARK 465 GLY B -3
REMARK 465 ARG B -2
REMARK 465 ALA B -1
REMARK 465 THR B 0
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 LYS B 3
REMARK 465 LEU B 4
REMARK 465 LEU B 5
REMARK 465 PRO B 6
REMARK 465 ALA B 7
REMARK 465 GLN B 8
REMARK 465 GLU B 9
REMARK 465 ALA B 10
REMARK 465 ALA B 11
REMARK 465 LYS B 12
REMARK 465 ILE B 13
REMARK 465 TYR B 14
REMARK 465 SER B 55
REMARK 465 THR B 56
REMARK 465 PRO B 57
REMARK 465 ASP B 153
REMARK 465 SER B 154
REMARK 465 SER B 155
REMARK 465 GLU B 156
REMARK 465 VAL B 157
REMARK 465 ARG B 158
REMARK 465 ARG B 159
REMARK 465 MET B 160
REMARK 465 CYS B 161
REMARK 465 GLY B 162
REMARK 465 GLU B 163
REMARK 465 GLN B 164
REMARK 465 THR B 165
REMARK 465 GLY B 166
REMARK 465 LYS B 167
REMARK 465 TYR B 168
REMARK 465 THR B 169
REMARK 465 LEU B 170
REMARK 465 GLY B 200
REMARK 465 TYR B 201
REMARK 465 ARG B 202
REMARK 465 GLN B 203
REMARK 465 ASP B 204
REMARK 465 LYS B 205
REMARK 465 LEU B 206
REMARK 465 LEU B 207
REMARK 465 PRO B 208
REMARK 465 ASP B 209
REMARK 465 ASP B 210
REMARK 465 TYR B 211
REMARK 465 LYS B 212
REMARK 465 ALA B 213
REMARK 465 ASP B 214
REMARK 465 GLY B 215
REMARK 465 ASN B 216
REMARK 465 GLU B 217
REMARK 465 GLU B 218
REMARK 465 VAL B 219
REMARK 465 PHE B 220
REMARK 465 GLU B 221
REMARK 465 GLY C 1140
REMARK 465 GLN C 1141
REMARK 465 TYR C 1142
REMARK 465 ASP C 1143
REMARK 465 ASP C 1144
REMARK 465 GLN C 1411
REMARK 465 ALA C 1412
REMARK 465 GLU C 1413
REMARK 465 CYS C 1414
REMARK 465 THR C 1415
REMARK 465 LYS C 1416
REMARK 465 THR C 1417
REMARK 465 ALA C 1418
REMARK 465 ARG C 1419
REMARK 465 ILE C 1420
REMARK 465 GLN C 1421
REMARK 465 SER C 1422
REMARK 465 ALA C 1423
REMARK 465 MET C 1424
REMARK 465 PRO C 1425
REMARK 465 ALA C 1426
REMARK 465 ALA C 1427
REMARK 465 LYS C 1428
REMARK 465 PRO C 1429
REMARK 465 ALA C 1430
REMARK 465 ALA C 1431
REMARK 465 PRO C 1432
REMARK 465 VAL C 1433
REMARK 465 PRO C 1434
REMARK 465 ALA C 1435
REMARK 465 ALA C 1436
REMARK 465 PRO C 1437
REMARK 465 ALA C 1438
REMARK 465 PRO C 1439
REMARK 465 PRO C 1440
REMARK 465 PRO C 1441
REMARK 465 PRO C 1442
REMARK 465 PRO C 1443
REMARK 465 PRO C 1444
REMARK 465 PRO C 1445
REMARK 465 PRO C 1446
REMARK 465 PRO C 1447
REMARK 465 PRO C 1448
REMARK 465 GLY C 1449
REMARK 465 ALA C 1450
REMARK 465 HIS C 1451
REMARK 465 LEU C 1452
REMARK 465 TYR C 1453
REMARK 465 GLU C 1454
REMARK 465 GLU C 1455
REMARK 465 LEU C 1456
REMARK 465 GLY C 1457
REMARK 465 GLU C 1458
REMARK 465 SER C 1459
REMARK 465 ALA C 1460
REMARK 465 MET C 1461
REMARK 465 HIS C 1462
REMARK 465 LYS C 1463
REMARK 465 TYR C 1464
REMARK 465 GLU C 1465
REMARK 465 THR C 1466
REMARK 465 ALA C 1467
REMARK 465 LEU C 1468
REMARK 465 PHE C 1469
REMARK 465 GLU C 1470
REMARK 465 SER C 1471
REMARK 465 ARG C 1472
REMARK 465 LEU C 1473
REMARK 465 VAL C 1474
REMARK 465 PRO C 1475
REMARK 465 ARG C 1476
REMARK 465 GLY D -6
REMARK 465 SER D -5
REMARK 465 GLY D -4
REMARK 465 GLY D -3
REMARK 465 ARG D -2
REMARK 465 ALA D -1
REMARK 465 THR D 0
REMARK 465 MET D 1
REMARK 465 VAL D 2
REMARK 465 LYS D 3
REMARK 465 LEU D 4
REMARK 465 LEU D 5
REMARK 465 PRO D 6
REMARK 465 ALA D 7
REMARK 465 GLN D 8
REMARK 465 GLU D 9
REMARK 465 ALA D 10
REMARK 465 ALA D 11
REMARK 465 LYS D 12
REMARK 465 ILE D 13
REMARK 465 TYR D 14
REMARK 465 SER D 55
REMARK 465 THR D 56
REMARK 465 PRO D 57
REMARK 465 ASP D 153
REMARK 465 SER D 154
REMARK 465 SER D 155
REMARK 465 GLU D 156
REMARK 465 VAL D 157
REMARK 465 ARG D 158
REMARK 465 ARG D 159
REMARK 465 MET D 160
REMARK 465 CYS D 161
REMARK 465 GLY D 162
REMARK 465 GLU D 163
REMARK 465 GLN D 164
REMARK 465 THR D 165
REMARK 465 GLY D 166
REMARK 465 LYS D 167
REMARK 465 TYR D 168
REMARK 465 THR D 169
REMARK 465 LEU D 170
REMARK 465 GLY D 200
REMARK 465 TYR D 201
REMARK 465 ARG D 202
REMARK 465 GLN D 203
REMARK 465 ASP D 204
REMARK 465 LYS D 205
REMARK 465 LEU D 206
REMARK 465 LEU D 207
REMARK 465 PRO D 208
REMARK 465 ASP D 209
REMARK 465 ASP D 210
REMARK 465 TYR D 211
REMARK 465 LYS D 212
REMARK 465 ALA D 213
REMARK 465 ASP D 214
REMARK 465 GLY D 215
REMARK 465 ASN D 216
REMARK 465 GLU D 217
REMARK 465 GLU D 218
REMARK 465 VAL D 219
REMARK 465 PHE D 220
REMARK 465 GLU D 221
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 THR A1361 C - N - CA ANGL. DEV. = 16.7 DEGREES
REMARK 500 CYS B 114 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 THR C1361 C - N - CA ANGL. DEV. = 17.0 DEGREES
REMARK 500 CYS D 114 CA - CB - SG ANGL. DEV. = 7.1 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 ASN A1180 58.09 -95.11
REMARK 500 TRP B 49 -62.48 -106.26
REMARK 500 LEU B 64 -7.81 66.15
REMARK 500 LEU B 73 18.85 58.73
REMARK 500 LEU B 117 36.20 -98.44
REMARK 500 ASN C1180 58.04 -95.34
REMARK 500 GLU C1195 15.91 59.98
REMARK 500 TRP D 49 -62.45 -106.31
REMARK 500 LEU D 64 -7.87 66.22
REMARK 500 LEU D 73 18.86 58.75
REMARK 500 LEU D 117 36.19 -98.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-7328 RELATED DB: EMDB
REMARK 900 CRYOEM STRUCTURE OF MEMBRANE PROTEIN COMPLEX
REMARK 900 RELATED ID: EMD-7327 RELATED DB: EMDB
DBREF 6C14 A 1144 1465 UNP Q99PJ1 PCD15_MOUSE 1144 1465
DBREF 6C14 B 1 219 UNP Q4KL25 LHPL5_MOUSE 1 219
DBREF 6C14 C 1144 1465 UNP Q99PJ1 PCD15_MOUSE 1144 1465
DBREF 6C14 D 1 219 UNP Q4KL25 LHPL5_MOUSE 1 219
SEQADV 6C14 GLY A 1140 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 GLN A 1141 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 TYR A 1142 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 ASP A 1143 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 THR A 1466 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 ALA A 1467 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 LEU A 1468 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 PHE A 1469 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 GLU A 1470 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 SER A 1471 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 ARG A 1472 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 LEU A 1473 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 VAL A 1474 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 PRO A 1475 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 ARG A 1476 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 GLY B -6 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 SER B -5 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 GLY B -4 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 GLY B -3 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 ARG B -2 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 ALA B -1 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 THR B 0 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 PHE B 220 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 GLU B 221 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 GLY C 1140 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 GLN C 1141 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 TYR C 1142 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 ASP C 1143 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 THR C 1466 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 ALA C 1467 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 LEU C 1468 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 PHE C 1469 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 GLU C 1470 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 SER C 1471 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 ARG C 1472 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 LEU C 1473 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 VAL C 1474 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 PRO C 1475 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 ARG C 1476 UNP Q99PJ1 EXPRESSION TAG
SEQADV 6C14 GLY D -6 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 SER D -5 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 GLY D -4 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 GLY D -3 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 ARG D -2 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 ALA D -1 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 THR D 0 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 PHE D 220 UNP Q4KL25 EXPRESSION TAG
SEQADV 6C14 GLU D 221 UNP Q4KL25 EXPRESSION TAG
SEQRES 1 A 337 GLY GLN TYR ASP ASP HIS PRO PRO VAL PHE GLN LYS LYS
SEQRES 2 A 337 PHE TYR ILE GLY GLY VAL SER GLU ASP ALA ARG MET PHE
SEQRES 3 A 337 ALA SER VAL LEU ARG VAL LYS ALA THR ASP ARG ASP THR
SEQRES 4 A 337 GLY ASN TYR SER ALA MET ALA TYR ARG LEU ILE ILE PRO
SEQRES 5 A 337 PRO ILE LYS GLU GLY LYS GLU GLY PHE VAL VAL GLU THR
SEQRES 6 A 337 TYR THR GLY LEU ILE LYS THR ALA MET LEU PHE HIS ASN
SEQRES 7 A 337 MET ARG ARG SER TYR PHE LYS PHE GLN VAL ILE ALA THR
SEQRES 8 A 337 ASP ASP TYR GLY LYS GLY LEU SER GLY LYS ALA ASP VAL
SEQRES 9 A 337 LEU VAL SER VAL VAL ASN GLN LEU ASP MET GLN VAL ILE
SEQRES 10 A 337 VAL SER ASN VAL PRO PRO THR LEU VAL GLU LYS LYS ILE
SEQRES 11 A 337 GLU ASP LEU THR GLU ILE LEU ASP ARG TYR VAL GLN GLU
SEQRES 12 A 337 GLN ILE PRO GLY ALA LYS VAL VAL VAL GLU SER ILE GLY
SEQRES 13 A 337 ALA ARG ARG HIS GLY ASP ALA TYR SER LEU GLU ASP TYR
SEQRES 14 A 337 SER LYS CYS ASP LEU THR VAL TYR ALA ILE ASP PRO GLN
SEQRES 15 A 337 THR ASN ARG ALA ILE ASP ARG ASN GLU LEU PHE LYS PHE
SEQRES 16 A 337 LEU ASP GLY LYS LEU LEU ASP ILE ASN LYS ASP PHE GLN
SEQRES 17 A 337 PRO TYR TYR GLY GLU GLY GLY ARG ILE LEU GLU ILE ARG
SEQRES 18 A 337 THR PRO GLU ALA VAL THR SER ILE LYS LYS ARG GLY GLU
SEQRES 19 A 337 SER LEU GLY TYR THR GLU GLY ALA LEU LEU ALA LEU ALA
SEQRES 20 A 337 PHE ILE ILE ILE LEU CYS CYS ILE PRO ALA ILE LEU VAL
SEQRES 21 A 337 VAL LEU VAL SER TYR ARG GLN PHE LYS VAL ARG GLN ALA
SEQRES 22 A 337 GLU CYS THR LYS THR ALA ARG ILE GLN SER ALA MET PRO
SEQRES 23 A 337 ALA ALA LYS PRO ALA ALA PRO VAL PRO ALA ALA PRO ALA
SEQRES 24 A 337 PRO PRO PRO PRO PRO PRO PRO PRO PRO PRO GLY ALA HIS
SEQRES 25 A 337 LEU TYR GLU GLU LEU GLY GLU SER ALA MET HIS LYS TYR
SEQRES 26 A 337 GLU THR ALA LEU PHE GLU SER ARG LEU VAL PRO ARG
SEQRES 1 B 228 GLY SER GLY GLY ARG ALA THR MET VAL LYS LEU LEU PRO
SEQRES 2 B 228 ALA GLN GLU ALA ALA LYS ILE TYR HIS THR ASN TYR VAL
SEQRES 3 B 228 ARG ASN SER ARG ALA VAL GLY VAL MET TRP GLY THR LEU
SEQRES 4 B 228 THR ILE CYS PHE SER VAL LEU VAL MET ALA LEU PHE ILE
SEQRES 5 B 228 GLN PRO TYR TRP ILE GLY ASP SER VAL SER THR PRO GLN
SEQRES 6 B 228 ALA GLY TYR PHE GLY LEU PHE SER TYR CYS VAL GLY ASN
SEQRES 7 B 228 VAL LEU SER SER GLU LEU ILE CYS LYS GLY GLY PRO LEU
SEQRES 8 B 228 ASP PHE SER SER ILE PRO SER ARG ALA PHE LYS THR ALA
SEQRES 9 B 228 MET PHE PHE VAL ALA LEU ALA MET PHE LEU ILE ILE GLY
SEQRES 10 B 228 SER ILE ILE CYS PHE SER LEU PHE PHE VAL CYS ASN THR
SEQRES 11 B 228 ALA THR VAL TYR LYS ILE CYS ALA TRP MET GLN LEU ALA
SEQRES 12 B 228 ALA ALA THR GLY LEU MET ILE GLY CYS LEU VAL TYR PRO
SEQRES 13 B 228 ASP GLY TRP ASP SER SER GLU VAL ARG ARG MET CYS GLY
SEQRES 14 B 228 GLU GLN THR GLY LYS TYR THR LEU GLY HIS CYS THR ILE
SEQRES 15 B 228 ARG TRP ALA PHE MET LEU ALA ILE LEU SER ILE GLY ASP
SEQRES 16 B 228 ALA LEU ILE LEU SER PHE LEU ALA PHE VAL LEU GLY TYR
SEQRES 17 B 228 ARG GLN ASP LYS LEU LEU PRO ASP ASP TYR LYS ALA ASP
SEQRES 18 B 228 GLY ASN GLU GLU VAL PHE GLU
SEQRES 1 C 337 GLY GLN TYR ASP ASP HIS PRO PRO VAL PHE GLN LYS LYS
SEQRES 2 C 337 PHE TYR ILE GLY GLY VAL SER GLU ASP ALA ARG MET PHE
SEQRES 3 C 337 ALA SER VAL LEU ARG VAL LYS ALA THR ASP ARG ASP THR
SEQRES 4 C 337 GLY ASN TYR SER ALA MET ALA TYR ARG LEU ILE ILE PRO
SEQRES 5 C 337 PRO ILE LYS GLU GLY LYS GLU GLY PHE VAL VAL GLU THR
SEQRES 6 C 337 TYR THR GLY LEU ILE LYS THR ALA MET LEU PHE HIS ASN
SEQRES 7 C 337 MET ARG ARG SER TYR PHE LYS PHE GLN VAL ILE ALA THR
SEQRES 8 C 337 ASP ASP TYR GLY LYS GLY LEU SER GLY LYS ALA ASP VAL
SEQRES 9 C 337 LEU VAL SER VAL VAL ASN GLN LEU ASP MET GLN VAL ILE
SEQRES 10 C 337 VAL SER ASN VAL PRO PRO THR LEU VAL GLU LYS LYS ILE
SEQRES 11 C 337 GLU ASP LEU THR GLU ILE LEU ASP ARG TYR VAL GLN GLU
SEQRES 12 C 337 GLN ILE PRO GLY ALA LYS VAL VAL VAL GLU SER ILE GLY
SEQRES 13 C 337 ALA ARG ARG HIS GLY ASP ALA TYR SER LEU GLU ASP TYR
SEQRES 14 C 337 SER LYS CYS ASP LEU THR VAL TYR ALA ILE ASP PRO GLN
SEQRES 15 C 337 THR ASN ARG ALA ILE ASP ARG ASN GLU LEU PHE LYS PHE
SEQRES 16 C 337 LEU ASP GLY LYS LEU LEU ASP ILE ASN LYS ASP PHE GLN
SEQRES 17 C 337 PRO TYR TYR GLY GLU GLY GLY ARG ILE LEU GLU ILE ARG
SEQRES 18 C 337 THR PRO GLU ALA VAL THR SER ILE LYS LYS ARG GLY GLU
SEQRES 19 C 337 SER LEU GLY TYR THR GLU GLY ALA LEU LEU ALA LEU ALA
SEQRES 20 C 337 PHE ILE ILE ILE LEU CYS CYS ILE PRO ALA ILE LEU VAL
SEQRES 21 C 337 VAL LEU VAL SER TYR ARG GLN PHE LYS VAL ARG GLN ALA
SEQRES 22 C 337 GLU CYS THR LYS THR ALA ARG ILE GLN SER ALA MET PRO
SEQRES 23 C 337 ALA ALA LYS PRO ALA ALA PRO VAL PRO ALA ALA PRO ALA
SEQRES 24 C 337 PRO PRO PRO PRO PRO PRO PRO PRO PRO PRO GLY ALA HIS
SEQRES 25 C 337 LEU TYR GLU GLU LEU GLY GLU SER ALA MET HIS LYS TYR
SEQRES 26 C 337 GLU THR ALA LEU PHE GLU SER ARG LEU VAL PRO ARG
SEQRES 1 D 228 GLY SER GLY GLY ARG ALA THR MET VAL LYS LEU LEU PRO
SEQRES 2 D 228 ALA GLN GLU ALA ALA LYS ILE TYR HIS THR ASN TYR VAL
SEQRES 3 D 228 ARG ASN SER ARG ALA VAL GLY VAL MET TRP GLY THR LEU
SEQRES 4 D 228 THR ILE CYS PHE SER VAL LEU VAL MET ALA LEU PHE ILE
SEQRES 5 D 228 GLN PRO TYR TRP ILE GLY ASP SER VAL SER THR PRO GLN
SEQRES 6 D 228 ALA GLY TYR PHE GLY LEU PHE SER TYR CYS VAL GLY ASN
SEQRES 7 D 228 VAL LEU SER SER GLU LEU ILE CYS LYS GLY GLY PRO LEU
SEQRES 8 D 228 ASP PHE SER SER ILE PRO SER ARG ALA PHE LYS THR ALA
SEQRES 9 D 228 MET PHE PHE VAL ALA LEU ALA MET PHE LEU ILE ILE GLY
SEQRES 10 D 228 SER ILE ILE CYS PHE SER LEU PHE PHE VAL CYS ASN THR
SEQRES 11 D 228 ALA THR VAL TYR LYS ILE CYS ALA TRP MET GLN LEU ALA
SEQRES 12 D 228 ALA ALA THR GLY LEU MET ILE GLY CYS LEU VAL TYR PRO
SEQRES 13 D 228 ASP GLY TRP ASP SER SER GLU VAL ARG ARG MET CYS GLY
SEQRES 14 D 228 GLU GLN THR GLY LYS TYR THR LEU GLY HIS CYS THR ILE
SEQRES 15 D 228 ARG TRP ALA PHE MET LEU ALA ILE LEU SER ILE GLY ASP
SEQRES 16 D 228 ALA LEU ILE LEU SER PHE LEU ALA PHE VAL LEU GLY TYR
SEQRES 17 D 228 ARG GLN ASP LYS LEU LEU PRO ASP ASP TYR LYS ALA ASP
SEQRES 18 D 228 GLY ASN GLU GLU VAL PHE GLU
HELIX 1 AA1 ASN A 1180 MET A 1184 5 5
HELIX 2 AA2 ILE A 1193 LYS A 1197 5 5
HELIX 3 AA3 ASP A 1231 LYS A 1235 1 5
HELIX 4 AA4 ASN A 1249 MET A 1253 5 5
HELIX 5 AA5 PRO A 1261 LYS A 1268 1 8
HELIX 6 AA6 LYS A 1268 VAL A 1280 1 13
HELIX 7 AA7 ASP A 1327 GLY A 1337 1 11
HELIX 8 AA8 LYS A 1338 LYS A 1344 1 7
HELIX 9 AA9 THR A 1366 GLY A 1372 1 7
HELIX 10 AB1 TYR A 1377 ARG A 1410 1 34
HELIX 11 AB2 THR B 16 ILE B 45 1 30
HELIX 12 AB3 SER B 91 LEU B 117 1 27
HELIX 13 AB4 ASN B 122 TRP B 152 1 31
HELIX 14 AB5 ARG B 176 LEU B 199 1 24
HELIX 15 AB6 ASN C 1180 MET C 1184 5 5
HELIX 16 AB7 ILE C 1193 LYS C 1197 5 5
HELIX 17 AB8 ASP C 1231 LYS C 1235 1 5
HELIX 18 AB9 ASN C 1249 MET C 1253 5 5
HELIX 19 AC1 PRO C 1261 LYS C 1268 1 8
HELIX 20 AC2 LYS C 1268 VAL C 1280 1 13
HELIX 21 AC3 ASP C 1327 GLY C 1337 1 11
HELIX 22 AC4 LYS C 1338 LYS C 1344 1 7
HELIX 23 AC5 THR C 1366 GLY C 1372 1 7
HELIX 24 AC6 TYR C 1377 ARG C 1410 1 34
HELIX 25 AC7 THR D 16 ILE D 45 1 30
HELIX 26 AC8 SER D 91 LEU D 117 1 27
HELIX 27 AC9 ASN D 122 TRP D 152 1 31
HELIX 28 AD1 ARG D 176 LEU D 199 1 24
SHEET 1 AA1 2 VAL A1148 PHE A1149 0
SHEET 2 AA1 2 ALA A1173 THR A1174 -1 O THR A1174 N VAL A1148
SHEET 1 AA2 4 PHE A1153 ILE A1155 0
SHEET 2 AA2 4 SER A1238 VAL A1245 1 O ASP A1242 N TYR A1154
SHEET 3 AA2 4 PHE A1223 THR A1230 -1 N VAL A1227 O ALA A1241
SHEET 4 AA2 4 ALA A1185 ILE A1189 -1 N ARG A1187 O ILE A1228
SHEET 1 AA3 2 VAL A1158 SER A1159 0
SHEET 2 AA3 2 VAL A1247 VAL A1248 1 O VAL A1248 N VAL A1158
SHEET 1 AA4 2 GLY A1199 VAL A1202 0
SHEET 2 AA4 2 ILE A1209 ALA A1212 -1 O ALA A1212 N GLY A1199
SHEET 1 AA5 3 CYS A1311 VAL A1315 0
SHEET 2 AA5 3 GLN A1254 SER A1258 -1 N ILE A1256 O LEU A1313
SHEET 3 AA5 3 ILE A1356 ARG A1360 -1 O GLU A1358 N VAL A1257
SHEET 1 AA6 2 ILE B 50 GLY B 51 0
SHEET 2 AA6 2 THR B 174 ILE B 175 -1 O THR B 174 N GLY B 51
SHEET 1 AA7 2 ALA B 59 GLY B 60 0
SHEET 2 AA7 2 VAL B 69 GLY B 70 -1 O GLY B 70 N ALA B 59
SHEET 1 AA8 2 VAL C1148 PHE C1149 0
SHEET 2 AA8 2 ALA C1173 THR C1174 -1 O THR C1174 N VAL C1148
SHEET 1 AA9 4 PHE C1153 ILE C1155 0
SHEET 2 AA9 4 SER C1238 VAL C1245 1 O ASP C1242 N TYR C1154
SHEET 3 AA9 4 PHE C1223 THR C1230 -1 N VAL C1227 O ALA C1241
SHEET 4 AA9 4 ALA C1185 ILE C1189 -1 N ARG C1187 O ILE C1228
SHEET 1 AB1 2 VAL C1158 SER C1159 0
SHEET 2 AB1 2 VAL C1247 VAL C1248 1 O VAL C1248 N VAL C1158
SHEET 1 AB2 2 GLY C1199 VAL C1202 0
SHEET 2 AB2 2 ILE C1209 ALA C1212 -1 O ALA C1212 N GLY C1199
SHEET 1 AB3 3 CYS C1311 VAL C1315 0
SHEET 2 AB3 3 GLN C1254 SER C1258 -1 N ILE C1256 O LEU C1313
SHEET 3 AB3 3 ILE C1356 ARG C1360 -1 O ARG C1360 N VAL C1255
SHEET 1 AB4 2 ARG C1297 HIS C1299 0
SHEET 2 AB4 2 LEU C1305 ASP C1307 -1 O ASP C1307 N ARG C1297
SHEET 1 AB5 2 ILE D 50 GLY D 51 0
SHEET 2 AB5 2 THR D 174 ILE D 175 -1 O THR D 174 N GLY D 51
SHEET 1 AB6 2 ALA D 59 GLY D 60 0
SHEET 2 AB6 2 VAL D 69 GLY D 70 -1 O GLY D 70 N ALA D 59
SSBOND 1 CYS B 68 CYS B 79 1555 1555 2.03
SSBOND 2 CYS B 114 CYS B 130 1555 1555 2.04
SSBOND 3 CYS D 68 CYS D 79 1555 1555 2.03
SSBOND 4 CYS D 114 CYS D 130 1555 1555 2.04
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
