HEADER MEMBRANE PROTEIN 08-MAR-18 6CNO
TITLE CRYO-EM STRUCTURE OF THE HUMAN SK4/CALMODULIN CHANNEL COMPLEX IN THE
TITLE 2 CA2+ BOUND STATE II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERMEDIATE CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM
COMPND 3 CHANNEL PROTEIN 4;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 SYNONYM: SK4 CHANNEL, SKCA4, IKCA1, IK1, KCA3.1, KCA4, PUTATIVE
COMPND 6 GARDOS CHANNEL;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CALMODULIN-1;
COMPND 10 CHAIN: E, F, G, H;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: KCNN4, IK1, IKCA1, KCA4, SK4;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: CALM1, CALM, CAM, CAM1;
SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS ION CHANNEL, NEUROSCIENCE, CALMODULIN, MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR C.H.LEE,R.MACKINNON
REVDAT 4 13-MAR-24 6CNO 1 REMARK
REVDAT 3 20-NOV-19 6CNO 1 REMARK
REVDAT 2 23-MAY-18 6CNO 1 JRNL
REVDAT 1 02-MAY-18 6CNO 0
JRNL AUTH C.H.LEE,R.MACKINNON
JRNL TITL ACTIVATION MECHANISM OF A HUMAN SK-CALMODULIN CHANNEL
JRNL TITL 2 COMPLEX ELUCIDATED BY CRYO-EM STRUCTURES.
JRNL REF SCIENCE V. 360 508 2018
JRNL REFN ESSN 1095-9203
JRNL PMID 29724949
JRNL DOI 10.1126/SCIENCE.AAS9466
REMARK 2
REMARK 2 RESOLUTION. 4.70 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) : 4.700
REMARK 3 NUMBER OF PARTICLES : 52056
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 6CNO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-18.
REMARK 100 THE DEPOSITION ID IS D_1000233106.
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 : HUMAN SK4/CALMODULIN CHANNEL
REMARK 245 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) : 7500.00
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: OCTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 GLY A 3
REMARK 465 ASP A 4
REMARK 465 LEU A 5
REMARK 465 VAL A 6
REMARK 465 LEU A 7
REMARK 465 GLY A 8
REMARK 465 GLY A 124
REMARK 465 PRO A 125
REMARK 465 PRO A 126
REMARK 465 CYS A 127
REMARK 465 VAL A 128
REMARK 465 GLN A 129
REMARK 465 ASP A 130
REMARK 465 LEU A 131
REMARK 465 GLY A 132
REMARK 465 ALA A 133
REMARK 465 PRO A 134
REMARK 465 LEU A 135
REMARK 465 THR A 136
REMARK 465 SER A 137
REMARK 465 PRO A 138
REMARK 465 GLN A 139
REMARK 465 PRO A 140
REMARK 465 TRP A 141
REMARK 465 SER A 387
REMARK 465 SER A 388
REMARK 465 HIS A 389
REMARK 465 ARG A 390
REMARK 465 ALA A 391
REMARK 465 LEU A 392
REMARK 465 GLU A 393
REMARK 465 LYS A 394
REMARK 465 GLN A 395
REMARK 465 ILE A 396
REMARK 465 ASP A 397
REMARK 465 THR A 398
REMARK 465 LEU A 399
REMARK 465 ALA A 400
REMARK 465 GLY A 401
REMARK 465 LYS A 402
REMARK 465 LEU A 403
REMARK 465 ASP A 404
REMARK 465 ALA A 405
REMARK 465 LEU A 406
REMARK 465 THR A 407
REMARK 465 GLU A 408
REMARK 465 LEU A 409
REMARK 465 LEU A 410
REMARK 465 SER A 411
REMARK 465 THR A 412
REMARK 465 ALA A 413
REMARK 465 LEU A 414
REMARK 465 GLY A 415
REMARK 465 PRO A 416
REMARK 465 ARG A 417
REMARK 465 GLN A 418
REMARK 465 LEU A 419
REMARK 465 PRO A 420
REMARK 465 GLU A 421
REMARK 465 PRO A 422
REMARK 465 SER A 423
REMARK 465 GLN A 424
REMARK 465 GLN A 425
REMARK 465 SER A 426
REMARK 465 LYS A 427
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 GLY B 3
REMARK 465 ASP B 4
REMARK 465 LEU B 5
REMARK 465 VAL B 6
REMARK 465 LEU B 7
REMARK 465 GLY B 8
REMARK 465 GLY B 124
REMARK 465 PRO B 125
REMARK 465 PRO B 126
REMARK 465 CYS B 127
REMARK 465 VAL B 128
REMARK 465 GLN B 129
REMARK 465 ASP B 130
REMARK 465 LEU B 131
REMARK 465 GLY B 132
REMARK 465 ALA B 133
REMARK 465 PRO B 134
REMARK 465 LEU B 135
REMARK 465 THR B 136
REMARK 465 SER B 137
REMARK 465 PRO B 138
REMARK 465 GLN B 139
REMARK 465 PRO B 140
REMARK 465 TRP B 141
REMARK 465 SER B 387
REMARK 465 SER B 388
REMARK 465 HIS B 389
REMARK 465 ARG B 390
REMARK 465 ALA B 391
REMARK 465 LEU B 392
REMARK 465 GLU B 393
REMARK 465 LYS B 394
REMARK 465 GLN B 395
REMARK 465 ILE B 396
REMARK 465 ASP B 397
REMARK 465 THR B 398
REMARK 465 LEU B 399
REMARK 465 ALA B 400
REMARK 465 GLY B 401
REMARK 465 LYS B 402
REMARK 465 LEU B 403
REMARK 465 ASP B 404
REMARK 465 ALA B 405
REMARK 465 LEU B 406
REMARK 465 THR B 407
REMARK 465 GLU B 408
REMARK 465 LEU B 409
REMARK 465 LEU B 410
REMARK 465 SER B 411
REMARK 465 THR B 412
REMARK 465 ALA B 413
REMARK 465 LEU B 414
REMARK 465 GLY B 415
REMARK 465 PRO B 416
REMARK 465 ARG B 417
REMARK 465 GLN B 418
REMARK 465 LEU B 419
REMARK 465 PRO B 420
REMARK 465 GLU B 421
REMARK 465 PRO B 422
REMARK 465 SER B 423
REMARK 465 GLN B 424
REMARK 465 GLN B 425
REMARK 465 SER B 426
REMARK 465 LYS B 427
REMARK 465 MET C 1
REMARK 465 GLY C 2
REMARK 465 GLY C 3
REMARK 465 ASP C 4
REMARK 465 LEU C 5
REMARK 465 VAL C 6
REMARK 465 LEU C 7
REMARK 465 GLY C 8
REMARK 465 GLY C 124
REMARK 465 PRO C 125
REMARK 465 PRO C 126
REMARK 465 CYS C 127
REMARK 465 VAL C 128
REMARK 465 GLN C 129
REMARK 465 ASP C 130
REMARK 465 LEU C 131
REMARK 465 GLY C 132
REMARK 465 ALA C 133
REMARK 465 PRO C 134
REMARK 465 LEU C 135
REMARK 465 THR C 136
REMARK 465 SER C 137
REMARK 465 PRO C 138
REMARK 465 GLN C 139
REMARK 465 PRO C 140
REMARK 465 TRP C 141
REMARK 465 SER C 387
REMARK 465 SER C 388
REMARK 465 HIS C 389
REMARK 465 ARG C 390
REMARK 465 ALA C 391
REMARK 465 LEU C 392
REMARK 465 GLU C 393
REMARK 465 LYS C 394
REMARK 465 GLN C 395
REMARK 465 ILE C 396
REMARK 465 ASP C 397
REMARK 465 THR C 398
REMARK 465 LEU C 399
REMARK 465 ALA C 400
REMARK 465 GLY C 401
REMARK 465 LYS C 402
REMARK 465 LEU C 403
REMARK 465 ASP C 404
REMARK 465 ALA C 405
REMARK 465 LEU C 406
REMARK 465 THR C 407
REMARK 465 GLU C 408
REMARK 465 LEU C 409
REMARK 465 LEU C 410
REMARK 465 SER C 411
REMARK 465 THR C 412
REMARK 465 ALA C 413
REMARK 465 LEU C 414
REMARK 465 GLY C 415
REMARK 465 PRO C 416
REMARK 465 ARG C 417
REMARK 465 GLN C 418
REMARK 465 LEU C 419
REMARK 465 PRO C 420
REMARK 465 GLU C 421
REMARK 465 PRO C 422
REMARK 465 SER C 423
REMARK 465 GLN C 424
REMARK 465 GLN C 425
REMARK 465 SER C 426
REMARK 465 LYS C 427
REMARK 465 MET D 1
REMARK 465 GLY D 2
REMARK 465 GLY D 3
REMARK 465 ASP D 4
REMARK 465 LEU D 5
REMARK 465 VAL D 6
REMARK 465 LEU D 7
REMARK 465 GLY D 8
REMARK 465 GLY D 124
REMARK 465 PRO D 125
REMARK 465 PRO D 126
REMARK 465 CYS D 127
REMARK 465 VAL D 128
REMARK 465 GLN D 129
REMARK 465 ASP D 130
REMARK 465 LEU D 131
REMARK 465 GLY D 132
REMARK 465 ALA D 133
REMARK 465 PRO D 134
REMARK 465 LEU D 135
REMARK 465 THR D 136
REMARK 465 SER D 137
REMARK 465 PRO D 138
REMARK 465 GLN D 139
REMARK 465 PRO D 140
REMARK 465 TRP D 141
REMARK 465 SER D 387
REMARK 465 SER D 388
REMARK 465 HIS D 389
REMARK 465 ARG D 390
REMARK 465 ALA D 391
REMARK 465 LEU D 392
REMARK 465 GLU D 393
REMARK 465 LYS D 394
REMARK 465 GLN D 395
REMARK 465 ILE D 396
REMARK 465 ASP D 397
REMARK 465 THR D 398
REMARK 465 LEU D 399
REMARK 465 ALA D 400
REMARK 465 GLY D 401
REMARK 465 LYS D 402
REMARK 465 LEU D 403
REMARK 465 ASP D 404
REMARK 465 ALA D 405
REMARK 465 LEU D 406
REMARK 465 THR D 407
REMARK 465 GLU D 408
REMARK 465 LEU D 409
REMARK 465 LEU D 410
REMARK 465 SER D 411
REMARK 465 THR D 412
REMARK 465 ALA D 413
REMARK 465 LEU D 414
REMARK 465 GLY D 415
REMARK 465 PRO D 416
REMARK 465 ARG D 417
REMARK 465 GLN D 418
REMARK 465 LEU D 419
REMARK 465 PRO D 420
REMARK 465 GLU D 421
REMARK 465 PRO D 422
REMARK 465 SER D 423
REMARK 465 GLN D 424
REMARK 465 GLN D 425
REMARK 465 SER D 426
REMARK 465 LYS D 427
REMARK 465 MET E 0
REMARK 465 ALA E 1
REMARK 465 LYS E 148
REMARK 465 MET F 0
REMARK 465 ALA F 1
REMARK 465 LYS F 148
REMARK 465 MET G 0
REMARK 465 ALA G 1
REMARK 465 LYS G 148
REMARK 465 MET H 0
REMARK 465 ALA H 1
REMARK 465 LYS H 148
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 CYS A 52 SG
REMARK 470 ASP A 95 CG OD1 OD2
REMARK 470 THR A 101 OG1 CG2
REMARK 470 VAL A 122 CG1 CG2
REMARK 470 ARG A 123 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 231 CG1 CG2
REMARK 470 ASN A 232 CG OD1 ND2
REMARK 470 THR A 234 OG1 CG2
REMARK 470 GLU A 290 CG CD OE1 OE2
REMARK 470 LYS A 332 CG CD CE NZ
REMARK 470 GLU A 333 CG CD OE1 OE2
REMARK 470 GLU A 363 CG CD OE1 OE2
REMARK 470 ASN A 366 CG OD1 ND2
REMARK 470 MET A 368 CG SD CE
REMARK 470 ASP A 370 CG OD1 OD2
REMARK 470 SER A 372 OG
REMARK 470 MET A 376 CG SD CE
REMARK 470 TYR A 379 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A 380 CG OD1 OD2
REMARK 470 LEU A 381 CG CD1 CD2
REMARK 470 GLN A 382 CG CD OE1 NE2
REMARK 470 GLN A 383 CG CD OE1 NE2
REMARK 470 ASN A 384 CG OD1 ND2
REMARK 470 LEU A 385 CG CD1 CD2
REMARK 470 SER A 386 OG
REMARK 470 CYS B 52 SG
REMARK 470 ASP B 95 CG OD1 OD2
REMARK 470 THR B 101 OG1 CG2
REMARK 470 VAL B 122 CG1 CG2
REMARK 470 ARG B 123 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 231 CG1 CG2
REMARK 470 ASN B 232 CG OD1 ND2
REMARK 470 THR B 234 OG1 CG2
REMARK 470 GLU B 290 CG CD OE1 OE2
REMARK 470 LYS B 332 CG CD CE NZ
REMARK 470 GLU B 333 CG CD OE1 OE2
REMARK 470 GLU B 363 CG CD OE1 OE2
REMARK 470 ASN B 366 CG OD1 ND2
REMARK 470 MET B 368 CG SD CE
REMARK 470 ASP B 370 CG OD1 OD2
REMARK 470 SER B 372 OG
REMARK 470 MET B 376 CG SD CE
REMARK 470 TYR B 379 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP B 380 CG OD1 OD2
REMARK 470 LEU B 381 CG CD1 CD2
REMARK 470 GLN B 382 CG CD OE1 NE2
REMARK 470 GLN B 383 CG CD OE1 NE2
REMARK 470 ASN B 384 CG OD1 ND2
REMARK 470 LEU B 385 CG CD1 CD2
REMARK 470 SER B 386 OG
REMARK 470 CYS C 52 SG
REMARK 470 ASP C 95 CG OD1 OD2
REMARK 470 THR C 101 OG1 CG2
REMARK 470 VAL C 122 CG1 CG2
REMARK 470 ARG C 123 CG CD NE CZ NH1 NH2
REMARK 470 VAL C 231 CG1 CG2
REMARK 470 ASN C 232 CG OD1 ND2
REMARK 470 THR C 234 OG1 CG2
REMARK 470 GLU C 290 CG CD OE1 OE2
REMARK 470 LYS C 332 CG CD CE NZ
REMARK 470 GLU C 333 CG CD OE1 OE2
REMARK 470 GLU C 363 CG CD OE1 OE2
REMARK 470 ASN C 366 CG OD1 ND2
REMARK 470 MET C 368 CG SD CE
REMARK 470 ASP C 370 CG OD1 OD2
REMARK 470 SER C 372 OG
REMARK 470 MET C 376 CG SD CE
REMARK 470 TYR C 379 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP C 380 CG OD1 OD2
REMARK 470 LEU C 381 CG CD1 CD2
REMARK 470 GLN C 382 CG CD OE1 NE2
REMARK 470 GLN C 383 CG CD OE1 NE2
REMARK 470 ASN C 384 CG OD1 ND2
REMARK 470 LEU C 385 CG CD1 CD2
REMARK 470 SER C 386 OG
REMARK 470 CYS D 52 SG
REMARK 470 ASP D 95 CG OD1 OD2
REMARK 470 THR D 101 OG1 CG2
REMARK 470 VAL D 122 CG1 CG2
REMARK 470 ARG D 123 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 231 CG1 CG2
REMARK 470 ASN D 232 CG OD1 ND2
REMARK 470 THR D 234 OG1 CG2
REMARK 470 GLU D 290 CG CD OE1 OE2
REMARK 470 LYS D 332 CG CD CE NZ
REMARK 470 GLU D 333 CG CD OE1 OE2
REMARK 470 GLU D 363 CG CD OE1 OE2
REMARK 470 ASN D 366 CG OD1 ND2
REMARK 470 MET D 368 CG SD CE
REMARK 470 ASP D 370 CG OD1 OD2
REMARK 470 SER D 372 OG
REMARK 470 MET D 376 CG SD CE
REMARK 470 TYR D 379 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP D 380 CG OD1 OD2
REMARK 470 LEU D 381 CG CD1 CD2
REMARK 470 GLN D 382 CG CD OE1 NE2
REMARK 470 GLN D 383 CG CD OE1 NE2
REMARK 470 ASN D 384 CG OD1 ND2
REMARK 470 LEU D 385 CG CD1 CD2
REMARK 470 SER D 386 OG
REMARK 470 ASP E 2 CG OD1 OD2
REMARK 470 GLN E 3 CG CD OE1 NE2
REMARK 470 ASP E 80 CG OD1 OD2
REMARK 470 LYS E 94 CG CD CE NZ
REMARK 470 ARG E 106 CG CD NE CZ NH1 NH2
REMARK 470 ASP E 118 CG OD1 OD2
REMARK 470 GLU E 119 CG CD OE1 OE2
REMARK 470 GLU E 120 CG CD OE1 OE2
REMARK 470 VAL E 121 CG1 CG2
REMARK 470 ASP E 122 CG OD1 OD2
REMARK 470 GLU E 123 CG CD OE1 OE2
REMARK 470 MET E 124 CG SD CE
REMARK 470 ILE E 125 CG1 CG2 CD1
REMARK 470 ARG E 126 CG CD NE CZ NH1 NH2
REMARK 470 GLU E 127 CG CD OE1 OE2
REMARK 470 ASP E 129 CG OD1 OD2
REMARK 470 ILE E 130 CG1 CG2 CD1
REMARK 470 ASP E 131 CG OD1 OD2
REMARK 470 ASP E 133 CG OD1 OD2
REMARK 470 GLU E 139 CG CD OE1 OE2
REMARK 470 GLU E 140 CG CD OE1 OE2
REMARK 470 VAL E 142 CG1 CG2
REMARK 470 ASP F 2 CG OD1 OD2
REMARK 470 GLN F 3 CG CD OE1 NE2
REMARK 470 ASP F 80 CG OD1 OD2
REMARK 470 LYS F 94 CG CD CE NZ
REMARK 470 ARG F 106 CG CD NE CZ NH1 NH2
REMARK 470 ASP F 118 CG OD1 OD2
REMARK 470 GLU F 119 CG CD OE1 OE2
REMARK 470 GLU F 120 CG CD OE1 OE2
REMARK 470 VAL F 121 CG1 CG2
REMARK 470 ASP F 122 CG OD1 OD2
REMARK 470 GLU F 123 CG CD OE1 OE2
REMARK 470 MET F 124 CG SD CE
REMARK 470 ILE F 125 CG1 CG2 CD1
REMARK 470 ARG F 126 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 127 CG CD OE1 OE2
REMARK 470 ASP F 129 CG OD1 OD2
REMARK 470 ILE F 130 CG1 CG2 CD1
REMARK 470 ASP F 131 CG OD1 OD2
REMARK 470 ASP F 133 CG OD1 OD2
REMARK 470 GLU F 139 CG CD OE1 OE2
REMARK 470 GLU F 140 CG CD OE1 OE2
REMARK 470 VAL F 142 CG1 CG2
REMARK 470 ASP G 2 CG OD1 OD2
REMARK 470 GLN G 3 CG CD OE1 NE2
REMARK 470 ASP G 80 CG OD1 OD2
REMARK 470 LYS G 94 CG CD CE NZ
REMARK 470 ARG G 106 CG CD NE CZ NH1 NH2
REMARK 470 ASP G 118 CG OD1 OD2
REMARK 470 GLU G 119 CG CD OE1 OE2
REMARK 470 GLU G 120 CG CD OE1 OE2
REMARK 470 VAL G 121 CG1 CG2
REMARK 470 ASP G 122 CG OD1 OD2
REMARK 470 GLU G 123 CG CD OE1 OE2
REMARK 470 MET G 124 CG SD CE
REMARK 470 ILE G 125 CG1 CG2 CD1
REMARK 470 ARG G 126 CG CD NE CZ NH1 NH2
REMARK 470 GLU G 127 CG CD OE1 OE2
REMARK 470 ASP G 129 CG OD1 OD2
REMARK 470 ILE G 130 CG1 CG2 CD1
REMARK 470 ASP G 131 CG OD1 OD2
REMARK 470 ASP G 133 CG OD1 OD2
REMARK 470 GLU G 139 CG CD OE1 OE2
REMARK 470 GLU G 140 CG CD OE1 OE2
REMARK 470 VAL G 142 CG1 CG2
REMARK 470 ASP H 2 CG OD1 OD2
REMARK 470 GLN H 3 CG CD OE1 NE2
REMARK 470 ASP H 80 CG OD1 OD2
REMARK 470 LYS H 94 CG CD CE NZ
REMARK 470 ARG H 106 CG CD NE CZ NH1 NH2
REMARK 470 ASP H 118 CG OD1 OD2
REMARK 470 GLU H 119 CG CD OE1 OE2
REMARK 470 GLU H 120 CG CD OE1 OE2
REMARK 470 VAL H 121 CG1 CG2
REMARK 470 ASP H 122 CG OD1 OD2
REMARK 470 GLU H 123 CG CD OE1 OE2
REMARK 470 MET H 124 CG SD CE
REMARK 470 ILE H 125 CG1 CG2 CD1
REMARK 470 ARG H 126 CG CD NE CZ NH1 NH2
REMARK 470 GLU H 127 CG CD OE1 OE2
REMARK 470 ASP H 129 CG OD1 OD2
REMARK 470 ILE H 130 CG1 CG2 CD1
REMARK 470 ASP H 131 CG OD1 OD2
REMARK 470 ASP H 133 CG OD1 OD2
REMARK 470 GLU H 139 CG CD OE1 OE2
REMARK 470 GLU H 140 CG CD OE1 OE2
REMARK 470 VAL H 142 CG1 CG2
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 OD1 ASP E 93 OD1 ASN E 97 1.94
REMARK 500 OD1 ASP H 93 OD1 ASN H 97 1.94
REMARK 500 OD1 ASP G 93 OD1 ASN G 97 1.94
REMARK 500 OD1 ASP F 93 OD1 ASN F 97 1.94
REMARK 500 OD1 ASP E 24 O THR E 26 2.00
REMARK 500 OD1 ASP G 24 O THR G 26 2.00
REMARK 500 OD1 ASP F 24 O THR F 26 2.00
REMARK 500 OD1 ASP H 24 O THR H 26 2.00
REMARK 500 OD1 ASP F 20 OD1 ASP F 22 2.07
REMARK 500 OD1 ASP H 20 OD1 ASP H 22 2.07
REMARK 500 OD1 ASP E 20 OD1 ASP E 22 2.07
REMARK 500 OD1 ASP G 20 OD1 ASP G 22 2.07
REMARK 500 OD1 ASN H 60 O THR H 62 2.11
REMARK 500 OD1 ASN F 60 O THR F 62 2.11
REMARK 500 OD1 ASN E 60 O THR E 62 2.11
REMARK 500 OD1 ASN G 60 O THR G 62 2.11
REMARK 500 OD1 ASP E 22 OE2 GLU E 31 2.16
REMARK 500 OD1 ASP F 22 OE2 GLU F 31 2.16
REMARK 500 OD1 ASP H 22 OE2 GLU H 31 2.16
REMARK 500 OD1 ASP G 22 OE2 GLU G 31 2.16
REMARK 500 OD1 ASP F 20 OD1 ASP F 24 2.19
REMARK 500 OD1 ASP G 20 OD1 ASP G 24 2.19
REMARK 500 OD1 ASP E 20 OD1 ASP E 24 2.19
REMARK 500 OD1 ASP H 20 OD1 ASP H 24 2.19
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 ARG A 94 -32.44 -131.70
REMARK 500 ARG A 189 77.00 59.83
REMARK 500 ARG B 94 -32.44 -131.79
REMARK 500 ARG B 189 77.03 59.77
REMARK 500 ARG C 94 -32.50 -131.75
REMARK 500 ARG C 189 76.98 59.77
REMARK 500 ARG D 94 -32.47 -131.73
REMARK 500 ARG D 189 77.02 59.81
REMARK 500 THR E 146 31.52 -98.42
REMARK 500 THR F 146 31.53 -98.39
REMARK 500 THR G 146 31.52 -98.44
REMARK 500 THR H 146 31.55 -98.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 20 OD1
REMARK 620 2 ASP E 22 OD1 51.8
REMARK 620 3 ASP E 24 OD1 59.0 88.5
REMARK 620 4 ASP E 24 OD2 119.5 108.7 64.8
REMARK 620 5 THR E 26 O 82.9 132.5 51.6 79.2
REMARK 620 6 GLU E 31 OE1 109.2 107.3 147.9 130.6 99.8
REMARK 620 7 GLU E 31 OE2 91.3 54.8 143.2 125.5 153.3 57.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 56 OD1
REMARK 620 2 ASP E 58 OD1 74.6
REMARK 620 3 ASP E 58 OD2 128.3 54.8
REMARK 620 4 ASN E 60 OD1 69.3 83.6 93.4
REMARK 620 5 THR E 62 O 94.6 136.0 113.5 53.2
REMARK 620 6 GLU E 67 OE1 101.9 128.7 116.7 144.3 95.1
REMARK 620 7 GLU E 67 OE2 110.4 78.0 71.5 160.8 143.4 54.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 93 OD1
REMARK 620 2 ASP E 95 OD1 56.2
REMARK 620 3 ASN E 97 OD1 49.7 77.7
REMARK 620 4 TYR E 99 O 85.4 139.7 67.0
REMARK 620 5 GLU E 104 OE1 124.6 118.7 157.6 91.8
REMARK 620 6 GLU E 104 OE2 112.4 68.0 144.6 148.2 56.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 20 OD1
REMARK 620 2 ASP F 22 OD1 51.6
REMARK 620 3 ASP F 24 OD1 58.5 88.5
REMARK 620 4 ASP F 24 OD2 119.8 110.0 65.3
REMARK 620 5 THR F 26 O 82.0 131.7 51.3 79.4
REMARK 620 6 GLU F 31 OE1 107.7 106.8 146.2 131.4 98.7
REMARK 620 7 GLU F 31 OE2 90.6 54.9 143.1 127.3 151.5 57.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 56 OD1
REMARK 620 2 ASP F 58 OD1 74.5
REMARK 620 3 ASP F 58 OD2 128.3 54.9
REMARK 620 4 ASN F 60 OD1 69.0 83.4 93.2
REMARK 620 5 THR F 62 O 94.2 135.5 113.3 52.9
REMARK 620 6 GLU F 67 OE1 101.9 129.2 117.2 144.0 95.0
REMARK 620 7 GLU F 67 OE2 110.6 78.4 71.8 160.9 143.6 55.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 93 OD1
REMARK 620 2 ASP F 95 OD1 55.9
REMARK 620 3 ASN F 97 OD1 49.5 77.2
REMARK 620 4 TYR F 99 O 85.5 139.4 67.1
REMARK 620 5 GLU F 104 OE1 124.7 118.5 158.3 92.5
REMARK 620 6 GLU F 104 OE2 112.0 67.7 143.7 148.9 56.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 20 OD1
REMARK 620 2 ASP G 22 OD1 51.7
REMARK 620 3 ASP G 24 OD1 59.0 88.6
REMARK 620 4 ASP G 24 OD2 119.8 109.1 65.1
REMARK 620 5 THR G 26 O 82.8 132.4 51.6 79.5
REMARK 620 6 GLU G 31 OE1 108.7 107.0 147.6 130.8 99.5
REMARK 620 7 GLU G 31 OE2 91.0 54.8 143.2 125.8 152.8 57.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 56 OD1
REMARK 620 2 ASP G 58 OD1 74.8
REMARK 620 3 ASP G 58 OD2 128.9 55.2
REMARK 620 4 ASN G 60 OD1 69.2 83.8 93.6
REMARK 620 5 THR G 62 O 94.2 136.0 113.5 52.9
REMARK 620 6 GLU G 67 OE1 101.7 129.2 117.0 143.5 94.6
REMARK 620 7 GLU G 67 OE2 110.7 78.6 71.9 161.6 143.0 54.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 93 OD1
REMARK 620 2 ASP G 95 OD1 56.0
REMARK 620 3 ASN G 97 OD1 49.6 77.5
REMARK 620 4 TYR G 99 O 85.4 139.5 67.1
REMARK 620 5 GLU G 104 OE1 124.3 118.4 157.8 92.1
REMARK 620 6 GLU G 104 OE2 112.0 67.8 144.2 148.4 56.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 20 OD1
REMARK 620 2 ASP H 22 OD1 52.2
REMARK 620 3 ASP H 24 OD1 60.3 89.5
REMARK 620 4 ASP H 24 OD2 121.2 108.4 65.6
REMARK 620 5 THR H 26 O 84.7 134.7 52.7 80.3
REMARK 620 6 GLU H 31 OE1 109.7 106.4 150.0 128.8 100.3
REMARK 620 7 GLU H 31 OE2 91.3 54.3 143.8 123.1 153.7 56.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 56 OD1
REMARK 620 2 ASP H 58 OD1 76.0
REMARK 620 3 ASP H 58 OD2 130.3 55.7
REMARK 620 4 ASN H 60 OD1 69.0 84.0 93.1
REMARK 620 5 THR H 62 O 93.2 134.9 111.8 51.8
REMARK 620 6 GLU H 67 OE1 102.3 131.8 117.5 141.5 93.2
REMARK 620 7 GLU H 67 OE2 112.8 80.4 72.8 163.1 141.8 55.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 93 OD1
REMARK 620 2 ASP H 95 OD1 56.1
REMARK 620 3 ASN H 97 OD1 50.5 78.1
REMARK 620 4 TYR H 99 O 87.4 141.9 69.2
REMARK 620 5 GLU H 104 OE1 123.8 115.8 160.1 92.4
REMARK 620 6 GLU H 104 OE2 110.5 66.2 143.2 147.4 55.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-7539 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF THE HUMAN SK4/CALMODULIN CHANNEL COMPLEX IN
REMARK 900 THE CA2+ BOUND STATE II
REMARK 900 RELATED ID: EMD-7537 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF THE HUMAN SK4/CALMODULIN CHANNEL COMPLEX
REMARK 900 RELATED ID: EMD-7538 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF THE HUMAN SK4/CALMODULIN CHANNEL COMPLEX IN
REMARK 900 THE CA2+ BOUND STATE I
DBREF 6CNO A 1 427 UNP O15554 KCNN4_HUMAN 1 427
DBREF 6CNO B 1 427 UNP O15554 KCNN4_HUMAN 1 427
DBREF 6CNO C 1 427 UNP O15554 KCNN4_HUMAN 1 427
DBREF 6CNO D 1 427 UNP O15554 KCNN4_HUMAN 1 427
DBREF 6CNO E 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6CNO F 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6CNO G 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6CNO H 0 148 UNP P0DP23 CALM1_HUMAN 1 149
SEQRES 1 A 427 MET GLY GLY ASP LEU VAL LEU GLY LEU GLY ALA LEU ARG
SEQRES 2 A 427 ARG ARG LYS ARG LEU LEU GLU GLN GLU LYS SER LEU ALA
SEQRES 3 A 427 GLY TRP ALA LEU VAL LEU ALA GLY THR GLY ILE GLY LEU
SEQRES 4 A 427 MET VAL LEU HIS ALA GLU MET LEU TRP PHE GLY GLY CYS
SEQRES 5 A 427 SER TRP ALA LEU TYR LEU PHE LEU VAL LYS CYS THR ILE
SEQRES 6 A 427 SER ILE SER THR PHE LEU LEU LEU CYS LEU ILE VAL ALA
SEQRES 7 A 427 PHE HIS ALA LYS GLU VAL GLN LEU PHE MET THR ASP ASN
SEQRES 8 A 427 GLY LEU ARG ASP TRP ARG VAL ALA LEU THR GLY ARG GLN
SEQRES 9 A 427 ALA ALA GLN ILE VAL LEU GLU LEU VAL VAL CYS GLY LEU
SEQRES 10 A 427 HIS PRO ALA PRO VAL ARG GLY PRO PRO CYS VAL GLN ASP
SEQRES 11 A 427 LEU GLY ALA PRO LEU THR SER PRO GLN PRO TRP PRO GLY
SEQRES 12 A 427 PHE LEU GLY GLN GLY GLU ALA LEU LEU SER LEU ALA MET
SEQRES 13 A 427 LEU LEU ARG LEU TYR LEU VAL PRO ARG ALA VAL LEU LEU
SEQRES 14 A 427 ARG SER GLY VAL LEU LEU ASN ALA SER TYR ARG SER ILE
SEQRES 15 A 427 GLY ALA LEU ASN GLN VAL ARG PHE ARG HIS TRP PHE VAL
SEQRES 16 A 427 ALA LYS LEU TYR MET ASN THR HIS PRO GLY ARG LEU LEU
SEQRES 17 A 427 LEU GLY LEU THR LEU GLY LEU TRP LEU THR THR ALA TRP
SEQRES 18 A 427 VAL LEU SER VAL ALA GLU ARG GLN ALA VAL ASN ALA THR
SEQRES 19 A 427 GLY HIS LEU SER ASP THR LEU TRP LEU ILE PRO ILE THR
SEQRES 20 A 427 PHE LEU THR ILE GLY TYR GLY ASP VAL VAL PRO GLY THR
SEQRES 21 A 427 MET TRP GLY LYS ILE VAL CYS LEU CYS THR GLY VAL MET
SEQRES 22 A 427 GLY VAL CYS CYS THR ALA LEU LEU VAL ALA VAL VAL ALA
SEQRES 23 A 427 ARG LYS LEU GLU PHE ASN LYS ALA GLU LYS HIS VAL HIS
SEQRES 24 A 427 ASN PHE MET MET ASP ILE GLN TYR THR LYS GLU MET LYS
SEQRES 25 A 427 GLU SER ALA ALA ARG VAL LEU GLN GLU ALA TRP MET PHE
SEQRES 26 A 427 TYR LYS HIS THR ARG ARG LYS GLU SER HIS ALA ALA ARG
SEQRES 27 A 427 ARG HIS GLN ARG LYS LEU LEU ALA ALA ILE ASN ALA PHE
SEQRES 28 A 427 ARG GLN VAL ARG LEU LYS HIS ARG LYS LEU ARG GLU GLN
SEQRES 29 A 427 VAL ASN SER MET VAL ASP ILE SER LYS MET HIS MET ILE
SEQRES 30 A 427 LEU TYR ASP LEU GLN GLN ASN LEU SER SER SER HIS ARG
SEQRES 31 A 427 ALA LEU GLU LYS GLN ILE ASP THR LEU ALA GLY LYS LEU
SEQRES 32 A 427 ASP ALA LEU THR GLU LEU LEU SER THR ALA LEU GLY PRO
SEQRES 33 A 427 ARG GLN LEU PRO GLU PRO SER GLN GLN SER LYS
SEQRES 1 B 427 MET GLY GLY ASP LEU VAL LEU GLY LEU GLY ALA LEU ARG
SEQRES 2 B 427 ARG ARG LYS ARG LEU LEU GLU GLN GLU LYS SER LEU ALA
SEQRES 3 B 427 GLY TRP ALA LEU VAL LEU ALA GLY THR GLY ILE GLY LEU
SEQRES 4 B 427 MET VAL LEU HIS ALA GLU MET LEU TRP PHE GLY GLY CYS
SEQRES 5 B 427 SER TRP ALA LEU TYR LEU PHE LEU VAL LYS CYS THR ILE
SEQRES 6 B 427 SER ILE SER THR PHE LEU LEU LEU CYS LEU ILE VAL ALA
SEQRES 7 B 427 PHE HIS ALA LYS GLU VAL GLN LEU PHE MET THR ASP ASN
SEQRES 8 B 427 GLY LEU ARG ASP TRP ARG VAL ALA LEU THR GLY ARG GLN
SEQRES 9 B 427 ALA ALA GLN ILE VAL LEU GLU LEU VAL VAL CYS GLY LEU
SEQRES 10 B 427 HIS PRO ALA PRO VAL ARG GLY PRO PRO CYS VAL GLN ASP
SEQRES 11 B 427 LEU GLY ALA PRO LEU THR SER PRO GLN PRO TRP PRO GLY
SEQRES 12 B 427 PHE LEU GLY GLN GLY GLU ALA LEU LEU SER LEU ALA MET
SEQRES 13 B 427 LEU LEU ARG LEU TYR LEU VAL PRO ARG ALA VAL LEU LEU
SEQRES 14 B 427 ARG SER GLY VAL LEU LEU ASN ALA SER TYR ARG SER ILE
SEQRES 15 B 427 GLY ALA LEU ASN GLN VAL ARG PHE ARG HIS TRP PHE VAL
SEQRES 16 B 427 ALA LYS LEU TYR MET ASN THR HIS PRO GLY ARG LEU LEU
SEQRES 17 B 427 LEU GLY LEU THR LEU GLY LEU TRP LEU THR THR ALA TRP
SEQRES 18 B 427 VAL LEU SER VAL ALA GLU ARG GLN ALA VAL ASN ALA THR
SEQRES 19 B 427 GLY HIS LEU SER ASP THR LEU TRP LEU ILE PRO ILE THR
SEQRES 20 B 427 PHE LEU THR ILE GLY TYR GLY ASP VAL VAL PRO GLY THR
SEQRES 21 B 427 MET TRP GLY LYS ILE VAL CYS LEU CYS THR GLY VAL MET
SEQRES 22 B 427 GLY VAL CYS CYS THR ALA LEU LEU VAL ALA VAL VAL ALA
SEQRES 23 B 427 ARG LYS LEU GLU PHE ASN LYS ALA GLU LYS HIS VAL HIS
SEQRES 24 B 427 ASN PHE MET MET ASP ILE GLN TYR THR LYS GLU MET LYS
SEQRES 25 B 427 GLU SER ALA ALA ARG VAL LEU GLN GLU ALA TRP MET PHE
SEQRES 26 B 427 TYR LYS HIS THR ARG ARG LYS GLU SER HIS ALA ALA ARG
SEQRES 27 B 427 ARG HIS GLN ARG LYS LEU LEU ALA ALA ILE ASN ALA PHE
SEQRES 28 B 427 ARG GLN VAL ARG LEU LYS HIS ARG LYS LEU ARG GLU GLN
SEQRES 29 B 427 VAL ASN SER MET VAL ASP ILE SER LYS MET HIS MET ILE
SEQRES 30 B 427 LEU TYR ASP LEU GLN GLN ASN LEU SER SER SER HIS ARG
SEQRES 31 B 427 ALA LEU GLU LYS GLN ILE ASP THR LEU ALA GLY LYS LEU
SEQRES 32 B 427 ASP ALA LEU THR GLU LEU LEU SER THR ALA LEU GLY PRO
SEQRES 33 B 427 ARG GLN LEU PRO GLU PRO SER GLN GLN SER LYS
SEQRES 1 C 427 MET GLY GLY ASP LEU VAL LEU GLY LEU GLY ALA LEU ARG
SEQRES 2 C 427 ARG ARG LYS ARG LEU LEU GLU GLN GLU LYS SER LEU ALA
SEQRES 3 C 427 GLY TRP ALA LEU VAL LEU ALA GLY THR GLY ILE GLY LEU
SEQRES 4 C 427 MET VAL LEU HIS ALA GLU MET LEU TRP PHE GLY GLY CYS
SEQRES 5 C 427 SER TRP ALA LEU TYR LEU PHE LEU VAL LYS CYS THR ILE
SEQRES 6 C 427 SER ILE SER THR PHE LEU LEU LEU CYS LEU ILE VAL ALA
SEQRES 7 C 427 PHE HIS ALA LYS GLU VAL GLN LEU PHE MET THR ASP ASN
SEQRES 8 C 427 GLY LEU ARG ASP TRP ARG VAL ALA LEU THR GLY ARG GLN
SEQRES 9 C 427 ALA ALA GLN ILE VAL LEU GLU LEU VAL VAL CYS GLY LEU
SEQRES 10 C 427 HIS PRO ALA PRO VAL ARG GLY PRO PRO CYS VAL GLN ASP
SEQRES 11 C 427 LEU GLY ALA PRO LEU THR SER PRO GLN PRO TRP PRO GLY
SEQRES 12 C 427 PHE LEU GLY GLN GLY GLU ALA LEU LEU SER LEU ALA MET
SEQRES 13 C 427 LEU LEU ARG LEU TYR LEU VAL PRO ARG ALA VAL LEU LEU
SEQRES 14 C 427 ARG SER GLY VAL LEU LEU ASN ALA SER TYR ARG SER ILE
SEQRES 15 C 427 GLY ALA LEU ASN GLN VAL ARG PHE ARG HIS TRP PHE VAL
SEQRES 16 C 427 ALA LYS LEU TYR MET ASN THR HIS PRO GLY ARG LEU LEU
SEQRES 17 C 427 LEU GLY LEU THR LEU GLY LEU TRP LEU THR THR ALA TRP
SEQRES 18 C 427 VAL LEU SER VAL ALA GLU ARG GLN ALA VAL ASN ALA THR
SEQRES 19 C 427 GLY HIS LEU SER ASP THR LEU TRP LEU ILE PRO ILE THR
SEQRES 20 C 427 PHE LEU THR ILE GLY TYR GLY ASP VAL VAL PRO GLY THR
SEQRES 21 C 427 MET TRP GLY LYS ILE VAL CYS LEU CYS THR GLY VAL MET
SEQRES 22 C 427 GLY VAL CYS CYS THR ALA LEU LEU VAL ALA VAL VAL ALA
SEQRES 23 C 427 ARG LYS LEU GLU PHE ASN LYS ALA GLU LYS HIS VAL HIS
SEQRES 24 C 427 ASN PHE MET MET ASP ILE GLN TYR THR LYS GLU MET LYS
SEQRES 25 C 427 GLU SER ALA ALA ARG VAL LEU GLN GLU ALA TRP MET PHE
SEQRES 26 C 427 TYR LYS HIS THR ARG ARG LYS GLU SER HIS ALA ALA ARG
SEQRES 27 C 427 ARG HIS GLN ARG LYS LEU LEU ALA ALA ILE ASN ALA PHE
SEQRES 28 C 427 ARG GLN VAL ARG LEU LYS HIS ARG LYS LEU ARG GLU GLN
SEQRES 29 C 427 VAL ASN SER MET VAL ASP ILE SER LYS MET HIS MET ILE
SEQRES 30 C 427 LEU TYR ASP LEU GLN GLN ASN LEU SER SER SER HIS ARG
SEQRES 31 C 427 ALA LEU GLU LYS GLN ILE ASP THR LEU ALA GLY LYS LEU
SEQRES 32 C 427 ASP ALA LEU THR GLU LEU LEU SER THR ALA LEU GLY PRO
SEQRES 33 C 427 ARG GLN LEU PRO GLU PRO SER GLN GLN SER LYS
SEQRES 1 D 427 MET GLY GLY ASP LEU VAL LEU GLY LEU GLY ALA LEU ARG
SEQRES 2 D 427 ARG ARG LYS ARG LEU LEU GLU GLN GLU LYS SER LEU ALA
SEQRES 3 D 427 GLY TRP ALA LEU VAL LEU ALA GLY THR GLY ILE GLY LEU
SEQRES 4 D 427 MET VAL LEU HIS ALA GLU MET LEU TRP PHE GLY GLY CYS
SEQRES 5 D 427 SER TRP ALA LEU TYR LEU PHE LEU VAL LYS CYS THR ILE
SEQRES 6 D 427 SER ILE SER THR PHE LEU LEU LEU CYS LEU ILE VAL ALA
SEQRES 7 D 427 PHE HIS ALA LYS GLU VAL GLN LEU PHE MET THR ASP ASN
SEQRES 8 D 427 GLY LEU ARG ASP TRP ARG VAL ALA LEU THR GLY ARG GLN
SEQRES 9 D 427 ALA ALA GLN ILE VAL LEU GLU LEU VAL VAL CYS GLY LEU
SEQRES 10 D 427 HIS PRO ALA PRO VAL ARG GLY PRO PRO CYS VAL GLN ASP
SEQRES 11 D 427 LEU GLY ALA PRO LEU THR SER PRO GLN PRO TRP PRO GLY
SEQRES 12 D 427 PHE LEU GLY GLN GLY GLU ALA LEU LEU SER LEU ALA MET
SEQRES 13 D 427 LEU LEU ARG LEU TYR LEU VAL PRO ARG ALA VAL LEU LEU
SEQRES 14 D 427 ARG SER GLY VAL LEU LEU ASN ALA SER TYR ARG SER ILE
SEQRES 15 D 427 GLY ALA LEU ASN GLN VAL ARG PHE ARG HIS TRP PHE VAL
SEQRES 16 D 427 ALA LYS LEU TYR MET ASN THR HIS PRO GLY ARG LEU LEU
SEQRES 17 D 427 LEU GLY LEU THR LEU GLY LEU TRP LEU THR THR ALA TRP
SEQRES 18 D 427 VAL LEU SER VAL ALA GLU ARG GLN ALA VAL ASN ALA THR
SEQRES 19 D 427 GLY HIS LEU SER ASP THR LEU TRP LEU ILE PRO ILE THR
SEQRES 20 D 427 PHE LEU THR ILE GLY TYR GLY ASP VAL VAL PRO GLY THR
SEQRES 21 D 427 MET TRP GLY LYS ILE VAL CYS LEU CYS THR GLY VAL MET
SEQRES 22 D 427 GLY VAL CYS CYS THR ALA LEU LEU VAL ALA VAL VAL ALA
SEQRES 23 D 427 ARG LYS LEU GLU PHE ASN LYS ALA GLU LYS HIS VAL HIS
SEQRES 24 D 427 ASN PHE MET MET ASP ILE GLN TYR THR LYS GLU MET LYS
SEQRES 25 D 427 GLU SER ALA ALA ARG VAL LEU GLN GLU ALA TRP MET PHE
SEQRES 26 D 427 TYR LYS HIS THR ARG ARG LYS GLU SER HIS ALA ALA ARG
SEQRES 27 D 427 ARG HIS GLN ARG LYS LEU LEU ALA ALA ILE ASN ALA PHE
SEQRES 28 D 427 ARG GLN VAL ARG LEU LYS HIS ARG LYS LEU ARG GLU GLN
SEQRES 29 D 427 VAL ASN SER MET VAL ASP ILE SER LYS MET HIS MET ILE
SEQRES 30 D 427 LEU TYR ASP LEU GLN GLN ASN LEU SER SER SER HIS ARG
SEQRES 31 D 427 ALA LEU GLU LYS GLN ILE ASP THR LEU ALA GLY LYS LEU
SEQRES 32 D 427 ASP ALA LEU THR GLU LEU LEU SER THR ALA LEU GLY PRO
SEQRES 33 D 427 ARG GLN LEU PRO GLU PRO SER GLN GLN SER LYS
SEQRES 1 E 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 E 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 E 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 E 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 E 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 E 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 E 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 E 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 E 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 E 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 E 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 E 149 GLN MET MET THR ALA LYS
SEQRES 1 F 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 F 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 F 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 F 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 F 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 F 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 F 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 F 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 F 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 F 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 F 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 F 149 GLN MET MET THR ALA LYS
SEQRES 1 G 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 G 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 G 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 G 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 G 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 G 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 G 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 G 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 G 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 G 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 G 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 G 149 GLN MET MET THR ALA LYS
SEQRES 1 H 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 H 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 H 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 H 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 H 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 H 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 H 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 H 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 H 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 H 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 H 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 H 149 GLN MET MET THR ALA LYS
HET CA E 201 1
HET CA E 202 1
HET CA E 203 1
HET CA F 201 1
HET CA F 202 1
HET CA F 203 1
HET CA G 201 1
HET CA G 202 1
HET CA G 203 1
HET CA H 201 1
HET CA H 202 1
HET CA H 203 1
HETNAM CA CALCIUM ION
FORMUL 9 CA 12(CA 2+)
HELIX 1 1 LEU A 9 PHE A 49 1 41
HELIX 2 2 ALA A 55 ASN A 91 1 37
HELIX 3 3 GLY A 102 CYS A 115 1 14
HELIX 4 4 GLN A 147 ALA A 155 1 9
HELIX 5 5 MET A 156 LEU A 162 5 7
HELIX 6 6 VAL A 163 ARG A 170 1 8
HELIX 7 7 ALA A 177 ASN A 186 1 10
HELIX 8 8 HIS A 192 THR A 202 1 11
HELIX 9 9 GLY A 205 GLU A 227 1 23
HELIX 10 10 LEU A 237 LEU A 249 1 13
HELIX 11 11 MET A 261 LEU A 289 1 29
HELIX 12 12 LYS A 293 ARG A 331 1 39
HELIX 13 13 SER A 334 SER A 367 1 34
HELIX 14 14 ASP A 370 SER A 386 1 17
HELIX 15 15 LEU B 9 PHE B 49 1 41
HELIX 16 16 ALA B 55 ASN B 91 1 37
HELIX 17 17 GLY B 102 CYS B 115 1 14
HELIX 18 18 GLN B 147 ALA B 155 1 9
HELIX 19 19 MET B 156 LEU B 162 5 7
HELIX 20 20 VAL B 163 ARG B 170 1 8
HELIX 21 21 ALA B 177 ASN B 186 1 10
HELIX 22 22 HIS B 192 THR B 202 1 11
HELIX 23 23 GLY B 205 GLU B 227 1 23
HELIX 24 24 LEU B 237 LEU B 249 1 13
HELIX 25 25 MET B 261 LEU B 289 1 29
HELIX 26 26 LYS B 293 ARG B 331 1 39
HELIX 27 27 SER B 334 SER B 367 1 34
HELIX 28 28 ASP B 370 SER B 386 1 17
HELIX 29 29 LEU C 9 PHE C 49 1 41
HELIX 30 30 ALA C 55 ASN C 91 1 37
HELIX 31 31 GLY C 102 CYS C 115 1 14
HELIX 32 32 GLN C 147 ALA C 155 1 9
HELIX 33 33 MET C 156 LEU C 162 5 7
HELIX 34 34 VAL C 163 ARG C 170 1 8
HELIX 35 35 ALA C 177 ASN C 186 1 10
HELIX 36 36 HIS C 192 THR C 202 1 11
HELIX 37 37 GLY C 205 GLU C 227 1 23
HELIX 38 38 LEU C 237 LEU C 249 1 13
HELIX 39 39 MET C 261 LEU C 289 1 29
HELIX 40 40 LYS C 293 ARG C 331 1 39
HELIX 41 41 SER C 334 SER C 367 1 34
HELIX 42 42 ASP C 370 SER C 386 1 17
HELIX 43 43 LEU D 9 PHE D 49 1 41
HELIX 44 44 ALA D 55 ASN D 91 1 37
HELIX 45 45 GLY D 102 CYS D 115 1 14
HELIX 46 46 GLN D 147 ALA D 155 1 9
HELIX 47 47 MET D 156 LEU D 162 5 7
HELIX 48 48 VAL D 163 ARG D 170 1 8
HELIX 49 49 ALA D 177 ASN D 186 1 10
HELIX 50 50 HIS D 192 THR D 202 1 11
HELIX 51 51 GLY D 205 GLU D 227 1 23
HELIX 52 52 LEU D 237 LEU D 249 1 13
HELIX 53 53 MET D 261 LEU D 289 1 29
HELIX 54 54 LYS D 293 ARG D 331 1 39
HELIX 55 55 SER D 334 SER D 367 1 34
HELIX 56 56 ASP D 370 SER D 386 1 17
HELIX 57 57 GLU E 6 ASP E 20 1 15
HELIX 58 58 THR E 29 LEU E 39 1 11
HELIX 59 59 THR E 44 VAL E 55 1 12
HELIX 60 60 PHE E 65 ARG E 74 1 10
HELIX 61 61 SER E 81 PHE E 92 1 12
HELIX 62 62 ALA E 102 THR E 110 1 9
HELIX 63 63 THR E 117 ASP E 129 1 13
HELIX 64 64 TYR E 138 ALA E 147 1 10
HELIX 65 65 GLU F 6 ASP F 20 1 15
HELIX 66 66 THR F 29 LEU F 39 1 11
HELIX 67 67 THR F 44 VAL F 55 1 12
HELIX 68 68 PHE F 65 ARG F 74 1 10
HELIX 69 69 SER F 81 PHE F 92 1 12
HELIX 70 70 ALA F 102 THR F 110 1 9
HELIX 71 71 THR F 117 ASP F 129 1 13
HELIX 72 72 TYR F 138 ALA F 147 1 10
HELIX 73 73 GLU G 6 ASP G 20 1 15
HELIX 74 74 THR G 29 LEU G 39 1 11
HELIX 75 75 THR G 44 VAL G 55 1 12
HELIX 76 76 PHE G 65 ARG G 74 1 10
HELIX 77 77 SER G 81 PHE G 92 1 12
HELIX 78 78 ALA G 102 THR G 110 1 9
HELIX 79 79 THR G 117 ASP G 129 1 13
HELIX 80 80 TYR G 138 ALA G 147 1 10
HELIX 81 81 GLU H 6 ASP H 20 1 15
HELIX 82 82 THR H 29 LEU H 39 1 11
HELIX 83 83 THR H 44 VAL H 55 1 12
HELIX 84 84 PHE H 65 ARG H 74 1 10
HELIX 85 85 SER H 81 PHE H 92 1 12
HELIX 86 86 ALA H 102 THR H 110 1 9
HELIX 87 87 THR H 117 ASP H 129 1 13
HELIX 88 88 TYR H 138 ALA H 147 1 10
SHEET 1 A 2 THR E 26 ILE E 27 0
SHEET 2 A 2 ILE E 63 ASP E 64 -1 O ILE E 63 N ILE E 27
SHEET 1 B 2 TYR E 99 SER E 101 0
SHEET 2 B 2 GLN E 135 ASN E 137 -1 O VAL E 136 N ILE E 100
SHEET 1 C 2 THR F 26 ILE F 27 0
SHEET 2 C 2 ILE F 63 ASP F 64 -1 O ILE F 63 N ILE F 27
SHEET 1 D 2 TYR F 99 SER F 101 0
SHEET 2 D 2 GLN F 135 ASN F 137 -1 O VAL F 136 N ILE F 100
SHEET 1 E 2 THR G 26 ILE G 27 0
SHEET 2 E 2 ILE G 63 ASP G 64 -1 O ILE G 63 N ILE G 27
SHEET 1 F 2 TYR G 99 SER G 101 0
SHEET 2 F 2 GLN G 135 ASN G 137 -1 O VAL G 136 N ILE G 100
SHEET 1 G 2 THR H 26 ILE H 27 0
SHEET 2 G 2 ILE H 63 ASP H 64 -1 O ILE H 63 N ILE H 27
SHEET 1 H 2 TYR H 99 SER H 101 0
SHEET 2 H 2 GLN H 135 ASN H 137 -1 O VAL H 136 N ILE H 100
LINK OD1 ASP E 20 CA CA E 201 1555 1555 2.31
LINK OD1 ASP E 22 CA CA E 201 1555 1555 2.43
LINK OD1 ASP E 24 CA CA E 201 1555 1555 2.12
LINK OD2 ASP E 24 CA CA E 201 1555 1555 1.97
LINK O THR E 26 CA CA E 201 1555 1555 2.43
LINK OE1 GLU E 31 CA CA E 201 1555 1555 2.31
LINK OE2 GLU E 31 CA CA E 201 1555 1555 2.25
LINK OD1 ASP E 56 CA CA E 202 1555 1555 2.45
LINK OD1 ASP E 58 CA CA E 202 1555 1555 2.10
LINK OD2 ASP E 58 CA CA E 202 1555 1555 2.53
LINK OD1 ASN E 60 CA CA E 202 1555 1555 2.29
LINK O THR E 62 CA CA E 202 1555 1555 2.43
LINK OE1 GLU E 67 CA CA E 202 1555 1555 2.41
LINK OE2 GLU E 67 CA CA E 202 1555 1555 2.36
LINK OD1 ASP E 93 CA CA E 203 1555 1555 2.38
LINK OD1 ASP E 95 CA CA E 203 1555 1555 2.31
LINK OD1 ASN E 97 CA CA E 203 1555 1555 2.21
LINK O TYR E 99 CA CA E 203 1555 1555 2.16
LINK OE1 GLU E 104 CA CA E 203 1555 1555 2.36
LINK OE2 GLU E 104 CA CA E 203 1555 1555 2.27
LINK OD1 ASP F 20 CA CA F 201 1555 1555 2.33
LINK OD1 ASP F 22 CA CA F 201 1555 1555 2.43
LINK OD1 ASP F 24 CA CA F 201 1555 1555 2.12
LINK OD2 ASP F 24 CA CA F 201 1555 1555 1.94
LINK O THR F 26 CA CA F 201 1555 1555 2.45
LINK OE1 GLU F 31 CA CA F 201 1555 1555 2.33
LINK OE2 GLU F 31 CA CA F 201 1555 1555 2.25
LINK OD1 ASP F 56 CA CA F 202 1555 1555 2.45
LINK OD1 ASP F 58 CA CA F 202 1555 1555 2.10
LINK OD2 ASP F 58 CA CA F 202 1555 1555 2.53
LINK OD1 ASN F 60 CA CA F 202 1555 1555 2.30
LINK O THR F 62 CA CA F 202 1555 1555 2.44
LINK OE1 GLU F 67 CA CA F 202 1555 1555 2.40
LINK OE2 GLU F 67 CA CA F 202 1555 1555 2.35
LINK OD1 ASP F 93 CA CA F 203 1555 1555 2.39
LINK OD1 ASP F 95 CA CA F 203 1555 1555 2.32
LINK OD1 ASN F 97 CA CA F 203 1555 1555 2.22
LINK O TYR F 99 CA CA F 203 1555 1555 2.15
LINK OE1 GLU F 104 CA CA F 203 1555 1555 2.35
LINK OE2 GLU F 104 CA CA F 203 1555 1555 2.27
LINK OD1 ASP G 20 CA CA G 201 1555 1555 2.31
LINK OD1 ASP G 22 CA CA G 201 1555 1555 2.44
LINK OD1 ASP G 24 CA CA G 201 1555 1555 2.12
LINK OD2 ASP G 24 CA CA G 201 1555 1555 1.96
LINK O THR G 26 CA CA G 201 1555 1555 2.43
LINK OE1 GLU G 31 CA CA G 201 1555 1555 2.31
LINK OE2 GLU G 31 CA CA G 201 1555 1555 2.25
LINK OD1 ASP G 56 CA CA G 202 1555 1555 2.45
LINK OD1 ASP G 58 CA CA G 202 1555 1555 2.08
LINK OD2 ASP G 58 CA CA G 202 1555 1555 2.52
LINK OD1 ASN G 60 CA CA G 202 1555 1555 2.29
LINK O THR G 62 CA CA G 202 1555 1555 2.45
LINK OE1 GLU G 67 CA CA G 202 1555 1555 2.41
LINK OE2 GLU G 67 CA CA G 202 1555 1555 2.35
LINK OD1 ASP G 93 CA CA G 203 1555 1555 2.39
LINK OD1 ASP G 95 CA CA G 203 1555 1555 2.32
LINK OD1 ASN G 97 CA CA G 203 1555 1555 2.21
LINK O TYR G 99 CA CA G 203 1555 1555 2.15
LINK OE1 GLU G 104 CA CA G 203 1555 1555 2.36
LINK OE2 GLU G 104 CA CA G 203 1555 1555 2.27
LINK OD1 ASP H 20 CA CA H 201 1555 1555 2.27
LINK OD1 ASP H 22 CA CA H 201 1555 1555 2.44
LINK OD1 ASP H 24 CA CA H 201 1555 1555 2.08
LINK OD2 ASP H 24 CA CA H 201 1555 1555 1.98
LINK O THR H 26 CA CA H 201 1555 1555 2.38
LINK OE1 GLU H 31 CA CA H 201 1555 1555 2.33
LINK OE2 GLU H 31 CA CA H 201 1555 1555 2.29
LINK OD1 ASP H 56 CA CA H 202 1555 1555 2.43
LINK OD1 ASP H 58 CA CA H 202 1555 1555 2.04
LINK OD2 ASP H 58 CA CA H 202 1555 1555 2.51
LINK OD1 ASN H 60 CA CA H 202 1555 1555 2.32
LINK O THR H 62 CA CA H 202 1555 1555 2.50
LINK OE1 GLU H 67 CA CA H 202 1555 1555 2.41
LINK OE2 GLU H 67 CA CA H 202 1555 1555 2.31
LINK OD1 ASP H 93 CA CA H 203 1555 1555 2.36
LINK OD1 ASP H 95 CA CA H 203 1555 1555 2.34
LINK OD1 ASN H 97 CA CA H 203 1555 1555 2.15
LINK O TYR H 99 CA CA H 203 1555 1555 2.09
LINK OE1 GLU H 104 CA CA H 203 1555 1555 2.40
LINK OE2 GLU H 104 CA CA H 203 1555 1555 2.34
SITE 1 AC1 5 ASP E 20 ASP E 22 ASP E 24 THR E 26
SITE 2 AC1 5 GLU E 31
SITE 1 AC2 5 ASP E 56 ASP E 58 ASN E 60 THR E 62
SITE 2 AC2 5 GLU E 67
SITE 1 AC3 5 ASP E 93 ASP E 95 ASN E 97 TYR E 99
SITE 2 AC3 5 GLU E 104
SITE 1 AC4 5 ASP F 20 ASP F 22 ASP F 24 THR F 26
SITE 2 AC4 5 GLU F 31
SITE 1 AC5 5 ASP F 56 ASP F 58 ASN F 60 THR F 62
SITE 2 AC5 5 GLU F 67
SITE 1 AC6 5 ASP F 93 ASP F 95 ASN F 97 TYR F 99
SITE 2 AC6 5 GLU F 104
SITE 1 AC7 5 ASP G 20 ASP G 22 ASP G 24 THR G 26
SITE 2 AC7 5 GLU G 31
SITE 1 AC8 5 ASP G 56 ASP G 58 ASN G 60 THR G 62
SITE 2 AC8 5 GLU G 67
SITE 1 AC9 5 ASP G 93 ASP G 95 ASN G 97 TYR G 99
SITE 2 AC9 5 GLU G 104
SITE 1 AD1 5 ASP H 20 ASP H 22 ASP H 24 THR H 26
SITE 2 AD1 5 GLU H 31
SITE 1 AD2 5 ASP H 56 ASP H 58 ASN H 60 THR H 62
SITE 2 AD2 5 GLU H 67
SITE 1 AD3 5 ASP H 93 ASP H 95 ASN H 97 TYR H 99
SITE 2 AD3 5 GLU H 104
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