HEADER TRANSPORT PROTEIN 08-DEC-16 5U6O
TITLE STRUCTURE OF THE HUMAN HCN1 HYPERPOLARIZATION-ACTIVATED CYCLIC
TITLE 2 NUCLEOTIDE-GATED ION CHANNEL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM/SODIUM HYPERPOLARIZATION-ACTIVATED CYCLIC
COMPND 3 NUCLEOTIDE-GATED CHANNEL 1;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 FRAGMENT: UNP RESIDUES 1-635,866-890;
COMPND 6 SYNONYM: BRAIN CYCLIC NUCLEOTIDE-GATED CHANNEL 1, BCNG-1;
COMPND 7 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: HCN1, BCNG1;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS PACEMAKER ION CHANNEL, TRANSPORT PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR C.-H.LEE,R.MACKINNON
REVDAT 3 13-MAR-24 5U6O 1 REMARK
REVDAT 2 27-SEP-17 5U6O 1 REMARK
REVDAT 1 25-JAN-17 5U6O 0
JRNL AUTH C.H.LEE,R.MACKINNON
JRNL TITL STRUCTURES OF THE HUMAN HCN1 HYPERPOLARIZATION-ACTIVATED
JRNL TITL 2 CHANNEL.
JRNL REF CELL V. 168 111 2017
JRNL REFN ISSN 1097-4172
JRNL PMID 28086084
JRNL DOI 10.1016/J.CELL.2016.12.023
REMARK 2
REMARK 2 RESOLUTION. 3.50 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) : 3.500
REMARK 3 NUMBER OF PARTICLES : 55870
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 5U6O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1000225402.
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 HCN1 HYPERPOLARIZATION
REMARK 245 -ACTIVATED CYCLIC NUCLEOTIDE-
REMARK 245 GATED ION CHANNEL
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 5.00
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) : 1500.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 3300.00
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) : 126.00
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 MET A 1
REMARK 465 GLU A 2
REMARK 465 GLY A 3
REMARK 465 GLY A 4
REMARK 465 GLY A 5
REMARK 465 LYS A 6
REMARK 465 PRO A 7
REMARK 465 ASN A 8
REMARK 465 SER A 9
REMARK 465 SER A 10
REMARK 465 SER A 11
REMARK 465 ASN A 12
REMARK 465 SER A 13
REMARK 465 ARG A 14
REMARK 465 ASP A 15
REMARK 465 ASP A 16
REMARK 465 GLY A 17
REMARK 465 ASN A 18
REMARK 465 SER A 19
REMARK 465 VAL A 20
REMARK 465 PHE A 21
REMARK 465 PRO A 22
REMARK 465 ALA A 23
REMARK 465 LYS A 24
REMARK 465 ALA A 25
REMARK 465 SER A 26
REMARK 465 ALA A 27
REMARK 465 THR A 28
REMARK 465 GLY A 29
REMARK 465 ALA A 30
REMARK 465 GLY A 31
REMARK 465 PRO A 32
REMARK 465 ALA A 33
REMARK 465 ALA A 34
REMARK 465 ALA A 35
REMARK 465 GLU A 36
REMARK 465 LYS A 37
REMARK 465 ARG A 38
REMARK 465 LEU A 39
REMARK 465 GLY A 40
REMARK 465 THR A 41
REMARK 465 PRO A 42
REMARK 465 PRO A 43
REMARK 465 GLY A 44
REMARK 465 GLY A 45
REMARK 465 GLY A 46
REMARK 465 GLY A 47
REMARK 465 ALA A 48
REMARK 465 GLY A 49
REMARK 465 ALA A 50
REMARK 465 LYS A 51
REMARK 465 GLU A 52
REMARK 465 HIS A 53
REMARK 465 GLY A 54
REMARK 465 ASN A 55
REMARK 465 SER A 56
REMARK 465 VAL A 57
REMARK 465 CYS A 58
REMARK 465 PHE A 59
REMARK 465 LYS A 60
REMARK 465 VAL A 61
REMARK 465 ASP A 62
REMARK 465 GLY A 63
REMARK 465 GLY A 64
REMARK 465 GLY A 65
REMARK 465 GLY A 66
REMARK 465 GLY A 67
REMARK 465 GLY A 68
REMARK 465 GLY A 69
REMARK 465 GLY A 70
REMARK 465 GLY A 71
REMARK 465 GLY A 72
REMARK 465 GLY A 73
REMARK 465 GLY A 74
REMARK 465 GLU A 75
REMARK 465 GLU A 76
REMARK 465 PRO A 77
REMARK 465 ALA A 78
REMARK 465 GLY A 79
REMARK 465 GLY A 80
REMARK 465 PHE A 81
REMARK 465 GLU A 82
REMARK 465 ASP A 83
REMARK 465 ALA A 84
REMARK 465 GLU A 85
REMARK 465 GLY A 86
REMARK 465 PRO A 87
REMARK 465 ARG A 88
REMARK 465 ARG A 89
REMARK 465 GLN A 90
REMARK 465 TYR A 91
REMARK 465 GLY A 92
REMARK 465 PHE A 93
REMARK 465 GLU A 201
REMARK 465 ASP A 202
REMARK 465 MET A 243
REMARK 465 ASP A 244
REMARK 465 SER A 245
REMARK 465 GLU A 246
REMARK 465 VAL A 247
REMARK 465 TYR A 248
REMARK 465 LYS A 249
REMARK 465 THR A 250
REMARK 465 ALA A 251
REMARK 465 ALA A 587
REMARK 465 ILE A 588
REMARK 465 ASP A 589
REMARK 465 ARG A 590
REMARK 465 LEU A 591
REMARK 465 ASP A 592
REMARK 465 ARG A 593
REMARK 465 ILE A 594
REMARK 465 GLY A 595
REMARK 465 LYS A 596
REMARK 465 LYS A 597
REMARK 465 ASN A 598
REMARK 465 SER A 599
REMARK 465 ILE A 600
REMARK 465 LEU A 601
REMARK 465 LEU A 602
REMARK 465 GLN A 603
REMARK 465 LYS A 604
REMARK 465 PHE A 605
REMARK 465 GLN A 606
REMARK 465 LYS A 607
REMARK 465 ASP A 608
REMARK 465 LEU A 609
REMARK 465 ASN A 610
REMARK 465 THR A 611
REMARK 465 GLY A 612
REMARK 465 VAL A 613
REMARK 465 PHE A 614
REMARK 465 ASN A 615
REMARK 465 ASN A 616
REMARK 465 GLN A 617
REMARK 465 GLU A 618
REMARK 465 ASN A 619
REMARK 465 GLU A 620
REMARK 465 ILE A 621
REMARK 465 LEU A 622
REMARK 465 LYS A 623
REMARK 465 GLN A 624
REMARK 465 ILE A 625
REMARK 465 VAL A 626
REMARK 465 LYS A 627
REMARK 465 HIS A 628
REMARK 465 ASP A 629
REMARK 465 ARG A 630
REMARK 465 GLU A 631
REMARK 465 MET A 632
REMARK 465 VAL A 633
REMARK 465 GLN A 634
REMARK 465 ALA A 635
REMARK 465 ALA A 636
REMARK 465 LEU A 637
REMARK 465 PRO A 638
REMARK 465 ARG A 639
REMARK 465 GLU A 640
REMARK 465 SER A 641
REMARK 465 SER A 642
REMARK 465 SER A 643
REMARK 465 VAL A 644
REMARK 465 LEU A 645
REMARK 465 ASN A 646
REMARK 465 THR A 647
REMARK 465 ASP A 648
REMARK 465 PRO A 649
REMARK 465 ASP A 650
REMARK 465 ALA A 651
REMARK 465 GLU A 652
REMARK 465 LYS A 653
REMARK 465 PRO A 654
REMARK 465 ARG A 655
REMARK 465 PHE A 656
REMARK 465 ALA A 657
REMARK 465 SER A 658
REMARK 465 ASN A 659
REMARK 465 LEU A 660
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 GLY B 3
REMARK 465 GLY B 4
REMARK 465 GLY B 5
REMARK 465 LYS B 6
REMARK 465 PRO B 7
REMARK 465 ASN B 8
REMARK 465 SER B 9
REMARK 465 SER B 10
REMARK 465 SER B 11
REMARK 465 ASN B 12
REMARK 465 SER B 13
REMARK 465 ARG B 14
REMARK 465 ASP B 15
REMARK 465 ASP B 16
REMARK 465 GLY B 17
REMARK 465 ASN B 18
REMARK 465 SER B 19
REMARK 465 VAL B 20
REMARK 465 PHE B 21
REMARK 465 PRO B 22
REMARK 465 ALA B 23
REMARK 465 LYS B 24
REMARK 465 ALA B 25
REMARK 465 SER B 26
REMARK 465 ALA B 27
REMARK 465 THR B 28
REMARK 465 GLY B 29
REMARK 465 ALA B 30
REMARK 465 GLY B 31
REMARK 465 PRO B 32
REMARK 465 ALA B 33
REMARK 465 ALA B 34
REMARK 465 ALA B 35
REMARK 465 GLU B 36
REMARK 465 LYS B 37
REMARK 465 ARG B 38
REMARK 465 LEU B 39
REMARK 465 GLY B 40
REMARK 465 THR B 41
REMARK 465 PRO B 42
REMARK 465 PRO B 43
REMARK 465 GLY B 44
REMARK 465 GLY B 45
REMARK 465 GLY B 46
REMARK 465 GLY B 47
REMARK 465 ALA B 48
REMARK 465 GLY B 49
REMARK 465 ALA B 50
REMARK 465 LYS B 51
REMARK 465 GLU B 52
REMARK 465 HIS B 53
REMARK 465 GLY B 54
REMARK 465 ASN B 55
REMARK 465 SER B 56
REMARK 465 VAL B 57
REMARK 465 CYS B 58
REMARK 465 PHE B 59
REMARK 465 LYS B 60
REMARK 465 VAL B 61
REMARK 465 ASP B 62
REMARK 465 GLY B 63
REMARK 465 GLY B 64
REMARK 465 GLY B 65
REMARK 465 GLY B 66
REMARK 465 GLY B 67
REMARK 465 GLY B 68
REMARK 465 GLY B 69
REMARK 465 GLY B 70
REMARK 465 GLY B 71
REMARK 465 GLY B 72
REMARK 465 GLY B 73
REMARK 465 GLY B 74
REMARK 465 GLU B 75
REMARK 465 GLU B 76
REMARK 465 PRO B 77
REMARK 465 ALA B 78
REMARK 465 GLY B 79
REMARK 465 GLY B 80
REMARK 465 PHE B 81
REMARK 465 GLU B 82
REMARK 465 ASP B 83
REMARK 465 ALA B 84
REMARK 465 GLU B 85
REMARK 465 GLY B 86
REMARK 465 PRO B 87
REMARK 465 ARG B 88
REMARK 465 ARG B 89
REMARK 465 GLN B 90
REMARK 465 TYR B 91
REMARK 465 GLY B 92
REMARK 465 PHE B 93
REMARK 465 GLU B 201
REMARK 465 ASP B 202
REMARK 465 MET B 243
REMARK 465 ASP B 244
REMARK 465 SER B 245
REMARK 465 GLU B 246
REMARK 465 VAL B 247
REMARK 465 TYR B 248
REMARK 465 LYS B 249
REMARK 465 THR B 250
REMARK 465 ALA B 251
REMARK 465 ALA B 587
REMARK 465 ILE B 588
REMARK 465 ASP B 589
REMARK 465 ARG B 590
REMARK 465 LEU B 591
REMARK 465 ASP B 592
REMARK 465 ARG B 593
REMARK 465 ILE B 594
REMARK 465 GLY B 595
REMARK 465 LYS B 596
REMARK 465 LYS B 597
REMARK 465 ASN B 598
REMARK 465 SER B 599
REMARK 465 ILE B 600
REMARK 465 LEU B 601
REMARK 465 LEU B 602
REMARK 465 GLN B 603
REMARK 465 LYS B 604
REMARK 465 PHE B 605
REMARK 465 GLN B 606
REMARK 465 LYS B 607
REMARK 465 ASP B 608
REMARK 465 LEU B 609
REMARK 465 ASN B 610
REMARK 465 THR B 611
REMARK 465 GLY B 612
REMARK 465 VAL B 613
REMARK 465 PHE B 614
REMARK 465 ASN B 615
REMARK 465 ASN B 616
REMARK 465 GLN B 617
REMARK 465 GLU B 618
REMARK 465 ASN B 619
REMARK 465 GLU B 620
REMARK 465 ILE B 621
REMARK 465 LEU B 622
REMARK 465 LYS B 623
REMARK 465 GLN B 624
REMARK 465 ILE B 625
REMARK 465 VAL B 626
REMARK 465 LYS B 627
REMARK 465 HIS B 628
REMARK 465 ASP B 629
REMARK 465 ARG B 630
REMARK 465 GLU B 631
REMARK 465 MET B 632
REMARK 465 VAL B 633
REMARK 465 GLN B 634
REMARK 465 ALA B 635
REMARK 465 ALA B 636
REMARK 465 LEU B 637
REMARK 465 PRO B 638
REMARK 465 ARG B 639
REMARK 465 GLU B 640
REMARK 465 SER B 641
REMARK 465 SER B 642
REMARK 465 SER B 643
REMARK 465 VAL B 644
REMARK 465 LEU B 645
REMARK 465 ASN B 646
REMARK 465 THR B 647
REMARK 465 ASP B 648
REMARK 465 PRO B 649
REMARK 465 ASP B 650
REMARK 465 ALA B 651
REMARK 465 GLU B 652
REMARK 465 LYS B 653
REMARK 465 PRO B 654
REMARK 465 ARG B 655
REMARK 465 PHE B 656
REMARK 465 ALA B 657
REMARK 465 SER B 658
REMARK 465 ASN B 659
REMARK 465 LEU B 660
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 GLY C 3
REMARK 465 GLY C 4
REMARK 465 GLY C 5
REMARK 465 LYS C 6
REMARK 465 PRO C 7
REMARK 465 ASN C 8
REMARK 465 SER C 9
REMARK 465 SER C 10
REMARK 465 SER C 11
REMARK 465 ASN C 12
REMARK 465 SER C 13
REMARK 465 ARG C 14
REMARK 465 ASP C 15
REMARK 465 ASP C 16
REMARK 465 GLY C 17
REMARK 465 ASN C 18
REMARK 465 SER C 19
REMARK 465 VAL C 20
REMARK 465 PHE C 21
REMARK 465 PRO C 22
REMARK 465 ALA C 23
REMARK 465 LYS C 24
REMARK 465 ALA C 25
REMARK 465 SER C 26
REMARK 465 ALA C 27
REMARK 465 THR C 28
REMARK 465 GLY C 29
REMARK 465 ALA C 30
REMARK 465 GLY C 31
REMARK 465 PRO C 32
REMARK 465 ALA C 33
REMARK 465 ALA C 34
REMARK 465 ALA C 35
REMARK 465 GLU C 36
REMARK 465 LYS C 37
REMARK 465 ARG C 38
REMARK 465 LEU C 39
REMARK 465 GLY C 40
REMARK 465 THR C 41
REMARK 465 PRO C 42
REMARK 465 PRO C 43
REMARK 465 GLY C 44
REMARK 465 GLY C 45
REMARK 465 GLY C 46
REMARK 465 GLY C 47
REMARK 465 ALA C 48
REMARK 465 GLY C 49
REMARK 465 ALA C 50
REMARK 465 LYS C 51
REMARK 465 GLU C 52
REMARK 465 HIS C 53
REMARK 465 GLY C 54
REMARK 465 ASN C 55
REMARK 465 SER C 56
REMARK 465 VAL C 57
REMARK 465 CYS C 58
REMARK 465 PHE C 59
REMARK 465 LYS C 60
REMARK 465 VAL C 61
REMARK 465 ASP C 62
REMARK 465 GLY C 63
REMARK 465 GLY C 64
REMARK 465 GLY C 65
REMARK 465 GLY C 66
REMARK 465 GLY C 67
REMARK 465 GLY C 68
REMARK 465 GLY C 69
REMARK 465 GLY C 70
REMARK 465 GLY C 71
REMARK 465 GLY C 72
REMARK 465 GLY C 73
REMARK 465 GLY C 74
REMARK 465 GLU C 75
REMARK 465 GLU C 76
REMARK 465 PRO C 77
REMARK 465 ALA C 78
REMARK 465 GLY C 79
REMARK 465 GLY C 80
REMARK 465 PHE C 81
REMARK 465 GLU C 82
REMARK 465 ASP C 83
REMARK 465 ALA C 84
REMARK 465 GLU C 85
REMARK 465 GLY C 86
REMARK 465 PRO C 87
REMARK 465 ARG C 88
REMARK 465 ARG C 89
REMARK 465 GLN C 90
REMARK 465 TYR C 91
REMARK 465 GLY C 92
REMARK 465 PHE C 93
REMARK 465 GLU C 201
REMARK 465 ASP C 202
REMARK 465 MET C 243
REMARK 465 ASP C 244
REMARK 465 SER C 245
REMARK 465 GLU C 246
REMARK 465 VAL C 247
REMARK 465 TYR C 248
REMARK 465 LYS C 249
REMARK 465 THR C 250
REMARK 465 ALA C 251
REMARK 465 ALA C 587
REMARK 465 ILE C 588
REMARK 465 ASP C 589
REMARK 465 ARG C 590
REMARK 465 LEU C 591
REMARK 465 ASP C 592
REMARK 465 ARG C 593
REMARK 465 ILE C 594
REMARK 465 GLY C 595
REMARK 465 LYS C 596
REMARK 465 LYS C 597
REMARK 465 ASN C 598
REMARK 465 SER C 599
REMARK 465 ILE C 600
REMARK 465 LEU C 601
REMARK 465 LEU C 602
REMARK 465 GLN C 603
REMARK 465 LYS C 604
REMARK 465 PHE C 605
REMARK 465 GLN C 606
REMARK 465 LYS C 607
REMARK 465 ASP C 608
REMARK 465 LEU C 609
REMARK 465 ASN C 610
REMARK 465 THR C 611
REMARK 465 GLY C 612
REMARK 465 VAL C 613
REMARK 465 PHE C 614
REMARK 465 ASN C 615
REMARK 465 ASN C 616
REMARK 465 GLN C 617
REMARK 465 GLU C 618
REMARK 465 ASN C 619
REMARK 465 GLU C 620
REMARK 465 ILE C 621
REMARK 465 LEU C 622
REMARK 465 LYS C 623
REMARK 465 GLN C 624
REMARK 465 ILE C 625
REMARK 465 VAL C 626
REMARK 465 LYS C 627
REMARK 465 HIS C 628
REMARK 465 ASP C 629
REMARK 465 ARG C 630
REMARK 465 GLU C 631
REMARK 465 MET C 632
REMARK 465 VAL C 633
REMARK 465 GLN C 634
REMARK 465 ALA C 635
REMARK 465 ALA C 636
REMARK 465 LEU C 637
REMARK 465 PRO C 638
REMARK 465 ARG C 639
REMARK 465 GLU C 640
REMARK 465 SER C 641
REMARK 465 SER C 642
REMARK 465 SER C 643
REMARK 465 VAL C 644
REMARK 465 LEU C 645
REMARK 465 ASN C 646
REMARK 465 THR C 647
REMARK 465 ASP C 648
REMARK 465 PRO C 649
REMARK 465 ASP C 650
REMARK 465 ALA C 651
REMARK 465 GLU C 652
REMARK 465 LYS C 653
REMARK 465 PRO C 654
REMARK 465 ARG C 655
REMARK 465 PHE C 656
REMARK 465 ALA C 657
REMARK 465 SER C 658
REMARK 465 ASN C 659
REMARK 465 LEU C 660
REMARK 465 MET D 1
REMARK 465 GLU D 2
REMARK 465 GLY D 3
REMARK 465 GLY D 4
REMARK 465 GLY D 5
REMARK 465 LYS D 6
REMARK 465 PRO D 7
REMARK 465 ASN D 8
REMARK 465 SER D 9
REMARK 465 SER D 10
REMARK 465 SER D 11
REMARK 465 ASN D 12
REMARK 465 SER D 13
REMARK 465 ARG D 14
REMARK 465 ASP D 15
REMARK 465 ASP D 16
REMARK 465 GLY D 17
REMARK 465 ASN D 18
REMARK 465 SER D 19
REMARK 465 VAL D 20
REMARK 465 PHE D 21
REMARK 465 PRO D 22
REMARK 465 ALA D 23
REMARK 465 LYS D 24
REMARK 465 ALA D 25
REMARK 465 SER D 26
REMARK 465 ALA D 27
REMARK 465 THR D 28
REMARK 465 GLY D 29
REMARK 465 ALA D 30
REMARK 465 GLY D 31
REMARK 465 PRO D 32
REMARK 465 ALA D 33
REMARK 465 ALA D 34
REMARK 465 ALA D 35
REMARK 465 GLU D 36
REMARK 465 LYS D 37
REMARK 465 ARG D 38
REMARK 465 LEU D 39
REMARK 465 GLY D 40
REMARK 465 THR D 41
REMARK 465 PRO D 42
REMARK 465 PRO D 43
REMARK 465 GLY D 44
REMARK 465 GLY D 45
REMARK 465 GLY D 46
REMARK 465 GLY D 47
REMARK 465 ALA D 48
REMARK 465 GLY D 49
REMARK 465 ALA D 50
REMARK 465 LYS D 51
REMARK 465 GLU D 52
REMARK 465 HIS D 53
REMARK 465 GLY D 54
REMARK 465 ASN D 55
REMARK 465 SER D 56
REMARK 465 VAL D 57
REMARK 465 CYS D 58
REMARK 465 PHE D 59
REMARK 465 LYS D 60
REMARK 465 VAL D 61
REMARK 465 ASP D 62
REMARK 465 GLY D 63
REMARK 465 GLY D 64
REMARK 465 GLY D 65
REMARK 465 GLY D 66
REMARK 465 GLY D 67
REMARK 465 GLY D 68
REMARK 465 GLY D 69
REMARK 465 GLY D 70
REMARK 465 GLY D 71
REMARK 465 GLY D 72
REMARK 465 GLY D 73
REMARK 465 GLY D 74
REMARK 465 GLU D 75
REMARK 465 GLU D 76
REMARK 465 PRO D 77
REMARK 465 ALA D 78
REMARK 465 GLY D 79
REMARK 465 GLY D 80
REMARK 465 PHE D 81
REMARK 465 GLU D 82
REMARK 465 ASP D 83
REMARK 465 ALA D 84
REMARK 465 GLU D 85
REMARK 465 GLY D 86
REMARK 465 PRO D 87
REMARK 465 ARG D 88
REMARK 465 ARG D 89
REMARK 465 GLN D 90
REMARK 465 TYR D 91
REMARK 465 GLY D 92
REMARK 465 PHE D 93
REMARK 465 GLU D 201
REMARK 465 ASP D 202
REMARK 465 MET D 243
REMARK 465 ASP D 244
REMARK 465 SER D 245
REMARK 465 GLU D 246
REMARK 465 VAL D 247
REMARK 465 TYR D 248
REMARK 465 LYS D 249
REMARK 465 THR D 250
REMARK 465 ALA D 251
REMARK 465 ALA D 587
REMARK 465 ILE D 588
REMARK 465 ASP D 589
REMARK 465 ARG D 590
REMARK 465 LEU D 591
REMARK 465 ASP D 592
REMARK 465 ARG D 593
REMARK 465 ILE D 594
REMARK 465 GLY D 595
REMARK 465 LYS D 596
REMARK 465 LYS D 597
REMARK 465 ASN D 598
REMARK 465 SER D 599
REMARK 465 ILE D 600
REMARK 465 LEU D 601
REMARK 465 LEU D 602
REMARK 465 GLN D 603
REMARK 465 LYS D 604
REMARK 465 PHE D 605
REMARK 465 GLN D 606
REMARK 465 LYS D 607
REMARK 465 ASP D 608
REMARK 465 LEU D 609
REMARK 465 ASN D 610
REMARK 465 THR D 611
REMARK 465 GLY D 612
REMARK 465 VAL D 613
REMARK 465 PHE D 614
REMARK 465 ASN D 615
REMARK 465 ASN D 616
REMARK 465 GLN D 617
REMARK 465 GLU D 618
REMARK 465 ASN D 619
REMARK 465 GLU D 620
REMARK 465 ILE D 621
REMARK 465 LEU D 622
REMARK 465 LYS D 623
REMARK 465 GLN D 624
REMARK 465 ILE D 625
REMARK 465 VAL D 626
REMARK 465 LYS D 627
REMARK 465 HIS D 628
REMARK 465 ASP D 629
REMARK 465 ARG D 630
REMARK 465 GLU D 631
REMARK 465 MET D 632
REMARK 465 VAL D 633
REMARK 465 GLN D 634
REMARK 465 ALA D 635
REMARK 465 ALA D 636
REMARK 465 LEU D 637
REMARK 465 PRO D 638
REMARK 465 ARG D 639
REMARK 465 GLU D 640
REMARK 465 SER D 641
REMARK 465 SER D 642
REMARK 465 SER D 643
REMARK 465 VAL D 644
REMARK 465 LEU D 645
REMARK 465 ASN D 646
REMARK 465 THR D 647
REMARK 465 ASP D 648
REMARK 465 PRO D 649
REMARK 465 ASP D 650
REMARK 465 ALA D 651
REMARK 465 GLU D 652
REMARK 465 LYS D 653
REMARK 465 PRO D 654
REMARK 465 ARG D 655
REMARK 465 PHE D 656
REMARK 465 ALA D 657
REMARK 465 SER D 658
REMARK 465 ASN D 659
REMARK 465 LEU D 660
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 MET A 94 CG SD CE
REMARK 470 ARG A 96 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 98 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER A 100 OG
REMARK 470 LEU A 102 CG CD1 CD2
REMARK 470 LEU A 111 CG CD1 CD2
REMARK 470 PHE A 132 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP A 133 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 133 CZ3 CH2
REMARK 470 THR A 168 OG1 CG2
REMARK 470 GLU A 169 CG CD OE1 OE2
REMARK 470 GLN A 170 CG CD OE1 NE2
REMARK 470 THR A 171 OG1 CG2
REMARK 470 THR A 173 OG1 CG2
REMARK 470 ILE A 177 CG1 CG2 CD1
REMARK 470 VAL A 180 CG1 CG2
REMARK 470 ASP A 183 CG OD1 OD2
REMARK 470 ARG A 195 CG CD NE CZ NH1 NH2
REMARK 470 THR A 196 OG1 CG2
REMARK 470 THR A 198 OG1 CG2
REMARK 470 ASN A 200 CG OD1 ND2
REMARK 470 SER A 203 OG
REMARK 470 SER A 204 OG
REMARK 470 GLU A 205 CG CD OE1 OE2
REMARK 470 ILE A 206 CG1 CG2 CD1
REMARK 470 ILE A 207 CG1 CG2 CD1
REMARK 470 LEU A 208 CG CD1 CD2
REMARK 470 ASP A 209 CG OD1 OD2
REMARK 470 LYS A 211 CG CD CE NZ
REMARK 470 VAL A 212 CG1 CG2
REMARK 470 ILE A 213 CG1 CG2 CD1
REMARK 470 LYS A 214 CG CD CE NZ
REMARK 470 MET A 215 CG SD CE
REMARK 470 ASN A 216 CG OD1 ND2
REMARK 470 LEU A 218 CG CD1 CD2
REMARK 470 LYS A 219 CG CD CE NZ
REMARK 470 SER A 220 OG
REMARK 470 VAL A 224 CG1 CG2
REMARK 470 GLU A 240 CG CD OE1 OE2
REMARK 470 LYS A 241 CG CD CE NZ
REMARK 470 ARG A 252 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 254 CG CD1 CD2
REMARK 470 ARG A 255 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 324 CG OD1 OD2
REMARK 470 ASP A 328 CG OD1 OD2
REMARK 470 GLU A 335 CG CD OE1 OE2
REMARK 470 ASP A 339 CG OD1 OD2
REMARK 470 GLU A 447 CG CD OE1 OE2
REMARK 470 ASP A 455 CG OD1 OD2
REMARK 470 ARG A 467 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 468 CG CD CE NZ
REMARK 470 LEU A 469 CG CD1 CD2
REMARK 470 VAL A 470 CG1 CG2
REMARK 470 THR A 472 OG1 CG2
REMARK 470 MET A 473 CG SD CE
REMARK 470 ASN A 478 CG OD1 ND2
REMARK 470 ASP A 480 CG OD1 OD2
REMARK 470 ASP A 500 CG OD1 OD2
REMARK 470 ILE A 503 CG1 CG2 CD1
REMARK 470 GLU A 505 CG CD OE1 OE2
REMARK 470 VAL A 508 CG1 CG2
REMARK 470 LYS A 510 CG CD CE NZ
REMARK 470 VAL A 519 CG1 CG2
REMARK 470 VAL A 522 CG1 CG2
REMARK 470 ILE A 523 CG1 CG2 CD1
REMARK 470 THR A 524 OG1 CG2
REMARK 470 LYS A 525 CG CD CE NZ
REMARK 470 SER A 526 OG
REMARK 470 SER A 527 OG
REMARK 470 LYS A 528 CG CD CE NZ
REMARK 470 GLU A 529 CG CD OE1 OE2
REMARK 470 MET A 530 CG SD CE
REMARK 470 LYS A 531 CG CD CE NZ
REMARK 470 THR A 533 OG1 CG2
REMARK 470 ASP A 534 CG OD1 OD2
REMARK 470 GLU A 540 CG CD OE1 OE2
REMARK 470 ILE A 541 CG1 CG2 CD1
REMARK 470 CYS A 542 SG
REMARK 470 LEU A 543 CG CD1 CD2
REMARK 470 LEU A 544 CG CD1 CD2
REMARK 470 THR A 545 OG1 CG2
REMARK 470 LYS A 546 CG CD CE NZ
REMARK 470 ARG A 548 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 549 CG CD NE CZ NH1 NH2
REMARK 470 THR A 550 OG1 CG2
REMARK 470 SER A 552 OG
REMARK 470 ASP A 556 CG OD1 OD2
REMARK 470 THR A 557 OG1 CG2
REMARK 470 ASP A 567 CG OD1 OD2
REMARK 470 GLU A 571 CG CD OE1 OE2
REMARK 470 VAL A 572 CG1 CG2
REMARK 470 GLU A 574 CG CD OE1 OE2
REMARK 470 GLU A 575 CG CD OE1 OE2
REMARK 470 MET A 578 CG SD CE
REMARK 470 MET A 579 CG SD CE
REMARK 470 ARG A 580 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 581 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 583 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 584 CG CD OE1 OE2
REMARK 470 THR A 585 OG1 CG2
REMARK 470 VAL A 586 CG1 CG2
REMARK 470 MET B 94 CG SD CE
REMARK 470 ARG B 96 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 98 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER B 100 OG
REMARK 470 LEU B 102 CG CD1 CD2
REMARK 470 LEU B 111 CG CD1 CD2
REMARK 470 PHE B 132 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP B 133 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 133 CZ3 CH2
REMARK 470 THR B 168 OG1 CG2
REMARK 470 GLU B 169 CG CD OE1 OE2
REMARK 470 GLN B 170 CG CD OE1 NE2
REMARK 470 THR B 171 OG1 CG2
REMARK 470 THR B 173 OG1 CG2
REMARK 470 ILE B 177 CG1 CG2 CD1
REMARK 470 VAL B 180 CG1 CG2
REMARK 470 ASP B 183 CG OD1 OD2
REMARK 470 ARG B 195 CG CD NE CZ NH1 NH2
REMARK 470 THR B 196 OG1 CG2
REMARK 470 THR B 198 OG1 CG2
REMARK 470 ASN B 200 CG OD1 ND2
REMARK 470 SER B 203 OG
REMARK 470 SER B 204 OG
REMARK 470 GLU B 205 CG CD OE1 OE2
REMARK 470 ILE B 206 CG1 CG2 CD1
REMARK 470 ILE B 207 CG1 CG2 CD1
REMARK 470 LEU B 208 CG CD1 CD2
REMARK 470 ASP B 209 CG OD1 OD2
REMARK 470 LYS B 211 CG CD CE NZ
REMARK 470 VAL B 212 CG1 CG2
REMARK 470 ILE B 213 CG1 CG2 CD1
REMARK 470 LYS B 214 CG CD CE NZ
REMARK 470 MET B 215 CG SD CE
REMARK 470 ASN B 216 CG OD1 ND2
REMARK 470 LEU B 218 CG CD1 CD2
REMARK 470 LYS B 219 CG CD CE NZ
REMARK 470 SER B 220 OG
REMARK 470 VAL B 224 CG1 CG2
REMARK 470 GLU B 240 CG CD OE1 OE2
REMARK 470 LYS B 241 CG CD CE NZ
REMARK 470 ARG B 252 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 254 CG CD1 CD2
REMARK 470 ARG B 255 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 324 CG OD1 OD2
REMARK 470 ASP B 328 CG OD1 OD2
REMARK 470 GLU B 335 CG CD OE1 OE2
REMARK 470 ASP B 339 CG OD1 OD2
REMARK 470 GLU B 447 CG CD OE1 OE2
REMARK 470 ASP B 455 CG OD1 OD2
REMARK 470 ARG B 467 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 468 CG CD CE NZ
REMARK 470 LEU B 469 CG CD1 CD2
REMARK 470 VAL B 470 CG1 CG2
REMARK 470 THR B 472 OG1 CG2
REMARK 470 MET B 473 CG SD CE
REMARK 470 ASN B 478 CG OD1 ND2
REMARK 470 ASP B 480 CG OD1 OD2
REMARK 470 ASP B 500 CG OD1 OD2
REMARK 470 ILE B 503 CG1 CG2 CD1
REMARK 470 GLU B 505 CG CD OE1 OE2
REMARK 470 VAL B 508 CG1 CG2
REMARK 470 LYS B 510 CG CD CE NZ
REMARK 470 VAL B 519 CG1 CG2
REMARK 470 VAL B 522 CG1 CG2
REMARK 470 ILE B 523 CG1 CG2 CD1
REMARK 470 THR B 524 OG1 CG2
REMARK 470 LYS B 525 CG CD CE NZ
REMARK 470 SER B 526 OG
REMARK 470 SER B 527 OG
REMARK 470 LYS B 528 CG CD CE NZ
REMARK 470 GLU B 529 CG CD OE1 OE2
REMARK 470 MET B 530 CG SD CE
REMARK 470 LYS B 531 CG CD CE NZ
REMARK 470 THR B 533 OG1 CG2
REMARK 470 ASP B 534 CG OD1 OD2
REMARK 470 GLU B 540 CG CD OE1 OE2
REMARK 470 ILE B 541 CG1 CG2 CD1
REMARK 470 CYS B 542 SG
REMARK 470 LEU B 543 CG CD1 CD2
REMARK 470 LEU B 544 CG CD1 CD2
REMARK 470 THR B 545 OG1 CG2
REMARK 470 LYS B 546 CG CD CE NZ
REMARK 470 ARG B 548 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 549 CG CD NE CZ NH1 NH2
REMARK 470 THR B 550 OG1 CG2
REMARK 470 SER B 552 OG
REMARK 470 ASP B 556 CG OD1 OD2
REMARK 470 THR B 557 OG1 CG2
REMARK 470 ASP B 567 CG OD1 OD2
REMARK 470 GLU B 571 CG CD OE1 OE2
REMARK 470 VAL B 572 CG1 CG2
REMARK 470 GLU B 574 CG CD OE1 OE2
REMARK 470 GLU B 575 CG CD OE1 OE2
REMARK 470 MET B 578 CG SD CE
REMARK 470 MET B 579 CG SD CE
REMARK 470 ARG B 580 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 581 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 583 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 584 CG CD OE1 OE2
REMARK 470 THR B 585 OG1 CG2
REMARK 470 VAL B 586 CG1 CG2
REMARK 470 MET C 94 CG SD CE
REMARK 470 ARG C 96 CG CD NE CZ NH1 NH2
REMARK 470 PHE C 98 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER C 100 OG
REMARK 470 LEU C 102 CG CD1 CD2
REMARK 470 LEU C 111 CG CD1 CD2
REMARK 470 PHE C 132 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP C 133 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 133 CZ3 CH2
REMARK 470 THR C 168 OG1 CG2
REMARK 470 GLU C 169 CG CD OE1 OE2
REMARK 470 GLN C 170 CG CD OE1 NE2
REMARK 470 THR C 171 OG1 CG2
REMARK 470 THR C 173 OG1 CG2
REMARK 470 ILE C 177 CG1 CG2 CD1
REMARK 470 VAL C 180 CG1 CG2
REMARK 470 ASP C 183 CG OD1 OD2
REMARK 470 ARG C 195 CG CD NE CZ NH1 NH2
REMARK 470 THR C 196 OG1 CG2
REMARK 470 THR C 198 OG1 CG2
REMARK 470 ASN C 200 CG OD1 ND2
REMARK 470 SER C 203 OG
REMARK 470 SER C 204 OG
REMARK 470 GLU C 205 CG CD OE1 OE2
REMARK 470 ILE C 206 CG1 CG2 CD1
REMARK 470 ILE C 207 CG1 CG2 CD1
REMARK 470 LEU C 208 CG CD1 CD2
REMARK 470 ASP C 209 CG OD1 OD2
REMARK 470 LYS C 211 CG CD CE NZ
REMARK 470 VAL C 212 CG1 CG2
REMARK 470 ILE C 213 CG1 CG2 CD1
REMARK 470 LYS C 214 CG CD CE NZ
REMARK 470 MET C 215 CG SD CE
REMARK 470 ASN C 216 CG OD1 ND2
REMARK 470 LEU C 218 CG CD1 CD2
REMARK 470 LYS C 219 CG CD CE NZ
REMARK 470 SER C 220 OG
REMARK 470 VAL C 224 CG1 CG2
REMARK 470 GLU C 240 CG CD OE1 OE2
REMARK 470 LYS C 241 CG CD CE NZ
REMARK 470 ARG C 252 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 254 CG CD1 CD2
REMARK 470 ARG C 255 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 324 CG OD1 OD2
REMARK 470 ASP C 328 CG OD1 OD2
REMARK 470 GLU C 335 CG CD OE1 OE2
REMARK 470 ASP C 339 CG OD1 OD2
REMARK 470 GLU C 447 CG CD OE1 OE2
REMARK 470 ASP C 455 CG OD1 OD2
REMARK 470 ARG C 467 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 468 CG CD CE NZ
REMARK 470 LEU C 469 CG CD1 CD2
REMARK 470 VAL C 470 CG1 CG2
REMARK 470 THR C 472 OG1 CG2
REMARK 470 MET C 473 CG SD CE
REMARK 470 ASN C 478 CG OD1 ND2
REMARK 470 ASP C 480 CG OD1 OD2
REMARK 470 ASP C 500 CG OD1 OD2
REMARK 470 ILE C 503 CG1 CG2 CD1
REMARK 470 GLU C 505 CG CD OE1 OE2
REMARK 470 VAL C 508 CG1 CG2
REMARK 470 LYS C 510 CG CD CE NZ
REMARK 470 VAL C 519 CG1 CG2
REMARK 470 VAL C 522 CG1 CG2
REMARK 470 ILE C 523 CG1 CG2 CD1
REMARK 470 THR C 524 OG1 CG2
REMARK 470 LYS C 525 CG CD CE NZ
REMARK 470 SER C 526 OG
REMARK 470 SER C 527 OG
REMARK 470 LYS C 528 CG CD CE NZ
REMARK 470 GLU C 529 CG CD OE1 OE2
REMARK 470 MET C 530 CG SD CE
REMARK 470 LYS C 531 CG CD CE NZ
REMARK 470 THR C 533 OG1 CG2
REMARK 470 ASP C 534 CG OD1 OD2
REMARK 470 GLU C 540 CG CD OE1 OE2
REMARK 470 ILE C 541 CG1 CG2 CD1
REMARK 470 CYS C 542 SG
REMARK 470 LEU C 543 CG CD1 CD2
REMARK 470 LEU C 544 CG CD1 CD2
REMARK 470 THR C 545 OG1 CG2
REMARK 470 LYS C 546 CG CD CE NZ
REMARK 470 ARG C 548 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 549 CG CD NE CZ NH1 NH2
REMARK 470 THR C 550 OG1 CG2
REMARK 470 SER C 552 OG
REMARK 470 ASP C 556 CG OD1 OD2
REMARK 470 THR C 557 OG1 CG2
REMARK 470 ASP C 567 CG OD1 OD2
REMARK 470 GLU C 571 CG CD OE1 OE2
REMARK 470 VAL C 572 CG1 CG2
REMARK 470 GLU C 574 CG CD OE1 OE2
REMARK 470 GLU C 575 CG CD OE1 OE2
REMARK 470 MET C 578 CG SD CE
REMARK 470 MET C 579 CG SD CE
REMARK 470 ARG C 580 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 581 CG CD NE CZ NH1 NH2
REMARK 470 PHE C 583 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU C 584 CG CD OE1 OE2
REMARK 470 THR C 585 OG1 CG2
REMARK 470 VAL C 586 CG1 CG2
REMARK 470 MET D 94 CG SD CE
REMARK 470 ARG D 96 CG CD NE CZ NH1 NH2
REMARK 470 PHE D 98 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 SER D 100 OG
REMARK 470 LEU D 102 CG CD1 CD2
REMARK 470 LEU D 111 CG CD1 CD2
REMARK 470 PHE D 132 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP D 133 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 133 CZ3 CH2
REMARK 470 THR D 168 OG1 CG2
REMARK 470 GLU D 169 CG CD OE1 OE2
REMARK 470 GLN D 170 CG CD OE1 NE2
REMARK 470 THR D 171 OG1 CG2
REMARK 470 THR D 173 OG1 CG2
REMARK 470 ILE D 177 CG1 CG2 CD1
REMARK 470 VAL D 180 CG1 CG2
REMARK 470 ASP D 183 CG OD1 OD2
REMARK 470 ARG D 195 CG CD NE CZ NH1 NH2
REMARK 470 THR D 196 OG1 CG2
REMARK 470 THR D 198 OG1 CG2
REMARK 470 ASN D 200 CG OD1 ND2
REMARK 470 SER D 203 OG
REMARK 470 SER D 204 OG
REMARK 470 GLU D 205 CG CD OE1 OE2
REMARK 470 ILE D 206 CG1 CG2 CD1
REMARK 470 ILE D 207 CG1 CG2 CD1
REMARK 470 LEU D 208 CG CD1 CD2
REMARK 470 ASP D 209 CG OD1 OD2
REMARK 470 LYS D 211 CG CD CE NZ
REMARK 470 VAL D 212 CG1 CG2
REMARK 470 ILE D 213 CG1 CG2 CD1
REMARK 470 LYS D 214 CG CD CE NZ
REMARK 470 MET D 215 CG SD CE
REMARK 470 ASN D 216 CG OD1 ND2
REMARK 470 LEU D 218 CG CD1 CD2
REMARK 470 LYS D 219 CG CD CE NZ
REMARK 470 SER D 220 OG
REMARK 470 VAL D 224 CG1 CG2
REMARK 470 GLU D 240 CG CD OE1 OE2
REMARK 470 LYS D 241 CG CD CE NZ
REMARK 470 ARG D 252 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 254 CG CD1 CD2
REMARK 470 ARG D 255 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 324 CG OD1 OD2
REMARK 470 ASP D 328 CG OD1 OD2
REMARK 470 GLU D 335 CG CD OE1 OE2
REMARK 470 ASP D 339 CG OD1 OD2
REMARK 470 GLU D 447 CG CD OE1 OE2
REMARK 470 ASP D 455 CG OD1 OD2
REMARK 470 ARG D 467 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 468 CG CD CE NZ
REMARK 470 LEU D 469 CG CD1 CD2
REMARK 470 VAL D 470 CG1 CG2
REMARK 470 THR D 472 OG1 CG2
REMARK 470 MET D 473 CG SD CE
REMARK 470 ASN D 478 CG OD1 ND2
REMARK 470 ASP D 480 CG OD1 OD2
REMARK 470 ASP D 500 CG OD1 OD2
REMARK 470 ILE D 503 CG1 CG2 CD1
REMARK 470 GLU D 505 CG CD OE1 OE2
REMARK 470 VAL D 508 CG1 CG2
REMARK 470 LYS D 510 CG CD CE NZ
REMARK 470 VAL D 519 CG1 CG2
REMARK 470 VAL D 522 CG1 CG2
REMARK 470 ILE D 523 CG1 CG2 CD1
REMARK 470 THR D 524 OG1 CG2
REMARK 470 LYS D 525 CG CD CE NZ
REMARK 470 SER D 526 OG
REMARK 470 SER D 527 OG
REMARK 470 LYS D 528 CG CD CE NZ
REMARK 470 GLU D 529 CG CD OE1 OE2
REMARK 470 MET D 530 CG SD CE
REMARK 470 LYS D 531 CG CD CE NZ
REMARK 470 THR D 533 OG1 CG2
REMARK 470 ASP D 534 CG OD1 OD2
REMARK 470 GLU D 540 CG CD OE1 OE2
REMARK 470 ILE D 541 CG1 CG2 CD1
REMARK 470 CYS D 542 SG
REMARK 470 LEU D 543 CG CD1 CD2
REMARK 470 LEU D 544 CG CD1 CD2
REMARK 470 THR D 545 OG1 CG2
REMARK 470 LYS D 546 CG CD CE NZ
REMARK 470 ARG D 548 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 549 CG CD NE CZ NH1 NH2
REMARK 470 THR D 550 OG1 CG2
REMARK 470 SER D 552 OG
REMARK 470 ASP D 556 CG OD1 OD2
REMARK 470 THR D 557 OG1 CG2
REMARK 470 ASP D 567 CG OD1 OD2
REMARK 470 GLU D 571 CG CD OE1 OE2
REMARK 470 VAL D 572 CG1 CG2
REMARK 470 GLU D 574 CG CD OE1 OE2
REMARK 470 GLU D 575 CG CD OE1 OE2
REMARK 470 MET D 578 CG SD CE
REMARK 470 MET D 579 CG SD CE
REMARK 470 ARG D 580 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 581 CG CD NE CZ NH1 NH2
REMARK 470 PHE D 583 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU D 584 CG CD OE1 OE2
REMARK 470 THR D 585 OG1 CG2
REMARK 470 VAL D 586 CG1 CG2
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 LYS A 128 1.31 -62.06
REMARK 500 ASP A 209 -70.91 -79.44
REMARK 500 SER A 220 -74.83 -118.25
REMARK 500 PHE A 325 71.38 52.16
REMARK 500 ASP A 328 54.34 -107.91
REMARK 500 LYS A 528 -119.56 65.73
REMARK 500 LEU A 543 -62.72 -121.56
REMARK 500 THR A 557 -167.68 -109.29
REMARK 500 LYS B 128 1.37 -62.04
REMARK 500 ASP B 209 -70.99 -79.31
REMARK 500 SER B 220 -74.76 -118.25
REMARK 500 PHE B 325 71.38 52.08
REMARK 500 ASP B 328 54.33 -107.77
REMARK 500 LYS B 528 -119.47 65.73
REMARK 500 LEU B 543 -62.71 -121.56
REMARK 500 THR B 557 -167.82 -109.65
REMARK 500 LYS C 128 1.37 -62.11
REMARK 500 ASP C 209 -70.81 -79.45
REMARK 500 SER C 220 -74.90 -118.20
REMARK 500 PHE C 325 71.38 52.17
REMARK 500 ASP C 328 54.35 -107.89
REMARK 500 LYS C 528 -119.55 65.76
REMARK 500 LEU C 543 -62.73 -121.53
REMARK 500 THR C 557 -167.69 -109.26
REMARK 500 LYS D 128 1.31 -62.05
REMARK 500 ASP D 209 -71.04 -79.31
REMARK 500 SER D 220 -74.83 -118.25
REMARK 500 PHE D 325 71.28 52.12
REMARK 500 ASP D 328 54.29 -107.77
REMARK 500 LYS D 528 -119.43 65.69
REMARK 500 LEU D 543 -62.78 -121.52
REMARK 500 THR D 557 -167.78 -109.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-8511 RELATED DB: EMDB
REMARK 900 STRUCTURE OF THE HUMAN HCN1 HYPERPOLARIZATION-ACTIVATED CYCLIC
REMARK 900 NUCLEOTIDE-GATED ION CHANNEL
REMARK 900 RELATED ID: EMD-8512 RELATED DB: EMDB
REMARK 900 STRUCTURE OF THE HUMAN HCN1 HYPERPOLARIZATION-ACTIVATED CYCLIC
REMARK 900 NUCLEOTIDE-GATED ION CHANNEL IN COMPLEX WITH CAMP
REMARK 900 RELATED ID: 5U6P RELATED DB: PDB
DBREF 5U6O A 1 635 UNP O60741 HCN1_HUMAN 1 635
DBREF 5U6O A 636 660 UNP O60741 HCN1_HUMAN 866 890
DBREF 5U6O B 1 635 UNP O60741 HCN1_HUMAN 1 635
DBREF 5U6O B 636 660 UNP O60741 HCN1_HUMAN 866 890
DBREF 5U6O C 1 635 UNP O60741 HCN1_HUMAN 1 635
DBREF 5U6O C 636 660 UNP O60741 HCN1_HUMAN 866 890
DBREF 5U6O D 1 635 UNP O60741 HCN1_HUMAN 1 635
DBREF 5U6O D 636 660 UNP O60741 HCN1_HUMAN 866 890
SEQRES 1 A 660 MET GLU GLY GLY GLY LYS PRO ASN SER SER SER ASN SER
SEQRES 2 A 660 ARG ASP ASP GLY ASN SER VAL PHE PRO ALA LYS ALA SER
SEQRES 3 A 660 ALA THR GLY ALA GLY PRO ALA ALA ALA GLU LYS ARG LEU
SEQRES 4 A 660 GLY THR PRO PRO GLY GLY GLY GLY ALA GLY ALA LYS GLU
SEQRES 5 A 660 HIS GLY ASN SER VAL CYS PHE LYS VAL ASP GLY GLY GLY
SEQRES 6 A 660 GLY GLY GLY GLY GLY GLY GLY GLY GLY GLU GLU PRO ALA
SEQRES 7 A 660 GLY GLY PHE GLU ASP ALA GLU GLY PRO ARG ARG GLN TYR
SEQRES 8 A 660 GLY PHE MET GLN ARG GLN PHE THR SER MET LEU GLN PRO
SEQRES 9 A 660 GLY VAL ASN LYS PHE SER LEU ARG MET PHE GLY SER GLN
SEQRES 10 A 660 LYS ALA VAL GLU LYS GLU GLN GLU ARG VAL LYS THR ALA
SEQRES 11 A 660 GLY PHE TRP ILE ILE HIS PRO TYR SER ASP PHE ARG PHE
SEQRES 12 A 660 TYR TRP ASP LEU ILE MET LEU ILE MET MET VAL GLY ASN
SEQRES 13 A 660 LEU VAL ILE ILE PRO VAL GLY ILE THR PHE PHE THR GLU
SEQRES 14 A 660 GLN THR THR THR PRO TRP ILE ILE PHE ASN VAL ALA SER
SEQRES 15 A 660 ASP THR VAL PHE LEU LEU ASP LEU ILE MET ASN PHE ARG
SEQRES 16 A 660 THR GLY THR VAL ASN GLU ASP SER SER GLU ILE ILE LEU
SEQRES 17 A 660 ASP PRO LYS VAL ILE LYS MET ASN TYR LEU LYS SER TRP
SEQRES 18 A 660 PHE VAL VAL ASP PHE ILE SER SER ILE PRO VAL ASP TYR
SEQRES 19 A 660 ILE PHE LEU ILE VAL GLU LYS GLY MET ASP SER GLU VAL
SEQRES 20 A 660 TYR LYS THR ALA ARG ALA LEU ARG ILE VAL ARG PHE THR
SEQRES 21 A 660 LYS ILE LEU SER LEU LEU ARG LEU LEU ARG LEU SER ARG
SEQRES 22 A 660 LEU ILE ARG TYR ILE HIS GLN TRP GLU GLU ILE PHE HIS
SEQRES 23 A 660 MET THR TYR ASP LEU ALA SER ALA VAL VAL ARG ILE PHE
SEQRES 24 A 660 ASN LEU ILE GLY MET MET LEU LEU LEU CYS HIS TRP ASP
SEQRES 25 A 660 GLY CYS LEU GLN PHE LEU VAL PRO LEU LEU GLN ASP PHE
SEQRES 26 A 660 PRO PRO ASP CYS TRP VAL SER LEU ASN GLU MET VAL ASN
SEQRES 27 A 660 ASP SER TRP GLY LYS GLN TYR SER TYR ALA LEU PHE LYS
SEQRES 28 A 660 ALA MET SER HIS MET LEU CYS ILE GLY TYR GLY ALA GLN
SEQRES 29 A 660 ALA PRO VAL SER MET SER ASP LEU TRP ILE THR MET LEU
SEQRES 30 A 660 SER MET ILE VAL GLY ALA THR CYS TYR ALA MET PHE VAL
SEQRES 31 A 660 GLY HIS ALA THR ALA LEU ILE GLN SER LEU ASP SER SER
SEQRES 32 A 660 ARG ARG GLN TYR GLN GLU LYS TYR LYS GLN VAL GLU GLN
SEQRES 33 A 660 TYR MET SER PHE HIS LYS LEU PRO ALA ASP MET ARG GLN
SEQRES 34 A 660 LYS ILE HIS ASP TYR TYR GLU HIS ARG TYR GLN GLY LYS
SEQRES 35 A 660 ILE PHE ASP GLU GLU ASN ILE LEU ASN GLU LEU ASN ASP
SEQRES 36 A 660 PRO LEU ARG GLU GLU ILE VAL ASN PHE ASN CYS ARG LYS
SEQRES 37 A 660 LEU VAL ALA THR MET PRO LEU PHE ALA ASN ALA ASP PRO
SEQRES 38 A 660 ASN PHE VAL THR ALA MET LEU SER LYS LEU ARG PHE GLU
SEQRES 39 A 660 VAL PHE GLN PRO GLY ASP TYR ILE ILE ARG GLU GLY ALA
SEQRES 40 A 660 VAL GLY LYS LYS MET TYR PHE ILE GLN HIS GLY VAL ALA
SEQRES 41 A 660 GLY VAL ILE THR LYS SER SER LYS GLU MET LYS LEU THR
SEQRES 42 A 660 ASP GLY SER TYR PHE GLY GLU ILE CYS LEU LEU THR LYS
SEQRES 43 A 660 GLY ARG ARG THR ALA SER VAL ARG ALA ASP THR TYR CYS
SEQRES 44 A 660 ARG LEU TYR SER LEU SER VAL ASP ASN PHE ASN GLU VAL
SEQRES 45 A 660 LEU GLU GLU TYR PRO MET MET ARG ARG ALA PHE GLU THR
SEQRES 46 A 660 VAL ALA ILE ASP ARG LEU ASP ARG ILE GLY LYS LYS ASN
SEQRES 47 A 660 SER ILE LEU LEU GLN LYS PHE GLN LYS ASP LEU ASN THR
SEQRES 48 A 660 GLY VAL PHE ASN ASN GLN GLU ASN GLU ILE LEU LYS GLN
SEQRES 49 A 660 ILE VAL LYS HIS ASP ARG GLU MET VAL GLN ALA ALA LEU
SEQRES 50 A 660 PRO ARG GLU SER SER SER VAL LEU ASN THR ASP PRO ASP
SEQRES 51 A 660 ALA GLU LYS PRO ARG PHE ALA SER ASN LEU
SEQRES 1 B 660 MET GLU GLY GLY GLY LYS PRO ASN SER SER SER ASN SER
SEQRES 2 B 660 ARG ASP ASP GLY ASN SER VAL PHE PRO ALA LYS ALA SER
SEQRES 3 B 660 ALA THR GLY ALA GLY PRO ALA ALA ALA GLU LYS ARG LEU
SEQRES 4 B 660 GLY THR PRO PRO GLY GLY GLY GLY ALA GLY ALA LYS GLU
SEQRES 5 B 660 HIS GLY ASN SER VAL CYS PHE LYS VAL ASP GLY GLY GLY
SEQRES 6 B 660 GLY GLY GLY GLY GLY GLY GLY GLY GLY GLU GLU PRO ALA
SEQRES 7 B 660 GLY GLY PHE GLU ASP ALA GLU GLY PRO ARG ARG GLN TYR
SEQRES 8 B 660 GLY PHE MET GLN ARG GLN PHE THR SER MET LEU GLN PRO
SEQRES 9 B 660 GLY VAL ASN LYS PHE SER LEU ARG MET PHE GLY SER GLN
SEQRES 10 B 660 LYS ALA VAL GLU LYS GLU GLN GLU ARG VAL LYS THR ALA
SEQRES 11 B 660 GLY PHE TRP ILE ILE HIS PRO TYR SER ASP PHE ARG PHE
SEQRES 12 B 660 TYR TRP ASP LEU ILE MET LEU ILE MET MET VAL GLY ASN
SEQRES 13 B 660 LEU VAL ILE ILE PRO VAL GLY ILE THR PHE PHE THR GLU
SEQRES 14 B 660 GLN THR THR THR PRO TRP ILE ILE PHE ASN VAL ALA SER
SEQRES 15 B 660 ASP THR VAL PHE LEU LEU ASP LEU ILE MET ASN PHE ARG
SEQRES 16 B 660 THR GLY THR VAL ASN GLU ASP SER SER GLU ILE ILE LEU
SEQRES 17 B 660 ASP PRO LYS VAL ILE LYS MET ASN TYR LEU LYS SER TRP
SEQRES 18 B 660 PHE VAL VAL ASP PHE ILE SER SER ILE PRO VAL ASP TYR
SEQRES 19 B 660 ILE PHE LEU ILE VAL GLU LYS GLY MET ASP SER GLU VAL
SEQRES 20 B 660 TYR LYS THR ALA ARG ALA LEU ARG ILE VAL ARG PHE THR
SEQRES 21 B 660 LYS ILE LEU SER LEU LEU ARG LEU LEU ARG LEU SER ARG
SEQRES 22 B 660 LEU ILE ARG TYR ILE HIS GLN TRP GLU GLU ILE PHE HIS
SEQRES 23 B 660 MET THR TYR ASP LEU ALA SER ALA VAL VAL ARG ILE PHE
SEQRES 24 B 660 ASN LEU ILE GLY MET MET LEU LEU LEU CYS HIS TRP ASP
SEQRES 25 B 660 GLY CYS LEU GLN PHE LEU VAL PRO LEU LEU GLN ASP PHE
SEQRES 26 B 660 PRO PRO ASP CYS TRP VAL SER LEU ASN GLU MET VAL ASN
SEQRES 27 B 660 ASP SER TRP GLY LYS GLN TYR SER TYR ALA LEU PHE LYS
SEQRES 28 B 660 ALA MET SER HIS MET LEU CYS ILE GLY TYR GLY ALA GLN
SEQRES 29 B 660 ALA PRO VAL SER MET SER ASP LEU TRP ILE THR MET LEU
SEQRES 30 B 660 SER MET ILE VAL GLY ALA THR CYS TYR ALA MET PHE VAL
SEQRES 31 B 660 GLY HIS ALA THR ALA LEU ILE GLN SER LEU ASP SER SER
SEQRES 32 B 660 ARG ARG GLN TYR GLN GLU LYS TYR LYS GLN VAL GLU GLN
SEQRES 33 B 660 TYR MET SER PHE HIS LYS LEU PRO ALA ASP MET ARG GLN
SEQRES 34 B 660 LYS ILE HIS ASP TYR TYR GLU HIS ARG TYR GLN GLY LYS
SEQRES 35 B 660 ILE PHE ASP GLU GLU ASN ILE LEU ASN GLU LEU ASN ASP
SEQRES 36 B 660 PRO LEU ARG GLU GLU ILE VAL ASN PHE ASN CYS ARG LYS
SEQRES 37 B 660 LEU VAL ALA THR MET PRO LEU PHE ALA ASN ALA ASP PRO
SEQRES 38 B 660 ASN PHE VAL THR ALA MET LEU SER LYS LEU ARG PHE GLU
SEQRES 39 B 660 VAL PHE GLN PRO GLY ASP TYR ILE ILE ARG GLU GLY ALA
SEQRES 40 B 660 VAL GLY LYS LYS MET TYR PHE ILE GLN HIS GLY VAL ALA
SEQRES 41 B 660 GLY VAL ILE THR LYS SER SER LYS GLU MET LYS LEU THR
SEQRES 42 B 660 ASP GLY SER TYR PHE GLY GLU ILE CYS LEU LEU THR LYS
SEQRES 43 B 660 GLY ARG ARG THR ALA SER VAL ARG ALA ASP THR TYR CYS
SEQRES 44 B 660 ARG LEU TYR SER LEU SER VAL ASP ASN PHE ASN GLU VAL
SEQRES 45 B 660 LEU GLU GLU TYR PRO MET MET ARG ARG ALA PHE GLU THR
SEQRES 46 B 660 VAL ALA ILE ASP ARG LEU ASP ARG ILE GLY LYS LYS ASN
SEQRES 47 B 660 SER ILE LEU LEU GLN LYS PHE GLN LYS ASP LEU ASN THR
SEQRES 48 B 660 GLY VAL PHE ASN ASN GLN GLU ASN GLU ILE LEU LYS GLN
SEQRES 49 B 660 ILE VAL LYS HIS ASP ARG GLU MET VAL GLN ALA ALA LEU
SEQRES 50 B 660 PRO ARG GLU SER SER SER VAL LEU ASN THR ASP PRO ASP
SEQRES 51 B 660 ALA GLU LYS PRO ARG PHE ALA SER ASN LEU
SEQRES 1 C 660 MET GLU GLY GLY GLY LYS PRO ASN SER SER SER ASN SER
SEQRES 2 C 660 ARG ASP ASP GLY ASN SER VAL PHE PRO ALA LYS ALA SER
SEQRES 3 C 660 ALA THR GLY ALA GLY PRO ALA ALA ALA GLU LYS ARG LEU
SEQRES 4 C 660 GLY THR PRO PRO GLY GLY GLY GLY ALA GLY ALA LYS GLU
SEQRES 5 C 660 HIS GLY ASN SER VAL CYS PHE LYS VAL ASP GLY GLY GLY
SEQRES 6 C 660 GLY GLY GLY GLY GLY GLY GLY GLY GLY GLU GLU PRO ALA
SEQRES 7 C 660 GLY GLY PHE GLU ASP ALA GLU GLY PRO ARG ARG GLN TYR
SEQRES 8 C 660 GLY PHE MET GLN ARG GLN PHE THR SER MET LEU GLN PRO
SEQRES 9 C 660 GLY VAL ASN LYS PHE SER LEU ARG MET PHE GLY SER GLN
SEQRES 10 C 660 LYS ALA VAL GLU LYS GLU GLN GLU ARG VAL LYS THR ALA
SEQRES 11 C 660 GLY PHE TRP ILE ILE HIS PRO TYR SER ASP PHE ARG PHE
SEQRES 12 C 660 TYR TRP ASP LEU ILE MET LEU ILE MET MET VAL GLY ASN
SEQRES 13 C 660 LEU VAL ILE ILE PRO VAL GLY ILE THR PHE PHE THR GLU
SEQRES 14 C 660 GLN THR THR THR PRO TRP ILE ILE PHE ASN VAL ALA SER
SEQRES 15 C 660 ASP THR VAL PHE LEU LEU ASP LEU ILE MET ASN PHE ARG
SEQRES 16 C 660 THR GLY THR VAL ASN GLU ASP SER SER GLU ILE ILE LEU
SEQRES 17 C 660 ASP PRO LYS VAL ILE LYS MET ASN TYR LEU LYS SER TRP
SEQRES 18 C 660 PHE VAL VAL ASP PHE ILE SER SER ILE PRO VAL ASP TYR
SEQRES 19 C 660 ILE PHE LEU ILE VAL GLU LYS GLY MET ASP SER GLU VAL
SEQRES 20 C 660 TYR LYS THR ALA ARG ALA LEU ARG ILE VAL ARG PHE THR
SEQRES 21 C 660 LYS ILE LEU SER LEU LEU ARG LEU LEU ARG LEU SER ARG
SEQRES 22 C 660 LEU ILE ARG TYR ILE HIS GLN TRP GLU GLU ILE PHE HIS
SEQRES 23 C 660 MET THR TYR ASP LEU ALA SER ALA VAL VAL ARG ILE PHE
SEQRES 24 C 660 ASN LEU ILE GLY MET MET LEU LEU LEU CYS HIS TRP ASP
SEQRES 25 C 660 GLY CYS LEU GLN PHE LEU VAL PRO LEU LEU GLN ASP PHE
SEQRES 26 C 660 PRO PRO ASP CYS TRP VAL SER LEU ASN GLU MET VAL ASN
SEQRES 27 C 660 ASP SER TRP GLY LYS GLN TYR SER TYR ALA LEU PHE LYS
SEQRES 28 C 660 ALA MET SER HIS MET LEU CYS ILE GLY TYR GLY ALA GLN
SEQRES 29 C 660 ALA PRO VAL SER MET SER ASP LEU TRP ILE THR MET LEU
SEQRES 30 C 660 SER MET ILE VAL GLY ALA THR CYS TYR ALA MET PHE VAL
SEQRES 31 C 660 GLY HIS ALA THR ALA LEU ILE GLN SER LEU ASP SER SER
SEQRES 32 C 660 ARG ARG GLN TYR GLN GLU LYS TYR LYS GLN VAL GLU GLN
SEQRES 33 C 660 TYR MET SER PHE HIS LYS LEU PRO ALA ASP MET ARG GLN
SEQRES 34 C 660 LYS ILE HIS ASP TYR TYR GLU HIS ARG TYR GLN GLY LYS
SEQRES 35 C 660 ILE PHE ASP GLU GLU ASN ILE LEU ASN GLU LEU ASN ASP
SEQRES 36 C 660 PRO LEU ARG GLU GLU ILE VAL ASN PHE ASN CYS ARG LYS
SEQRES 37 C 660 LEU VAL ALA THR MET PRO LEU PHE ALA ASN ALA ASP PRO
SEQRES 38 C 660 ASN PHE VAL THR ALA MET LEU SER LYS LEU ARG PHE GLU
SEQRES 39 C 660 VAL PHE GLN PRO GLY ASP TYR ILE ILE ARG GLU GLY ALA
SEQRES 40 C 660 VAL GLY LYS LYS MET TYR PHE ILE GLN HIS GLY VAL ALA
SEQRES 41 C 660 GLY VAL ILE THR LYS SER SER LYS GLU MET LYS LEU THR
SEQRES 42 C 660 ASP GLY SER TYR PHE GLY GLU ILE CYS LEU LEU THR LYS
SEQRES 43 C 660 GLY ARG ARG THR ALA SER VAL ARG ALA ASP THR TYR CYS
SEQRES 44 C 660 ARG LEU TYR SER LEU SER VAL ASP ASN PHE ASN GLU VAL
SEQRES 45 C 660 LEU GLU GLU TYR PRO MET MET ARG ARG ALA PHE GLU THR
SEQRES 46 C 660 VAL ALA ILE ASP ARG LEU ASP ARG ILE GLY LYS LYS ASN
SEQRES 47 C 660 SER ILE LEU LEU GLN LYS PHE GLN LYS ASP LEU ASN THR
SEQRES 48 C 660 GLY VAL PHE ASN ASN GLN GLU ASN GLU ILE LEU LYS GLN
SEQRES 49 C 660 ILE VAL LYS HIS ASP ARG GLU MET VAL GLN ALA ALA LEU
SEQRES 50 C 660 PRO ARG GLU SER SER SER VAL LEU ASN THR ASP PRO ASP
SEQRES 51 C 660 ALA GLU LYS PRO ARG PHE ALA SER ASN LEU
SEQRES 1 D 660 MET GLU GLY GLY GLY LYS PRO ASN SER SER SER ASN SER
SEQRES 2 D 660 ARG ASP ASP GLY ASN SER VAL PHE PRO ALA LYS ALA SER
SEQRES 3 D 660 ALA THR GLY ALA GLY PRO ALA ALA ALA GLU LYS ARG LEU
SEQRES 4 D 660 GLY THR PRO PRO GLY GLY GLY GLY ALA GLY ALA LYS GLU
SEQRES 5 D 660 HIS GLY ASN SER VAL CYS PHE LYS VAL ASP GLY GLY GLY
SEQRES 6 D 660 GLY GLY GLY GLY GLY GLY GLY GLY GLY GLU GLU PRO ALA
SEQRES 7 D 660 GLY GLY PHE GLU ASP ALA GLU GLY PRO ARG ARG GLN TYR
SEQRES 8 D 660 GLY PHE MET GLN ARG GLN PHE THR SER MET LEU GLN PRO
SEQRES 9 D 660 GLY VAL ASN LYS PHE SER LEU ARG MET PHE GLY SER GLN
SEQRES 10 D 660 LYS ALA VAL GLU LYS GLU GLN GLU ARG VAL LYS THR ALA
SEQRES 11 D 660 GLY PHE TRP ILE ILE HIS PRO TYR SER ASP PHE ARG PHE
SEQRES 12 D 660 TYR TRP ASP LEU ILE MET LEU ILE MET MET VAL GLY ASN
SEQRES 13 D 660 LEU VAL ILE ILE PRO VAL GLY ILE THR PHE PHE THR GLU
SEQRES 14 D 660 GLN THR THR THR PRO TRP ILE ILE PHE ASN VAL ALA SER
SEQRES 15 D 660 ASP THR VAL PHE LEU LEU ASP LEU ILE MET ASN PHE ARG
SEQRES 16 D 660 THR GLY THR VAL ASN GLU ASP SER SER GLU ILE ILE LEU
SEQRES 17 D 660 ASP PRO LYS VAL ILE LYS MET ASN TYR LEU LYS SER TRP
SEQRES 18 D 660 PHE VAL VAL ASP PHE ILE SER SER ILE PRO VAL ASP TYR
SEQRES 19 D 660 ILE PHE LEU ILE VAL GLU LYS GLY MET ASP SER GLU VAL
SEQRES 20 D 660 TYR LYS THR ALA ARG ALA LEU ARG ILE VAL ARG PHE THR
SEQRES 21 D 660 LYS ILE LEU SER LEU LEU ARG LEU LEU ARG LEU SER ARG
SEQRES 22 D 660 LEU ILE ARG TYR ILE HIS GLN TRP GLU GLU ILE PHE HIS
SEQRES 23 D 660 MET THR TYR ASP LEU ALA SER ALA VAL VAL ARG ILE PHE
SEQRES 24 D 660 ASN LEU ILE GLY MET MET LEU LEU LEU CYS HIS TRP ASP
SEQRES 25 D 660 GLY CYS LEU GLN PHE LEU VAL PRO LEU LEU GLN ASP PHE
SEQRES 26 D 660 PRO PRO ASP CYS TRP VAL SER LEU ASN GLU MET VAL ASN
SEQRES 27 D 660 ASP SER TRP GLY LYS GLN TYR SER TYR ALA LEU PHE LYS
SEQRES 28 D 660 ALA MET SER HIS MET LEU CYS ILE GLY TYR GLY ALA GLN
SEQRES 29 D 660 ALA PRO VAL SER MET SER ASP LEU TRP ILE THR MET LEU
SEQRES 30 D 660 SER MET ILE VAL GLY ALA THR CYS TYR ALA MET PHE VAL
SEQRES 31 D 660 GLY HIS ALA THR ALA LEU ILE GLN SER LEU ASP SER SER
SEQRES 32 D 660 ARG ARG GLN TYR GLN GLU LYS TYR LYS GLN VAL GLU GLN
SEQRES 33 D 660 TYR MET SER PHE HIS LYS LEU PRO ALA ASP MET ARG GLN
SEQRES 34 D 660 LYS ILE HIS ASP TYR TYR GLU HIS ARG TYR GLN GLY LYS
SEQRES 35 D 660 ILE PHE ASP GLU GLU ASN ILE LEU ASN GLU LEU ASN ASP
SEQRES 36 D 660 PRO LEU ARG GLU GLU ILE VAL ASN PHE ASN CYS ARG LYS
SEQRES 37 D 660 LEU VAL ALA THR MET PRO LEU PHE ALA ASN ALA ASP PRO
SEQRES 38 D 660 ASN PHE VAL THR ALA MET LEU SER LYS LEU ARG PHE GLU
SEQRES 39 D 660 VAL PHE GLN PRO GLY ASP TYR ILE ILE ARG GLU GLY ALA
SEQRES 40 D 660 VAL GLY LYS LYS MET TYR PHE ILE GLN HIS GLY VAL ALA
SEQRES 41 D 660 GLY VAL ILE THR LYS SER SER LYS GLU MET LYS LEU THR
SEQRES 42 D 660 ASP GLY SER TYR PHE GLY GLU ILE CYS LEU LEU THR LYS
SEQRES 43 D 660 GLY ARG ARG THR ALA SER VAL ARG ALA ASP THR TYR CYS
SEQRES 44 D 660 ARG LEU TYR SER LEU SER VAL ASP ASN PHE ASN GLU VAL
SEQRES 45 D 660 LEU GLU GLU TYR PRO MET MET ARG ARG ALA PHE GLU THR
SEQRES 46 D 660 VAL ALA ILE ASP ARG LEU ASP ARG ILE GLY LYS LYS ASN
SEQRES 47 D 660 SER ILE LEU LEU GLN LYS PHE GLN LYS ASP LEU ASN THR
SEQRES 48 D 660 GLY VAL PHE ASN ASN GLN GLU ASN GLU ILE LEU LYS GLN
SEQRES 49 D 660 ILE VAL LYS HIS ASP ARG GLU MET VAL GLN ALA ALA LEU
SEQRES 50 D 660 PRO ARG GLU SER SER SER VAL LEU ASN THR ASP PRO ASP
SEQRES 51 D 660 ALA GLU LYS PRO ARG PHE ALA SER ASN LEU
HELIX 1 AA1 MET A 94 GLN A 103 1 10
HELIX 2 AA2 ASN A 107 GLY A 115 1 9
HELIX 3 AA3 SER A 116 LYS A 128 1 13
HELIX 4 AA4 SER A 139 PHE A 167 1 29
HELIX 5 AA5 THR A 172 THR A 196 1 25
HELIX 6 AA6 LYS A 211 LYS A 219 1 9
HELIX 7 AA7 TRP A 221 ILE A 230 1 10
HELIX 8 AA8 PRO A 231 GLY A 242 1 12
HELIX 9 AA9 ALA A 253 LEU A 265 1 13
HELIX 10 AB1 LEU A 266 LEU A 268 5 3
HELIX 11 AB2 LEU A 269 ASP A 290 1 22
HELIX 12 AB3 ALA A 292 GLN A 323 1 32
HELIX 13 AB4 CYS A 329 ASN A 334 1 6
HELIX 14 AB5 SER A 340 CYS A 358 1 19
HELIX 15 AB6 SER A 368 ASP A 401 1 34
HELIX 16 AB7 ASP A 401 LYS A 422 1 22
HELIX 17 AB8 PRO A 424 GLN A 440 1 17
HELIX 18 AB9 ASP A 445 LEU A 453 1 9
HELIX 19 AC1 ASN A 454 MET A 473 1 20
HELIX 20 AC2 ASP A 480 LEU A 491 1 12
HELIX 21 AC3 VAL A 566 TYR A 576 1 11
HELIX 22 AC4 TYR A 576 THR A 585 1 10
HELIX 23 AC5 GLN B 95 GLN B 103 1 9
HELIX 24 AC6 ASN B 107 GLY B 115 1 9
HELIX 25 AC7 SER B 116 LYS B 128 1 13
HELIX 26 AC8 SER B 139 PHE B 167 1 29
HELIX 27 AC9 THR B 172 THR B 196 1 25
HELIX 28 AD1 LYS B 211 LYS B 219 1 9
HELIX 29 AD2 TRP B 221 ILE B 230 1 10
HELIX 30 AD3 PRO B 231 GLY B 242 1 12
HELIX 31 AD4 ALA B 253 LEU B 265 1 13
HELIX 32 AD5 LEU B 266 LEU B 268 5 3
HELIX 33 AD6 LEU B 269 ASP B 290 1 22
HELIX 34 AD7 ALA B 292 GLN B 323 1 32
HELIX 35 AD8 CYS B 329 ASN B 334 1 6
HELIX 36 AD9 SER B 340 CYS B 358 1 19
HELIX 37 AE1 SER B 368 ASP B 401 1 34
HELIX 38 AE2 ASP B 401 LYS B 422 1 22
HELIX 39 AE3 PRO B 424 GLN B 440 1 17
HELIX 40 AE4 ASP B 445 LEU B 453 1 9
HELIX 41 AE5 ASN B 454 MET B 473 1 20
HELIX 42 AE6 ASP B 480 LEU B 491 1 12
HELIX 43 AE7 VAL B 566 TYR B 576 1 11
HELIX 44 AE8 TYR B 576 THR B 585 1 10
HELIX 45 AE9 GLN C 95 GLN C 103 1 9
HELIX 46 AF1 ASN C 107 GLY C 115 1 9
HELIX 47 AF2 SER C 116 LYS C 128 1 13
HELIX 48 AF3 SER C 139 PHE C 167 1 29
HELIX 49 AF4 THR C 172 THR C 196 1 25
HELIX 50 AF5 LYS C 211 LYS C 219 1 9
HELIX 51 AF6 TRP C 221 ILE C 230 1 10
HELIX 52 AF7 PRO C 231 GLY C 242 1 12
HELIX 53 AF8 ALA C 253 LEU C 265 1 13
HELIX 54 AF9 LEU C 266 LEU C 268 5 3
HELIX 55 AG1 LEU C 269 ASP C 290 1 22
HELIX 56 AG2 ALA C 292 GLN C 323 1 32
HELIX 57 AG3 CYS C 329 ASN C 334 1 6
HELIX 58 AG4 SER C 340 CYS C 358 1 19
HELIX 59 AG5 SER C 368 ASP C 401 1 34
HELIX 60 AG6 ASP C 401 LYS C 422 1 22
HELIX 61 AG7 PRO C 424 GLN C 440 1 17
HELIX 62 AG8 ASP C 445 LEU C 453 1 9
HELIX 63 AG9 ASN C 454 MET C 473 1 20
HELIX 64 AH1 ASP C 480 LEU C 491 1 12
HELIX 65 AH2 VAL C 566 TYR C 576 1 11
HELIX 66 AH3 TYR C 576 THR C 585 1 10
HELIX 67 AH4 GLN D 95 GLN D 103 1 9
HELIX 68 AH5 ASN D 107 GLY D 115 1 9
HELIX 69 AH6 SER D 116 LYS D 128 1 13
HELIX 70 AH7 SER D 139 PHE D 167 1 29
HELIX 71 AH8 THR D 172 THR D 196 1 25
HELIX 72 AH9 LYS D 211 LYS D 219 1 9
HELIX 73 AI1 TRP D 221 ILE D 230 1 10
HELIX 74 AI2 PRO D 231 GLY D 242 1 12
HELIX 75 AI3 ALA D 253 LEU D 265 1 13
HELIX 76 AI4 LEU D 266 LEU D 268 5 3
HELIX 77 AI5 LEU D 269 ASP D 290 1 22
HELIX 78 AI6 ALA D 292 GLN D 323 1 32
HELIX 79 AI7 CYS D 329 ASN D 334 1 6
HELIX 80 AI8 SER D 340 CYS D 358 1 19
HELIX 81 AI9 SER D 368 ASP D 401 1 34
HELIX 82 AJ1 ASP D 401 LYS D 422 1 22
HELIX 83 AJ2 PRO D 424 GLN D 440 1 17
HELIX 84 AJ3 ASP D 445 LEU D 453 1 9
HELIX 85 AJ4 ASN D 454 MET D 473 1 20
HELIX 86 AJ5 ASP D 480 LEU D 491 1 12
HELIX 87 AJ6 VAL D 566 TYR D 576 1 11
HELIX 88 AJ7 TYR D 576 THR D 585 1 10
SHEET 1 AA1 4 ARG A 492 PHE A 496 0
SHEET 2 AA1 4 SER A 552 SER A 565 -1 O SER A 563 N ARG A 492
SHEET 3 AA1 4 LYS A 511 ILE A 523 -1 N MET A 512 O LEU A 564
SHEET 4 AA1 4 GLU A 529 MET A 530 -1 O MET A 530 N VAL A 522
SHEET 1 AA2 4 TYR A 501 ILE A 503 0
SHEET 2 AA2 4 SER A 552 SER A 565 -1 O VAL A 553 N ILE A 503
SHEET 3 AA2 4 LYS A 511 ILE A 523 -1 N MET A 512 O LEU A 564
SHEET 4 AA2 4 TYR A 537 PHE A 538 -1 O PHE A 538 N TYR A 513
SHEET 1 AA3 4 ARG B 492 PHE B 496 0
SHEET 2 AA3 4 SER B 552 SER B 565 -1 O SER B 563 N ARG B 492
SHEET 3 AA3 4 LYS B 511 ILE B 523 -1 N MET B 512 O LEU B 564
SHEET 4 AA3 4 GLU B 529 MET B 530 -1 O MET B 530 N VAL B 522
SHEET 1 AA4 4 TYR B 501 ILE B 503 0
SHEET 2 AA4 4 SER B 552 SER B 565 -1 O VAL B 553 N ILE B 503
SHEET 3 AA4 4 LYS B 511 ILE B 523 -1 N MET B 512 O LEU B 564
SHEET 4 AA4 4 TYR B 537 PHE B 538 -1 O PHE B 538 N TYR B 513
SHEET 1 AA5 4 ARG C 492 PHE C 496 0
SHEET 2 AA5 4 SER C 552 SER C 565 -1 O SER C 563 N ARG C 492
SHEET 3 AA5 4 LYS C 511 ILE C 523 -1 N MET C 512 O LEU C 564
SHEET 4 AA5 4 GLU C 529 MET C 530 -1 O MET C 530 N VAL C 522
SHEET 1 AA6 4 TYR C 501 ILE C 503 0
SHEET 2 AA6 4 SER C 552 SER C 565 -1 O VAL C 553 N ILE C 503
SHEET 3 AA6 4 LYS C 511 ILE C 523 -1 N MET C 512 O LEU C 564
SHEET 4 AA6 4 TYR C 537 PHE C 538 -1 O PHE C 538 N TYR C 513
SHEET 1 AA7 4 ARG D 492 PHE D 496 0
SHEET 2 AA7 4 SER D 552 SER D 565 -1 O SER D 563 N ARG D 492
SHEET 3 AA7 4 LYS D 511 ILE D 523 -1 N MET D 512 O LEU D 564
SHEET 4 AA7 4 GLU D 529 MET D 530 -1 O MET D 530 N VAL D 522
SHEET 1 AA8 4 TYR D 501 ILE D 503 0
SHEET 2 AA8 4 SER D 552 SER D 565 -1 O VAL D 553 N ILE D 503
SHEET 3 AA8 4 LYS D 511 ILE D 523 -1 N MET D 512 O LEU D 564
SHEET 4 AA8 4 TYR D 537 PHE D 538 -1 O PHE D 538 N TYR D 513
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 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 0.001246 0.999999 0.000332 -0.09105 1
MTRIX2 2 -0.999999 0.001246 0.000723 124.71944 1
MTRIX3 2 0.000723 -0.000332 1.000000 -0.01601 1
MTRIX1 3 -0.999999 0.001310 0.000614 124.73636 1
MTRIX2 3 -0.001310 -0.999999 0.000725 124.87591 1
MTRIX3 3 0.000615 0.000724 1.000000 -0.07010 1
MTRIX1 4 0.000198 -1.000000 0.000119 124.81739 1
MTRIX2 4 1.000000 0.000198 -0.000115 -0.01223 1
MTRIX3 4 0.000115 0.000119 1.000000 -0.01129 1
(ATOM LINES ARE NOT SHOWN.)
END