HEADER MEMBRANE PROTEIN 25-APR-18 6D7T
TITLE CRYO-EM STRUCTURE OF HUMAN TRPV6-Y467A IN COMPLEX WITH 2-
TITLE 2 AMINOETHOXYDIPHENYL BORATE (2-APB)
CAVEAT 6D7T RESIDUES ILE C 540 AND ILE C 541 THAT ARE NEXT TO EACH OTHER
CAVEAT 2 6D7T IN THE SAMPLE SEQUENCE ARE NOT PROPERLY LINKED: DISTANCE
CAVEAT 3 6D7T BETWEEN C AND N IS 1.10. RESIDUES PRO D 544 AND ALA D 545
CAVEAT 4 6D7T THAT ARE NEXT TO EACH OTHER IN THE SAMPLE SEQUENCE ARE NOT
CAVEAT 5 6D7T PROPERLY LINKED: DISTANCE BETWEEN C AND N IS 1.73.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY V
COMPND 3 MEMBER 6;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 SYNONYM: TRPV6,CAT-LIKE,CAT-L,CALCIUM TRANSPORT PROTEIN 1,CAT1,
COMPND 6 EPITHELIAL CALCIUM CHANNEL 2,ECAC2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TRPV6, ECAC2;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS ION CHANNELS, TRANSPORTER, CALCIUM CHANNEL, EPITHELIAL CALCIUM
KEYWDS 2 CHANNEL, MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR A.K.SINGH,K.SAOTOME,L.L.MCGOLDRICK,A.I.SOBOLEVSKY
REVDAT 2 18-DEC-19 6D7T 1 SCALE
REVDAT 1 18-JUL-18 6D7T 0
JRNL AUTH A.K.SINGH,K.SAOTOME,L.L.MCGOLDRICK,A.I.SOBOLEVSKY
JRNL TITL STRUCTURAL BASES OF TRP CHANNEL TRPV6 ALLOSTERIC MODULATION
JRNL TITL 2 BY 2-APB.
JRNL REF NAT COMMUN V. 9 2465 2018
JRNL REFN ESSN 2041-1723
JRNL PMID 29941865
JRNL DOI 10.1038/S41467-018-04828-Y
REMARK 2
REMARK 2 RESOLUTION. 4.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : RELION, MOTIONCORR2, RELION
REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE
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) : 4.440
REMARK 3 NUMBER OF PARTICLES : 77460
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 6D7T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-18.
REMARK 100 THE DEPOSITION ID IS D_1000234134.
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 : TRPV6 IN AMPHIPOLS
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.50
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 TECNAI 20
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) : 43.00
REMARK 245 ILLUMINATION MODE : SPOT SCAN
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 200
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 GLY A 2
REMARK 465 LEU A 3
REMARK 465 SER A 4
REMARK 465 LEU A 5
REMARK 465 PRO A 6
REMARK 465 LYS A 7
REMARK 465 GLU A 8
REMARK 465 LYS A 9
REMARK 465 GLY A 10
REMARK 465 LEU A 11
REMARK 465 ILE A 12
REMARK 465 LEU A 13
REMARK 465 CYS A 14
REMARK 465 LEU A 15
REMARK 465 TRP A 16
REMARK 465 SER A 17
REMARK 465 LYS A 18
REMARK 465 PHE A 19
REMARK 465 CYS A 20
REMARK 465 ARG A 21
REMARK 465 TRP A 22
REMARK 465 PHE A 23
REMARK 465 GLN A 24
REMARK 465 ARG A 25
REMARK 465 ARG A 26
REMARK 465 GLU A 27
REMARK 465 LEU A 639
REMARK 465 ASN A 640
REMARK 465 ARG A 641
REMARK 465 GLN A 642
REMARK 465 ARG A 643
REMARK 465 ILE A 644
REMARK 465 GLN A 645
REMARK 465 ARG A 646
REMARK 465 TYR A 647
REMARK 465 ALA A 648
REMARK 465 GLN A 649
REMARK 465 ALA A 650
REMARK 465 PHE A 651
REMARK 465 HIS A 652
REMARK 465 THR A 653
REMARK 465 ARG A 654
REMARK 465 GLY A 655
REMARK 465 SER A 656
REMARK 465 GLU A 657
REMARK 465 ASP A 658
REMARK 465 LEU A 659
REMARK 465 ASP A 660
REMARK 465 LYS A 661
REMARK 465 ASP A 662
REMARK 465 SER A 663
REMARK 465 VAL A 664
REMARK 465 GLU A 665
REMARK 465 LYS A 666
REMARK 465 LEU A 667
REMARK 465 GLU A 668
REMARK 465 LEU A 669
REMARK 465 GLY A 670
REMARK 465 CYS A 671
REMARK 465 PRO A 672
REMARK 465 PHE A 673
REMARK 465 SER A 674
REMARK 465 PRO A 675
REMARK 465 HIS A 676
REMARK 465 LEU A 677
REMARK 465 SER A 678
REMARK 465 LEU A 679
REMARK 465 PRO A 680
REMARK 465 MET A 681
REMARK 465 PRO A 682
REMARK 465 SER A 683
REMARK 465 VAL A 684
REMARK 465 SER A 685
REMARK 465 ARG A 686
REMARK 465 SER A 687
REMARK 465 THR A 688
REMARK 465 SER A 689
REMARK 465 ARG A 690
REMARK 465 SER A 691
REMARK 465 SER A 692
REMARK 465 ALA A 693
REMARK 465 ASN A 694
REMARK 465 TRP A 695
REMARK 465 GLU A 696
REMARK 465 ARG A 697
REMARK 465 LEU A 698
REMARK 465 ARG A 699
REMARK 465 GLN A 700
REMARK 465 GLY A 701
REMARK 465 THR A 702
REMARK 465 LEU A 703
REMARK 465 ARG A 704
REMARK 465 ARG A 705
REMARK 465 ASP A 706
REMARK 465 LEU A 707
REMARK 465 ARG A 708
REMARK 465 GLY A 709
REMARK 465 ILE A 710
REMARK 465 ILE A 711
REMARK 465 ASN A 712
REMARK 465 ARG A 713
REMARK 465 GLY A 714
REMARK 465 LEU A 715
REMARK 465 GLU A 716
REMARK 465 ASP A 717
REMARK 465 GLY A 718
REMARK 465 GLU A 719
REMARK 465 SER A 720
REMARK 465 TRP A 721
REMARK 465 GLU A 722
REMARK 465 TYR A 723
REMARK 465 GLN A 724
REMARK 465 ILE A 725
REMARK 465 LEU A 726
REMARK 465 VAL A 727
REMARK 465 PRO A 728
REMARK 465 ARG A 729
REMARK 465 GLY A 730
REMARK 465 SER A 731
REMARK 465 ALA A 732
REMARK 465 ALA A 733
REMARK 465 ALA A 734
REMARK 465 TRP A 735
REMARK 465 SER A 736
REMARK 465 HIS A 737
REMARK 465 PRO A 738
REMARK 465 GLN A 739
REMARK 465 PHE A 740
REMARK 465 GLU A 741
REMARK 465 LYS A 742
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 LEU B 3
REMARK 465 SER B 4
REMARK 465 LEU B 5
REMARK 465 PRO B 6
REMARK 465 LYS B 7
REMARK 465 GLU B 8
REMARK 465 LYS B 9
REMARK 465 GLY B 10
REMARK 465 LEU B 11
REMARK 465 ILE B 12
REMARK 465 LEU B 13
REMARK 465 CYS B 14
REMARK 465 LEU B 15
REMARK 465 TRP B 16
REMARK 465 SER B 17
REMARK 465 LYS B 18
REMARK 465 PHE B 19
REMARK 465 CYS B 20
REMARK 465 ARG B 21
REMARK 465 TRP B 22
REMARK 465 PHE B 23
REMARK 465 GLN B 24
REMARK 465 ARG B 25
REMARK 465 ARG B 26
REMARK 465 GLU B 27
REMARK 465 LEU B 639
REMARK 465 ASN B 640
REMARK 465 ARG B 641
REMARK 465 GLN B 642
REMARK 465 ARG B 643
REMARK 465 ILE B 644
REMARK 465 GLN B 645
REMARK 465 ARG B 646
REMARK 465 TYR B 647
REMARK 465 ALA B 648
REMARK 465 GLN B 649
REMARK 465 ALA B 650
REMARK 465 PHE B 651
REMARK 465 HIS B 652
REMARK 465 THR B 653
REMARK 465 ARG B 654
REMARK 465 GLY B 655
REMARK 465 SER B 656
REMARK 465 GLU B 657
REMARK 465 ASP B 658
REMARK 465 LEU B 659
REMARK 465 ASP B 660
REMARK 465 LYS B 661
REMARK 465 ASP B 662
REMARK 465 SER B 663
REMARK 465 VAL B 664
REMARK 465 GLU B 665
REMARK 465 LYS B 666
REMARK 465 LEU B 667
REMARK 465 GLU B 668
REMARK 465 LEU B 669
REMARK 465 GLY B 670
REMARK 465 CYS B 671
REMARK 465 PRO B 672
REMARK 465 PHE B 673
REMARK 465 SER B 674
REMARK 465 PRO B 675
REMARK 465 HIS B 676
REMARK 465 LEU B 677
REMARK 465 SER B 678
REMARK 465 LEU B 679
REMARK 465 PRO B 680
REMARK 465 MET B 681
REMARK 465 PRO B 682
REMARK 465 SER B 683
REMARK 465 VAL B 684
REMARK 465 SER B 685
REMARK 465 ARG B 686
REMARK 465 SER B 687
REMARK 465 THR B 688
REMARK 465 SER B 689
REMARK 465 ARG B 690
REMARK 465 SER B 691
REMARK 465 SER B 692
REMARK 465 ALA B 693
REMARK 465 ASN B 694
REMARK 465 TRP B 695
REMARK 465 GLU B 696
REMARK 465 ARG B 697
REMARK 465 LEU B 698
REMARK 465 ARG B 699
REMARK 465 GLN B 700
REMARK 465 GLY B 701
REMARK 465 THR B 702
REMARK 465 LEU B 703
REMARK 465 ARG B 704
REMARK 465 ARG B 705
REMARK 465 ASP B 706
REMARK 465 LEU B 707
REMARK 465 ARG B 708
REMARK 465 GLY B 709
REMARK 465 ILE B 710
REMARK 465 ILE B 711
REMARK 465 ASN B 712
REMARK 465 ARG B 713
REMARK 465 GLY B 714
REMARK 465 LEU B 715
REMARK 465 GLU B 716
REMARK 465 ASP B 717
REMARK 465 GLY B 718
REMARK 465 GLU B 719
REMARK 465 SER B 720
REMARK 465 TRP B 721
REMARK 465 GLU B 722
REMARK 465 TYR B 723
REMARK 465 GLN B 724
REMARK 465 ILE B 725
REMARK 465 LEU B 726
REMARK 465 VAL B 727
REMARK 465 PRO B 728
REMARK 465 ARG B 729
REMARK 465 GLY B 730
REMARK 465 SER B 731
REMARK 465 ALA B 732
REMARK 465 ALA B 733
REMARK 465 ALA B 734
REMARK 465 TRP B 735
REMARK 465 SER B 736
REMARK 465 HIS B 737
REMARK 465 PRO B 738
REMARK 465 GLN B 739
REMARK 465 PHE B 740
REMARK 465 GLU B 741
REMARK 465 LYS B 742
REMARK 465 MET C 1
REMARK 465 GLY C 2
REMARK 465 LEU C 3
REMARK 465 SER C 4
REMARK 465 LEU C 5
REMARK 465 PRO C 6
REMARK 465 LYS C 7
REMARK 465 GLU C 8
REMARK 465 LYS C 9
REMARK 465 GLY C 10
REMARK 465 LEU C 11
REMARK 465 ILE C 12
REMARK 465 LEU C 13
REMARK 465 CYS C 14
REMARK 465 LEU C 15
REMARK 465 TRP C 16
REMARK 465 SER C 17
REMARK 465 LYS C 18
REMARK 465 PHE C 19
REMARK 465 CYS C 20
REMARK 465 ARG C 21
REMARK 465 TRP C 22
REMARK 465 PHE C 23
REMARK 465 GLN C 24
REMARK 465 ARG C 25
REMARK 465 ARG C 26
REMARK 465 GLU C 27
REMARK 465 LEU C 639
REMARK 465 ASN C 640
REMARK 465 ARG C 641
REMARK 465 GLN C 642
REMARK 465 ARG C 643
REMARK 465 ILE C 644
REMARK 465 GLN C 645
REMARK 465 ARG C 646
REMARK 465 TYR C 647
REMARK 465 ALA C 648
REMARK 465 GLN C 649
REMARK 465 ALA C 650
REMARK 465 PHE C 651
REMARK 465 HIS C 652
REMARK 465 THR C 653
REMARK 465 ARG C 654
REMARK 465 GLY C 655
REMARK 465 SER C 656
REMARK 465 GLU C 657
REMARK 465 ASP C 658
REMARK 465 LEU C 659
REMARK 465 ASP C 660
REMARK 465 LYS C 661
REMARK 465 ASP C 662
REMARK 465 SER C 663
REMARK 465 VAL C 664
REMARK 465 GLU C 665
REMARK 465 LYS C 666
REMARK 465 LEU C 667
REMARK 465 GLU C 668
REMARK 465 LEU C 669
REMARK 465 GLY C 670
REMARK 465 CYS C 671
REMARK 465 PRO C 672
REMARK 465 PHE C 673
REMARK 465 SER C 674
REMARK 465 PRO C 675
REMARK 465 HIS C 676
REMARK 465 LEU C 677
REMARK 465 SER C 678
REMARK 465 LEU C 679
REMARK 465 PRO C 680
REMARK 465 MET C 681
REMARK 465 PRO C 682
REMARK 465 SER C 683
REMARK 465 VAL C 684
REMARK 465 SER C 685
REMARK 465 ARG C 686
REMARK 465 SER C 687
REMARK 465 THR C 688
REMARK 465 SER C 689
REMARK 465 ARG C 690
REMARK 465 SER C 691
REMARK 465 SER C 692
REMARK 465 ALA C 693
REMARK 465 ASN C 694
REMARK 465 TRP C 695
REMARK 465 GLU C 696
REMARK 465 ARG C 697
REMARK 465 LEU C 698
REMARK 465 ARG C 699
REMARK 465 GLN C 700
REMARK 465 GLY C 701
REMARK 465 THR C 702
REMARK 465 LEU C 703
REMARK 465 ARG C 704
REMARK 465 ARG C 705
REMARK 465 ASP C 706
REMARK 465 LEU C 707
REMARK 465 ARG C 708
REMARK 465 GLY C 709
REMARK 465 ILE C 710
REMARK 465 ILE C 711
REMARK 465 ASN C 712
REMARK 465 ARG C 713
REMARK 465 GLY C 714
REMARK 465 LEU C 715
REMARK 465 GLU C 716
REMARK 465 ASP C 717
REMARK 465 GLY C 718
REMARK 465 GLU C 719
REMARK 465 SER C 720
REMARK 465 TRP C 721
REMARK 465 GLU C 722
REMARK 465 TYR C 723
REMARK 465 GLN C 724
REMARK 465 ILE C 725
REMARK 465 LEU C 726
REMARK 465 VAL C 727
REMARK 465 PRO C 728
REMARK 465 ARG C 729
REMARK 465 GLY C 730
REMARK 465 SER C 731
REMARK 465 ALA C 732
REMARK 465 ALA C 733
REMARK 465 ALA C 734
REMARK 465 TRP C 735
REMARK 465 SER C 736
REMARK 465 HIS C 737
REMARK 465 PRO C 738
REMARK 465 GLN C 739
REMARK 465 PHE C 740
REMARK 465 GLU C 741
REMARK 465 LYS C 742
REMARK 465 MET D 1
REMARK 465 GLY D 2
REMARK 465 LEU D 3
REMARK 465 SER D 4
REMARK 465 LEU D 5
REMARK 465 PRO D 6
REMARK 465 LYS D 7
REMARK 465 GLU D 8
REMARK 465 LYS D 9
REMARK 465 GLY D 10
REMARK 465 LEU D 11
REMARK 465 ILE D 12
REMARK 465 LEU D 13
REMARK 465 CYS D 14
REMARK 465 LEU D 15
REMARK 465 TRP D 16
REMARK 465 SER D 17
REMARK 465 LYS D 18
REMARK 465 PHE D 19
REMARK 465 CYS D 20
REMARK 465 ARG D 21
REMARK 465 TRP D 22
REMARK 465 PHE D 23
REMARK 465 GLN D 24
REMARK 465 ARG D 25
REMARK 465 ARG D 26
REMARK 465 GLU D 27
REMARK 465 LEU D 639
REMARK 465 ASN D 640
REMARK 465 ARG D 641
REMARK 465 GLN D 642
REMARK 465 ARG D 643
REMARK 465 ILE D 644
REMARK 465 GLN D 645
REMARK 465 ARG D 646
REMARK 465 TYR D 647
REMARK 465 ALA D 648
REMARK 465 GLN D 649
REMARK 465 ALA D 650
REMARK 465 PHE D 651
REMARK 465 HIS D 652
REMARK 465 THR D 653
REMARK 465 ARG D 654
REMARK 465 GLY D 655
REMARK 465 SER D 656
REMARK 465 GLU D 657
REMARK 465 ASP D 658
REMARK 465 LEU D 659
REMARK 465 ASP D 660
REMARK 465 LYS D 661
REMARK 465 ASP D 662
REMARK 465 SER D 663
REMARK 465 VAL D 664
REMARK 465 GLU D 665
REMARK 465 LYS D 666
REMARK 465 LEU D 667
REMARK 465 GLU D 668
REMARK 465 LEU D 669
REMARK 465 GLY D 670
REMARK 465 CYS D 671
REMARK 465 PRO D 672
REMARK 465 PHE D 673
REMARK 465 SER D 674
REMARK 465 PRO D 675
REMARK 465 HIS D 676
REMARK 465 LEU D 677
REMARK 465 SER D 678
REMARK 465 LEU D 679
REMARK 465 PRO D 680
REMARK 465 MET D 681
REMARK 465 PRO D 682
REMARK 465 SER D 683
REMARK 465 VAL D 684
REMARK 465 SER D 685
REMARK 465 ARG D 686
REMARK 465 SER D 687
REMARK 465 THR D 688
REMARK 465 SER D 689
REMARK 465 ARG D 690
REMARK 465 SER D 691
REMARK 465 SER D 692
REMARK 465 ALA D 693
REMARK 465 ASN D 694
REMARK 465 TRP D 695
REMARK 465 GLU D 696
REMARK 465 ARG D 697
REMARK 465 LEU D 698
REMARK 465 ARG D 699
REMARK 465 GLN D 700
REMARK 465 GLY D 701
REMARK 465 THR D 702
REMARK 465 LEU D 703
REMARK 465 ARG D 704
REMARK 465 ARG D 705
REMARK 465 ASP D 706
REMARK 465 LEU D 707
REMARK 465 ARG D 708
REMARK 465 GLY D 709
REMARK 465 ILE D 710
REMARK 465 ILE D 711
REMARK 465 ASN D 712
REMARK 465 ARG D 713
REMARK 465 GLY D 714
REMARK 465 LEU D 715
REMARK 465 GLU D 716
REMARK 465 ASP D 717
REMARK 465 GLY D 718
REMARK 465 GLU D 719
REMARK 465 SER D 720
REMARK 465 TRP D 721
REMARK 465 GLU D 722
REMARK 465 TYR D 723
REMARK 465 GLN D 724
REMARK 465 ILE D 725
REMARK 465 LEU D 726
REMARK 465 VAL D 727
REMARK 465 PRO D 728
REMARK 465 ARG D 729
REMARK 465 GLY D 730
REMARK 465 SER D 731
REMARK 465 ALA D 732
REMARK 465 ALA D 733
REMARK 465 ALA D 734
REMARK 465 TRP D 735
REMARK 465 SER D 736
REMARK 465 HIS D 737
REMARK 465 PRO D 738
REMARK 465 GLN D 739
REMARK 465 PHE D 740
REMARK 465 GLU D 741
REMARK 465 LYS D 742
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 ND1 HIS A 426 O14 FZ4 A 801 1.78
REMARK 500 ND1 HIS B 426 O14 FZ4 B 801 1.78
REMARK 500 ND1 HIS C 426 O14 FZ4 C 801 1.78
REMARK 500 ND1 HIS D 426 O14 FZ4 D 801 1.78
REMARK 500 O PRO D 544 OH TYR D 555 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ILE A 540 C ILE A 541 N 0.174
REMARK 500 ILE B 540 C ILE B 541 N 0.174
REMARK 500 ILE C 540 C ILE C 541 N -0.233
REMARK 500 ILE D 540 C ILE D 541 N 0.216
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 34 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 153 CG - CD - NE ANGL. DEV. = 15.6 DEGREES
REMARK 500 ARG A 190 CD - NE - CZ ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG A 190 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 190 NE - CZ - NH2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 LEU A 229 CA - CB - CG ANGL. DEV. = 18.0 DEGREES
REMARK 500 LEU A 352 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 LEU A 367 CA - CB - CG ANGL. DEV. = 16.6 DEGREES
REMARK 500 LEU A 372 CA - CB - CG ANGL. DEV. = 18.5 DEGREES
REMARK 500 LEU A 608 CA - CB - CG ANGL. DEV. = 16.3 DEGREES
REMARK 500 ASP B 34 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG B 153 CG - CD - NE ANGL. DEV. = 15.6 DEGREES
REMARK 500 ARG B 153 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG B 190 CD - NE - CZ ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG B 190 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B 190 NE - CZ - NH2 ANGL. DEV. = 5.2 DEGREES
REMARK 500 LEU B 229 CA - CB - CG ANGL. DEV. = 18.0 DEGREES
REMARK 500 LEU B 352 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 LEU B 367 CA - CB - CG ANGL. DEV. = 16.6 DEGREES
REMARK 500 LEU B 372 CA - CB - CG ANGL. DEV. = 18.5 DEGREES
REMARK 500 LEU B 608 CA - CB - CG ANGL. DEV. = 16.2 DEGREES
REMARK 500 ASP C 34 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG C 153 CG - CD - NE ANGL. DEV. = 15.5 DEGREES
REMARK 500 ARG C 190 CD - NE - CZ ANGL. DEV. = 8.9 DEGREES
REMARK 500 ARG C 190 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG C 190 NE - CZ - NH2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 LEU C 229 CA - CB - CG ANGL. DEV. = 18.0 DEGREES
REMARK 500 LEU C 352 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 LEU C 367 CA - CB - CG ANGL. DEV. = 16.7 DEGREES
REMARK 500 LEU C 372 CA - CB - CG ANGL. DEV. = 18.5 DEGREES
REMARK 500 LEU C 608 CA - CB - CG ANGL. DEV. = 16.3 DEGREES
REMARK 500 ASP D 34 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG D 153 CG - CD - NE ANGL. DEV. = 15.5 DEGREES
REMARK 500 ARG D 153 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG D 190 CD - NE - CZ ANGL. DEV. = 8.8 DEGREES
REMARK 500 ARG D 190 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG D 190 NE - CZ - NH2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 LEU D 229 CA - CB - CG ANGL. DEV. = 18.0 DEGREES
REMARK 500 LEU D 352 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 LEU D 367 CA - CB - CG ANGL. DEV. = 16.7 DEGREES
REMARK 500 LEU D 372 CA - CB - CG ANGL. DEV. = 18.5 DEGREES
REMARK 500 ILE D 540 CA - C - N ANGL. DEV. = -14.6 DEGREES
REMARK 500 ILE D 540 O - C - N ANGL. DEV. = 9.8 DEGREES
REMARK 500 ILE D 541 C - N - CA ANGL. DEV. = -19.1 DEGREES
REMARK 500 LEU D 608 CA - CB - CG ANGL. DEV. = 16.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 55 -167.23 -117.06
REMARK 500 HIS A 73 42.58 -109.97
REMARK 500 MET A 78 41.88 -108.53
REMARK 500 TYR A 89 42.02 -93.07
REMARK 500 GLU A 113 -19.27 68.81
REMARK 500 LEU A 114 -38.86 -132.10
REMARK 500 GLN A 128 -24.88 71.30
REMARK 500 ASN A 129 165.97 174.21
REMARK 500 GLU A 164 -11.39 -140.41
REMARK 500 PRO A 231 47.97 -88.91
REMARK 500 LEU A 232 -18.49 67.36
REMARK 500 GLN A 267 -159.64 -93.91
REMARK 500 LEU A 280 62.50 60.24
REMARK 500 SER A 286 -162.29 -125.20
REMARK 500 GLU A 289 34.64 -94.03
REMARK 500 TYR A 324 45.38 39.69
REMARK 500 ARG A 363 -8.92 68.34
REMARK 500 LEU A 367 45.60 -94.61
REMARK 500 GLN A 369 14.35 -140.67
REMARK 500 LYS A 371 -5.22 65.37
REMARK 500 LEU A 372 80.43 59.09
REMARK 500 LEU A 373 147.79 -37.19
REMARK 500 MET A 474 -3.31 61.32
REMARK 500 ALA A 545 115.92 -165.66
REMARK 500 LEU A 568 -62.29 -97.25
REMARK 500 ARG A 584 -144.17 -79.26
REMARK 500 VAL A 585 -36.12 -30.80
REMARK 500 HIS A 587 -57.75 -123.53
REMARK 500 GLU A 588 35.88 -141.79
REMARK 500 PRO A 609 -168.69 -75.09
REMARK 500 ARG A 610 -166.02 -77.80
REMARK 500 ARG A 621 -8.95 71.69
REMARK 500 ASP B 55 -167.26 -117.05
REMARK 500 HIS B 73 42.59 -109.96
REMARK 500 MET B 78 41.85 -108.59
REMARK 500 TYR B 89 42.02 -93.07
REMARK 500 GLU B 113 -19.25 68.85
REMARK 500 LEU B 114 -38.77 -132.05
REMARK 500 GLN B 128 -24.86 71.23
REMARK 500 ASN B 129 165.93 174.10
REMARK 500 GLU B 164 -11.40 -140.41
REMARK 500 PRO B 231 48.04 -88.92
REMARK 500 LEU B 232 -18.46 67.34
REMARK 500 GLN B 267 -159.61 -93.93
REMARK 500 LEU B 280 62.56 60.25
REMARK 500 SER B 286 -162.32 -125.25
REMARK 500 GLU B 289 34.66 -94.04
REMARK 500 TYR B 324 45.39 39.67
REMARK 500 ARG B 363 -8.93 68.35
REMARK 500 LEU B 367 45.68 -94.67
REMARK 500
REMARK 500 THIS ENTRY HAS 127 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASN A 129 MET A 130 142.43
REMARK 500 ASP A 223 ARG A 224 -147.92
REMARK 500 PRO A 351 LEU A 352 147.15
REMARK 500 ASN B 129 MET B 130 142.52
REMARK 500 ASP B 223 ARG B 224 -147.88
REMARK 500 PRO B 351 LEU B 352 147.20
REMARK 500 ASN C 129 MET C 130 142.46
REMARK 500 ASP C 223 ARG C 224 -147.96
REMARK 500 PRO C 351 LEU C 352 147.09
REMARK 500 ASN D 129 MET D 130 142.51
REMARK 500 ASP D 223 ARG D 224 -147.92
REMARK 500 PRO D 351 LEU D 352 147.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 PRO C 544 -11.55
REMARK 500 ILE D 540 10.46
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 A 803 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 542 OD1
REMARK 620 2 ASP B 542 OD1 86.8
REMARK 620 3 ASP C 542 OD1 151.7 80.0
REMARK 620 4 ASP D 542 OD1 73.1 151.1 108.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 803
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-7825 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF HUMAN TRPV6-Y467A IN COMPLEX WITH 2-
REMARK 900 AMINOETHOXYDIPHENYL BORATE (2-APB)
DBREF 6D7T A 1 725 UNP Q9H1D0 TRPV6_HUMAN 41 765
DBREF 6D7T B 1 725 UNP Q9H1D0 TRPV6_HUMAN 41 765
DBREF 6D7T C 1 725 UNP Q9H1D0 TRPV6_HUMAN 41 765
DBREF 6D7T D 1 725 UNP Q9H1D0 TRPV6_HUMAN 41 765
SEQADV 6D7T ALA A 467 UNP Q9H1D0 TYR 507 ENGINEERED MUTATION
SEQADV 6D7T LEU A 726 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T VAL A 727 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T PRO A 728 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ARG A 729 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T GLY A 730 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T SER A 731 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ALA A 732 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ALA A 733 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ALA A 734 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T TRP A 735 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T SER A 736 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T HIS A 737 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T PRO A 738 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T GLN A 739 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T PHE A 740 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T GLU A 741 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T LYS A 742 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ALA B 467 UNP Q9H1D0 TYR 507 ENGINEERED MUTATION
SEQADV 6D7T LEU B 726 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T VAL B 727 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T PRO B 728 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ARG B 729 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T GLY B 730 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T SER B 731 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ALA B 732 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ALA B 733 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ALA B 734 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T TRP B 735 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T SER B 736 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T HIS B 737 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T PRO B 738 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T GLN B 739 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T PHE B 740 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T GLU B 741 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T LYS B 742 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ALA C 467 UNP Q9H1D0 TYR 507 ENGINEERED MUTATION
SEQADV 6D7T LEU C 726 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T VAL C 727 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T PRO C 728 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ARG C 729 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T GLY C 730 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T SER C 731 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ALA C 732 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ALA C 733 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ALA C 734 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T TRP C 735 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T SER C 736 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T HIS C 737 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T PRO C 738 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T GLN C 739 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T PHE C 740 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T GLU C 741 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T LYS C 742 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ALA D 467 UNP Q9H1D0 TYR 507 ENGINEERED MUTATION
SEQADV 6D7T LEU D 726 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T VAL D 727 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T PRO D 728 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ARG D 729 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T GLY D 730 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T SER D 731 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ALA D 732 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ALA D 733 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T ALA D 734 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T TRP D 735 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T SER D 736 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T HIS D 737 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T PRO D 738 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T GLN D 739 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T PHE D 740 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T GLU D 741 UNP Q9H1D0 EXPRESSION TAG
SEQADV 6D7T LYS D 742 UNP Q9H1D0 EXPRESSION TAG
SEQRES 1 A 742 MET GLY LEU SER LEU PRO LYS GLU LYS GLY LEU ILE LEU
SEQRES 2 A 742 CYS LEU TRP SER LYS PHE CYS ARG TRP PHE GLN ARG ARG
SEQRES 3 A 742 GLU SER TRP ALA GLN SER ARG ASP GLU GLN ASN LEU LEU
SEQRES 4 A 742 GLN GLN LYS ARG ILE TRP GLU SER PRO LEU LEU LEU ALA
SEQRES 5 A 742 ALA LYS ASP ASN ASP VAL GLN ALA LEU ASN LYS LEU LEU
SEQRES 6 A 742 LYS TYR GLU ASP CYS LYS VAL HIS GLN ARG GLY ALA MET
SEQRES 7 A 742 GLY GLU THR ALA LEU HIS ILE ALA ALA LEU TYR ASP ASN
SEQRES 8 A 742 LEU GLU ALA ALA MET VAL LEU MET GLU ALA ALA PRO GLU
SEQRES 9 A 742 LEU VAL PHE GLU PRO MET THR SER GLU LEU TYR GLU GLY
SEQRES 10 A 742 GLN THR ALA LEU HIS ILE ALA VAL VAL ASN GLN ASN MET
SEQRES 11 A 742 ASN LEU VAL ARG ALA LEU LEU ALA ARG ARG ALA SER VAL
SEQRES 12 A 742 SER ALA ARG ALA THR GLY THR ALA PHE ARG ARG SER PRO
SEQRES 13 A 742 CYS ASN LEU ILE TYR PHE GLY GLU HIS PRO LEU SER PHE
SEQRES 14 A 742 ALA ALA CYS VAL ASN SER GLU GLU ILE VAL ARG LEU LEU
SEQRES 15 A 742 ILE GLU HIS GLY ALA ASP ILE ARG ALA GLN ASP SER LEU
SEQRES 16 A 742 GLY ASN THR VAL LEU HIS ILE LEU ILE LEU GLN PRO ASN
SEQRES 17 A 742 LYS THR PHE ALA CYS GLN MET TYR ASN LEU LEU LEU SER
SEQRES 18 A 742 TYR ASP ARG HIS GLY ASP HIS LEU GLN PRO LEU ASP LEU
SEQRES 19 A 742 VAL PRO ASN HIS GLN GLY LEU THR PRO PHE LYS LEU ALA
SEQRES 20 A 742 GLY VAL GLU GLY ASN THR VAL MET PHE GLN HIS LEU MET
SEQRES 21 A 742 GLN LYS ARG LYS HIS THR GLN TRP THR TYR GLY PRO LEU
SEQRES 22 A 742 THR SER THR LEU TYR ASP LEU THR GLU ILE ASP SER SER
SEQRES 23 A 742 GLY ASP GLU GLN SER LEU LEU GLU LEU ILE ILE THR THR
SEQRES 24 A 742 LYS LYS ARG GLU ALA ARG GLN ILE LEU ASP GLN THR PRO
SEQRES 25 A 742 VAL LYS GLU LEU VAL SER LEU LYS TRP LYS ARG TYR GLY
SEQRES 26 A 742 ARG PRO TYR PHE CYS MET LEU GLY ALA ILE TYR LEU LEU
SEQRES 27 A 742 TYR ILE ILE CYS PHE THR MET CYS CYS ILE TYR ARG PRO
SEQRES 28 A 742 LEU LYS PRO ARG THR ASN ASN ARG THR SER PRO ARG ASP
SEQRES 29 A 742 ASN THR LEU LEU GLN GLN LYS LEU LEU GLN GLU ALA TYR
SEQRES 30 A 742 MET THR PRO LYS ASP ASP ILE ARG LEU VAL GLY GLU LEU
SEQRES 31 A 742 VAL THR VAL ILE GLY ALA ILE ILE ILE LEU LEU VAL GLU
SEQRES 32 A 742 VAL PRO ASP ILE PHE ARG MET GLY VAL THR ARG PHE PHE
SEQRES 33 A 742 GLY GLN THR ILE LEU GLY GLY PRO PHE HIS VAL LEU ILE
SEQRES 34 A 742 ILE THR TYR ALA PHE MET VAL LEU VAL THR MET VAL MET
SEQRES 35 A 742 ARG LEU ILE SER ALA SER GLY GLU VAL VAL PRO MET SER
SEQRES 36 A 742 PHE ALA LEU VAL LEU GLY TRP CYS ASN VAL MET ALA PHE
SEQRES 37 A 742 ALA ARG GLY PHE GLN MET LEU GLY PRO PHE THR ILE MET
SEQRES 38 A 742 ILE GLN LYS MET ILE PHE GLY ASP LEU MET ARG PHE CYS
SEQRES 39 A 742 TRP LEU MET ALA VAL VAL ILE LEU GLY PHE ALA SER ALA
SEQRES 40 A 742 PHE TYR ILE ILE PHE GLN THR GLU ASP PRO GLU GLU LEU
SEQRES 41 A 742 GLY HIS PHE TYR ASP TYR PRO MET ALA LEU PHE SER THR
SEQRES 42 A 742 PHE GLU LEU PHE LEU THR ILE ILE ASP GLY PRO ALA ASN
SEQRES 43 A 742 TYR ASN VAL ASP LEU PRO PHE MET TYR SER ILE THR TYR
SEQRES 44 A 742 ALA ALA PHE ALA ILE ILE ALA THR LEU LEU MET LEU ASN
SEQRES 45 A 742 LEU LEU ILE ALA MET MET GLY ASP THR HIS TRP ARG VAL
SEQRES 46 A 742 ALA HIS GLU ARG ASP GLU LEU TRP ARG ALA GLN ILE VAL
SEQRES 47 A 742 ALA THR THR VAL MET LEU GLU ARG LYS LEU PRO ARG CYS
SEQRES 48 A 742 LEU TRP PRO ARG SER GLY ILE CYS GLY ARG GLU TYR GLY
SEQRES 49 A 742 LEU GLY ASP ARG TRP PHE LEU ARG VAL GLU ASP ARG GLN
SEQRES 50 A 742 ASP LEU ASN ARG GLN ARG ILE GLN ARG TYR ALA GLN ALA
SEQRES 51 A 742 PHE HIS THR ARG GLY SER GLU ASP LEU ASP LYS ASP SER
SEQRES 52 A 742 VAL GLU LYS LEU GLU LEU GLY CYS PRO PHE SER PRO HIS
SEQRES 53 A 742 LEU SER LEU PRO MET PRO SER VAL SER ARG SER THR SER
SEQRES 54 A 742 ARG SER SER ALA ASN TRP GLU ARG LEU ARG GLN GLY THR
SEQRES 55 A 742 LEU ARG ARG ASP LEU ARG GLY ILE ILE ASN ARG GLY LEU
SEQRES 56 A 742 GLU ASP GLY GLU SER TRP GLU TYR GLN ILE LEU VAL PRO
SEQRES 57 A 742 ARG GLY SER ALA ALA ALA TRP SER HIS PRO GLN PHE GLU
SEQRES 58 A 742 LYS
SEQRES 1 B 742 MET GLY LEU SER LEU PRO LYS GLU LYS GLY LEU ILE LEU
SEQRES 2 B 742 CYS LEU TRP SER LYS PHE CYS ARG TRP PHE GLN ARG ARG
SEQRES 3 B 742 GLU SER TRP ALA GLN SER ARG ASP GLU GLN ASN LEU LEU
SEQRES 4 B 742 GLN GLN LYS ARG ILE TRP GLU SER PRO LEU LEU LEU ALA
SEQRES 5 B 742 ALA LYS ASP ASN ASP VAL GLN ALA LEU ASN LYS LEU LEU
SEQRES 6 B 742 LYS TYR GLU ASP CYS LYS VAL HIS GLN ARG GLY ALA MET
SEQRES 7 B 742 GLY GLU THR ALA LEU HIS ILE ALA ALA LEU TYR ASP ASN
SEQRES 8 B 742 LEU GLU ALA ALA MET VAL LEU MET GLU ALA ALA PRO GLU
SEQRES 9 B 742 LEU VAL PHE GLU PRO MET THR SER GLU LEU TYR GLU GLY
SEQRES 10 B 742 GLN THR ALA LEU HIS ILE ALA VAL VAL ASN GLN ASN MET
SEQRES 11 B 742 ASN LEU VAL ARG ALA LEU LEU ALA ARG ARG ALA SER VAL
SEQRES 12 B 742 SER ALA ARG ALA THR GLY THR ALA PHE ARG ARG SER PRO
SEQRES 13 B 742 CYS ASN LEU ILE TYR PHE GLY GLU HIS PRO LEU SER PHE
SEQRES 14 B 742 ALA ALA CYS VAL ASN SER GLU GLU ILE VAL ARG LEU LEU
SEQRES 15 B 742 ILE GLU HIS GLY ALA ASP ILE ARG ALA GLN ASP SER LEU
SEQRES 16 B 742 GLY ASN THR VAL LEU HIS ILE LEU ILE LEU GLN PRO ASN
SEQRES 17 B 742 LYS THR PHE ALA CYS GLN MET TYR ASN LEU LEU LEU SER
SEQRES 18 B 742 TYR ASP ARG HIS GLY ASP HIS LEU GLN PRO LEU ASP LEU
SEQRES 19 B 742 VAL PRO ASN HIS GLN GLY LEU THR PRO PHE LYS LEU ALA
SEQRES 20 B 742 GLY VAL GLU GLY ASN THR VAL MET PHE GLN HIS LEU MET
SEQRES 21 B 742 GLN LYS ARG LYS HIS THR GLN TRP THR TYR GLY PRO LEU
SEQRES 22 B 742 THR SER THR LEU TYR ASP LEU THR GLU ILE ASP SER SER
SEQRES 23 B 742 GLY ASP GLU GLN SER LEU LEU GLU LEU ILE ILE THR THR
SEQRES 24 B 742 LYS LYS ARG GLU ALA ARG GLN ILE LEU ASP GLN THR PRO
SEQRES 25 B 742 VAL LYS GLU LEU VAL SER LEU LYS TRP LYS ARG TYR GLY
SEQRES 26 B 742 ARG PRO TYR PHE CYS MET LEU GLY ALA ILE TYR LEU LEU
SEQRES 27 B 742 TYR ILE ILE CYS PHE THR MET CYS CYS ILE TYR ARG PRO
SEQRES 28 B 742 LEU LYS PRO ARG THR ASN ASN ARG THR SER PRO ARG ASP
SEQRES 29 B 742 ASN THR LEU LEU GLN GLN LYS LEU LEU GLN GLU ALA TYR
SEQRES 30 B 742 MET THR PRO LYS ASP ASP ILE ARG LEU VAL GLY GLU LEU
SEQRES 31 B 742 VAL THR VAL ILE GLY ALA ILE ILE ILE LEU LEU VAL GLU
SEQRES 32 B 742 VAL PRO ASP ILE PHE ARG MET GLY VAL THR ARG PHE PHE
SEQRES 33 B 742 GLY GLN THR ILE LEU GLY GLY PRO PHE HIS VAL LEU ILE
SEQRES 34 B 742 ILE THR TYR ALA PHE MET VAL LEU VAL THR MET VAL MET
SEQRES 35 B 742 ARG LEU ILE SER ALA SER GLY GLU VAL VAL PRO MET SER
SEQRES 36 B 742 PHE ALA LEU VAL LEU GLY TRP CYS ASN VAL MET ALA PHE
SEQRES 37 B 742 ALA ARG GLY PHE GLN MET LEU GLY PRO PHE THR ILE MET
SEQRES 38 B 742 ILE GLN LYS MET ILE PHE GLY ASP LEU MET ARG PHE CYS
SEQRES 39 B 742 TRP LEU MET ALA VAL VAL ILE LEU GLY PHE ALA SER ALA
SEQRES 40 B 742 PHE TYR ILE ILE PHE GLN THR GLU ASP PRO GLU GLU LEU
SEQRES 41 B 742 GLY HIS PHE TYR ASP TYR PRO MET ALA LEU PHE SER THR
SEQRES 42 B 742 PHE GLU LEU PHE LEU THR ILE ILE ASP GLY PRO ALA ASN
SEQRES 43 B 742 TYR ASN VAL ASP LEU PRO PHE MET TYR SER ILE THR TYR
SEQRES 44 B 742 ALA ALA PHE ALA ILE ILE ALA THR LEU LEU MET LEU ASN
SEQRES 45 B 742 LEU LEU ILE ALA MET MET GLY ASP THR HIS TRP ARG VAL
SEQRES 46 B 742 ALA HIS GLU ARG ASP GLU LEU TRP ARG ALA GLN ILE VAL
SEQRES 47 B 742 ALA THR THR VAL MET LEU GLU ARG LYS LEU PRO ARG CYS
SEQRES 48 B 742 LEU TRP PRO ARG SER GLY ILE CYS GLY ARG GLU TYR GLY
SEQRES 49 B 742 LEU GLY ASP ARG TRP PHE LEU ARG VAL GLU ASP ARG GLN
SEQRES 50 B 742 ASP LEU ASN ARG GLN ARG ILE GLN ARG TYR ALA GLN ALA
SEQRES 51 B 742 PHE HIS THR ARG GLY SER GLU ASP LEU ASP LYS ASP SER
SEQRES 52 B 742 VAL GLU LYS LEU GLU LEU GLY CYS PRO PHE SER PRO HIS
SEQRES 53 B 742 LEU SER LEU PRO MET PRO SER VAL SER ARG SER THR SER
SEQRES 54 B 742 ARG SER SER ALA ASN TRP GLU ARG LEU ARG GLN GLY THR
SEQRES 55 B 742 LEU ARG ARG ASP LEU ARG GLY ILE ILE ASN ARG GLY LEU
SEQRES 56 B 742 GLU ASP GLY GLU SER TRP GLU TYR GLN ILE LEU VAL PRO
SEQRES 57 B 742 ARG GLY SER ALA ALA ALA TRP SER HIS PRO GLN PHE GLU
SEQRES 58 B 742 LYS
SEQRES 1 C 742 MET GLY LEU SER LEU PRO LYS GLU LYS GLY LEU ILE LEU
SEQRES 2 C 742 CYS LEU TRP SER LYS PHE CYS ARG TRP PHE GLN ARG ARG
SEQRES 3 C 742 GLU SER TRP ALA GLN SER ARG ASP GLU GLN ASN LEU LEU
SEQRES 4 C 742 GLN GLN LYS ARG ILE TRP GLU SER PRO LEU LEU LEU ALA
SEQRES 5 C 742 ALA LYS ASP ASN ASP VAL GLN ALA LEU ASN LYS LEU LEU
SEQRES 6 C 742 LYS TYR GLU ASP CYS LYS VAL HIS GLN ARG GLY ALA MET
SEQRES 7 C 742 GLY GLU THR ALA LEU HIS ILE ALA ALA LEU TYR ASP ASN
SEQRES 8 C 742 LEU GLU ALA ALA MET VAL LEU MET GLU ALA ALA PRO GLU
SEQRES 9 C 742 LEU VAL PHE GLU PRO MET THR SER GLU LEU TYR GLU GLY
SEQRES 10 C 742 GLN THR ALA LEU HIS ILE ALA VAL VAL ASN GLN ASN MET
SEQRES 11 C 742 ASN LEU VAL ARG ALA LEU LEU ALA ARG ARG ALA SER VAL
SEQRES 12 C 742 SER ALA ARG ALA THR GLY THR ALA PHE ARG ARG SER PRO
SEQRES 13 C 742 CYS ASN LEU ILE TYR PHE GLY GLU HIS PRO LEU SER PHE
SEQRES 14 C 742 ALA ALA CYS VAL ASN SER GLU GLU ILE VAL ARG LEU LEU
SEQRES 15 C 742 ILE GLU HIS GLY ALA ASP ILE ARG ALA GLN ASP SER LEU
SEQRES 16 C 742 GLY ASN THR VAL LEU HIS ILE LEU ILE LEU GLN PRO ASN
SEQRES 17 C 742 LYS THR PHE ALA CYS GLN MET TYR ASN LEU LEU LEU SER
SEQRES 18 C 742 TYR ASP ARG HIS GLY ASP HIS LEU GLN PRO LEU ASP LEU
SEQRES 19 C 742 VAL PRO ASN HIS GLN GLY LEU THR PRO PHE LYS LEU ALA
SEQRES 20 C 742 GLY VAL GLU GLY ASN THR VAL MET PHE GLN HIS LEU MET
SEQRES 21 C 742 GLN LYS ARG LYS HIS THR GLN TRP THR TYR GLY PRO LEU
SEQRES 22 C 742 THR SER THR LEU TYR ASP LEU THR GLU ILE ASP SER SER
SEQRES 23 C 742 GLY ASP GLU GLN SER LEU LEU GLU LEU ILE ILE THR THR
SEQRES 24 C 742 LYS LYS ARG GLU ALA ARG GLN ILE LEU ASP GLN THR PRO
SEQRES 25 C 742 VAL LYS GLU LEU VAL SER LEU LYS TRP LYS ARG TYR GLY
SEQRES 26 C 742 ARG PRO TYR PHE CYS MET LEU GLY ALA ILE TYR LEU LEU
SEQRES 27 C 742 TYR ILE ILE CYS PHE THR MET CYS CYS ILE TYR ARG PRO
SEQRES 28 C 742 LEU LYS PRO ARG THR ASN ASN ARG THR SER PRO ARG ASP
SEQRES 29 C 742 ASN THR LEU LEU GLN GLN LYS LEU LEU GLN GLU ALA TYR
SEQRES 30 C 742 MET THR PRO LYS ASP ASP ILE ARG LEU VAL GLY GLU LEU
SEQRES 31 C 742 VAL THR VAL ILE GLY ALA ILE ILE ILE LEU LEU VAL GLU
SEQRES 32 C 742 VAL PRO ASP ILE PHE ARG MET GLY VAL THR ARG PHE PHE
SEQRES 33 C 742 GLY GLN THR ILE LEU GLY GLY PRO PHE HIS VAL LEU ILE
SEQRES 34 C 742 ILE THR TYR ALA PHE MET VAL LEU VAL THR MET VAL MET
SEQRES 35 C 742 ARG LEU ILE SER ALA SER GLY GLU VAL VAL PRO MET SER
SEQRES 36 C 742 PHE ALA LEU VAL LEU GLY TRP CYS ASN VAL MET ALA PHE
SEQRES 37 C 742 ALA ARG GLY PHE GLN MET LEU GLY PRO PHE THR ILE MET
SEQRES 38 C 742 ILE GLN LYS MET ILE PHE GLY ASP LEU MET ARG PHE CYS
SEQRES 39 C 742 TRP LEU MET ALA VAL VAL ILE LEU GLY PHE ALA SER ALA
SEQRES 40 C 742 PHE TYR ILE ILE PHE GLN THR GLU ASP PRO GLU GLU LEU
SEQRES 41 C 742 GLY HIS PHE TYR ASP TYR PRO MET ALA LEU PHE SER THR
SEQRES 42 C 742 PHE GLU LEU PHE LEU THR ILE ILE ASP GLY PRO ALA ASN
SEQRES 43 C 742 TYR ASN VAL ASP LEU PRO PHE MET TYR SER ILE THR TYR
SEQRES 44 C 742 ALA ALA PHE ALA ILE ILE ALA THR LEU LEU MET LEU ASN
SEQRES 45 C 742 LEU LEU ILE ALA MET MET GLY ASP THR HIS TRP ARG VAL
SEQRES 46 C 742 ALA HIS GLU ARG ASP GLU LEU TRP ARG ALA GLN ILE VAL
SEQRES 47 C 742 ALA THR THR VAL MET LEU GLU ARG LYS LEU PRO ARG CYS
SEQRES 48 C 742 LEU TRP PRO ARG SER GLY ILE CYS GLY ARG GLU TYR GLY
SEQRES 49 C 742 LEU GLY ASP ARG TRP PHE LEU ARG VAL GLU ASP ARG GLN
SEQRES 50 C 742 ASP LEU ASN ARG GLN ARG ILE GLN ARG TYR ALA GLN ALA
SEQRES 51 C 742 PHE HIS THR ARG GLY SER GLU ASP LEU ASP LYS ASP SER
SEQRES 52 C 742 VAL GLU LYS LEU GLU LEU GLY CYS PRO PHE SER PRO HIS
SEQRES 53 C 742 LEU SER LEU PRO MET PRO SER VAL SER ARG SER THR SER
SEQRES 54 C 742 ARG SER SER ALA ASN TRP GLU ARG LEU ARG GLN GLY THR
SEQRES 55 C 742 LEU ARG ARG ASP LEU ARG GLY ILE ILE ASN ARG GLY LEU
SEQRES 56 C 742 GLU ASP GLY GLU SER TRP GLU TYR GLN ILE LEU VAL PRO
SEQRES 57 C 742 ARG GLY SER ALA ALA ALA TRP SER HIS PRO GLN PHE GLU
SEQRES 58 C 742 LYS
SEQRES 1 D 742 MET GLY LEU SER LEU PRO LYS GLU LYS GLY LEU ILE LEU
SEQRES 2 D 742 CYS LEU TRP SER LYS PHE CYS ARG TRP PHE GLN ARG ARG
SEQRES 3 D 742 GLU SER TRP ALA GLN SER ARG ASP GLU GLN ASN LEU LEU
SEQRES 4 D 742 GLN GLN LYS ARG ILE TRP GLU SER PRO LEU LEU LEU ALA
SEQRES 5 D 742 ALA LYS ASP ASN ASP VAL GLN ALA LEU ASN LYS LEU LEU
SEQRES 6 D 742 LYS TYR GLU ASP CYS LYS VAL HIS GLN ARG GLY ALA MET
SEQRES 7 D 742 GLY GLU THR ALA LEU HIS ILE ALA ALA LEU TYR ASP ASN
SEQRES 8 D 742 LEU GLU ALA ALA MET VAL LEU MET GLU ALA ALA PRO GLU
SEQRES 9 D 742 LEU VAL PHE GLU PRO MET THR SER GLU LEU TYR GLU GLY
SEQRES 10 D 742 GLN THR ALA LEU HIS ILE ALA VAL VAL ASN GLN ASN MET
SEQRES 11 D 742 ASN LEU VAL ARG ALA LEU LEU ALA ARG ARG ALA SER VAL
SEQRES 12 D 742 SER ALA ARG ALA THR GLY THR ALA PHE ARG ARG SER PRO
SEQRES 13 D 742 CYS ASN LEU ILE TYR PHE GLY GLU HIS PRO LEU SER PHE
SEQRES 14 D 742 ALA ALA CYS VAL ASN SER GLU GLU ILE VAL ARG LEU LEU
SEQRES 15 D 742 ILE GLU HIS GLY ALA ASP ILE ARG ALA GLN ASP SER LEU
SEQRES 16 D 742 GLY ASN THR VAL LEU HIS ILE LEU ILE LEU GLN PRO ASN
SEQRES 17 D 742 LYS THR PHE ALA CYS GLN MET TYR ASN LEU LEU LEU SER
SEQRES 18 D 742 TYR ASP ARG HIS GLY ASP HIS LEU GLN PRO LEU ASP LEU
SEQRES 19 D 742 VAL PRO ASN HIS GLN GLY LEU THR PRO PHE LYS LEU ALA
SEQRES 20 D 742 GLY VAL GLU GLY ASN THR VAL MET PHE GLN HIS LEU MET
SEQRES 21 D 742 GLN LYS ARG LYS HIS THR GLN TRP THR TYR GLY PRO LEU
SEQRES 22 D 742 THR SER THR LEU TYR ASP LEU THR GLU ILE ASP SER SER
SEQRES 23 D 742 GLY ASP GLU GLN SER LEU LEU GLU LEU ILE ILE THR THR
SEQRES 24 D 742 LYS LYS ARG GLU ALA ARG GLN ILE LEU ASP GLN THR PRO
SEQRES 25 D 742 VAL LYS GLU LEU VAL SER LEU LYS TRP LYS ARG TYR GLY
SEQRES 26 D 742 ARG PRO TYR PHE CYS MET LEU GLY ALA ILE TYR LEU LEU
SEQRES 27 D 742 TYR ILE ILE CYS PHE THR MET CYS CYS ILE TYR ARG PRO
SEQRES 28 D 742 LEU LYS PRO ARG THR ASN ASN ARG THR SER PRO ARG ASP
SEQRES 29 D 742 ASN THR LEU LEU GLN GLN LYS LEU LEU GLN GLU ALA TYR
SEQRES 30 D 742 MET THR PRO LYS ASP ASP ILE ARG LEU VAL GLY GLU LEU
SEQRES 31 D 742 VAL THR VAL ILE GLY ALA ILE ILE ILE LEU LEU VAL GLU
SEQRES 32 D 742 VAL PRO ASP ILE PHE ARG MET GLY VAL THR ARG PHE PHE
SEQRES 33 D 742 GLY GLN THR ILE LEU GLY GLY PRO PHE HIS VAL LEU ILE
SEQRES 34 D 742 ILE THR TYR ALA PHE MET VAL LEU VAL THR MET VAL MET
SEQRES 35 D 742 ARG LEU ILE SER ALA SER GLY GLU VAL VAL PRO MET SER
SEQRES 36 D 742 PHE ALA LEU VAL LEU GLY TRP CYS ASN VAL MET ALA PHE
SEQRES 37 D 742 ALA ARG GLY PHE GLN MET LEU GLY PRO PHE THR ILE MET
SEQRES 38 D 742 ILE GLN LYS MET ILE PHE GLY ASP LEU MET ARG PHE CYS
SEQRES 39 D 742 TRP LEU MET ALA VAL VAL ILE LEU GLY PHE ALA SER ALA
SEQRES 40 D 742 PHE TYR ILE ILE PHE GLN THR GLU ASP PRO GLU GLU LEU
SEQRES 41 D 742 GLY HIS PHE TYR ASP TYR PRO MET ALA LEU PHE SER THR
SEQRES 42 D 742 PHE GLU LEU PHE LEU THR ILE ILE ASP GLY PRO ALA ASN
SEQRES 43 D 742 TYR ASN VAL ASP LEU PRO PHE MET TYR SER ILE THR TYR
SEQRES 44 D 742 ALA ALA PHE ALA ILE ILE ALA THR LEU LEU MET LEU ASN
SEQRES 45 D 742 LEU LEU ILE ALA MET MET GLY ASP THR HIS TRP ARG VAL
SEQRES 46 D 742 ALA HIS GLU ARG ASP GLU LEU TRP ARG ALA GLN ILE VAL
SEQRES 47 D 742 ALA THR THR VAL MET LEU GLU ARG LYS LEU PRO ARG CYS
SEQRES 48 D 742 LEU TRP PRO ARG SER GLY ILE CYS GLY ARG GLU TYR GLY
SEQRES 49 D 742 LEU GLY ASP ARG TRP PHE LEU ARG VAL GLU ASP ARG GLN
SEQRES 50 D 742 ASP LEU ASN ARG GLN ARG ILE GLN ARG TYR ALA GLN ALA
SEQRES 51 D 742 PHE HIS THR ARG GLY SER GLU ASP LEU ASP LYS ASP SER
SEQRES 52 D 742 VAL GLU LYS LEU GLU LEU GLY CYS PRO PHE SER PRO HIS
SEQRES 53 D 742 LEU SER LEU PRO MET PRO SER VAL SER ARG SER THR SER
SEQRES 54 D 742 ARG SER SER ALA ASN TRP GLU ARG LEU ARG GLN GLY THR
SEQRES 55 D 742 LEU ARG ARG ASP LEU ARG GLY ILE ILE ASN ARG GLY LEU
SEQRES 56 D 742 GLU ASP GLY GLU SER TRP GLU TYR GLN ILE LEU VAL PRO
SEQRES 57 D 742 ARG GLY SER ALA ALA ALA TRP SER HIS PRO GLN PHE GLU
SEQRES 58 D 742 LYS
HET FZ4 A 801 17
HET CA A 802 1
HET CA A 803 1
HET FZ4 B 801 17
HET FZ4 C 801 17
HET FZ4 D 801 17
HETNAM FZ4 2-AMINOETHYL DIPHENYLBORINATE
HETNAM CA CALCIUM ION
FORMUL 5 FZ4 4(C14 H16 B N O)
FORMUL 6 CA 2(CA 2+)
HELIX 1 AA1 ALA A 30 SER A 47 1 18
HELIX 2 AA2 SER A 47 ASP A 55 1 9
HELIX 3 AA3 ASP A 57 LYS A 66 1 10
HELIX 4 AA4 THR A 81 TYR A 89 1 9
HELIX 5 AA5 ALA A 102 PHE A 107 5 6
HELIX 6 AA6 THR A 119 VAL A 125 1 7
HELIX 7 AA7 ASN A 131 ALA A 138 1 8
HELIX 8 AA8 GLY A 149 ARG A 153 5 5
HELIX 9 AA9 HIS A 165 ASN A 174 1 10
HELIX 10 AB1 SER A 175 GLU A 184 1 10
HELIX 11 AB2 THR A 198 LEU A 205 1 8
HELIX 12 AB3 ASN A 208 GLN A 214 1 7
HELIX 13 AB4 GLN A 214 SER A 221 1 8
HELIX 14 AB5 THR A 242 GLY A 251 1 10
HELIX 15 AB6 ASN A 252 LYS A 262 1 11
HELIX 16 AB7 SER A 291 THR A 299 1 9
HELIX 17 AB8 GLU A 303 GLN A 310 5 8
HELIX 18 AB9 PRO A 312 ARG A 323 1 12
HELIX 19 AC1 GLY A 325 TYR A 349 1 25
HELIX 20 AC2 ASP A 383 VAL A 402 1 20
HELIX 21 AC3 VAL A 402 GLY A 411 1 10
HELIX 22 AC4 PHE A 415 ILE A 420 1 6
HELIX 23 AC5 PRO A 424 SER A 446 1 23
HELIX 24 AC6 GLU A 450 ASN A 464 1 15
HELIX 25 AC7 VAL A 465 GLY A 471 5 7
HELIX 26 AC8 LEU A 475 PHE A 487 1 13
HELIX 27 AC9 ASP A 489 PHE A 512 1 24
HELIX 28 AD1 ASP A 525 LEU A 538 1 14
HELIX 29 AD2 MET A 554 THR A 567 1 14
HELIX 30 AD3 LEU A 568 HIS A 582 1 15
HELIX 31 AD4 ARG A 589 LEU A 608 1 20
HELIX 32 AD5 ALA B 30 SER B 47 1 18
HELIX 33 AD6 SER B 47 ASP B 55 1 9
HELIX 34 AD7 ASP B 57 LYS B 66 1 10
HELIX 35 AD8 THR B 81 TYR B 89 1 9
HELIX 36 AD9 ALA B 102 PHE B 107 5 6
HELIX 37 AE1 THR B 119 VAL B 125 1 7
HELIX 38 AE2 ASN B 131 ALA B 138 1 8
HELIX 39 AE3 GLY B 149 ARG B 153 5 5
HELIX 40 AE4 HIS B 165 ASN B 174 1 10
HELIX 41 AE5 SER B 175 GLU B 184 1 10
HELIX 42 AE6 THR B 198 LEU B 205 1 8
HELIX 43 AE7 ASN B 208 GLN B 214 1 7
HELIX 44 AE8 GLN B 214 SER B 221 1 8
HELIX 45 AE9 THR B 242 GLY B 251 1 10
HELIX 46 AF1 ASN B 252 LYS B 262 1 11
HELIX 47 AF2 SER B 291 THR B 299 1 9
HELIX 48 AF3 GLU B 303 GLN B 310 5 8
HELIX 49 AF4 PRO B 312 ARG B 323 1 12
HELIX 50 AF5 GLY B 325 TYR B 349 1 25
HELIX 51 AF6 ASP B 383 VAL B 402 1 20
HELIX 52 AF7 VAL B 402 GLY B 411 1 10
HELIX 53 AF8 PHE B 415 ILE B 420 1 6
HELIX 54 AF9 PRO B 424 SER B 446 1 23
HELIX 55 AG1 GLU B 450 ASN B 464 1 15
HELIX 56 AG2 VAL B 465 GLY B 471 5 7
HELIX 57 AG3 LEU B 475 PHE B 487 1 13
HELIX 58 AG4 ASP B 489 PHE B 512 1 24
HELIX 59 AG5 ASP B 525 LEU B 538 1 14
HELIX 60 AG6 MET B 554 THR B 567 1 14
HELIX 61 AG7 LEU B 568 HIS B 582 1 15
HELIX 62 AG8 ARG B 589 LEU B 608 1 20
HELIX 63 AG9 ALA C 30 SER C 47 1 18
HELIX 64 AH1 SER C 47 ASP C 55 1 9
HELIX 65 AH2 ASP C 57 LYS C 66 1 10
HELIX 66 AH3 THR C 81 TYR C 89 1 9
HELIX 67 AH4 ALA C 102 PHE C 107 5 6
HELIX 68 AH5 THR C 119 VAL C 125 1 7
HELIX 69 AH6 ASN C 131 ALA C 138 1 8
HELIX 70 AH7 GLY C 149 ARG C 153 5 5
HELIX 71 AH8 HIS C 165 ASN C 174 1 10
HELIX 72 AH9 SER C 175 GLU C 184 1 10
HELIX 73 AI1 THR C 198 LEU C 205 1 8
HELIX 74 AI2 ASN C 208 GLN C 214 1 7
HELIX 75 AI3 GLN C 214 SER C 221 1 8
HELIX 76 AI4 THR C 242 GLY C 251 1 10
HELIX 77 AI5 ASN C 252 LYS C 262 1 11
HELIX 78 AI6 SER C 291 THR C 299 1 9
HELIX 79 AI7 GLU C 303 GLN C 310 5 8
HELIX 80 AI8 PRO C 312 ARG C 323 1 12
HELIX 81 AI9 GLY C 325 TYR C 349 1 25
HELIX 82 AJ1 ASP C 383 VAL C 402 1 20
HELIX 83 AJ2 VAL C 402 GLY C 411 1 10
HELIX 84 AJ3 PHE C 415 ILE C 420 1 6
HELIX 85 AJ4 PRO C 424 SER C 446 1 23
HELIX 86 AJ5 GLU C 450 ASN C 464 1 15
HELIX 87 AJ6 VAL C 465 GLY C 471 5 7
HELIX 88 AJ7 LEU C 475 PHE C 487 1 13
HELIX 89 AJ8 ASP C 489 PHE C 512 1 24
HELIX 90 AJ9 ASP C 525 LEU C 538 1 14
HELIX 91 AK1 MET C 554 THR C 567 1 14
HELIX 92 AK2 LEU C 568 HIS C 582 1 15
HELIX 93 AK3 ARG C 589 LEU C 608 1 20
HELIX 94 AK4 ALA D 30 SER D 47 1 18
HELIX 95 AK5 SER D 47 ASP D 55 1 9
HELIX 96 AK6 ASP D 57 LYS D 66 1 10
HELIX 97 AK7 THR D 81 TYR D 89 1 9
HELIX 98 AK8 ALA D 102 PHE D 107 5 6
HELIX 99 AK9 THR D 119 VAL D 125 1 7
HELIX 100 AL1 ASN D 131 ALA D 138 1 8
HELIX 101 AL2 GLY D 149 ARG D 153 5 5
HELIX 102 AL3 HIS D 165 ASN D 174 1 10
HELIX 103 AL4 SER D 175 GLU D 184 1 10
HELIX 104 AL5 THR D 198 LEU D 205 1 8
HELIX 105 AL6 ASN D 208 GLN D 214 1 7
HELIX 106 AL7 GLN D 214 SER D 221 1 8
HELIX 107 AL8 THR D 242 GLY D 251 1 10
HELIX 108 AL9 ASN D 252 LYS D 262 1 11
HELIX 109 AM1 SER D 291 THR D 299 1 9
HELIX 110 AM2 GLU D 303 GLN D 310 5 8
HELIX 111 AM3 PRO D 312 ARG D 323 1 12
HELIX 112 AM4 GLY D 325 TYR D 349 1 25
HELIX 113 AM5 ASP D 383 VAL D 402 1 20
HELIX 114 AM6 VAL D 402 GLY D 411 1 10
HELIX 115 AM7 PHE D 415 ILE D 420 1 6
HELIX 116 AM8 PRO D 424 SER D 446 1 23
HELIX 117 AM9 GLU D 450 ASN D 464 1 15
HELIX 118 AN1 VAL D 465 GLY D 471 5 7
HELIX 119 AN2 LEU D 475 PHE D 487 1 13
HELIX 120 AN3 ASP D 489 PHE D 512 1 24
HELIX 121 AN4 ASP D 525 LEU D 538 1 14
HELIX 122 AN5 MET D 554 THR D 567 1 14
HELIX 123 AN6 LEU D 568 HIS D 582 1 15
HELIX 124 AN7 ARG D 589 LEU D 608 1 20
SHEET 1 AA1 3 HIS A 265 TYR A 270 0
SHEET 2 AA1 3 LEU A 273 TYR A 278 -1 O LEU A 277 N HIS A 265
SHEET 3 AA1 3 LEU A 631 VAL A 633 -1 O LEU A 631 N TYR A 278
SHEET 1 AA2 3 HIS B 265 TYR B 270 0
SHEET 2 AA2 3 LEU B 273 TYR B 278 -1 O LEU B 277 N HIS B 265
SHEET 3 AA2 3 LEU B 631 VAL B 633 -1 O LEU B 631 N TYR B 278
SHEET 1 AA3 3 HIS C 265 TYR C 270 0
SHEET 2 AA3 3 LEU C 273 TYR C 278 -1 O LEU C 277 N HIS C 265
SHEET 3 AA3 3 LEU C 631 VAL C 633 -1 O LEU C 631 N TYR C 278
SHEET 1 AA4 3 HIS D 265 TYR D 270 0
SHEET 2 AA4 3 LEU D 273 TYR D 278 -1 O LEU D 277 N HIS D 265
SHEET 3 AA4 3 LEU D 631 VAL D 633 -1 O LEU D 631 N TYR D 278
LINK ND1 HIS A 426 C15 FZ4 A 801 1555 1555 1.43
LINK OD1 ASP A 542 CA CA A 803 1555 1555 2.33
LINK ND1 HIS B 426 C15 FZ4 B 801 1555 1555 1.43
LINK OD1 ASP B 542 CA CA A 803 1555 1555 2.31
LINK ND1 HIS C 426 C15 FZ4 C 801 1555 1555 1.43
LINK OD1 ASP C 542 CA CA A 803 1555 1555 2.03
LINK ND1 HIS D 426 C15 FZ4 D 801 1555 1555 1.43
LINK OD1 ASP D 542 CA CA A 803 1555 1555 2.00
SITE 1 AC1 4 ASP A 542 ASP B 542 ASP C 542 ASP D 542
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
