HEADER MEMBRANE PROTEIN 11-JUL-18 6E2F
TITLE CRYO-EM STRUCTURE OF HUMAN TRPV6 IN COMPLEX WITH CALMODULIN
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 MOL_ID: 2;
COMPND 9 MOLECULE: CALMODULIN-1;
COMPND 10 CHAIN: E;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TRPV6, ECAC2;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: CALM1, CALM, CAM, CAM1;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 83333
KEYWDS TRPV6, TRP CHANNELS, CALCIUM CHANNELS, MEMBRANE PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR A.K.SINGH,L.L.MCGOLDRICK,A.I.SOBOLEVSKY
REVDAT 3 18-DEC-19 6E2F 1 SCALE
REVDAT 2 24-OCT-18 6E2F 1 JRNL
REVDAT 1 22-AUG-18 6E2F 0
JRNL AUTH A.K.SINGH,L.L.MCGOLDRICK,E.C.TWOMEY,A.I.SOBOLEVSKY
JRNL TITL MECHANISM OF CALMODULIN INACTIVATION OF THE
JRNL TITL 2 CALCIUM-SELECTIVE TRP CHANNEL TRPV6.
JRNL REF SCI ADV V. 4 U6088 2018
JRNL REFN ESSN 2375-2548
JRNL PMID 30116787
JRNL DOI 10.1126/SCIADV.AAU6088
REMARK 2
REMARK 2 RESOLUTION. 3.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : RELION, MOTIONCORR2, CRYOSPARC,
REMARK 3 LEGINON, CRYOSPARC
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : REAL
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) : 3.900
REMARK 3 NUMBER OF PARTICLES : 180600
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 6E2F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1000235601.
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-CALMODULIN
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.60
REMARK 245 SAMPLE SUPPORT DETAILS : UNIDENTIFIED
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 8.00
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 55.00
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) : 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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 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 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 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 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 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 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 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 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 MET E 0
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 LEU A 372 CA - CB - CG ANGL. DEV. = 18.8 DEGREES
REMARK 500 LEU B 372 CA - CB - CG ANGL. DEV. = 16.5 DEGREES
REMARK 500 LEU C 372 CA - CB - CG ANGL. DEV. = 19.4 DEGREES
REMARK 500 LEU D 372 CA - CB - CG ANGL. DEV. = 17.4 DEGREES
REMARK 500 LEU D 639 CA - CB - CG ANGL. DEV. = 19.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 56 55.57 -93.02
REMARK 500 GLN A 74 97.31 -69.75
REMARK 500 TYR A 89 49.30 -94.50
REMARK 500 ASP A 90 43.82 34.05
REMARK 500 GLU A 113 -10.85 70.24
REMARK 500 GLN A 128 -18.21 74.67
REMARK 500 ASP A 223 42.89 -97.73
REMARK 500 LEU A 232 -11.97 71.10
REMARK 500 LEU A 280 61.84 62.73
REMARK 500 SER A 285 34.17 -93.07
REMARK 500 GLN A 290 -23.14 75.29
REMARK 500 SER A 291 -30.67 65.21
REMARK 500 LEU A 292 -47.71 -146.47
REMARK 500 TYR A 324 -7.36 72.44
REMARK 500 LEU A 372 85.02 52.72
REMARK 500 LEU A 373 140.79 -37.18
REMARK 500 MET A 410 48.57 -93.02
REMARK 500 PRO A 424 41.18 -84.28
REMARK 500 PHE A 425 -72.85 -109.25
REMARK 500 HIS A 426 1.36 38.04
REMARK 500 SER A 448 -66.05 -92.50
REMARK 500 PHE A 472 -28.60 70.31
REMARK 500 GLN A 473 -177.37 169.97
REMARK 500 ILE A 540 -55.04 -120.09
REMARK 500 ASN A 546 -37.26 -130.93
REMARK 500 TYR A 547 -0.33 65.37
REMARK 500 ARG A 589 -37.06 -134.10
REMARK 500 TRP A 613 79.93 45.42
REMARK 500 ARG A 621 -1.17 58.23
REMARK 500 ASN B 56 52.07 -95.72
REMARK 500 HIS B 73 33.75 -93.61
REMARK 500 TYR B 89 50.27 -92.71
REMARK 500 ASP B 90 44.29 34.20
REMARK 500 GLU B 113 -12.31 72.08
REMARK 500 LEU B 114 -39.27 -130.27
REMARK 500 GLN B 128 -16.12 75.56
REMARK 500 MET B 130 -2.69 -140.38
REMARK 500 ARG B 139 34.16 -94.72
REMARK 500 LEU B 232 -13.68 70.22
REMARK 500 SER B 285 33.08 -92.55
REMARK 500 GLN B 290 -21.68 75.03
REMARK 500 SER B 291 -29.81 65.27
REMARK 500 LEU B 292 -49.16 -146.30
REMARK 500 TYR B 324 -8.22 71.91
REMARK 500 THR B 366 31.86 -140.91
REMARK 500 LYS B 371 61.72 60.20
REMARK 500 LEU B 372 82.30 46.80
REMARK 500 GLN B 374 -66.92 -91.33
REMARK 500 GLU B 375 49.14 -140.53
REMARK 500 MET B 410 51.12 -91.57
REMARK 500
REMARK 500 THIS ENTRY HAS 135 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 GLN A 290 SER A 291 134.74
REMARK 500 LYS A 371 LEU A 372 141.20
REMARK 500 PHE A 425 HIS A 426 143.40
REMARK 500 GLN B 290 SER B 291 140.61
REMARK 500 LYS B 371 LEU B 372 134.17
REMARK 500 PHE B 425 HIS B 426 142.21
REMARK 500 ASN C 129 MET C 130 149.12
REMARK 500 GLN C 290 SER C 291 140.38
REMARK 500 LYS C 371 LEU C 372 135.91
REMARK 500 PHE C 425 HIS C 426 147.98
REMARK 500 GLN D 290 SER D 291 142.20
REMARK 500 LYS D 371 LEU D 372 134.55
REMARK 500 PHE D 425 HIS D 426 145.72
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 901 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 542 OD1
REMARK 620 2 ASP B 542 OD1 64.2
REMARK 620 3 ASP D 542 OD1 63.3 92.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 20 OD1
REMARK 620 2 THR E 26 O 73.2
REMARK 620 3 GLU E 31 OE1 79.7 71.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 56 OD1
REMARK 620 2 ASP E 58 OD1 65.3
REMARK 620 3 ASN E 60 OD1 73.1 70.0
REMARK 620 4 THR E 62 O 67.0 123.4 68.4
REMARK 620 5 GLU E 67 OE1 68.3 110.9 135.6 76.7
REMARK 620 6 GLU E 67 OE2 67.1 65.7 129.4 119.1 50.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 93 OD1
REMARK 620 2 ASP E 95 OD1 58.3
REMARK 620 3 ASN E 97 OD1 66.2 73.8
REMARK 620 4 TYR E 99 O 99.8 142.6 69.3
REMARK 620 5 GLU E 104 OE1 74.0 105.7 133.0 94.9
REMARK 620 6 GLU E 104 OE2 76.7 64.8 134.8 145.0 50.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 129 OD1
REMARK 620 2 ASP E 131 OD1 68.2
REMARK 620 3 ASP E 133 OD1 72.8 81.2
REMARK 620 4 GLN E 135 O 75.2 135.2 63.5
REMARK 620 5 ASN E 137 OD1 135.1 102.3 151.5 122.0
REMARK 620 6 GLU E 140 OE1 66.6 112.7 126.3 73.2 78.9
REMARK 620 7 GLU E 140 OE2 68.7 71.5 138.8 118.0 66.8 46.9
REMARK 620 N 1 2 3 4 5 6
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 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA E 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-8961 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF HUMAN TRPV6 IN COMPLEX WITH CALMODULIN
DBREF 6E2F A 1 725 UNP Q9H1D0 TRPV6_HUMAN 41 765
DBREF 6E2F B 1 725 UNP Q9H1D0 TRPV6_HUMAN 41 765
DBREF 6E2F C 1 725 UNP Q9H1D0 TRPV6_HUMAN 41 765
DBREF 6E2F D 1 725 UNP Q9H1D0 TRPV6_HUMAN 41 765
DBREF 6E2F E 0 148 UNP P0DP23 CALM1_HUMAN 1 149
SEQRES 1 A 725 MET GLY LEU SER LEU PRO LYS GLU LYS GLY LEU ILE LEU
SEQRES 2 A 725 CYS LEU TRP SER LYS PHE CYS ARG TRP PHE GLN ARG ARG
SEQRES 3 A 725 GLU SER TRP ALA GLN SER ARG ASP GLU GLN ASN LEU LEU
SEQRES 4 A 725 GLN GLN LYS ARG ILE TRP GLU SER PRO LEU LEU LEU ALA
SEQRES 5 A 725 ALA LYS ASP ASN ASP VAL GLN ALA LEU ASN LYS LEU LEU
SEQRES 6 A 725 LYS TYR GLU ASP CYS LYS VAL HIS GLN ARG GLY ALA MET
SEQRES 7 A 725 GLY GLU THR ALA LEU HIS ILE ALA ALA LEU TYR ASP ASN
SEQRES 8 A 725 LEU GLU ALA ALA MET VAL LEU MET GLU ALA ALA PRO GLU
SEQRES 9 A 725 LEU VAL PHE GLU PRO MET THR SER GLU LEU TYR GLU GLY
SEQRES 10 A 725 GLN THR ALA LEU HIS ILE ALA VAL VAL ASN GLN ASN MET
SEQRES 11 A 725 ASN LEU VAL ARG ALA LEU LEU ALA ARG ARG ALA SER VAL
SEQRES 12 A 725 SER ALA ARG ALA THR GLY THR ALA PHE ARG ARG SER PRO
SEQRES 13 A 725 CYS ASN LEU ILE TYR PHE GLY GLU HIS PRO LEU SER PHE
SEQRES 14 A 725 ALA ALA CYS VAL ASN SER GLU GLU ILE VAL ARG LEU LEU
SEQRES 15 A 725 ILE GLU HIS GLY ALA ASP ILE ARG ALA GLN ASP SER LEU
SEQRES 16 A 725 GLY ASN THR VAL LEU HIS ILE LEU ILE LEU GLN PRO ASN
SEQRES 17 A 725 LYS THR PHE ALA CYS GLN MET TYR ASN LEU LEU LEU SER
SEQRES 18 A 725 TYR ASP ARG HIS GLY ASP HIS LEU GLN PRO LEU ASP LEU
SEQRES 19 A 725 VAL PRO ASN HIS GLN GLY LEU THR PRO PHE LYS LEU ALA
SEQRES 20 A 725 GLY VAL GLU GLY ASN THR VAL MET PHE GLN HIS LEU MET
SEQRES 21 A 725 GLN LYS ARG LYS HIS THR GLN TRP THR TYR GLY PRO LEU
SEQRES 22 A 725 THR SER THR LEU TYR ASP LEU THR GLU ILE ASP SER SER
SEQRES 23 A 725 GLY ASP GLU GLN SER LEU LEU GLU LEU ILE ILE THR THR
SEQRES 24 A 725 LYS LYS ARG GLU ALA ARG GLN ILE LEU ASP GLN THR PRO
SEQRES 25 A 725 VAL LYS GLU LEU VAL SER LEU LYS TRP LYS ARG TYR GLY
SEQRES 26 A 725 ARG PRO TYR PHE CYS MET LEU GLY ALA ILE TYR LEU LEU
SEQRES 27 A 725 TYR ILE ILE CYS PHE THR MET CYS CYS ILE TYR ARG PRO
SEQRES 28 A 725 LEU LYS PRO ARG THR ASN ASN ARG THR SER PRO ARG ASP
SEQRES 29 A 725 ASN THR LEU LEU GLN GLN LYS LEU LEU GLN GLU ALA TYR
SEQRES 30 A 725 MET THR PRO LYS ASP ASP ILE ARG LEU VAL GLY GLU LEU
SEQRES 31 A 725 VAL THR VAL ILE GLY ALA ILE ILE ILE LEU LEU VAL GLU
SEQRES 32 A 725 VAL PRO ASP ILE PHE ARG MET GLY VAL THR ARG PHE PHE
SEQRES 33 A 725 GLY GLN THR ILE LEU GLY GLY PRO PHE HIS VAL LEU ILE
SEQRES 34 A 725 ILE THR TYR ALA PHE MET VAL LEU VAL THR MET VAL MET
SEQRES 35 A 725 ARG LEU ILE SER ALA SER GLY GLU VAL VAL PRO MET SER
SEQRES 36 A 725 PHE ALA LEU VAL LEU GLY TRP CYS ASN VAL MET TYR PHE
SEQRES 37 A 725 ALA ARG GLY PHE GLN MET LEU GLY PRO PHE THR ILE MET
SEQRES 38 A 725 ILE GLN LYS MET ILE PHE GLY ASP LEU MET ARG PHE CYS
SEQRES 39 A 725 TRP LEU MET ALA VAL VAL ILE LEU GLY PHE ALA SER ALA
SEQRES 40 A 725 PHE TYR ILE ILE PHE GLN THR GLU ASP PRO GLU GLU LEU
SEQRES 41 A 725 GLY HIS PHE TYR ASP TYR PRO MET ALA LEU PHE SER THR
SEQRES 42 A 725 PHE GLU LEU PHE LEU THR ILE ILE ASP GLY PRO ALA ASN
SEQRES 43 A 725 TYR ASN VAL ASP LEU PRO PHE MET TYR SER ILE THR TYR
SEQRES 44 A 725 ALA ALA PHE ALA ILE ILE ALA THR LEU LEU MET LEU ASN
SEQRES 45 A 725 LEU LEU ILE ALA MET MET GLY ASP THR HIS TRP ARG VAL
SEQRES 46 A 725 ALA HIS GLU ARG ASP GLU LEU TRP ARG ALA GLN ILE VAL
SEQRES 47 A 725 ALA THR THR VAL MET LEU GLU ARG LYS LEU PRO ARG CYS
SEQRES 48 A 725 LEU TRP PRO ARG SER GLY ILE CYS GLY ARG GLU TYR GLY
SEQRES 49 A 725 LEU GLY ASP ARG TRP PHE LEU ARG VAL GLU ASP ARG GLN
SEQRES 50 A 725 ASP LEU ASN ARG GLN ARG ILE GLN ARG TYR ALA GLN ALA
SEQRES 51 A 725 PHE HIS THR ARG GLY SER GLU ASP LEU ASP LYS ASP SER
SEQRES 52 A 725 VAL GLU LYS LEU GLU LEU GLY CYS PRO PHE SER PRO HIS
SEQRES 53 A 725 LEU SER LEU PRO MET PRO SER VAL SER ARG SER THR SER
SEQRES 54 A 725 ARG SER SER ALA ASN TRP GLU ARG LEU ARG GLN GLY THR
SEQRES 55 A 725 LEU ARG ARG ASP LEU ARG GLY ILE ILE ASN ARG GLY LEU
SEQRES 56 A 725 GLU ASP GLY GLU SER TRP GLU TYR GLN ILE
SEQRES 1 B 725 MET GLY LEU SER LEU PRO LYS GLU LYS GLY LEU ILE LEU
SEQRES 2 B 725 CYS LEU TRP SER LYS PHE CYS ARG TRP PHE GLN ARG ARG
SEQRES 3 B 725 GLU SER TRP ALA GLN SER ARG ASP GLU GLN ASN LEU LEU
SEQRES 4 B 725 GLN GLN LYS ARG ILE TRP GLU SER PRO LEU LEU LEU ALA
SEQRES 5 B 725 ALA LYS ASP ASN ASP VAL GLN ALA LEU ASN LYS LEU LEU
SEQRES 6 B 725 LYS TYR GLU ASP CYS LYS VAL HIS GLN ARG GLY ALA MET
SEQRES 7 B 725 GLY GLU THR ALA LEU HIS ILE ALA ALA LEU TYR ASP ASN
SEQRES 8 B 725 LEU GLU ALA ALA MET VAL LEU MET GLU ALA ALA PRO GLU
SEQRES 9 B 725 LEU VAL PHE GLU PRO MET THR SER GLU LEU TYR GLU GLY
SEQRES 10 B 725 GLN THR ALA LEU HIS ILE ALA VAL VAL ASN GLN ASN MET
SEQRES 11 B 725 ASN LEU VAL ARG ALA LEU LEU ALA ARG ARG ALA SER VAL
SEQRES 12 B 725 SER ALA ARG ALA THR GLY THR ALA PHE ARG ARG SER PRO
SEQRES 13 B 725 CYS ASN LEU ILE TYR PHE GLY GLU HIS PRO LEU SER PHE
SEQRES 14 B 725 ALA ALA CYS VAL ASN SER GLU GLU ILE VAL ARG LEU LEU
SEQRES 15 B 725 ILE GLU HIS GLY ALA ASP ILE ARG ALA GLN ASP SER LEU
SEQRES 16 B 725 GLY ASN THR VAL LEU HIS ILE LEU ILE LEU GLN PRO ASN
SEQRES 17 B 725 LYS THR PHE ALA CYS GLN MET TYR ASN LEU LEU LEU SER
SEQRES 18 B 725 TYR ASP ARG HIS GLY ASP HIS LEU GLN PRO LEU ASP LEU
SEQRES 19 B 725 VAL PRO ASN HIS GLN GLY LEU THR PRO PHE LYS LEU ALA
SEQRES 20 B 725 GLY VAL GLU GLY ASN THR VAL MET PHE GLN HIS LEU MET
SEQRES 21 B 725 GLN LYS ARG LYS HIS THR GLN TRP THR TYR GLY PRO LEU
SEQRES 22 B 725 THR SER THR LEU TYR ASP LEU THR GLU ILE ASP SER SER
SEQRES 23 B 725 GLY ASP GLU GLN SER LEU LEU GLU LEU ILE ILE THR THR
SEQRES 24 B 725 LYS LYS ARG GLU ALA ARG GLN ILE LEU ASP GLN THR PRO
SEQRES 25 B 725 VAL LYS GLU LEU VAL SER LEU LYS TRP LYS ARG TYR GLY
SEQRES 26 B 725 ARG PRO TYR PHE CYS MET LEU GLY ALA ILE TYR LEU LEU
SEQRES 27 B 725 TYR ILE ILE CYS PHE THR MET CYS CYS ILE TYR ARG PRO
SEQRES 28 B 725 LEU LYS PRO ARG THR ASN ASN ARG THR SER PRO ARG ASP
SEQRES 29 B 725 ASN THR LEU LEU GLN GLN LYS LEU LEU GLN GLU ALA TYR
SEQRES 30 B 725 MET THR PRO LYS ASP ASP ILE ARG LEU VAL GLY GLU LEU
SEQRES 31 B 725 VAL THR VAL ILE GLY ALA ILE ILE ILE LEU LEU VAL GLU
SEQRES 32 B 725 VAL PRO ASP ILE PHE ARG MET GLY VAL THR ARG PHE PHE
SEQRES 33 B 725 GLY GLN THR ILE LEU GLY GLY PRO PHE HIS VAL LEU ILE
SEQRES 34 B 725 ILE THR TYR ALA PHE MET VAL LEU VAL THR MET VAL MET
SEQRES 35 B 725 ARG LEU ILE SER ALA SER GLY GLU VAL VAL PRO MET SER
SEQRES 36 B 725 PHE ALA LEU VAL LEU GLY TRP CYS ASN VAL MET TYR PHE
SEQRES 37 B 725 ALA ARG GLY PHE GLN MET LEU GLY PRO PHE THR ILE MET
SEQRES 38 B 725 ILE GLN LYS MET ILE PHE GLY ASP LEU MET ARG PHE CYS
SEQRES 39 B 725 TRP LEU MET ALA VAL VAL ILE LEU GLY PHE ALA SER ALA
SEQRES 40 B 725 PHE TYR ILE ILE PHE GLN THR GLU ASP PRO GLU GLU LEU
SEQRES 41 B 725 GLY HIS PHE TYR ASP TYR PRO MET ALA LEU PHE SER THR
SEQRES 42 B 725 PHE GLU LEU PHE LEU THR ILE ILE ASP GLY PRO ALA ASN
SEQRES 43 B 725 TYR ASN VAL ASP LEU PRO PHE MET TYR SER ILE THR TYR
SEQRES 44 B 725 ALA ALA PHE ALA ILE ILE ALA THR LEU LEU MET LEU ASN
SEQRES 45 B 725 LEU LEU ILE ALA MET MET GLY ASP THR HIS TRP ARG VAL
SEQRES 46 B 725 ALA HIS GLU ARG ASP GLU LEU TRP ARG ALA GLN ILE VAL
SEQRES 47 B 725 ALA THR THR VAL MET LEU GLU ARG LYS LEU PRO ARG CYS
SEQRES 48 B 725 LEU TRP PRO ARG SER GLY ILE CYS GLY ARG GLU TYR GLY
SEQRES 49 B 725 LEU GLY ASP ARG TRP PHE LEU ARG VAL GLU ASP ARG GLN
SEQRES 50 B 725 ASP LEU ASN ARG GLN ARG ILE GLN ARG TYR ALA GLN ALA
SEQRES 51 B 725 PHE HIS THR ARG GLY SER GLU ASP LEU ASP LYS ASP SER
SEQRES 52 B 725 VAL GLU LYS LEU GLU LEU GLY CYS PRO PHE SER PRO HIS
SEQRES 53 B 725 LEU SER LEU PRO MET PRO SER VAL SER ARG SER THR SER
SEQRES 54 B 725 ARG SER SER ALA ASN TRP GLU ARG LEU ARG GLN GLY THR
SEQRES 55 B 725 LEU ARG ARG ASP LEU ARG GLY ILE ILE ASN ARG GLY LEU
SEQRES 56 B 725 GLU ASP GLY GLU SER TRP GLU TYR GLN ILE
SEQRES 1 C 725 MET GLY LEU SER LEU PRO LYS GLU LYS GLY LEU ILE LEU
SEQRES 2 C 725 CYS LEU TRP SER LYS PHE CYS ARG TRP PHE GLN ARG ARG
SEQRES 3 C 725 GLU SER TRP ALA GLN SER ARG ASP GLU GLN ASN LEU LEU
SEQRES 4 C 725 GLN GLN LYS ARG ILE TRP GLU SER PRO LEU LEU LEU ALA
SEQRES 5 C 725 ALA LYS ASP ASN ASP VAL GLN ALA LEU ASN LYS LEU LEU
SEQRES 6 C 725 LYS TYR GLU ASP CYS LYS VAL HIS GLN ARG GLY ALA MET
SEQRES 7 C 725 GLY GLU THR ALA LEU HIS ILE ALA ALA LEU TYR ASP ASN
SEQRES 8 C 725 LEU GLU ALA ALA MET VAL LEU MET GLU ALA ALA PRO GLU
SEQRES 9 C 725 LEU VAL PHE GLU PRO MET THR SER GLU LEU TYR GLU GLY
SEQRES 10 C 725 GLN THR ALA LEU HIS ILE ALA VAL VAL ASN GLN ASN MET
SEQRES 11 C 725 ASN LEU VAL ARG ALA LEU LEU ALA ARG ARG ALA SER VAL
SEQRES 12 C 725 SER ALA ARG ALA THR GLY THR ALA PHE ARG ARG SER PRO
SEQRES 13 C 725 CYS ASN LEU ILE TYR PHE GLY GLU HIS PRO LEU SER PHE
SEQRES 14 C 725 ALA ALA CYS VAL ASN SER GLU GLU ILE VAL ARG LEU LEU
SEQRES 15 C 725 ILE GLU HIS GLY ALA ASP ILE ARG ALA GLN ASP SER LEU
SEQRES 16 C 725 GLY ASN THR VAL LEU HIS ILE LEU ILE LEU GLN PRO ASN
SEQRES 17 C 725 LYS THR PHE ALA CYS GLN MET TYR ASN LEU LEU LEU SER
SEQRES 18 C 725 TYR ASP ARG HIS GLY ASP HIS LEU GLN PRO LEU ASP LEU
SEQRES 19 C 725 VAL PRO ASN HIS GLN GLY LEU THR PRO PHE LYS LEU ALA
SEQRES 20 C 725 GLY VAL GLU GLY ASN THR VAL MET PHE GLN HIS LEU MET
SEQRES 21 C 725 GLN LYS ARG LYS HIS THR GLN TRP THR TYR GLY PRO LEU
SEQRES 22 C 725 THR SER THR LEU TYR ASP LEU THR GLU ILE ASP SER SER
SEQRES 23 C 725 GLY ASP GLU GLN SER LEU LEU GLU LEU ILE ILE THR THR
SEQRES 24 C 725 LYS LYS ARG GLU ALA ARG GLN ILE LEU ASP GLN THR PRO
SEQRES 25 C 725 VAL LYS GLU LEU VAL SER LEU LYS TRP LYS ARG TYR GLY
SEQRES 26 C 725 ARG PRO TYR PHE CYS MET LEU GLY ALA ILE TYR LEU LEU
SEQRES 27 C 725 TYR ILE ILE CYS PHE THR MET CYS CYS ILE TYR ARG PRO
SEQRES 28 C 725 LEU LYS PRO ARG THR ASN ASN ARG THR SER PRO ARG ASP
SEQRES 29 C 725 ASN THR LEU LEU GLN GLN LYS LEU LEU GLN GLU ALA TYR
SEQRES 30 C 725 MET THR PRO LYS ASP ASP ILE ARG LEU VAL GLY GLU LEU
SEQRES 31 C 725 VAL THR VAL ILE GLY ALA ILE ILE ILE LEU LEU VAL GLU
SEQRES 32 C 725 VAL PRO ASP ILE PHE ARG MET GLY VAL THR ARG PHE PHE
SEQRES 33 C 725 GLY GLN THR ILE LEU GLY GLY PRO PHE HIS VAL LEU ILE
SEQRES 34 C 725 ILE THR TYR ALA PHE MET VAL LEU VAL THR MET VAL MET
SEQRES 35 C 725 ARG LEU ILE SER ALA SER GLY GLU VAL VAL PRO MET SER
SEQRES 36 C 725 PHE ALA LEU VAL LEU GLY TRP CYS ASN VAL MET TYR PHE
SEQRES 37 C 725 ALA ARG GLY PHE GLN MET LEU GLY PRO PHE THR ILE MET
SEQRES 38 C 725 ILE GLN LYS MET ILE PHE GLY ASP LEU MET ARG PHE CYS
SEQRES 39 C 725 TRP LEU MET ALA VAL VAL ILE LEU GLY PHE ALA SER ALA
SEQRES 40 C 725 PHE TYR ILE ILE PHE GLN THR GLU ASP PRO GLU GLU LEU
SEQRES 41 C 725 GLY HIS PHE TYR ASP TYR PRO MET ALA LEU PHE SER THR
SEQRES 42 C 725 PHE GLU LEU PHE LEU THR ILE ILE ASP GLY PRO ALA ASN
SEQRES 43 C 725 TYR ASN VAL ASP LEU PRO PHE MET TYR SER ILE THR TYR
SEQRES 44 C 725 ALA ALA PHE ALA ILE ILE ALA THR LEU LEU MET LEU ASN
SEQRES 45 C 725 LEU LEU ILE ALA MET MET GLY ASP THR HIS TRP ARG VAL
SEQRES 46 C 725 ALA HIS GLU ARG ASP GLU LEU TRP ARG ALA GLN ILE VAL
SEQRES 47 C 725 ALA THR THR VAL MET LEU GLU ARG LYS LEU PRO ARG CYS
SEQRES 48 C 725 LEU TRP PRO ARG SER GLY ILE CYS GLY ARG GLU TYR GLY
SEQRES 49 C 725 LEU GLY ASP ARG TRP PHE LEU ARG VAL GLU ASP ARG GLN
SEQRES 50 C 725 ASP LEU ASN ARG GLN ARG ILE GLN ARG TYR ALA GLN ALA
SEQRES 51 C 725 PHE HIS THR ARG GLY SER GLU ASP LEU ASP LYS ASP SER
SEQRES 52 C 725 VAL GLU LYS LEU GLU LEU GLY CYS PRO PHE SER PRO HIS
SEQRES 53 C 725 LEU SER LEU PRO MET PRO SER VAL SER ARG SER THR SER
SEQRES 54 C 725 ARG SER SER ALA ASN TRP GLU ARG LEU ARG GLN GLY THR
SEQRES 55 C 725 LEU ARG ARG ASP LEU ARG GLY ILE ILE ASN ARG GLY LEU
SEQRES 56 C 725 GLU ASP GLY GLU SER TRP GLU TYR GLN ILE
SEQRES 1 D 725 MET GLY LEU SER LEU PRO LYS GLU LYS GLY LEU ILE LEU
SEQRES 2 D 725 CYS LEU TRP SER LYS PHE CYS ARG TRP PHE GLN ARG ARG
SEQRES 3 D 725 GLU SER TRP ALA GLN SER ARG ASP GLU GLN ASN LEU LEU
SEQRES 4 D 725 GLN GLN LYS ARG ILE TRP GLU SER PRO LEU LEU LEU ALA
SEQRES 5 D 725 ALA LYS ASP ASN ASP VAL GLN ALA LEU ASN LYS LEU LEU
SEQRES 6 D 725 LYS TYR GLU ASP CYS LYS VAL HIS GLN ARG GLY ALA MET
SEQRES 7 D 725 GLY GLU THR ALA LEU HIS ILE ALA ALA LEU TYR ASP ASN
SEQRES 8 D 725 LEU GLU ALA ALA MET VAL LEU MET GLU ALA ALA PRO GLU
SEQRES 9 D 725 LEU VAL PHE GLU PRO MET THR SER GLU LEU TYR GLU GLY
SEQRES 10 D 725 GLN THR ALA LEU HIS ILE ALA VAL VAL ASN GLN ASN MET
SEQRES 11 D 725 ASN LEU VAL ARG ALA LEU LEU ALA ARG ARG ALA SER VAL
SEQRES 12 D 725 SER ALA ARG ALA THR GLY THR ALA PHE ARG ARG SER PRO
SEQRES 13 D 725 CYS ASN LEU ILE TYR PHE GLY GLU HIS PRO LEU SER PHE
SEQRES 14 D 725 ALA ALA CYS VAL ASN SER GLU GLU ILE VAL ARG LEU LEU
SEQRES 15 D 725 ILE GLU HIS GLY ALA ASP ILE ARG ALA GLN ASP SER LEU
SEQRES 16 D 725 GLY ASN THR VAL LEU HIS ILE LEU ILE LEU GLN PRO ASN
SEQRES 17 D 725 LYS THR PHE ALA CYS GLN MET TYR ASN LEU LEU LEU SER
SEQRES 18 D 725 TYR ASP ARG HIS GLY ASP HIS LEU GLN PRO LEU ASP LEU
SEQRES 19 D 725 VAL PRO ASN HIS GLN GLY LEU THR PRO PHE LYS LEU ALA
SEQRES 20 D 725 GLY VAL GLU GLY ASN THR VAL MET PHE GLN HIS LEU MET
SEQRES 21 D 725 GLN LYS ARG LYS HIS THR GLN TRP THR TYR GLY PRO LEU
SEQRES 22 D 725 THR SER THR LEU TYR ASP LEU THR GLU ILE ASP SER SER
SEQRES 23 D 725 GLY ASP GLU GLN SER LEU LEU GLU LEU ILE ILE THR THR
SEQRES 24 D 725 LYS LYS ARG GLU ALA ARG GLN ILE LEU ASP GLN THR PRO
SEQRES 25 D 725 VAL LYS GLU LEU VAL SER LEU LYS TRP LYS ARG TYR GLY
SEQRES 26 D 725 ARG PRO TYR PHE CYS MET LEU GLY ALA ILE TYR LEU LEU
SEQRES 27 D 725 TYR ILE ILE CYS PHE THR MET CYS CYS ILE TYR ARG PRO
SEQRES 28 D 725 LEU LYS PRO ARG THR ASN ASN ARG THR SER PRO ARG ASP
SEQRES 29 D 725 ASN THR LEU LEU GLN GLN LYS LEU LEU GLN GLU ALA TYR
SEQRES 30 D 725 MET THR PRO LYS ASP ASP ILE ARG LEU VAL GLY GLU LEU
SEQRES 31 D 725 VAL THR VAL ILE GLY ALA ILE ILE ILE LEU LEU VAL GLU
SEQRES 32 D 725 VAL PRO ASP ILE PHE ARG MET GLY VAL THR ARG PHE PHE
SEQRES 33 D 725 GLY GLN THR ILE LEU GLY GLY PRO PHE HIS VAL LEU ILE
SEQRES 34 D 725 ILE THR TYR ALA PHE MET VAL LEU VAL THR MET VAL MET
SEQRES 35 D 725 ARG LEU ILE SER ALA SER GLY GLU VAL VAL PRO MET SER
SEQRES 36 D 725 PHE ALA LEU VAL LEU GLY TRP CYS ASN VAL MET TYR PHE
SEQRES 37 D 725 ALA ARG GLY PHE GLN MET LEU GLY PRO PHE THR ILE MET
SEQRES 38 D 725 ILE GLN LYS MET ILE PHE GLY ASP LEU MET ARG PHE CYS
SEQRES 39 D 725 TRP LEU MET ALA VAL VAL ILE LEU GLY PHE ALA SER ALA
SEQRES 40 D 725 PHE TYR ILE ILE PHE GLN THR GLU ASP PRO GLU GLU LEU
SEQRES 41 D 725 GLY HIS PHE TYR ASP TYR PRO MET ALA LEU PHE SER THR
SEQRES 42 D 725 PHE GLU LEU PHE LEU THR ILE ILE ASP GLY PRO ALA ASN
SEQRES 43 D 725 TYR ASN VAL ASP LEU PRO PHE MET TYR SER ILE THR TYR
SEQRES 44 D 725 ALA ALA PHE ALA ILE ILE ALA THR LEU LEU MET LEU ASN
SEQRES 45 D 725 LEU LEU ILE ALA MET MET GLY ASP THR HIS TRP ARG VAL
SEQRES 46 D 725 ALA HIS GLU ARG ASP GLU LEU TRP ARG ALA GLN ILE VAL
SEQRES 47 D 725 ALA THR THR VAL MET LEU GLU ARG LYS LEU PRO ARG CYS
SEQRES 48 D 725 LEU TRP PRO ARG SER GLY ILE CYS GLY ARG GLU TYR GLY
SEQRES 49 D 725 LEU GLY ASP ARG TRP PHE LEU ARG VAL GLU ASP ARG GLN
SEQRES 50 D 725 ASP LEU ASN ARG GLN ARG ILE GLN ARG TYR ALA GLN ALA
SEQRES 51 D 725 PHE HIS THR ARG GLY SER GLU ASP LEU ASP LYS ASP SER
SEQRES 52 D 725 VAL GLU LYS LEU GLU LEU GLY CYS PRO PHE SER PRO HIS
SEQRES 53 D 725 LEU SER LEU PRO MET PRO SER VAL SER ARG SER THR SER
SEQRES 54 D 725 ARG SER SER ALA ASN TRP GLU ARG LEU ARG GLN GLY THR
SEQRES 55 D 725 LEU ARG ARG ASP LEU ARG GLY ILE ILE ASN ARG GLY LEU
SEQRES 56 D 725 GLU ASP GLY GLU SER TRP GLU TYR GLN ILE
SEQRES 1 E 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 E 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 E 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 E 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 E 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 E 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 E 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 E 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 E 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 E 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 E 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 E 149 GLN MET MET THR ALA LYS
HET CA A 901 1
HET CA A 902 1
HET CA E 401 1
HET CA E 402 1
HET CA E 403 1
HET CA E 404 1
HETNAM CA CALCIUM ION
FORMUL 6 CA 6(CA 2+)
HELIX 1 AA1 SER A 28 SER A 47 1 20
HELIX 2 AA2 SER A 47 ASP A 55 1 9
HELIX 3 AA3 ASP A 57 GLU A 68 1 12
HELIX 4 AA4 THR A 81 TYR A 89 1 9
HELIX 5 AA5 ASN A 91 ALA A 102 1 12
HELIX 6 AA6 THR A 119 ASN A 127 1 9
HELIX 7 AA7 ASN A 131 ARG A 139 1 9
HELIX 8 AA8 GLY A 149 ARG A 153 5 5
HELIX 9 AA9 HIS A 165 VAL A 173 1 9
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 LYS A 209 PHE A 211 5 3
HELIX 13 AB4 ALA A 212 TYR A 222 1 11
HELIX 14 AB5 THR A 242 GLY A 251 1 10
HELIX 15 AB6 ASN A 252 GLN A 261 1 10
HELIX 16 AB7 LEU A 292 THR A 298 1 7
HELIX 17 AB8 ARG A 302 ASP A 309 5 8
HELIX 18 AB9 GLN A 310 ARG A 323 1 14
HELIX 19 AC1 GLY A 325 TYR A 349 1 25
HELIX 20 AC2 PRO A 380 PHE A 408 1 29
HELIX 21 AC3 VAL A 412 GLY A 423 1 12
HELIX 22 AC4 VAL A 427 SER A 446 1 20
HELIX 23 AC5 GLU A 450 ASN A 464 1 15
HELIX 24 AC6 VAL A 465 ARG A 470 5 6
HELIX 25 AC7 PRO A 477 PHE A 487 1 11
HELIX 26 AC8 LEU A 490 PHE A 512 1 23
HELIX 27 AC9 LEU A 520 TYR A 524 5 5
HELIX 28 AD1 ASP A 525 PHE A 537 1 13
HELIX 29 AD2 MET A 554 THR A 567 1 14
HELIX 30 AD3 LEU A 569 THR A 581 1 13
HELIX 31 AD4 ARG A 589 LYS A 607 1 19
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 GLU B 68 1 12
HELIX 35 AD8 THR B 81 TYR B 89 1 9
HELIX 36 AD9 ASN B 91 ALA B 102 1 12
HELIX 37 AE1 GLU B 104 GLU B 108 5 5
HELIX 38 AE2 THR B 119 ASN B 127 1 9
HELIX 39 AE3 ASN B 131 ARG B 139 1 9
HELIX 40 AE4 GLY B 149 ARG B 153 5 5
HELIX 41 AE5 HIS B 165 VAL B 173 1 9
HELIX 42 AE6 SER B 175 GLU B 184 1 10
HELIX 43 AE7 THR B 198 LEU B 205 1 8
HELIX 44 AE8 LYS B 209 SER B 221 1 13
HELIX 45 AE9 THR B 242 GLY B 251 1 10
HELIX 46 AF1 ASN B 252 GLN B 261 1 10
HELIX 47 AF2 LEU B 292 THR B 298 1 7
HELIX 48 AF3 ARG B 302 ASP B 309 5 8
HELIX 49 AF4 GLN B 310 ARG B 323 1 14
HELIX 50 AF5 GLY B 325 TYR B 349 1 25
HELIX 51 AF6 THR B 379 VAL B 404 1 26
HELIX 52 AF7 VAL B 412 ILE B 420 1 9
HELIX 53 AF8 VAL B 427 SER B 446 1 20
HELIX 54 AF9 GLU B 450 ASN B 464 1 15
HELIX 55 AG1 VAL B 465 GLY B 471 5 7
HELIX 56 AG2 PRO B 477 PHE B 487 1 11
HELIX 57 AG3 LEU B 490 PHE B 512 1 23
HELIX 58 AG4 LEU B 520 TYR B 524 5 5
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 569 HIS B 582 1 14
HELIX 62 AG8 ALA B 586 LYS B 607 1 22
HELIX 63 AG9 LEU B 639 GLN B 645 1 7
HELIX 64 AH1 TRP C 29 SER C 47 1 19
HELIX 65 AH2 SER C 47 ASP C 55 1 9
HELIX 66 AH3 ASP C 57 GLU C 68 1 12
HELIX 67 AH4 THR C 81 TYR C 89 1 9
HELIX 68 AH5 ASN C 91 ALA C 102 1 12
HELIX 69 AH6 GLU C 104 GLU C 108 5 5
HELIX 70 AH7 THR C 119 ASN C 127 1 9
HELIX 71 AH8 LEU C 132 ARG C 139 1 8
HELIX 72 AH9 HIS C 165 VAL C 173 1 9
HELIX 73 AI1 SER C 175 GLU C 184 1 10
HELIX 74 AI2 THR C 198 LEU C 205 1 8
HELIX 75 AI3 LYS C 209 PHE C 211 5 3
HELIX 76 AI4 ALA C 212 SER C 221 1 10
HELIX 77 AI5 THR C 242 GLY C 251 1 10
HELIX 78 AI6 ASN C 252 GLN C 261 1 10
HELIX 79 AI7 LEU C 292 THR C 298 1 7
HELIX 80 AI8 ARG C 302 ASP C 309 5 8
HELIX 81 AI9 GLN C 310 ARG C 323 1 14
HELIX 82 AJ1 GLY C 325 TYR C 349 1 25
HELIX 83 AJ2 PRO C 380 GLU C 403 1 24
HELIX 84 AJ3 GLU C 403 MET C 410 1 8
HELIX 85 AJ4 VAL C 412 GLY C 423 1 12
HELIX 86 AJ5 VAL C 427 SER C 446 1 20
HELIX 87 AJ6 GLU C 450 ASN C 464 1 15
HELIX 88 AJ7 VAL C 465 ARG C 470 5 6
HELIX 89 AJ8 PRO C 477 PHE C 487 1 11
HELIX 90 AJ9 GLY C 488 PHE C 512 1 25
HELIX 91 AK1 ASP C 525 LEU C 538 1 14
HELIX 92 AK2 MET C 554 THR C 567 1 14
HELIX 93 AK3 LEU C 569 ARG C 584 1 16
HELIX 94 AK4 ALA C 586 LYS C 607 1 22
HELIX 95 AK5 ASN C 640 HIS C 652 1 13
HELIX 96 AK6 SER C 687 LEU C 703 1 17
HELIX 97 AK7 ALA D 30 SER D 47 1 18
HELIX 98 AK8 SER D 47 ASP D 55 1 9
HELIX 99 AK9 ASP D 57 LYS D 66 1 10
HELIX 100 AL1 THR D 81 TYR D 89 1 9
HELIX 101 AL2 ASN D 91 ALA D 102 1 12
HELIX 102 AL3 THR D 119 ASN D 127 1 9
HELIX 103 AL4 LEU D 132 ARG D 139 1 8
HELIX 104 AL5 GLY D 149 ARG D 153 5 5
HELIX 105 AL6 HIS D 165 VAL D 173 1 9
HELIX 106 AL7 SER D 175 GLU D 184 1 10
HELIX 107 AL8 THR D 198 LEU D 205 1 8
HELIX 108 AL9 LYS D 209 PHE D 211 5 3
HELIX 109 AM1 ALA D 212 TYR D 222 1 11
HELIX 110 AM2 THR D 242 GLY D 251 1 10
HELIX 111 AM3 ASN D 252 GLN D 261 1 10
HELIX 112 AM4 LEU D 292 THR D 298 1 7
HELIX 113 AM5 ARG D 302 GLN D 310 5 9
HELIX 114 AM6 VAL D 313 ARG D 323 1 11
HELIX 115 AM7 GLY D 325 CYS D 346 1 22
HELIX 116 AM8 THR D 379 PHE D 408 1 30
HELIX 117 AM9 VAL D 412 GLY D 423 1 12
HELIX 118 AN1 VAL D 427 ILE D 445 1 19
HELIX 119 AN2 GLU D 450 VAL D 465 1 16
HELIX 120 AN3 MET D 466 GLY D 471 5 6
HELIX 121 AN4 PRO D 477 PHE D 487 1 11
HELIX 122 AN5 GLY D 488 PHE D 512 1 25
HELIX 123 AN6 LEU D 520 TYR D 524 5 5
HELIX 124 AN7 ASP D 525 LEU D 538 1 14
HELIX 125 AN8 PRO D 552 THR D 567 1 16
HELIX 126 AN9 LEU D 569 ARG D 584 1 16
HELIX 127 AO1 ALA D 586 LYS D 607 1 22
HELIX 128 AO2 THR E 5 ASP E 20 1 16
HELIX 129 AO3 THR E 28 LEU E 39 1 12
HELIX 130 AO4 ALA E 46 ASP E 56 1 11
HELIX 131 AO5 ASP E 64 LYS E 75 1 12
HELIX 132 AO6 GLU E 83 ASP E 93 1 11
HELIX 133 AO7 SER E 101 GLY E 113 1 13
HELIX 134 AO8 THR E 117 ASP E 129 1 13
HELIX 135 AO9 ASN E 137 THR E 146 1 10
SHEET 1 AA1 3 THR A 269 TYR A 270 0
SHEET 2 AA1 3 LEU A 273 TYR A 278 -1 O LEU A 273 N TYR A 270
SHEET 3 AA1 3 LEU A 631 ARG A 636 -1 O VAL A 633 N THR A 276
SHEET 1 AA2 3 THR B 269 TYR B 270 0
SHEET 2 AA2 3 LEU B 273 TYR B 278 -1 O LEU B 273 N TYR B 270
SHEET 3 AA2 3 LEU B 631 ARG B 636 -1 O VAL B 633 N THR B 276
SHEET 1 AA3 3 THR C 269 TYR C 270 0
SHEET 2 AA3 3 LEU C 273 TYR C 278 -1 O LEU C 273 N TYR C 270
SHEET 3 AA3 3 LEU C 631 ARG C 636 -1 O ASP C 635 N THR C 274
SHEET 1 AA4 3 THR D 269 TYR D 270 0
SHEET 2 AA4 3 LEU D 273 TYR D 278 -1 O LEU D 273 N TYR D 270
SHEET 3 AA4 3 LEU D 631 ARG D 636 -1 O LEU D 631 N TYR D 278
LINK OD1 ASP A 542 CA CA A 901 1555 1555 2.83
LINK OD1 ASP B 542 CA CA A 901 1555 1555 2.52
LINK OD1 ASP D 542 CA CA A 901 1555 1555 2.59
LINK OD1 ASP E 20 CA CA E 401 1555 1555 2.52
LINK O THR E 26 CA CA E 401 1555 1555 2.55
LINK OE1 GLU E 31 CA CA E 401 1555 1555 2.50
LINK OD1 ASP E 56 CA CA E 402 1555 1555 2.65
LINK OD1 ASP E 58 CA CA E 402 1555 1555 2.58
LINK OD1 ASN E 60 CA CA E 402 1555 1555 2.49
LINK O THR E 62 CA CA E 402 1555 1555 2.64
LINK OE1 GLU E 67 CA CA E 402 1555 1555 2.50
LINK OE2 GLU E 67 CA CA E 402 1555 1555 2.67
LINK OD1 ASP E 93 CA CA E 403 1555 1555 2.88
LINK OD1 ASP E 95 CA CA E 403 1555 1555 2.97
LINK OD1 ASN E 97 CA CA E 403 1555 1555 2.52
LINK O TYR E 99 CA CA E 403 1555 1555 2.54
LINK OE1 GLU E 104 CA CA E 403 1555 1555 2.63
LINK OE2 GLU E 104 CA CA E 403 1555 1555 2.51
LINK OD1 ASP E 129 CA CA E 404 1555 1555 2.55
LINK OD1 ASP E 131 CA CA E 404 1555 1555 2.52
LINK OD1 ASP E 133 CA CA E 404 1555 1555 2.79
LINK O GLN E 135 CA CA E 404 1555 1555 2.67
LINK OD1 ASN E 137 CA CA E 404 1555 1555 3.00
LINK OE1 GLU E 140 CA CA E 404 1555 1555 2.88
LINK OE2 GLU E 140 CA CA E 404 1555 1555 2.58
SITE 1 AC1 4 ASP A 542 CA A 902 ASP B 542 ASP D 542
SITE 1 AC2 1 CA A 901
SITE 1 AC3 4 ASP E 20 THR E 26 ILE E 27 GLU E 31
SITE 1 AC4 6 ASP E 56 ASP E 58 ASN E 60 THR E 62
SITE 2 AC4 6 ASP E 64 GLU E 67
SITE 1 AC5 5 ASP E 93 ASP E 95 ASN E 97 TYR E 99
SITE 2 AC5 5 GLU E 104
SITE 1 AC6 6 ASP E 129 ASP E 131 ASP E 133 GLN E 135
SITE 2 AC6 6 ASN E 137 GLU E 140
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
