HEADER TRANSPORT PROTEIN 18-NOV-17 6BOB
TITLE CRYO-EM STRUCTURE OF RAT TRPV6* IN NANODISCS
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,CALCIUM TRANSPORT PROTEIN 1,CAT1,EPITHELIAL CALCIUM
COMPND 6 CHANNEL 2,ECAC2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: TRPV6;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606
KEYWDS ION CHANNEL, MEMBRANE PROTEIN, TRANSPORT PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR L.L.MCGOLDRICK,A.K.SINGH,K.SAOTOME,M.V.YELSHANSKAYA,E.C.TWOMEY,
AUTHOR 2 R.A.GRASSUCCI,A.I.SOBOLEVSKY
REVDAT 7 13-MAR-24 6BOB 1 REMARK
REVDAT 6 18-DEC-19 6BOB 1 SCALE
REVDAT 5 04-DEC-19 6BOB 1 REMARK
REVDAT 4 24-JAN-18 6BOB 1 JRNL
REVDAT 3 17-JAN-18 6BOB 1 REMARK
REVDAT 2 03-JAN-18 6BOB 1 JRNL
REVDAT 1 20-DEC-17 6BOB 0
JRNL AUTH L.L.MCGOLDRICK,A.K.SINGH,K.SAOTOME,M.V.YELSHANSKAYA,
JRNL AUTH 2 E.C.TWOMEY,R.A.GRASSUCCI,A.I.SOBOLEVSKY
JRNL TITL OPENING OF THE HUMAN EPITHELIAL CALCIUM CHANNEL TRPV6.
JRNL REF NATURE V. 553 233 2018
JRNL REFN ESSN 1476-4687
JRNL PMID 29258289
JRNL DOI 10.1038/NATURE25182
REMARK 2
REMARK 2 RESOLUTION. 3.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : RELION
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : REAL
REMARK 3 REFINEMENT PROTOCOL : OTHER
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 : 20808
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 6BOB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1000231197.
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* ION CHANNEL IN CLOSED
REMARK 245 STATES
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 F30
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) : 6700.00
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: 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 TRP 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 ASN 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 HIS A 24
REMARK 465 ARG A 25
REMARK 465 ARG A 26
REMARK 465 PHE A 415
REMARK 465 GLY A 416
REMARK 465 GLN A 417
REMARK 465 THR A 418
REMARK 465 ILE A 419
REMARK 465 LEU A 420
REMARK 465 GLY A 421
REMARK 465 GLY A 422
REMARK 465 LEU A 638
REMARK 465 ASN A 639
REMARK 465 ARG A 640
REMARK 465 GLN A 641
REMARK 465 ARG A 642
REMARK 465 ILE A 643
REMARK 465 ARG A 644
REMARK 465 ARG A 645
REMARK 465 TYR A 646
REMARK 465 ALA A 647
REMARK 465 GLN A 648
REMARK 465 ALA A 649
REMARK 465 PHE A 650
REMARK 465 GLN A 651
REMARK 465 GLN A 652
REMARK 465 GLN A 653
REMARK 465 ASP A 654
REMARK 465 ASP A 655
REMARK 465 LEU A 656
REMARK 465 TYR A 657
REMARK 465 SER A 658
REMARK 465 GLU A 659
REMARK 465 ASP A 660
REMARK 465 LEU A 661
REMARK 465 GLU A 662
REMARK 465 LYS A 663
REMARK 465 ASP A 664
REMARK 465 SER A 665
REMARK 465 GLY A 666
REMARK 465 GLU A 667
REMARK 465 LYS A 668
REMARK 465 LEU A 669
REMARK 465 VAL A 670
REMARK 465 PRO A 671
REMARK 465 ARG A 672
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 TRP 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 ASN 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 HIS B 24
REMARK 465 ARG B 25
REMARK 465 ARG B 26
REMARK 465 PHE B 415
REMARK 465 GLY B 416
REMARK 465 GLN B 417
REMARK 465 THR B 418
REMARK 465 ILE B 419
REMARK 465 LEU B 420
REMARK 465 GLY B 421
REMARK 465 GLY B 422
REMARK 465 LEU B 638
REMARK 465 ASN B 639
REMARK 465 ARG B 640
REMARK 465 GLN B 641
REMARK 465 ARG B 642
REMARK 465 ILE B 643
REMARK 465 ARG B 644
REMARK 465 ARG B 645
REMARK 465 TYR B 646
REMARK 465 ALA B 647
REMARK 465 GLN B 648
REMARK 465 ALA B 649
REMARK 465 PHE B 650
REMARK 465 GLN B 651
REMARK 465 GLN B 652
REMARK 465 GLN B 653
REMARK 465 ASP B 654
REMARK 465 ASP B 655
REMARK 465 LEU B 656
REMARK 465 TYR B 657
REMARK 465 SER B 658
REMARK 465 GLU B 659
REMARK 465 ASP B 660
REMARK 465 LEU B 661
REMARK 465 GLU B 662
REMARK 465 LYS B 663
REMARK 465 ASP B 664
REMARK 465 SER B 665
REMARK 465 GLY B 666
REMARK 465 GLU B 667
REMARK 465 LYS B 668
REMARK 465 LEU B 669
REMARK 465 VAL B 670
REMARK 465 PRO B 671
REMARK 465 ARG B 672
REMARK 465 MET C 1
REMARK 465 GLY C 2
REMARK 465 TRP 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 ASN 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 HIS C 24
REMARK 465 ARG C 25
REMARK 465 ARG C 26
REMARK 465 PHE C 415
REMARK 465 GLY C 416
REMARK 465 GLN C 417
REMARK 465 THR C 418
REMARK 465 ILE C 419
REMARK 465 LEU C 420
REMARK 465 GLY C 421
REMARK 465 GLY C 422
REMARK 465 LEU C 638
REMARK 465 ASN C 639
REMARK 465 ARG C 640
REMARK 465 GLN C 641
REMARK 465 ARG C 642
REMARK 465 ILE C 643
REMARK 465 ARG C 644
REMARK 465 ARG C 645
REMARK 465 TYR C 646
REMARK 465 ALA C 647
REMARK 465 GLN C 648
REMARK 465 ALA C 649
REMARK 465 PHE C 650
REMARK 465 GLN C 651
REMARK 465 GLN C 652
REMARK 465 GLN C 653
REMARK 465 ASP C 654
REMARK 465 ASP C 655
REMARK 465 LEU C 656
REMARK 465 TYR C 657
REMARK 465 SER C 658
REMARK 465 GLU C 659
REMARK 465 ASP C 660
REMARK 465 LEU C 661
REMARK 465 GLU C 662
REMARK 465 LYS C 663
REMARK 465 ASP C 664
REMARK 465 SER C 665
REMARK 465 GLY C 666
REMARK 465 GLU C 667
REMARK 465 LYS C 668
REMARK 465 LEU C 669
REMARK 465 VAL C 670
REMARK 465 PRO C 671
REMARK 465 ARG C 672
REMARK 465 MET D 1
REMARK 465 GLY D 2
REMARK 465 TRP 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 ASN 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 HIS D 24
REMARK 465 ARG D 25
REMARK 465 ARG D 26
REMARK 465 PHE D 415
REMARK 465 GLY D 416
REMARK 465 GLN D 417
REMARK 465 THR D 418
REMARK 465 ILE D 419
REMARK 465 LEU D 420
REMARK 465 GLY D 421
REMARK 465 GLY D 422
REMARK 465 LEU D 638
REMARK 465 ASN D 639
REMARK 465 ARG D 640
REMARK 465 GLN D 641
REMARK 465 ARG D 642
REMARK 465 ILE D 643
REMARK 465 ARG D 644
REMARK 465 ARG D 645
REMARK 465 TYR D 646
REMARK 465 ALA D 647
REMARK 465 GLN D 648
REMARK 465 ALA D 649
REMARK 465 PHE D 650
REMARK 465 GLN D 651
REMARK 465 GLN D 652
REMARK 465 GLN D 653
REMARK 465 ASP D 654
REMARK 465 ASP D 655
REMARK 465 LEU D 656
REMARK 465 TYR D 657
REMARK 465 SER D 658
REMARK 465 GLU D 659
REMARK 465 ASP D 660
REMARK 465 LEU D 661
REMARK 465 GLU D 662
REMARK 465 LYS D 663
REMARK 465 ASP D 664
REMARK 465 SER D 665
REMARK 465 GLY D 666
REMARK 465 GLU D 667
REMARK 465 LYS D 668
REMARK 465 LEU D 669
REMARK 465 VAL D 670
REMARK 465 PRO D 671
REMARK 465 ARG D 672
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 49 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 LEU A 228 CA - CB - CG ANGL. DEV. = 19.9 DEGREES
REMARK 500 ASP A 287 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 LEU B 49 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 LEU B 228 CA - CB - CG ANGL. DEV. = 19.9 DEGREES
REMARK 500 ASP B 287 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 LEU C 49 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 LEU C 228 CA - CB - CG ANGL. DEV. = 19.9 DEGREES
REMARK 500 ASP C 287 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 LEU D 49 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 LEU D 228 CA - CB - CG ANGL. DEV. = 19.9 DEGREES
REMARK 500 ASP D 287 CB - CG - OD1 ANGL. DEV. = 5.6 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 SER A 47 74.30 51.81
REMARK 500 PRO A 48 4.65 -67.13
REMARK 500 PRO A 103 44.58 -83.77
REMARK 500 THR A 148 32.70 -96.92
REMARK 500 HIS A 227 -66.30 -95.26
REMARK 500 LEU A 228 -21.95 66.62
REMARK 500 LEU A 231 -12.89 70.91
REMARK 500 TYR A 269 88.28 -150.40
REMARK 500 ASP A 287 20.57 42.53
REMARK 500 ASP A 288 -3.28 61.36
REMARK 500 TYR A 323 30.45 -142.62
REMARK 500 ARG A 354 -13.69 -143.43
REMARK 500 ILE A 355 -30.71 -30.61
REMARK 500 ASN A 364 32.59 -140.63
REMARK 500 LEU A 372 -66.57 -95.50
REMARK 500 GLN A 373 25.03 -143.19
REMARK 500 VAL A 411 -68.00 -121.19
REMARK 500 THR A 412 57.60 35.06
REMARK 500 THR A 513 47.03 -96.53
REMARK 500 GLU A 621 -7.92 72.95
REMARK 500 ASP A 626 -11.97 72.71
REMARK 500 SER B 47 74.35 51.74
REMARK 500 PRO B 48 4.68 -67.14
REMARK 500 PRO B 103 44.54 -83.73
REMARK 500 THR B 148 32.77 -96.96
REMARK 500 HIS B 227 -66.27 -95.22
REMARK 500 LEU B 228 -21.90 66.54
REMARK 500 LEU B 231 -12.94 70.95
REMARK 500 TYR B 269 88.30 -150.42
REMARK 500 ASP B 287 20.61 42.53
REMARK 500 ASP B 288 -3.29 61.32
REMARK 500 TYR B 323 30.50 -142.57
REMARK 500 ARG B 354 -13.68 -143.45
REMARK 500 ILE B 355 -30.55 -30.72
REMARK 500 ASN B 364 32.64 -140.66
REMARK 500 LEU B 372 -66.58 -95.50
REMARK 500 GLN B 373 25.08 -143.17
REMARK 500 VAL B 411 -68.01 -121.13
REMARK 500 THR B 412 57.59 35.08
REMARK 500 THR B 513 46.99 -96.52
REMARK 500 GLU B 621 -7.95 73.05
REMARK 500 ASP B 626 -11.90 72.64
REMARK 500 SER C 47 74.36 51.68
REMARK 500 PRO C 48 4.64 -67.13
REMARK 500 PRO C 103 44.51 -83.65
REMARK 500 THR C 148 32.81 -96.96
REMARK 500 HIS C 227 -66.23 -95.26
REMARK 500 LEU C 228 -21.89 66.53
REMARK 500 LEU C 231 -12.87 70.96
REMARK 500 TYR C 269 88.22 -150.41
REMARK 500
REMARK 500 THIS ENTRY HAS 84 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 ARG A 354 ILE A 355 -132.25
REMARK 500 THR A 356 ASN A 357 -149.37
REMARK 500 ARG B 354 ILE B 355 -132.20
REMARK 500 THR B 356 ASN B 357 -149.41
REMARK 500 ARG C 354 ILE C 355 -132.25
REMARK 500 THR C 356 ASN C 357 -149.37
REMARK 500 ARG D 354 ILE D 355 -132.25
REMARK 500 THR D 356 ASN D 357 -149.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-7123 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF RAT TRPV6* IN NANODISCS
REMARK 900 RELATED ID: EMD-7122 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-7121 RELATED DB: EMDB
REMARK 900 RELATED ID: EMD-7120 RELATED DB: EMDB
DBREF 6BOB A 1 668 UNP Q9R186 TRPV6_RAT 41 708
DBREF 6BOB B 1 668 UNP Q9R186 TRPV6_RAT 41 708
DBREF 6BOB C 1 668 UNP Q9R186 TRPV6_RAT 41 708
DBREF 6BOB D 1 668 UNP Q9R186 TRPV6_RAT 41 708
SEQADV 6BOB TYR A 62 UNP Q9R186 ILE 102 CONFLICT
SEQADV 6BOB ASN A 92 UNP Q9R186 LEU 132 CONFLICT
SEQADV 6BOB GLN A 96 UNP Q9R186 MET 136 CONFLICT
SEQADV 6BOB LEU A 669 UNP Q9R186 EXPRESSION TAG
SEQADV 6BOB VAL A 670 UNP Q9R186 EXPRESSION TAG
SEQADV 6BOB PRO A 671 UNP Q9R186 EXPRESSION TAG
SEQADV 6BOB ARG A 672 UNP Q9R186 EXPRESSION TAG
SEQADV 6BOB TYR B 62 UNP Q9R186 ILE 102 CONFLICT
SEQADV 6BOB ASN B 92 UNP Q9R186 LEU 132 CONFLICT
SEQADV 6BOB GLN B 96 UNP Q9R186 MET 136 CONFLICT
SEQADV 6BOB LEU B 669 UNP Q9R186 EXPRESSION TAG
SEQADV 6BOB VAL B 670 UNP Q9R186 EXPRESSION TAG
SEQADV 6BOB PRO B 671 UNP Q9R186 EXPRESSION TAG
SEQADV 6BOB ARG B 672 UNP Q9R186 EXPRESSION TAG
SEQADV 6BOB TYR C 62 UNP Q9R186 ILE 102 CONFLICT
SEQADV 6BOB ASN C 92 UNP Q9R186 LEU 132 CONFLICT
SEQADV 6BOB GLN C 96 UNP Q9R186 MET 136 CONFLICT
SEQADV 6BOB LEU C 669 UNP Q9R186 EXPRESSION TAG
SEQADV 6BOB VAL C 670 UNP Q9R186 EXPRESSION TAG
SEQADV 6BOB PRO C 671 UNP Q9R186 EXPRESSION TAG
SEQADV 6BOB ARG C 672 UNP Q9R186 EXPRESSION TAG
SEQADV 6BOB TYR D 62 UNP Q9R186 ILE 102 CONFLICT
SEQADV 6BOB ASN D 92 UNP Q9R186 LEU 132 CONFLICT
SEQADV 6BOB GLN D 96 UNP Q9R186 MET 136 CONFLICT
SEQADV 6BOB LEU D 669 UNP Q9R186 EXPRESSION TAG
SEQADV 6BOB VAL D 670 UNP Q9R186 EXPRESSION TAG
SEQADV 6BOB PRO D 671 UNP Q9R186 EXPRESSION TAG
SEQADV 6BOB ARG D 672 UNP Q9R186 EXPRESSION TAG
SEQRES 1 A 672 MET GLY TRP SER LEU PRO LYS GLU LYS GLY LEU ILE LEU
SEQRES 2 A 672 CYS LEU TRP ASN LYS PHE CYS ARG TRP PHE HIS ARG ARG
SEQRES 3 A 672 GLU SER TRP ALA GLN SER ARG ASP GLU GLN ASN LEU LEU
SEQRES 4 A 672 GLN GLN LYS ARG ILE TRP GLU SER PRO LEU LEU LEU ALA
SEQRES 5 A 672 ALA LYS GLU ASN ASN VAL GLN ALA LEU TYR LYS LEU LEU
SEQRES 6 A 672 LYS PHE GLU GLY CYS GLU VAL HIS GLN LYS GLY ALA MET
SEQRES 7 A 672 GLY GLU THR ALA LEU HIS ILE ALA ALA LEU TYR ASP ASN
SEQRES 8 A 672 ASN GLU ALA ALA GLN VAL LEU MET GLU ALA ALA PRO GLU
SEQRES 9 A 672 LEU VAL PHE GLU PRO MET THR SER GLU LEU TYR GLU GLY
SEQRES 10 A 672 GLN THR ALA LEU HIS ILE ALA VAL ILE ASN GLN ASN VAL
SEQRES 11 A 672 ASN LEU VAL ARG ALA LEU LEU ALA ARG GLY ALA SER VAL
SEQRES 12 A 672 SER ALA ARG ALA THR GLY SER VAL PHE HIS TYR ARG PRO
SEQRES 13 A 672 HIS ASN LEU ILE TYR TYR GLY GLU HIS PRO LEU SER PHE
SEQRES 14 A 672 ALA ALA CYS VAL GLY SER GLU GLU ILE VAL ARG LEU LEU
SEQRES 15 A 672 ILE GLU HIS GLY ALA ASP ILE ARG ALA GLN ASP SER LEU
SEQRES 16 A 672 GLY ASN THR VAL LEU HIS ILE LEU ILE LEU GLN PRO ASN
SEQRES 17 A 672 LYS THR PHE ALA CYS GLN MET TYR ASN LEU LEU LEU SER
SEQRES 18 A 672 TYR ASP GLY GLY ASP HIS LEU LYS SER LEU GLU LEU VAL
SEQRES 19 A 672 PRO ASN ASN GLN GLY LEU THR PRO PHE LYS LEU ALA GLY
SEQRES 20 A 672 VAL GLU GLY ASN ILE VAL MET PHE GLN HIS LEU MET GLN
SEQRES 21 A 672 LYS ARG LYS HIS ILE GLN TRP THR TYR GLY PRO LEU THR
SEQRES 22 A 672 SER THR LEU TYR ASP LEU THR GLU ILE ASP SER SER GLY
SEQRES 23 A 672 ASP ASP GLN SER LEU LEU GLU LEU ILE VAL THR THR LYS
SEQRES 24 A 672 LYS ARG GLU ALA ARG GLN ILE LEU ASP GLN THR PRO VAL
SEQRES 25 A 672 LYS GLU LEU VAL SER LEU LYS TRP LYS ARG TYR GLY ARG
SEQRES 26 A 672 PRO TYR PHE CYS VAL LEU GLY ALA ILE TYR VAL LEU TYR
SEQRES 27 A 672 ILE ILE CYS PHE THR MET CYS CYS VAL TYR ARG PRO LEU
SEQRES 28 A 672 LYS PRO ARG ILE THR ASN ARG THR ASN PRO ARG ASP ASN
SEQRES 29 A 672 THR LEU LEU GLN GLN LYS LEU LEU GLN GLU ALA TYR VAL
SEQRES 30 A 672 THR PRO LYS ASP ASP LEU ARG LEU VAL GLY GLU LEU VAL
SEQRES 31 A 672 SER ILE VAL GLY ALA VAL ILE ILE LEU LEU VAL GLU ILE
SEQRES 32 A 672 PRO ASP ILE PHE ARG LEU GLY VAL THR ARG PHE PHE GLY
SEQRES 33 A 672 GLN THR ILE LEU GLY GLY PRO PHE HIS VAL ILE ILE VAL
SEQRES 34 A 672 THR TYR ALA PHE MET VAL LEU VAL THR MET VAL MET ARG
SEQRES 35 A 672 LEU THR ASN SER ASP GLY GLU VAL VAL PRO MET SER PHE
SEQRES 36 A 672 ALA LEU VAL LEU GLY TRP CYS ASN VAL MET TYR PHE ALA
SEQRES 37 A 672 ARG GLY PHE GLN MET LEU GLY PRO PHE THR ILE MET ILE
SEQRES 38 A 672 GLN LYS MET ILE PHE GLY ASP LEU MET ARG PHE CYS TRP
SEQRES 39 A 672 LEU MET ALA VAL VAL ILE LEU GLY PHE ALA SER ALA PHE
SEQRES 40 A 672 TYR ILE ILE PHE GLN THR GLU ASP PRO ASP GLU LEU GLY
SEQRES 41 A 672 HIS PHE TYR ASP TYR PRO MET ALA LEU PHE SER THR PHE
SEQRES 42 A 672 GLU LEU PHE LEU THR ILE ILE ASP GLY PRO ALA ASN TYR
SEQRES 43 A 672 ASP VAL ASP LEU PRO PHE MET TYR SER ILE THR TYR ALA
SEQRES 44 A 672 ALA PHE ALA ILE ILE ALA THR LEU LEU MET LEU ASN LEU
SEQRES 45 A 672 LEU ILE ALA MET MET GLY ASP THR HIS TRP ARG VAL ALA
SEQRES 46 A 672 HIS GLU ARG ASP GLU LEU TRP ARG ALA GLN VAL VAL ALA
SEQRES 47 A 672 THR THR VAL MET LEU GLU ARG LYS LEU PRO ARG CYS LEU
SEQRES 48 A 672 TRP PRO ARG SER GLY ILE CYS GLY ARG GLU TYR GLY LEU
SEQRES 49 A 672 GLY ASP ARG TRP PHE LEU ARG VAL GLU ASP ARG GLN ASP
SEQRES 50 A 672 LEU ASN ARG GLN ARG ILE ARG ARG TYR ALA GLN ALA PHE
SEQRES 51 A 672 GLN GLN GLN ASP ASP LEU TYR SER GLU ASP LEU GLU LYS
SEQRES 52 A 672 ASP SER GLY GLU LYS LEU VAL PRO ARG
SEQRES 1 B 672 MET GLY TRP SER LEU PRO LYS GLU LYS GLY LEU ILE LEU
SEQRES 2 B 672 CYS LEU TRP ASN LYS PHE CYS ARG TRP PHE HIS ARG ARG
SEQRES 3 B 672 GLU SER TRP ALA GLN SER ARG ASP GLU GLN ASN LEU LEU
SEQRES 4 B 672 GLN GLN LYS ARG ILE TRP GLU SER PRO LEU LEU LEU ALA
SEQRES 5 B 672 ALA LYS GLU ASN ASN VAL GLN ALA LEU TYR LYS LEU LEU
SEQRES 6 B 672 LYS PHE GLU GLY CYS GLU VAL HIS GLN LYS GLY ALA MET
SEQRES 7 B 672 GLY GLU THR ALA LEU HIS ILE ALA ALA LEU TYR ASP ASN
SEQRES 8 B 672 ASN GLU ALA ALA GLN VAL LEU MET GLU ALA ALA PRO GLU
SEQRES 9 B 672 LEU VAL PHE GLU PRO MET THR SER GLU LEU TYR GLU GLY
SEQRES 10 B 672 GLN THR ALA LEU HIS ILE ALA VAL ILE ASN GLN ASN VAL
SEQRES 11 B 672 ASN LEU VAL ARG ALA LEU LEU ALA ARG GLY ALA SER VAL
SEQRES 12 B 672 SER ALA ARG ALA THR GLY SER VAL PHE HIS TYR ARG PRO
SEQRES 13 B 672 HIS ASN LEU ILE TYR TYR GLY GLU HIS PRO LEU SER PHE
SEQRES 14 B 672 ALA ALA CYS VAL GLY SER GLU GLU ILE VAL ARG LEU LEU
SEQRES 15 B 672 ILE GLU HIS GLY ALA ASP ILE ARG ALA GLN ASP SER LEU
SEQRES 16 B 672 GLY ASN THR VAL LEU HIS ILE LEU ILE LEU GLN PRO ASN
SEQRES 17 B 672 LYS THR PHE ALA CYS GLN MET TYR ASN LEU LEU LEU SER
SEQRES 18 B 672 TYR ASP GLY GLY ASP HIS LEU LYS SER LEU GLU LEU VAL
SEQRES 19 B 672 PRO ASN ASN GLN GLY LEU THR PRO PHE LYS LEU ALA GLY
SEQRES 20 B 672 VAL GLU GLY ASN ILE VAL MET PHE GLN HIS LEU MET GLN
SEQRES 21 B 672 LYS ARG LYS HIS ILE GLN TRP THR TYR GLY PRO LEU THR
SEQRES 22 B 672 SER THR LEU TYR ASP LEU THR GLU ILE ASP SER SER GLY
SEQRES 23 B 672 ASP ASP GLN SER LEU LEU GLU LEU ILE VAL THR THR LYS
SEQRES 24 B 672 LYS ARG GLU ALA ARG GLN ILE LEU ASP GLN THR PRO VAL
SEQRES 25 B 672 LYS GLU LEU VAL SER LEU LYS TRP LYS ARG TYR GLY ARG
SEQRES 26 B 672 PRO TYR PHE CYS VAL LEU GLY ALA ILE TYR VAL LEU TYR
SEQRES 27 B 672 ILE ILE CYS PHE THR MET CYS CYS VAL TYR ARG PRO LEU
SEQRES 28 B 672 LYS PRO ARG ILE THR ASN ARG THR ASN PRO ARG ASP ASN
SEQRES 29 B 672 THR LEU LEU GLN GLN LYS LEU LEU GLN GLU ALA TYR VAL
SEQRES 30 B 672 THR PRO LYS ASP ASP LEU ARG LEU VAL GLY GLU LEU VAL
SEQRES 31 B 672 SER ILE VAL GLY ALA VAL ILE ILE LEU LEU VAL GLU ILE
SEQRES 32 B 672 PRO ASP ILE PHE ARG LEU GLY VAL THR ARG PHE PHE GLY
SEQRES 33 B 672 GLN THR ILE LEU GLY GLY PRO PHE HIS VAL ILE ILE VAL
SEQRES 34 B 672 THR TYR ALA PHE MET VAL LEU VAL THR MET VAL MET ARG
SEQRES 35 B 672 LEU THR ASN SER ASP GLY GLU VAL VAL PRO MET SER PHE
SEQRES 36 B 672 ALA LEU VAL LEU GLY TRP CYS ASN VAL MET TYR PHE ALA
SEQRES 37 B 672 ARG GLY PHE GLN MET LEU GLY PRO PHE THR ILE MET ILE
SEQRES 38 B 672 GLN LYS MET ILE PHE GLY ASP LEU MET ARG PHE CYS TRP
SEQRES 39 B 672 LEU MET ALA VAL VAL ILE LEU GLY PHE ALA SER ALA PHE
SEQRES 40 B 672 TYR ILE ILE PHE GLN THR GLU ASP PRO ASP GLU LEU GLY
SEQRES 41 B 672 HIS PHE TYR ASP TYR PRO MET ALA LEU PHE SER THR PHE
SEQRES 42 B 672 GLU LEU PHE LEU THR ILE ILE ASP GLY PRO ALA ASN TYR
SEQRES 43 B 672 ASP VAL ASP LEU PRO PHE MET TYR SER ILE THR TYR ALA
SEQRES 44 B 672 ALA PHE ALA ILE ILE ALA THR LEU LEU MET LEU ASN LEU
SEQRES 45 B 672 LEU ILE ALA MET MET GLY ASP THR HIS TRP ARG VAL ALA
SEQRES 46 B 672 HIS GLU ARG ASP GLU LEU TRP ARG ALA GLN VAL VAL ALA
SEQRES 47 B 672 THR THR VAL MET LEU GLU ARG LYS LEU PRO ARG CYS LEU
SEQRES 48 B 672 TRP PRO ARG SER GLY ILE CYS GLY ARG GLU TYR GLY LEU
SEQRES 49 B 672 GLY ASP ARG TRP PHE LEU ARG VAL GLU ASP ARG GLN ASP
SEQRES 50 B 672 LEU ASN ARG GLN ARG ILE ARG ARG TYR ALA GLN ALA PHE
SEQRES 51 B 672 GLN GLN GLN ASP ASP LEU TYR SER GLU ASP LEU GLU LYS
SEQRES 52 B 672 ASP SER GLY GLU LYS LEU VAL PRO ARG
SEQRES 1 C 672 MET GLY TRP SER LEU PRO LYS GLU LYS GLY LEU ILE LEU
SEQRES 2 C 672 CYS LEU TRP ASN LYS PHE CYS ARG TRP PHE HIS ARG ARG
SEQRES 3 C 672 GLU SER TRP ALA GLN SER ARG ASP GLU GLN ASN LEU LEU
SEQRES 4 C 672 GLN GLN LYS ARG ILE TRP GLU SER PRO LEU LEU LEU ALA
SEQRES 5 C 672 ALA LYS GLU ASN ASN VAL GLN ALA LEU TYR LYS LEU LEU
SEQRES 6 C 672 LYS PHE GLU GLY CYS GLU VAL HIS GLN LYS GLY ALA MET
SEQRES 7 C 672 GLY GLU THR ALA LEU HIS ILE ALA ALA LEU TYR ASP ASN
SEQRES 8 C 672 ASN GLU ALA ALA GLN VAL LEU MET GLU ALA ALA PRO GLU
SEQRES 9 C 672 LEU VAL PHE GLU PRO MET THR SER GLU LEU TYR GLU GLY
SEQRES 10 C 672 GLN THR ALA LEU HIS ILE ALA VAL ILE ASN GLN ASN VAL
SEQRES 11 C 672 ASN LEU VAL ARG ALA LEU LEU ALA ARG GLY ALA SER VAL
SEQRES 12 C 672 SER ALA ARG ALA THR GLY SER VAL PHE HIS TYR ARG PRO
SEQRES 13 C 672 HIS ASN LEU ILE TYR TYR GLY GLU HIS PRO LEU SER PHE
SEQRES 14 C 672 ALA ALA CYS VAL GLY SER GLU GLU ILE VAL ARG LEU LEU
SEQRES 15 C 672 ILE GLU HIS GLY ALA ASP ILE ARG ALA GLN ASP SER LEU
SEQRES 16 C 672 GLY ASN THR VAL LEU HIS ILE LEU ILE LEU GLN PRO ASN
SEQRES 17 C 672 LYS THR PHE ALA CYS GLN MET TYR ASN LEU LEU LEU SER
SEQRES 18 C 672 TYR ASP GLY GLY ASP HIS LEU LYS SER LEU GLU LEU VAL
SEQRES 19 C 672 PRO ASN ASN GLN GLY LEU THR PRO PHE LYS LEU ALA GLY
SEQRES 20 C 672 VAL GLU GLY ASN ILE VAL MET PHE GLN HIS LEU MET GLN
SEQRES 21 C 672 LYS ARG LYS HIS ILE GLN TRP THR TYR GLY PRO LEU THR
SEQRES 22 C 672 SER THR LEU TYR ASP LEU THR GLU ILE ASP SER SER GLY
SEQRES 23 C 672 ASP ASP GLN SER LEU LEU GLU LEU ILE VAL THR THR LYS
SEQRES 24 C 672 LYS ARG GLU ALA ARG GLN ILE LEU ASP GLN THR PRO VAL
SEQRES 25 C 672 LYS GLU LEU VAL SER LEU LYS TRP LYS ARG TYR GLY ARG
SEQRES 26 C 672 PRO TYR PHE CYS VAL LEU GLY ALA ILE TYR VAL LEU TYR
SEQRES 27 C 672 ILE ILE CYS PHE THR MET CYS CYS VAL TYR ARG PRO LEU
SEQRES 28 C 672 LYS PRO ARG ILE THR ASN ARG THR ASN PRO ARG ASP ASN
SEQRES 29 C 672 THR LEU LEU GLN GLN LYS LEU LEU GLN GLU ALA TYR VAL
SEQRES 30 C 672 THR PRO LYS ASP ASP LEU ARG LEU VAL GLY GLU LEU VAL
SEQRES 31 C 672 SER ILE VAL GLY ALA VAL ILE ILE LEU LEU VAL GLU ILE
SEQRES 32 C 672 PRO ASP ILE PHE ARG LEU GLY VAL THR ARG PHE PHE GLY
SEQRES 33 C 672 GLN THR ILE LEU GLY GLY PRO PHE HIS VAL ILE ILE VAL
SEQRES 34 C 672 THR TYR ALA PHE MET VAL LEU VAL THR MET VAL MET ARG
SEQRES 35 C 672 LEU THR ASN SER ASP GLY GLU VAL VAL PRO MET SER PHE
SEQRES 36 C 672 ALA LEU VAL LEU GLY TRP CYS ASN VAL MET TYR PHE ALA
SEQRES 37 C 672 ARG GLY PHE GLN MET LEU GLY PRO PHE THR ILE MET ILE
SEQRES 38 C 672 GLN LYS MET ILE PHE GLY ASP LEU MET ARG PHE CYS TRP
SEQRES 39 C 672 LEU MET ALA VAL VAL ILE LEU GLY PHE ALA SER ALA PHE
SEQRES 40 C 672 TYR ILE ILE PHE GLN THR GLU ASP PRO ASP GLU LEU GLY
SEQRES 41 C 672 HIS PHE TYR ASP TYR PRO MET ALA LEU PHE SER THR PHE
SEQRES 42 C 672 GLU LEU PHE LEU THR ILE ILE ASP GLY PRO ALA ASN TYR
SEQRES 43 C 672 ASP VAL ASP LEU PRO PHE MET TYR SER ILE THR TYR ALA
SEQRES 44 C 672 ALA PHE ALA ILE ILE ALA THR LEU LEU MET LEU ASN LEU
SEQRES 45 C 672 LEU ILE ALA MET MET GLY ASP THR HIS TRP ARG VAL ALA
SEQRES 46 C 672 HIS GLU ARG ASP GLU LEU TRP ARG ALA GLN VAL VAL ALA
SEQRES 47 C 672 THR THR VAL MET LEU GLU ARG LYS LEU PRO ARG CYS LEU
SEQRES 48 C 672 TRP PRO ARG SER GLY ILE CYS GLY ARG GLU TYR GLY LEU
SEQRES 49 C 672 GLY ASP ARG TRP PHE LEU ARG VAL GLU ASP ARG GLN ASP
SEQRES 50 C 672 LEU ASN ARG GLN ARG ILE ARG ARG TYR ALA GLN ALA PHE
SEQRES 51 C 672 GLN GLN GLN ASP ASP LEU TYR SER GLU ASP LEU GLU LYS
SEQRES 52 C 672 ASP SER GLY GLU LYS LEU VAL PRO ARG
SEQRES 1 D 672 MET GLY TRP SER LEU PRO LYS GLU LYS GLY LEU ILE LEU
SEQRES 2 D 672 CYS LEU TRP ASN LYS PHE CYS ARG TRP PHE HIS ARG ARG
SEQRES 3 D 672 GLU SER TRP ALA GLN SER ARG ASP GLU GLN ASN LEU LEU
SEQRES 4 D 672 GLN GLN LYS ARG ILE TRP GLU SER PRO LEU LEU LEU ALA
SEQRES 5 D 672 ALA LYS GLU ASN ASN VAL GLN ALA LEU TYR LYS LEU LEU
SEQRES 6 D 672 LYS PHE GLU GLY CYS GLU VAL HIS GLN LYS GLY ALA MET
SEQRES 7 D 672 GLY GLU THR ALA LEU HIS ILE ALA ALA LEU TYR ASP ASN
SEQRES 8 D 672 ASN GLU ALA ALA GLN VAL LEU MET GLU ALA ALA PRO GLU
SEQRES 9 D 672 LEU VAL PHE GLU PRO MET THR SER GLU LEU TYR GLU GLY
SEQRES 10 D 672 GLN THR ALA LEU HIS ILE ALA VAL ILE ASN GLN ASN VAL
SEQRES 11 D 672 ASN LEU VAL ARG ALA LEU LEU ALA ARG GLY ALA SER VAL
SEQRES 12 D 672 SER ALA ARG ALA THR GLY SER VAL PHE HIS TYR ARG PRO
SEQRES 13 D 672 HIS ASN LEU ILE TYR TYR GLY GLU HIS PRO LEU SER PHE
SEQRES 14 D 672 ALA ALA CYS VAL GLY SER GLU GLU ILE VAL ARG LEU LEU
SEQRES 15 D 672 ILE GLU HIS GLY ALA ASP ILE ARG ALA GLN ASP SER LEU
SEQRES 16 D 672 GLY ASN THR VAL LEU HIS ILE LEU ILE LEU GLN PRO ASN
SEQRES 17 D 672 LYS THR PHE ALA CYS GLN MET TYR ASN LEU LEU LEU SER
SEQRES 18 D 672 TYR ASP GLY GLY ASP HIS LEU LYS SER LEU GLU LEU VAL
SEQRES 19 D 672 PRO ASN ASN GLN GLY LEU THR PRO PHE LYS LEU ALA GLY
SEQRES 20 D 672 VAL GLU GLY ASN ILE VAL MET PHE GLN HIS LEU MET GLN
SEQRES 21 D 672 LYS ARG LYS HIS ILE GLN TRP THR TYR GLY PRO LEU THR
SEQRES 22 D 672 SER THR LEU TYR ASP LEU THR GLU ILE ASP SER SER GLY
SEQRES 23 D 672 ASP ASP GLN SER LEU LEU GLU LEU ILE VAL THR THR LYS
SEQRES 24 D 672 LYS ARG GLU ALA ARG GLN ILE LEU ASP GLN THR PRO VAL
SEQRES 25 D 672 LYS GLU LEU VAL SER LEU LYS TRP LYS ARG TYR GLY ARG
SEQRES 26 D 672 PRO TYR PHE CYS VAL LEU GLY ALA ILE TYR VAL LEU TYR
SEQRES 27 D 672 ILE ILE CYS PHE THR MET CYS CYS VAL TYR ARG PRO LEU
SEQRES 28 D 672 LYS PRO ARG ILE THR ASN ARG THR ASN PRO ARG ASP ASN
SEQRES 29 D 672 THR LEU LEU GLN GLN LYS LEU LEU GLN GLU ALA TYR VAL
SEQRES 30 D 672 THR PRO LYS ASP ASP LEU ARG LEU VAL GLY GLU LEU VAL
SEQRES 31 D 672 SER ILE VAL GLY ALA VAL ILE ILE LEU LEU VAL GLU ILE
SEQRES 32 D 672 PRO ASP ILE PHE ARG LEU GLY VAL THR ARG PHE PHE GLY
SEQRES 33 D 672 GLN THR ILE LEU GLY GLY PRO PHE HIS VAL ILE ILE VAL
SEQRES 34 D 672 THR TYR ALA PHE MET VAL LEU VAL THR MET VAL MET ARG
SEQRES 35 D 672 LEU THR ASN SER ASP GLY GLU VAL VAL PRO MET SER PHE
SEQRES 36 D 672 ALA LEU VAL LEU GLY TRP CYS ASN VAL MET TYR PHE ALA
SEQRES 37 D 672 ARG GLY PHE GLN MET LEU GLY PRO PHE THR ILE MET ILE
SEQRES 38 D 672 GLN LYS MET ILE PHE GLY ASP LEU MET ARG PHE CYS TRP
SEQRES 39 D 672 LEU MET ALA VAL VAL ILE LEU GLY PHE ALA SER ALA PHE
SEQRES 40 D 672 TYR ILE ILE PHE GLN THR GLU ASP PRO ASP GLU LEU GLY
SEQRES 41 D 672 HIS PHE TYR ASP TYR PRO MET ALA LEU PHE SER THR PHE
SEQRES 42 D 672 GLU LEU PHE LEU THR ILE ILE ASP GLY PRO ALA ASN TYR
SEQRES 43 D 672 ASP VAL ASP LEU PRO PHE MET TYR SER ILE THR TYR ALA
SEQRES 44 D 672 ALA PHE ALA ILE ILE ALA THR LEU LEU MET LEU ASN LEU
SEQRES 45 D 672 LEU ILE ALA MET MET GLY ASP THR HIS TRP ARG VAL ALA
SEQRES 46 D 672 HIS GLU ARG ASP GLU LEU TRP ARG ALA GLN VAL VAL ALA
SEQRES 47 D 672 THR THR VAL MET LEU GLU ARG LYS LEU PRO ARG CYS LEU
SEQRES 48 D 672 TRP PRO ARG SER GLY ILE CYS GLY ARG GLU TYR GLY LEU
SEQRES 49 D 672 GLY ASP ARG TRP PHE LEU ARG VAL GLU ASP ARG GLN ASP
SEQRES 50 D 672 LEU ASN ARG GLN ARG ILE ARG ARG TYR ALA GLN ALA PHE
SEQRES 51 D 672 GLN GLN GLN ASP ASP LEU TYR SER GLU ASP LEU GLU LYS
SEQRES 52 D 672 ASP SER GLY GLU LYS LEU VAL PRO ARG
HELIX 1 AA1 TRP A 29 ARG A 43 1 15
HELIX 2 AA2 PRO A 48 ASN A 56 1 9
HELIX 3 AA3 ASN A 57 LEU A 64 1 8
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 129 GLY A 140 1 12
HELIX 8 AA8 HIS A 165 ALA A 171 1 7
HELIX 9 AA9 SER A 175 HIS A 185 1 11
HELIX 10 AB1 THR A 198 LEU A 205 1 8
HELIX 11 AB2 PHE A 211 TYR A 222 1 12
HELIX 12 AB3 THR A 241 GLY A 250 1 10
HELIX 13 AB4 ASN A 251 GLN A 260 1 10
HELIX 14 AB5 SER A 290 VAL A 296 1 7
HELIX 15 AB6 ARG A 301 ASP A 308 5 8
HELIX 16 AB7 GLN A 309 GLY A 324 1 16
HELIX 17 AB8 GLY A 324 TYR A 348 1 25
HELIX 18 AB9 ASP A 381 PHE A 407 1 27
HELIX 19 AC1 ARG A 408 GLY A 410 5 3
HELIX 20 AC2 PHE A 424 ARG A 442 1 19
HELIX 21 AC3 GLU A 449 ASN A 463 1 15
HELIX 22 AC4 VAL A 464 ARG A 469 5 6
HELIX 23 AC5 LEU A 474 PHE A 486 1 13
HELIX 24 AC6 LEU A 489 PHE A 511 1 23
HELIX 25 AC7 GLN A 512 GLU A 514 5 3
HELIX 26 AC8 ASP A 524 LEU A 537 1 14
HELIX 27 AC9 PRO A 551 ASP A 579 1 29
HELIX 28 AD1 ARG A 588 LEU A 607 1 20
HELIX 29 AD2 TRP B 29 ARG B 43 1 15
HELIX 30 AD3 PRO B 48 ASN B 56 1 9
HELIX 31 AD4 ASN B 57 LEU B 64 1 8
HELIX 32 AD5 THR B 81 TYR B 89 1 9
HELIX 33 AD6 ASN B 91 ALA B 102 1 12
HELIX 34 AD7 THR B 119 ASN B 127 1 9
HELIX 35 AD8 ASN B 129 GLY B 140 1 12
HELIX 36 AD9 HIS B 165 ALA B 171 1 7
HELIX 37 AE1 SER B 175 HIS B 185 1 11
HELIX 38 AE2 THR B 198 LEU B 205 1 8
HELIX 39 AE3 PHE B 211 TYR B 222 1 12
HELIX 40 AE4 THR B 241 GLY B 250 1 10
HELIX 41 AE5 ASN B 251 GLN B 260 1 10
HELIX 42 AE6 SER B 290 VAL B 296 1 7
HELIX 43 AE7 ARG B 301 ASP B 308 5 8
HELIX 44 AE8 GLN B 309 GLY B 324 1 16
HELIX 45 AE9 GLY B 324 TYR B 348 1 25
HELIX 46 AF1 ASP B 381 PHE B 407 1 27
HELIX 47 AF2 ARG B 408 GLY B 410 5 3
HELIX 48 AF3 PHE B 424 ARG B 442 1 19
HELIX 49 AF4 GLU B 449 ASN B 463 1 15
HELIX 50 AF5 VAL B 464 ARG B 469 5 6
HELIX 51 AF6 LEU B 474 PHE B 486 1 13
HELIX 52 AF7 LEU B 489 PHE B 511 1 23
HELIX 53 AF8 GLN B 512 GLU B 514 5 3
HELIX 54 AF9 ASP B 524 LEU B 537 1 14
HELIX 55 AG1 PRO B 551 ASP B 579 1 29
HELIX 56 AG2 ARG B 588 LEU B 607 1 20
HELIX 57 AG3 TRP C 29 ARG C 43 1 15
HELIX 58 AG4 PRO C 48 ASN C 56 1 9
HELIX 59 AG5 ASN C 57 LEU C 64 1 8
HELIX 60 AG6 THR C 81 TYR C 89 1 9
HELIX 61 AG7 ASN C 91 ALA C 102 1 12
HELIX 62 AG8 THR C 119 ASN C 127 1 9
HELIX 63 AG9 ASN C 129 GLY C 140 1 12
HELIX 64 AH1 HIS C 165 ALA C 171 1 7
HELIX 65 AH2 SER C 175 HIS C 185 1 11
HELIX 66 AH3 THR C 198 LEU C 205 1 8
HELIX 67 AH4 PHE C 211 TYR C 222 1 12
HELIX 68 AH5 THR C 241 GLY C 250 1 10
HELIX 69 AH6 ASN C 251 GLN C 260 1 10
HELIX 70 AH7 SER C 290 VAL C 296 1 7
HELIX 71 AH8 ARG C 301 ASP C 308 5 8
HELIX 72 AH9 GLN C 309 GLY C 324 1 16
HELIX 73 AI1 GLY C 324 TYR C 348 1 25
HELIX 74 AI2 ASP C 381 PHE C 407 1 27
HELIX 75 AI3 ARG C 408 GLY C 410 5 3
HELIX 76 AI4 PHE C 424 ARG C 442 1 19
HELIX 77 AI5 GLU C 449 ASN C 463 1 15
HELIX 78 AI6 VAL C 464 ARG C 469 5 6
HELIX 79 AI7 LEU C 474 PHE C 486 1 13
HELIX 80 AI8 LEU C 489 PHE C 511 1 23
HELIX 81 AI9 GLN C 512 GLU C 514 5 3
HELIX 82 AJ1 ASP C 524 LEU C 537 1 14
HELIX 83 AJ2 PRO C 551 ASP C 579 1 29
HELIX 84 AJ3 ARG C 588 LEU C 607 1 20
HELIX 85 AJ4 TRP D 29 ARG D 43 1 15
HELIX 86 AJ5 PRO D 48 ASN D 56 1 9
HELIX 87 AJ6 ASN D 57 LEU D 64 1 8
HELIX 88 AJ7 THR D 81 TYR D 89 1 9
HELIX 89 AJ8 ASN D 91 ALA D 102 1 12
HELIX 90 AJ9 THR D 119 ASN D 127 1 9
HELIX 91 AK1 ASN D 129 GLY D 140 1 12
HELIX 92 AK2 HIS D 165 ALA D 171 1 7
HELIX 93 AK3 SER D 175 HIS D 185 1 11
HELIX 94 AK4 THR D 198 LEU D 205 1 8
HELIX 95 AK5 PHE D 211 TYR D 222 1 12
HELIX 96 AK6 THR D 241 GLY D 250 1 10
HELIX 97 AK7 ASN D 251 GLN D 260 1 10
HELIX 98 AK8 SER D 290 VAL D 296 1 7
HELIX 99 AK9 ARG D 301 ASP D 308 5 8
HELIX 100 AL1 GLN D 309 GLY D 324 1 16
HELIX 101 AL2 GLY D 324 TYR D 348 1 25
HELIX 102 AL3 ASP D 381 PHE D 407 1 27
HELIX 103 AL4 ARG D 408 GLY D 410 5 3
HELIX 104 AL5 PHE D 424 ARG D 442 1 19
HELIX 105 AL6 GLU D 449 ASN D 463 1 15
HELIX 106 AL7 VAL D 464 ARG D 469 5 6
HELIX 107 AL8 LEU D 474 PHE D 486 1 13
HELIX 108 AL9 LEU D 489 PHE D 511 1 23
HELIX 109 AM1 GLN D 512 GLU D 514 5 3
HELIX 110 AM2 ASP D 524 LEU D 537 1 14
HELIX 111 AM3 PRO D 551 ASP D 579 1 29
HELIX 112 AM4 ARG D 588 LEU D 607 1 20
SHEET 1 AA1 3 LYS A 263 TYR A 269 0
SHEET 2 AA1 3 LEU A 272 TYR A 277 -1 O LEU A 272 N TYR A 269
SHEET 3 AA1 3 LEU A 630 ASP A 634 -1 O VAL A 632 N THR A 275
SHEET 1 AA2 3 LYS B 263 TYR B 269 0
SHEET 2 AA2 3 LEU B 272 TYR B 277 -1 O LEU B 272 N TYR B 269
SHEET 3 AA2 3 LEU B 630 ASP B 634 -1 O VAL B 632 N THR B 275
SHEET 1 AA3 3 LYS C 263 TYR C 269 0
SHEET 2 AA3 3 LEU C 272 TYR C 277 -1 O LEU C 272 N TYR C 269
SHEET 3 AA3 3 LEU C 630 ASP C 634 -1 O VAL C 632 N THR C 275
SHEET 1 AA4 3 LYS D 263 TYR D 269 0
SHEET 2 AA4 3 LEU D 272 TYR D 277 -1 O LEU D 272 N TYR D 269
SHEET 3 AA4 3 LEU D 630 ASP D 634 -1 O VAL D 632 N THR D 275
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
