HEADER TRANSPORT PROTEIN 22-MAR-16 5IWP
TITLE STRUCTURE OF TRANSIENT RECEPTOR POTENTIAL (TRP) CHANNEL TRPV6 IN THE
TITLE 2 PRESENCE OF CALCIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY V
COMPND 3 MEMBER 6;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: TRPV6,CALCIUM TRANSPORT PROTEIN 1,CAT1,EPITHELIAL CALCIUM
COMPND 6 CHANNEL 2,ECAC2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: 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 TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SAOTOME,A.K.SINGH,M.V.YELSHANSKAYA,A.I.SOBOLEVSKY
REVDAT 6 27-SEP-23 5IWP 1 REMARK
REVDAT 5 18-DEC-19 5IWP 1 REMARK
REVDAT 4 20-SEP-17 5IWP 1 REMARK
REVDAT 3 06-JUL-16 5IWP 1 REMARK
REVDAT 2 29-JUN-16 5IWP 1 JRNL
REVDAT 1 15-JUN-16 5IWP 0
JRNL AUTH K.SAOTOME,A.K.SINGH,M.V.YELSHANSKAYA,A.I.SOBOLEVSKY
JRNL TITL CRYSTAL STRUCTURE OF THE EPITHELIAL CALCIUM CHANNEL TRPV6.
JRNL REF NATURE V. 534 506 2016
JRNL REFN ESSN 1476-4687
JRNL PMID 27296226
JRNL DOI 10.1038/NATURE17975
REMARK 2
REMARK 2 RESOLUTION. 3.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.56
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 25414
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.273
REMARK 3 R VALUE (WORKING SET) : 0.273
REMARK 3 FREE R VALUE : 0.283
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1265
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.5605 - 7.5843 1.00 2675 136 0.2542 0.2401
REMARK 3 2 7.5843 - 6.0232 1.00 2706 146 0.2638 0.3227
REMARK 3 3 6.0232 - 5.2628 1.00 2664 142 0.2855 0.3400
REMARK 3 4 5.2628 - 4.7821 1.00 2713 142 0.2544 0.2630
REMARK 3 5 4.7821 - 4.4396 1.00 2676 143 0.2538 0.2500
REMARK 3 6 4.4396 - 4.1779 1.00 2665 135 0.2786 0.2725
REMARK 3 7 4.1779 - 3.9688 1.00 2704 142 0.3104 0.3168
REMARK 3 8 3.9688 - 3.7961 1.00 2671 144 0.3318 0.3143
REMARK 3 9 3.7961 - 3.6500 0.99 2675 135 0.3765 0.4109
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.540
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 4839
REMARK 3 ANGLE : 1.035 6572
REMARK 3 CHIRALITY : 0.038 749
REMARK 3 PLANARITY : 0.005 832
REMARK 3 DIHEDRAL : 14.718 1762
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5IWP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219571.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0-8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.75
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25439
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.650
REMARK 200 RESOLUTION RANGE LOW (A) : 49.560
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 26.50
REMARK 200 R MERGE (I) : 0.01000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 17.20
REMARK 200 R MERGE FOR SHELL (I) : 1.43100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2RFA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-24% PEG 350 MME, 50 MM NACL, AND 50
REMARK 280 MM TRIS-HCL PH 8.0-8.5, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 72.17500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 72.17500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 72.17500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 72.17500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 72.17500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 72.17500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 72.17500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 72.17500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 109600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -153.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 -144.35000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 -72.17500
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 72.17500
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 -72.17500
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 -72.17500
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CA CA A 701 LIES ON A SPECIAL POSITION.
REMARK 375 CA CA A 702 LIES ON A SPECIAL POSITION.
REMARK 375 CA CA A 703 LIES ON A SPECIAL POSITION.
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 LEU A 409
REMARK 465 GLY A 410
REMARK 465 VAL A 411
REMARK 465 THR A 412
REMARK 465 ARG A 413
REMARK 465 PHE A 414
REMARK 465 PHE A 415
REMARK 465 GLY A 416
REMARK 465 PHE A 471
REMARK 465 GLN A 472
REMARK 465 MET A 473
REMARK 465 LEU A 474
REMARK 465 GLY A 475
REMARK 465 PRO A 476
REMARK 465 PHE A 477
REMARK 465 THR A 478
REMARK 465 ILE A 479
REMARK 465 MET A 480
REMARK 465 ILE A 481
REMARK 465 GLN A 482
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 362 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 370 CG CD CE NZ
REMARK 470 ASP A 637 CG OD1 OD2
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 O GLY A 619 O LEU A 624 1.26
REMARK 500 C GLY A 619 O LEU A 624 2.08
REMARK 500 O PRO A 543 OH TYR A 554 2.15
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 PHE A 67 CB - CA - C ANGL. DEV. = 13.7 DEGREES
REMARK 500 PHE A 67 N - CA - C ANGL. DEV. = -21.0 DEGREES
REMARK 500 GLU A 68 N - CA - CB ANGL. DEV. = 12.0 DEGREES
REMARK 500 GLU A 68 N - CA - C ANGL. DEV. = -23.9 DEGREES
REMARK 500 THR A 359 N - CA - CB ANGL. DEV. = 16.0 DEGREES
REMARK 500 THR A 359 N - CA - C ANGL. DEV. = -18.9 DEGREES
REMARK 500 ALA A 375 N - CA - C ANGL. DEV. = -18.4 DEGREES
REMARK 500 THR A 378 N - CA - CB ANGL. DEV. = -12.6 DEGREES
REMARK 500 THR A 378 N - CA - C ANGL. DEV. = 17.6 DEGREES
REMARK 500 ARG A 442 NE - CZ - NH2 ANGL. DEV. = -3.4 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 GLU A 71 105.60 -59.43
REMARK 500 HIS A 73 31.15 -83.37
REMARK 500 MET A 78 30.48 -94.02
REMARK 500 ASP A 90 106.14 -57.12
REMARK 500 ALA A 102 80.87 -158.83
REMARK 500 ASN A 208 85.19 -69.65
REMARK 500 TYR A 269 79.78 -113.99
REMARK 500 THR A 280 -69.88 -100.29
REMARK 500 SER A 290 137.87 -175.60
REMARK 500 TYR A 323 -55.60 66.93
REMARK 500 TYR A 348 63.41 -115.56
REMARK 500 PRO A 353 178.61 -57.19
REMARK 500 ILE A 355 -54.66 71.00
REMARK 500 GLN A 368 64.44 -103.53
REMARK 500 ALA A 375 145.11 -179.93
REMARK 500 TYR A 376 -90.26 -58.85
REMARK 500 VAL A 377 14.84 89.42
REMARK 500 PRO A 379 -91.00 -117.64
REMARK 500 PRO A 423 33.92 -83.44
REMARK 500 THR A 444 -9.34 -142.79
REMARK 500 THR A 538 18.71 56.58
REMARK 500 ASP A 541 4.11 -66.58
REMARK 500 PRO A 543 108.06 -56.39
REMARK 500 ARG A 583 18.02 -69.39
REMARK 500 TRP A 612 77.84 57.93
REMARK 500 GLU A 621 75.78 43.76
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 LEU A 351 LYS A 352 32.89
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 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 541 OD2
REMARK 620 2 ASP A 541 OD2 0.0
REMARK 620 N 1
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 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DTB A 704
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5IWK RELATED DB: PDB
REMARK 900 RELATED ID: 5IWR RELATED DB: PDB
REMARK 900 RELATED ID: 5IWT RELATED DB: PDB
DBREF 5IWP A 1 669 UNP Q9R186 TRPV6_RAT 41 709
SEQADV 5IWP TYR A 62 UNP Q9R186 ILE 102 ENGINEERED MUTATION
SEQADV 5IWP ASN A 92 UNP Q9R186 LEU 132 ENGINEERED MUTATION
SEQADV 5IWP GLN A 96 UNP Q9R186 MET 136 ENGINEERED MUTATION
SEQADV 5IWP GLN A 495 UNP Q9R186 LEU 535 ENGINEERED MUTATION
SEQADV 5IWP VAL A 670 UNP Q9R186 EXPRESSION TAG
SEQADV 5IWP PRO A 671 UNP Q9R186 EXPRESSION TAG
SEQADV 5IWP ARG A 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 GLN 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
HET CA A 701 1
HET CA A 702 1
HET CA A 703 1
HET DTB A 704 15
HETNAM CA CALCIUM ION
HETNAM DTB 6-(5-METHYL-2-OXO-IMIDAZOLIDIN-4-YL)-HEXANOIC ACID
HETSYN DTB D-DESTHIOBIOTIN
FORMUL 2 CA 3(CA 2+)
FORMUL 5 DTB C10 H18 N2 O3
HELIX 1 AA1 TRP A 29 SER A 47 1 19
HELIX 2 AA2 SER A 47 ASN A 56 1 10
HELIX 3 AA3 ASN A 57 LYS A 66 1 10
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 PRO A 103 PHE A 107 5 5
HELIX 7 AA7 THR A 119 ASN A 127 1 9
HELIX 8 AA8 ASN A 129 GLY A 140 1 12
HELIX 9 AA9 HIS A 165 GLY A 174 1 10
HELIX 10 AB1 SER A 175 HIS A 185 1 11
HELIX 11 AB2 THR A 198 LEU A 205 1 8
HELIX 12 AB3 ASN A 208 TYR A 222 1 15
HELIX 13 AB4 SER A 230 VAL A 234 5 5
HELIX 14 AB5 THR A 241 GLY A 250 1 10
HELIX 15 AB6 ASN A 251 LYS A 261 1 11
HELIX 16 AB7 SER A 290 THR A 297 1 8
HELIX 17 AB8 LYS A 300 GLN A 309 5 10
HELIX 18 AB9 VAL A 312 ARG A 322 1 11
HELIX 19 AC1 TYR A 323 TYR A 348 1 26
HELIX 20 AC2 LYS A 380 PHE A 407 1 28
HELIX 21 AC3 PRO A 423 ARG A 442 1 20
HELIX 22 AC4 GLU A 449 CYS A 462 1 14
HELIX 23 AC5 VAL A 464 GLY A 470 5 7
HELIX 24 AC6 MET A 484 THR A 513 1 30
HELIX 25 AC7 ASP A 524 LEU A 537 1 14
HELIX 26 AC8 MET A 553 GLY A 578 1 26
HELIX 27 AC9 ARG A 583 LEU A 607 1 25
SHEET 1 AA1 4 LYS A 263 TYR A 269 0
SHEET 2 AA1 4 LEU A 272 TYR A 277 -1 O LEU A 276 N HIS A 264
SHEET 3 AA1 4 TRP A 628 ARG A 635 -1 O VAL A 632 N THR A 275
SHEET 4 AA1 4 ILE A 617 CYS A 618 -1 N ILE A 617 O PHE A 629
LINK OD2 ASP A 541 CA CA A 701 1555 1555 2.61
LINK OD2 ASP A 541 CA CA A 701 1555 4445 2.61
CISPEP 1 GLU A 27 SER A 28 0 -0.45
CISPEP 2 PHE A 67 GLU A 68 0 1.36
CISPEP 3 SER A 284 SER A 285 0 3.23
CISPEP 4 SER A 285 GLY A 286 0 1.67
CISPEP 5 GLY A 286 ASP A 287 0 -3.46
CISPEP 6 LEU A 372 GLN A 373 0 17.71
CISPEP 7 GLN A 373 GLU A 374 0 -10.63
CISPEP 8 ALA A 375 TYR A 376 0 7.03
CISPEP 9 LEU A 420 GLY A 421 0 3.32
CISPEP 10 GLU A 621 TYR A 622 0 11.53
CISPEP 11 GLY A 625 ASP A 626 0 -13.03
SITE 1 AC1 1 ASP A 541
SITE 1 AC2 8 GLN A 40 LEU A 88 TYR A 115 VAL A 151
SITE 2 AC2 8 TRP A 267 TYR A 269 LEU A 272 GLU A 633
CRYST1 144.350 144.350 113.370 90.00 90.00 90.00 P 4 21 2 8
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 0.006928 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006928 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008821 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
