HEADER CALCIUM-BINDING PROTEIN 11-JUL-11 3SUI
TITLE CRYSTAL STRUCTURE OF CA2+-CALMODULIN IN COMPLEX WITH A TRPV1 C-
TITLE 2 TERMINAL PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CAM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY V
COMPND 8 MEMBER 1;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 767-801;
COMPND 11 SYNONYM: TRPV1, CAPSAICIN RECEPTOR, OSM-9-LIKE TRP CHANNEL 1, OTRPC1,
COMPND 12 VANILLOID RECEPTOR 1, VANILLOID RECEPTOR TYPE 1-LIKE;
COMPND 13 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: CALM, CALM1, CALM2, CALM3, CALML2, CAM, CAM1, CAM2, CAM3,
SOURCE 6 CAMB, CAMC, CAMIII;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET21;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 14 ORGANISM_COMMON: RAT;
SOURCE 15 ORGANISM_TAXID: 10116;
SOURCE 16 GENE: TRPV1, VR1, VR1L;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PMALC2
KEYWDS CALMODULIN, CALCIUM-CALMODULIN, TRPV1, TRPV1 C-TERMINUS, CALMODULIN
KEYWDS 2 COMPLEX, THERMOSENSOR, TRP CHANNEL, EF HANDS, 1-10 MOTIF, CALCIUM
KEYWDS 3 CHANNEL, CALMODULIN-BINDING, ION CHANNEL, CALCIUM BINDING PROTEIN,
KEYWDS 4 CALCIUM-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.-Y.LAU,R.GAUDET
REVDAT 4 13-SEP-23 3SUI 1 REMARK SEQADV LINK
REVDAT 3 08-NOV-17 3SUI 1 REMARK
REVDAT 2 14-NOV-12 3SUI 1 JRNL
REVDAT 1 12-SEP-12 3SUI 0
JRNL AUTH S.Y.LAU,E.PROCKO,R.GAUDET
JRNL TITL DISTINCT PROPERTIES OF CA2+-CALMODULIN BINDING TO N- AND
JRNL TITL 2 C-TERMINAL REGULATORY REGIONS OF THE TRPV1 CHANNEL.
JRNL REF J.GEN.PHYSIOL. V. 140 541 2012
JRNL REFN ISSN 0022-1295
JRNL PMID 23109716
JRNL DOI 10.1085/JGP.201210810
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 13172
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 690
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 885
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.2570
REMARK 3 BIN FREE R VALUE SET COUNT : 47
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1268
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 91
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.98
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.47000
REMARK 3 B22 (A**2) : 0.47000
REMARK 3 B33 (A**2) : -0.70000
REMARK 3 B12 (A**2) : 0.23000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.168
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.164
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.173
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1372 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1866 ; 1.519 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 182 ; 4.707 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 81 ;36.926 ;26.296
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 256 ;16.447 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;19.427 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 202 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1077 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 830 ; 0.972 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1341 ; 1.728 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 542 ; 2.525 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 513 ; 4.141 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 80
REMARK 3 RESIDUE RANGE : A 501 A 502
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9420 -25.8990 -17.7520
REMARK 3 T TENSOR
REMARK 3 T11: 0.3192 T22: 0.1938
REMARK 3 T33: 0.0356 T12: 0.0009
REMARK 3 T13: 0.0272 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 2.3932 L22: 3.2130
REMARK 3 L33: 5.9637 L12: -1.1152
REMARK 3 L13: 1.2655 L23: -1.8376
REMARK 3 S TENSOR
REMARK 3 S11: 0.1125 S12: 0.1300 S13: -0.0104
REMARK 3 S21: -0.2230 S22: -0.0082 S23: -0.0218
REMARK 3 S31: 0.2080 S32: -0.2905 S33: -0.1043
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 81 A 148
REMARK 3 RESIDUE RANGE : A 503 A 504
REMARK 3 ORIGIN FOR THE GROUP (A): -12.4150 -9.6580 -6.2110
REMARK 3 T TENSOR
REMARK 3 T11: 0.3531 T22: 0.1727
REMARK 3 T33: 0.0478 T12: -0.0116
REMARK 3 T13: 0.0095 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 3.2946 L22: 3.7392
REMARK 3 L33: 2.6175 L12: -1.8878
REMARK 3 L13: -0.4618 L23: 0.0066
REMARK 3 S TENSOR
REMARK 3 S11: 0.0013 S12: 0.1104 S13: -0.0225
REMARK 3 S21: -0.1786 S22: -0.0292 S23: -0.1591
REMARK 3 S31: 0.1166 S32: 0.0833 S33: 0.0279
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 784 B 798
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3290 -17.9790 -12.6830
REMARK 3 T TENSOR
REMARK 3 T11: 0.3192 T22: 0.2687
REMARK 3 T33: 0.0575 T12: 0.0318
REMARK 3 T13: 0.0243 T23: -0.0702
REMARK 3 L TENSOR
REMARK 3 L11: 11.4538 L22: 30.8631
REMARK 3 L33: 13.1870 L12: 0.7982
REMARK 3 L13: -1.6430 L23: 0.5393
REMARK 3 S TENSOR
REMARK 3 S11: 0.1270 S12: 0.2760 S13: -0.1402
REMARK 3 S21: -0.8867 S22: -0.2584 S23: 0.2787
REMARK 3 S31: -0.0152 S32: -0.2764 S33: 0.1314
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3SUI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066667.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.97949
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13862
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.46900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3DVE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH6.0, 2.2-2.8M AMMONIUM
REMARK 280 SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.84433
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 227.68867
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 170.76650
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 284.61083
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 56.92217
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 113.84433
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 227.68867
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 284.61083
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 170.76650
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 56.92217
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 0
REMARK 465 ALA A 1
REMARK 465 ASP A 2
REMARK 465 GLY B 765
REMARK 465 PRO B 766
REMARK 465 GLU B 767
REMARK 465 GLY B 768
REMARK 465 VAL B 769
REMARK 465 LYS B 770
REMARK 465 ARG B 771
REMARK 465 THR B 772
REMARK 465 LEU B 773
REMARK 465 SER B 774
REMARK 465 PHE B 775
REMARK 465 SER B 776
REMARK 465 LEU B 777
REMARK 465 ARG B 778
REMARK 465 SER B 779
REMARK 465 GLY B 780
REMARK 465 ARG B 781
REMARK 465 VAL B 782
REMARK 465 SER B 783
REMARK 465 ALA B 799
REMARK 465 SER B 800
REMARK 465 THR B 801
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 GLU A 7 CG CD OE1 OE2
REMARK 470 LYS A 148 CG CD CE NZ
REMARK 470 ASP B 798 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 OD1 ASN A 53 O HOH A 234 2.02
REMARK 500 OE2 GLU A 139 O HOH A 227 2.05
REMARK 500 OE2 GLU A 123 NH1 ARG A 126 2.09
REMARK 500 OD1 ASN A 53 O HOH A 235 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP B 787 CB TRP B 787 CG 0.139
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 TRP B 787 CA - CB - CG ANGL. DEV. = 13.8 DEGREES
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 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD1 75.9
REMARK 620 3 ASP A 24 OD2 83.1 79.6
REMARK 620 4 THR A 26 O 83.8 153.8 81.7
REMARK 620 5 GLU A 31 OE2 94.3 76.1 155.4 122.5
REMARK 620 6 GLU A 31 OE1 117.2 126.8 148.5 77.2 52.8
REMARK 620 7 HOH A 195 O 157.6 81.8 90.3 116.5 82.9 78.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD2
REMARK 620 2 ASP A 58 OD2 82.3
REMARK 620 3 ASN A 60 OD1 87.0 78.6
REMARK 620 4 THR A 62 O 90.6 156.9 79.1
REMARK 620 5 GLU A 67 OE1 109.4 122.9 153.7 80.2
REMARK 620 6 GLU A 67 OE2 90.6 73.4 152.0 128.9 51.5
REMARK 620 7 HOH A 175 O 159.3 77.8 83.4 105.5 86.6 89.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD2
REMARK 620 2 ASP A 95 OD1 84.9
REMARK 620 3 ASN A 97 OD1 90.2 75.1
REMARK 620 4 TYR A 99 O 90.4 156.5 82.0
REMARK 620 5 GLU A 104 OE2 99.9 126.4 156.7 77.1
REMARK 620 6 GLU A 104 OE1 95.2 73.8 147.7 129.6 52.6
REMARK 620 7 HOH A 166 O 166.2 81.4 84.5 101.4 89.8 82.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD2
REMARK 620 2 ASP A 131 OD1 81.8
REMARK 620 3 ASP A 133 OD2 92.5 78.2
REMARK 620 4 GLN A 135 O 86.7 154.5 79.7
REMARK 620 5 GLU A 140 OE1 110.0 124.1 149.5 81.2
REMARK 620 6 GLU A 140 OE2 85.7 77.1 155.2 124.7 51.1
REMARK 620 7 HOH A 159 O 165.7 84.7 80.0 103.8 81.6 96.0
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 149
DBREF 3SUI A 0 148 UNP P62158 CALM_HUMAN 1 149
DBREF 3SUI B 767 801 UNP O35433 TRPV1_RAT 767 801
SEQADV 3SUI GLY B 765 UNP O35433 EXPRESSION TAG
SEQADV 3SUI PRO B 766 UNP O35433 EXPRESSION TAG
SEQRES 1 A 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 A 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 A 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 A 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 A 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 A 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 A 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 A 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 A 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 A 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 A 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 A 149 GLN MET MET THR ALA LYS
SEQRES 1 B 37 GLY PRO GLU GLY VAL LYS ARG THR LEU SER PHE SER LEU
SEQRES 2 B 37 ARG SER GLY ARG VAL SER GLY ARG ASN TRP LYS ASN PHE
SEQRES 3 B 37 ALA LEU VAL PRO LEU LEU ARG ASP ALA SER THR
HET CA A 501 1
HET CA A 502 1
HET CA A 503 1
HET CA A 504 1
HET SO4 A 149 5
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
FORMUL 3 CA 4(CA 2+)
FORMUL 7 SO4 O4 S 2-
FORMUL 8 HOH *91(H2 O)
HELIX 1 1 THR A 5 ASP A 20 1 16
HELIX 2 2 THR A 28 LEU A 39 1 12
HELIX 3 3 THR A 44 GLU A 54 1 11
HELIX 4 4 ASP A 64 THR A 79 1 16
HELIX 5 5 SER A 81 ASP A 93 1 13
HELIX 6 6 SER A 101 GLY A 113 1 13
HELIX 7 7 THR A 117 ASP A 129 1 13
HELIX 8 8 TYR A 138 ALA A 147 1 10
HELIX 9 9 TRP B 787 VAL B 793 1 7
HELIX 10 10 PRO B 794 LEU B 796 5 3
SHEET 1 A 2 TYR A 99 ILE A 100 0
SHEET 2 A 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
LINK OD1 ASP A 20 CA CA A 501 1555 1555 2.37
LINK OD1 ASP A 22 CA CA A 501 1555 1555 2.51
LINK OD2 ASP A 24 CA CA A 501 1555 1555 2.42
LINK O THR A 26 CA CA A 501 1555 1555 2.30
LINK OE2 GLU A 31 CA CA A 501 1555 1555 2.41
LINK OE1 GLU A 31 CA CA A 501 1555 1555 2.48
LINK OD2 ASP A 56 CA CA A 502 1555 1555 2.25
LINK OD2 ASP A 58 CA CA A 502 1555 1555 2.35
LINK OD1 ASN A 60 CA CA A 502 1555 1555 2.37
LINK O THR A 62 CA CA A 502 1555 1555 2.35
LINK OE1 GLU A 67 CA CA A 502 1555 1555 2.38
LINK OE2 GLU A 67 CA CA A 502 1555 1555 2.66
LINK OD2 ASP A 93 CA CA A 503 1555 1555 2.32
LINK OD1 ASP A 95 CA CA A 503 1555 1555 2.38
LINK OD1 ASN A 97 CA CA A 503 1555 1555 2.37
LINK O TYR A 99 CA CA A 503 1555 1555 2.21
LINK OE2 GLU A 104 CA CA A 503 1555 1555 2.44
LINK OE1 GLU A 104 CA CA A 503 1555 1555 2.49
LINK OD2 ASP A 129 CA CA A 504 1555 1555 2.24
LINK OD1 ASP A 131 CA CA A 504 1555 1555 2.38
LINK OD2 ASP A 133 CA CA A 504 1555 1555 2.32
LINK O GLN A 135 CA CA A 504 1555 1555 2.35
LINK OE1 GLU A 140 CA CA A 504 1555 1555 2.44
LINK OE2 GLU A 140 CA CA A 504 1555 1555 2.60
LINK O HOH A 159 CA CA A 504 1555 1555 2.46
LINK O HOH A 166 CA CA A 503 1555 1555 2.20
LINK O HOH A 175 CA CA A 502 1555 1555 2.14
LINK O HOH A 195 CA CA A 501 1555 1555 2.40
SITE 1 AC1 6 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 6 GLU A 31 HOH A 195
SITE 1 AC2 6 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 6 GLU A 67 HOH A 175
SITE 1 AC3 6 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC3 6 GLU A 104 HOH A 166
SITE 1 AC4 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC4 6 GLU A 140 HOH A 159
SITE 1 AC5 3 GLN A 41 ASN A 42 ARG B 797
CRYST1 41.681 41.681 341.533 90.00 90.00 120.00 P 61 2 2 12
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 0.023992 0.013852 0.000000 0.00000
SCALE2 0.000000 0.027703 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002928 0.00000
(ATOM LINES ARE NOT SHOWN.)
END