HEADER MEMBRANE PROTEIN 19-SEP-09 3JXI
TITLE CRYSTAL STRUCTURE OF THE CHICKEN TRPV4 ANKYRIN REPEAT DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VANILLOID RECEPTOR-RELATED OSMOTICALLY ACTIVATED CHANNEL
COMPND 3 PROTEIN;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 FRAGMENT: UNP RESIDUES 133-382, ANKYRIN REPEAT DOMAIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 GENE: TRPV4, VR-OAC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21-C6H
KEYWDS ANKYRIN REPEATS, ANK REPEAT, ION TRANSPORT, IONIC CHANNEL, RECEPTOR,
KEYWDS 2 TRANSMEMBRANE, TRANSPORT, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.B.PHELPS,R.R.WANG,R.GAUDET
REVDAT 5 06-SEP-23 3JXI 1 SEQADV
REVDAT 4 01-NOV-17 3JXI 1 REMARK
REVDAT 3 13-JUL-11 3JXI 1 VERSN
REVDAT 2 09-FEB-10 3JXI 1 JRNL
REVDAT 1 22-DEC-09 3JXI 0
JRNL AUTH G.LANDOURE,A.A.ZDEBIK,T.L.MARTINEZ,B.G.BURNETT,H.C.STANESCU,
JRNL AUTH 2 H.INADA,Y.SHI,A.A.TAYE,L.KONG,C.H.MUNNS,S.S.CHOO,C.B.PHELPS,
JRNL AUTH 3 R.PAUDEL,H.HOULDEN,C.L.LUDLOW,M.J.CATERINA,R.GAUDET,R.KLETA,
JRNL AUTH 4 K.H.FISCHBECK,C.J.SUMNER
JRNL TITL MUTATIONS IN TRPV4 CAUSE CHARCOT-MARIE-TOOTH DISEASE TYPE
JRNL TITL 2 2C.
JRNL REF NAT.GENET. V. 42 170 2010
JRNL REFN ISSN 1061-4036
JRNL PMID 20037586
JRNL DOI 10.1038/NG.512
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0066
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 57722
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1178
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4089
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 79
REMARK 3 BIN FREE R VALUE : 0.4170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8005
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 534
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.21000
REMARK 3 B22 (A**2) : 0.23000
REMARK 3 B33 (A**2) : -0.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.294
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.221
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.167
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.892
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8184 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 5703 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11049 ; 1.473 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13845 ; 1.007 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1009 ; 6.744 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 389 ;34.767 ;23.111
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1466 ;17.951 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 73 ;18.067 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1239 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9056 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1705 ; 0.001 ; 0.020
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): 5019 ; 0.563 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2036 ; 0.133 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8073 ; 1.049 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3165 ; 1.745 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2972 ; 2.792 ; 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 : 24
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 132 A 165
REMARK 3 ORIGIN FOR THE GROUP (A): -29.3551 -13.9962 10.3746
REMARK 3 T TENSOR
REMARK 3 T11: 0.0761 T22: 0.1603
REMARK 3 T33: 0.3049 T12: -0.0019
REMARK 3 T13: -0.0886 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 5.5523 L22: 2.9501
REMARK 3 L33: 6.1402 L12: -0.3693
REMARK 3 L13: -4.8108 L23: 0.7147
REMARK 3 S TENSOR
REMARK 3 S11: -0.0307 S12: -0.5343 S13: -0.1605
REMARK 3 S21: 0.2561 S22: -0.1746 S23: -0.2555
REMARK 3 S31: 0.1199 S32: 0.2434 S33: 0.2053
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 166 A 210
REMARK 3 ORIGIN FOR THE GROUP (A): -35.7376 -10.6721 2.6802
REMARK 3 T TENSOR
REMARK 3 T11: 0.0539 T22: 0.0886
REMARK 3 T33: 0.2225 T12: 0.0106
REMARK 3 T13: -0.0542 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 3.0708 L22: 2.5197
REMARK 3 L33: 3.0843 L12: 0.5182
REMARK 3 L13: -0.9839 L23: -1.4267
REMARK 3 S TENSOR
REMARK 3 S11: 0.0027 S12: -0.0217 S13: -0.0853
REMARK 3 S21: 0.0378 S22: -0.0653 S23: -0.0099
REMARK 3 S31: 0.0473 S32: -0.0305 S33: 0.0625
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 : A 211 A 261
REMARK 3 ORIGIN FOR THE GROUP (A): -41.5085 -3.2286 -6.1198
REMARK 3 T TENSOR
REMARK 3 T11: 0.0523 T22: 0.1127
REMARK 3 T33: 0.2035 T12: 0.0196
REMARK 3 T13: -0.0301 T23: -0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 3.2828 L22: 2.4853
REMARK 3 L33: 2.7721 L12: -0.1231
REMARK 3 L13: 0.2367 L23: -1.2666
REMARK 3 S TENSOR
REMARK 3 S11: 0.0604 S12: 0.1360 S13: 0.0837
REMARK 3 S21: -0.0903 S22: -0.0896 S23: -0.1450
REMARK 3 S31: 0.0114 S32: 0.1829 S33: 0.0291
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 262 A 326
REMARK 3 ORIGIN FOR THE GROUP (A): -48.7688 -1.3657 -17.1689
REMARK 3 T TENSOR
REMARK 3 T11: 0.0961 T22: 0.1592
REMARK 3 T33: 0.1826 T12: 0.0513
REMARK 3 T13: -0.0436 T23: -0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 3.1606 L22: 2.3027
REMARK 3 L33: 2.8685 L12: -0.9289
REMARK 3 L13: 0.4722 L23: -0.9238
REMARK 3 S TENSOR
REMARK 3 S11: 0.1579 S12: 0.4374 S13: -0.0602
REMARK 3 S21: -0.4254 S22: -0.1554 S23: -0.1489
REMARK 3 S31: 0.1562 S32: 0.0907 S33: -0.0026
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 327 A 374
REMARK 3 ORIGIN FOR THE GROUP (A): -57.0505 2.0703 -23.6111
REMARK 3 T TENSOR
REMARK 3 T11: 0.1454 T22: 0.2938
REMARK 3 T33: 0.1395 T12: 0.0783
REMARK 3 T13: -0.1152 T23: -0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 2.8272 L22: 5.6191
REMARK 3 L33: 3.9147 L12: -0.2735
REMARK 3 L13: -0.2383 L23: 1.3650
REMARK 3 S TENSOR
REMARK 3 S11: 0.1482 S12: 0.5582 S13: -0.2524
REMARK 3 S21: -0.2251 S22: -0.1387 S23: 0.1605
REMARK 3 S31: 0.3334 S32: -0.1875 S33: -0.0096
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 375 A 384
REMARK 3 ORIGIN FOR THE GROUP (A): -62.8170 0.9677 -34.2671
REMARK 3 T TENSOR
REMARK 3 T11: 0.4804 T22: 0.4412
REMARK 3 T33: 0.4700 T12: 0.1755
REMARK 3 T13: 0.0219 T23: 0.0402
REMARK 3 L TENSOR
REMARK 3 L11: 12.8771 L22: 9.1745
REMARK 3 L33: 6.7891 L12: 10.8463
REMARK 3 L13: 9.3481 L23: 7.8633
REMARK 3 S TENSOR
REMARK 3 S11: 0.0195 S12: -0.4913 S13: -0.6072
REMARK 3 S21: -0.0128 S22: 0.1926 S23: 1.3890
REMARK 3 S31: 0.2837 S32: -0.4199 S33: -0.2121
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 132 B 162
REMARK 3 ORIGIN FOR THE GROUP (A): -24.0220 9.0799 -10.5763
REMARK 3 T TENSOR
REMARK 3 T11: 0.0559 T22: 0.1419
REMARK 3 T33: 0.2625 T12: -0.0068
REMARK 3 T13: -0.0786 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 3.9106 L22: 2.7097
REMARK 3 L33: 5.8251 L12: 0.8017
REMARK 3 L13: -4.1716 L23: -1.5704
REMARK 3 S TENSOR
REMARK 3 S11: -0.0106 S12: 0.4106 S13: -0.0125
REMARK 3 S21: -0.1447 S22: -0.0620 S23: 0.2437
REMARK 3 S31: 0.1600 S32: -0.2887 S33: 0.0726
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 163 B 178
REMARK 3 ORIGIN FOR THE GROUP (A): -18.3224 20.1546 -9.7931
REMARK 3 T TENSOR
REMARK 3 T11: 0.1157 T22: 0.1006
REMARK 3 T33: 0.2280 T12: -0.0156
REMARK 3 T13: -0.0401 T23: 0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 1.9630 L22: 8.9174
REMARK 3 L33: 9.4657 L12: -3.0602
REMARK 3 L13: -2.9715 L23: 9.1146
REMARK 3 S TENSOR
REMARK 3 S11: 0.0965 S12: 0.1687 S13: 0.2454
REMARK 3 S21: -0.4444 S22: 0.0921 S23: -0.2234
REMARK 3 S31: -0.4407 S32: 0.1229 S33: -0.1886
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 179 B 209
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4834 9.2500 -1.6064
REMARK 3 T TENSOR
REMARK 3 T11: 0.0887 T22: 0.0734
REMARK 3 T33: 0.2204 T12: -0.0175
REMARK 3 T13: -0.0575 T23: 0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 3.3610 L22: 2.2902
REMARK 3 L33: 4.2121 L12: 0.1893
REMARK 3 L13: -1.2107 L23: 1.8057
REMARK 3 S TENSOR
REMARK 3 S11: -0.1051 S12: -0.1131 S13: -0.1411
REMARK 3 S21: 0.1778 S22: -0.0482 S23: 0.1312
REMARK 3 S31: 0.1906 S32: -0.1203 S33: 0.1532
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 210 B 234
REMARK 3 ORIGIN FOR THE GROUP (A): -12.9416 21.4338 3.4107
REMARK 3 T TENSOR
REMARK 3 T11: 0.0541 T22: 0.1683
REMARK 3 T33: 0.3071 T12: -0.0071
REMARK 3 T13: -0.0622 T23: 0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 3.1147 L22: 8.1922
REMARK 3 L33: 5.0712 L12: -0.7717
REMARK 3 L13: 1.0602 L23: 2.1732
REMARK 3 S TENSOR
REMARK 3 S11: 0.0573 S12: -0.0925 S13: 0.2050
REMARK 3 S21: -0.1386 S22: -0.0859 S23: 0.2336
REMARK 3 S31: -0.2910 S32: -0.3732 S33: 0.0286
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 235 B 259
REMARK 3 ORIGIN FOR THE GROUP (A): -8.6942 17.6365 6.1611
REMARK 3 T TENSOR
REMARK 3 T11: 0.0657 T22: 0.1251
REMARK 3 T33: 0.1899 T12: -0.0034
REMARK 3 T13: -0.0685 T23: 0.0264
REMARK 3 L TENSOR
REMARK 3 L11: 3.5827 L22: 1.3635
REMARK 3 L33: 2.4531 L12: 0.8543
REMARK 3 L13: 0.0922 L23: 0.9678
REMARK 3 S TENSOR
REMARK 3 S11: -0.0225 S12: -0.0940 S13: -0.0345
REMARK 3 S21: 0.0421 S22: -0.0019 S23: 0.1323
REMARK 3 S31: 0.1718 S32: -0.1044 S33: 0.0244
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 264 B 376
REMARK 3 ORIGIN FOR THE GROUP (A): -0.6640 22.7511 19.9028
REMARK 3 T TENSOR
REMARK 3 T11: 0.0834 T22: 0.1358
REMARK 3 T33: 0.1461 T12: -0.0076
REMARK 3 T13: -0.0336 T23: 0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 2.2032 L22: 1.9755
REMARK 3 L33: 2.1132 L12: 1.1701
REMARK 3 L13: 0.9772 L23: 0.8375
REMARK 3 S TENSOR
REMARK 3 S11: 0.1356 S12: -0.3592 S13: -0.0450
REMARK 3 S21: 0.2525 S22: -0.0857 S23: 0.0973
REMARK 3 S31: 0.2071 S32: -0.1582 S33: -0.0499
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 377 B 387
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4860 20.4208 34.1708
REMARK 3 T TENSOR
REMARK 3 T11: 0.3397 T22: 0.2788
REMARK 3 T33: 0.2405 T12: -0.0367
REMARK 3 T13: -0.1142 T23: 0.0410
REMARK 3 L TENSOR
REMARK 3 L11: 8.7364 L22: 4.0802
REMARK 3 L33: 4.9871 L12: 0.8969
REMARK 3 L13: 5.4510 L23: -0.6172
REMARK 3 S TENSOR
REMARK 3 S11: 0.3687 S12: -0.1195 S13: -0.6806
REMARK 3 S21: 0.2714 S22: -0.1443 S23: -0.6267
REMARK 3 S31: 0.6744 S32: 0.4536 S33: -0.2244
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 132 C 210
REMARK 3 ORIGIN FOR THE GROUP (A): -47.5239 24.5657 -59.0692
REMARK 3 T TENSOR
REMARK 3 T11: 0.3071 T22: 0.3773
REMARK 3 T33: 0.1285 T12: 0.0833
REMARK 3 T13: -0.1391 T23: 0.0744
REMARK 3 L TENSOR
REMARK 3 L11: 5.0456 L22: 0.8946
REMARK 3 L33: 3.6871 L12: 0.2411
REMARK 3 L13: -0.5826 L23: 0.1077
REMARK 3 S TENSOR
REMARK 3 S11: -0.0159 S12: 0.4143 S13: 0.2494
REMARK 3 S21: -0.0731 S22: 0.0790 S23: 0.2208
REMARK 3 S31: -0.2461 S32: -0.3489 S33: -0.0631
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 211 C 269
REMARK 3 ORIGIN FOR THE GROUP (A): -34.2312 17.6152 -50.1398
REMARK 3 T TENSOR
REMARK 3 T11: 0.2881 T22: 0.3078
REMARK 3 T33: 0.0690 T12: 0.0588
REMARK 3 T13: -0.1164 T23: 0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 3.5341 L22: 3.1800
REMARK 3 L33: 3.4503 L12: 0.4383
REMARK 3 L13: 0.7961 L23: -0.3524
REMARK 3 S TENSOR
REMARK 3 S11: -0.1347 S12: 0.2491 S13: -0.1608
REMARK 3 S21: -0.2464 S22: 0.0911 S23: -0.1206
REMARK 3 S31: 0.0615 S32: 0.1538 S33: 0.0435
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 270 C 376
REMARK 3 ORIGIN FOR THE GROUP (A): -20.4426 16.7254 -38.3691
REMARK 3 T TENSOR
REMARK 3 T11: 0.2966 T22: 0.3078
REMARK 3 T33: 0.1516 T12: 0.0233
REMARK 3 T13: -0.1121 T23: 0.0498
REMARK 3 L TENSOR
REMARK 3 L11: 3.9722 L22: 1.8855
REMARK 3 L33: 2.4602 L12: -1.4703
REMARK 3 L13: 1.4177 L23: -0.8052
REMARK 3 S TENSOR
REMARK 3 S11: -0.1329 S12: 0.0019 S13: 0.1814
REMARK 3 S21: 0.0253 S22: 0.0367 S23: -0.1176
REMARK 3 S31: -0.2864 S32: 0.0277 S33: 0.0962
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 377 C 388
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6232 18.9707 -23.6512
REMARK 3 T TENSOR
REMARK 3 T11: 0.2732 T22: 0.2839
REMARK 3 T33: 0.3505 T12: 0.0246
REMARK 3 T13: -0.0249 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 2.4654 L22: 4.8655
REMARK 3 L33: 15.6154 L12: -0.3995
REMARK 3 L13: -1.5508 L23: 2.4331
REMARK 3 S TENSOR
REMARK 3 S11: -0.1419 S12: -0.1463 S13: 0.2806
REMARK 3 S21: 0.2202 S22: -0.1185 S23: 0.4397
REMARK 3 S31: 0.0474 S32: -0.6022 S33: 0.2604
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 132 D 136
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3813 35.7214 -65.7347
REMARK 3 T TENSOR
REMARK 3 T11: 0.5702 T22: 0.8547
REMARK 3 T33: 1.3237 T12: 0.3984
REMARK 3 T13: -0.5261 T23: 0.0826
REMARK 3 L TENSOR
REMARK 3 L11: 11.1204 L22: 1.3234
REMARK 3 L33: 2.1939 L12: 3.8363
REMARK 3 L13: -4.9393 L23: -1.7040
REMARK 3 S TENSOR
REMARK 3 S11: 1.9924 S12: 0.2645 S13: 0.2263
REMARK 3 S21: 1.4259 S22: -0.7789 S23: -1.3884
REMARK 3 S31: 0.9824 S32: 1.5341 S33: -1.2135
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 137 D 149
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4400 35.1046 -64.1616
REMARK 3 T TENSOR
REMARK 3 T11: 0.6119 T22: 0.9061
REMARK 3 T33: 1.1220 T12: 0.2028
REMARK 3 T13: -0.4664 T23: 0.0407
REMARK 3 L TENSOR
REMARK 3 L11: 2.2785 L22: 5.7180
REMARK 3 L33: 4.1316 L12: 0.3803
REMARK 3 L13: -3.0600 L23: -0.1588
REMARK 3 S TENSOR
REMARK 3 S11: 0.8643 S12: 0.7561 S13: -0.4753
REMARK 3 S21: -1.2846 S22: -0.0322 S23: 0.9949
REMARK 3 S31: -0.4956 S32: -0.2772 S33: -0.8321
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 150 D 181
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4045 29.8195 -59.0233
REMARK 3 T TENSOR
REMARK 3 T11: 0.2903 T22: 0.7385
REMARK 3 T33: 1.6922 T12: 0.1975
REMARK 3 T13: -0.5441 T23: 0.2578
REMARK 3 L TENSOR
REMARK 3 L11: 0.7553 L22: 3.9613
REMARK 3 L33: 7.6035 L12: -1.6587
REMARK 3 L13: -2.1150 L23: 5.3767
REMARK 3 S TENSOR
REMARK 3 S11: -0.0499 S12: 0.9527 S13: -0.7750
REMARK 3 S21: 0.2304 S22: 0.4004 S23: 0.9645
REMARK 3 S31: 0.5468 S32: -0.7890 S33: -0.3506
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 182 D 223
REMARK 3 ORIGIN FOR THE GROUP (A): 12.1666 29.6848 -53.0975
REMARK 3 T TENSOR
REMARK 3 T11: 0.3248 T22: 0.6494
REMARK 3 T33: 0.8807 T12: 0.0479
REMARK 3 T13: -0.3175 T23: 0.1352
REMARK 3 L TENSOR
REMARK 3 L11: 4.0601 L22: 9.2469
REMARK 3 L33: 5.3037 L12: -1.6376
REMARK 3 L13: -2.9757 L23: -0.3732
REMARK 3 S TENSOR
REMARK 3 S11: 0.2047 S12: 0.0184 S13: -0.8819
REMARK 3 S21: -0.1306 S22: -0.1384 S23: 1.0507
REMARK 3 S31: -0.0128 S32: -0.0681 S33: -0.0664
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 224 D 268
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9307 26.3123 -47.7821
REMARK 3 T TENSOR
REMARK 3 T11: 0.1781 T22: 0.4641
REMARK 3 T33: 0.8602 T12: 0.1619
REMARK 3 T13: -0.2516 T23: 0.1830
REMARK 3 L TENSOR
REMARK 3 L11: 5.1119 L22: 8.2052
REMARK 3 L33: 4.4846 L12: 0.3619
REMARK 3 L13: 1.3805 L23: -3.7057
REMARK 3 S TENSOR
REMARK 3 S11: 0.0783 S12: -0.0208 S13: -0.8367
REMARK 3 S21: -0.5635 S22: 0.3833 S23: 1.5060
REMARK 3 S31: 0.0040 S32: -0.2501 S33: -0.4616
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 269 D 367
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8202 20.9840 -37.6292
REMARK 3 T TENSOR
REMARK 3 T11: 0.1606 T22: 0.4179
REMARK 3 T33: 0.6040 T12: 0.1824
REMARK 3 T13: -0.0355 T23: 0.1225
REMARK 3 L TENSOR
REMARK 3 L11: 2.5430 L22: 3.9736
REMARK 3 L33: 4.2346 L12: -2.4528
REMARK 3 L13: 0.8157 L23: -1.8759
REMARK 3 S TENSOR
REMARK 3 S11: -0.0401 S12: -0.4641 S13: -0.2400
REMARK 3 S21: 0.3975 S22: 0.3450 S23: 1.2995
REMARK 3 S31: -0.3066 S32: -0.3705 S33: -0.3049
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 368 D 388
REMARK 3 ORIGIN FOR THE GROUP (A): 45.2430 18.9499 -28.9143
REMARK 3 T TENSOR
REMARK 3 T11: 0.3111 T22: 0.3721
REMARK 3 T33: 0.2446 T12: 0.1297
REMARK 3 T13: -0.0079 T23: 0.0413
REMARK 3 L TENSOR
REMARK 3 L11: 2.0051 L22: 2.0996
REMARK 3 L33: 7.7122 L12: -0.1799
REMARK 3 L13: 3.1373 L23: 1.3300
REMARK 3 S TENSOR
REMARK 3 S11: -0.1807 S12: -0.1688 S13: 0.2496
REMARK 3 S21: 0.4543 S22: 0.0810 S23: 0.3116
REMARK 3 S31: -0.1955 S32: -0.0152 S33: 0.0997
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 3JXI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1000055283.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65393
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.59800
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: PDB ENTRY 2ETB (TRPV2 ANKYRIN REPEATS)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE PH 5.0, 10% MPD,
REMARK 280 2% PEG8000, 4.3% TRIFLUOROETHANOL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 24.05950
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ALA A 385
REMARK 465 HIS A 386
REMARK 465 HIS A 387
REMARK 465 HIS A 388
REMARK 465 HIS A 389
REMARK 465 HIS A 390
REMARK 465 HIS A 391
REMARK 465 HIS B 388
REMARK 465 HIS B 389
REMARK 465 HIS B 390
REMARK 465 HIS B 391
REMARK 465 PHE C 259
REMARK 465 GLN C 260
REMARK 465 PRO C 261
REMARK 465 LYS C 262
REMARK 465 ASP C 263
REMARK 465 GLU C 264
REMARK 465 GLY C 265
REMARK 465 GLY C 266
REMARK 465 HIS C 389
REMARK 465 HIS C 390
REMARK 465 HIS C 391
REMARK 465 PHE D 259
REMARK 465 GLN D 260
REMARK 465 PRO D 261
REMARK 465 LYS D 262
REMARK 465 ASP D 263
REMARK 465 GLU D 264
REMARK 465 GLY D 265
REMARK 465 GLY D 266
REMARK 465 HIS D 389
REMARK 465 HIS D 390
REMARK 465 HIS D 391
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 ASP B 319 O HOH B 753 2.08
REMARK 500 O HOH B 551 O HOH B 775 2.11
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 ARG A 137 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 378 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 378 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 219 -152.43 -126.55
REMARK 500 ARG A 235 34.91 72.29
REMARK 500 ASP A 263 109.57 -42.80
REMARK 500 GLU A 272 -35.43 62.85
REMARK 500 ASP B 219 -154.94 -124.01
REMARK 500 CYS B 236 77.96 -100.95
REMARK 500 ASP B 263 -20.02 91.39
REMARK 500 GLU B 272 -37.11 63.23
REMARK 500 GLN B 283 71.67 -119.53
REMARK 500 LYS B 296 116.99 -175.08
REMARK 500 LYS C 133 -72.26 -44.40
REMARK 500 ASN C 187 52.74 -150.46
REMARK 500 GLU C 272 -45.38 69.22
REMARK 500 HIS C 295 -68.88 -105.87
REMARK 500 LEU D 160 -55.51 -143.32
REMARK 500 LYS D 163 65.71 62.68
REMARK 500 THR D 176 -33.49 -136.57
REMARK 500 ASN D 208 -5.76 -146.49
REMARK 500 ASN D 214 31.38 -86.42
REMARK 500 PHE D 217 -161.49 -127.46
REMARK 500 ARG D 235 42.35 72.35
REMARK 500 ARG D 257 58.74 -164.12
REMARK 500 GLU D 272 -53.62 70.05
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 LYS B 262 ASP B 263 130.47
REMARK 500 ASP B 263 GLU B 264 -133.49
REMARK 500 GLY C 207 ASN C 208 -149.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PNN RELATED DB: PDB
REMARK 900 TRPV1 ANKYRIN REPEATS
REMARK 900 RELATED ID: 2ETB RELATED DB: PDB
REMARK 900 TRPV2 ANKYRIN REPEATS
REMARK 900 RELATED ID: 2RFA RELATED DB: PDB
REMARK 900 TRPV6 ANKYRIN REPEATS
REMARK 900 RELATED ID: 3JZJ RELATED DB: PDB
DBREF 3JXI A 133 382 UNP Q9DFS3 Q9DFS3_CHICK 133 382
DBREF 3JXI B 133 382 UNP Q9DFS3 Q9DFS3_CHICK 133 382
DBREF 3JXI C 133 382 UNP Q9DFS3 Q9DFS3_CHICK 133 382
DBREF 3JXI D 133 382 UNP Q9DFS3 Q9DFS3_CHICK 133 382
SEQADV 3JXI MET A 132 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI ALA A 383 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI ALA A 384 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI ALA A 385 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS A 386 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS A 387 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS A 388 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS A 389 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS A 390 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS A 391 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI MET B 132 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI ALA B 383 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI ALA B 384 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI ALA B 385 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS B 386 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS B 387 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS B 388 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS B 389 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS B 390 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS B 391 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI MET C 132 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI ALA C 383 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI ALA C 384 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI ALA C 385 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS C 386 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS C 387 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS C 388 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS C 389 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS C 390 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS C 391 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI MET D 132 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI ALA D 383 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI ALA D 384 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI ALA D 385 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS D 386 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS D 387 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS D 388 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS D 389 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS D 390 UNP Q9DFS3 EXPRESSION TAG
SEQADV 3JXI HIS D 391 UNP Q9DFS3 EXPRESSION TAG
SEQRES 1 A 260 MET LYS VAL PHE ASN ARG PRO ILE LEU PHE ASP ILE VAL
SEQRES 2 A 260 SER ARG GLY SER PRO ASP GLY LEU GLU GLY LEU LEU SER
SEQRES 3 A 260 PHE LEU LEU THR HIS LYS LYS ARG LEU THR ASP GLU GLU
SEQRES 4 A 260 PHE ARG GLU PRO SER THR GLY LYS THR CYS LEU PRO LYS
SEQRES 5 A 260 ALA LEU LEU ASN LEU SER ALA GLY ARG ASN ASP THR ILE
SEQRES 6 A 260 PRO ILE LEU LEU ASP ILE ALA GLU LYS THR GLY ASN MET
SEQRES 7 A 260 ARG GLU PHE ILE ASN SER PRO PHE ARG ASP VAL TYR TYR
SEQRES 8 A 260 ARG GLY GLN THR ALA LEU HIS ILE ALA ILE GLU ARG ARG
SEQRES 9 A 260 CYS LYS HIS TYR VAL GLU LEU LEU VAL GLU LYS GLY ALA
SEQRES 10 A 260 ASP VAL HIS ALA GLN ALA ARG GLY ARG PHE PHE GLN PRO
SEQRES 11 A 260 LYS ASP GLU GLY GLY TYR PHE TYR PHE GLY GLU LEU PRO
SEQRES 12 A 260 LEU SER LEU ALA ALA CYS THR ASN GLN PRO HIS ILE VAL
SEQRES 13 A 260 HIS TYR LEU THR GLU ASN GLY HIS LYS GLN ALA ASP LEU
SEQRES 14 A 260 ARG ARG GLN ASP SER ARG GLY ASN THR VAL LEU HIS ALA
SEQRES 15 A 260 LEU VAL ALA ILE ALA ASP ASN THR ARG GLU ASN THR LYS
SEQRES 16 A 260 PHE VAL THR LYS MET TYR ASP LEU LEU LEU ILE LYS CYS
SEQRES 17 A 260 ALA LYS LEU PHE PRO ASP THR ASN LEU GLU ALA LEU LEU
SEQRES 18 A 260 ASN ASN ASP GLY LEU SER PRO LEU MET MET ALA ALA LYS
SEQRES 19 A 260 THR GLY LYS ILE GLY ILE PHE GLN HIS ILE ILE ARG ARG
SEQRES 20 A 260 GLU ILE ALA ASP ALA ALA ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 B 260 MET LYS VAL PHE ASN ARG PRO ILE LEU PHE ASP ILE VAL
SEQRES 2 B 260 SER ARG GLY SER PRO ASP GLY LEU GLU GLY LEU LEU SER
SEQRES 3 B 260 PHE LEU LEU THR HIS LYS LYS ARG LEU THR ASP GLU GLU
SEQRES 4 B 260 PHE ARG GLU PRO SER THR GLY LYS THR CYS LEU PRO LYS
SEQRES 5 B 260 ALA LEU LEU ASN LEU SER ALA GLY ARG ASN ASP THR ILE
SEQRES 6 B 260 PRO ILE LEU LEU ASP ILE ALA GLU LYS THR GLY ASN MET
SEQRES 7 B 260 ARG GLU PHE ILE ASN SER PRO PHE ARG ASP VAL TYR TYR
SEQRES 8 B 260 ARG GLY GLN THR ALA LEU HIS ILE ALA ILE GLU ARG ARG
SEQRES 9 B 260 CYS LYS HIS TYR VAL GLU LEU LEU VAL GLU LYS GLY ALA
SEQRES 10 B 260 ASP VAL HIS ALA GLN ALA ARG GLY ARG PHE PHE GLN PRO
SEQRES 11 B 260 LYS ASP GLU GLY GLY TYR PHE TYR PHE GLY GLU LEU PRO
SEQRES 12 B 260 LEU SER LEU ALA ALA CYS THR ASN GLN PRO HIS ILE VAL
SEQRES 13 B 260 HIS TYR LEU THR GLU ASN GLY HIS LYS GLN ALA ASP LEU
SEQRES 14 B 260 ARG ARG GLN ASP SER ARG GLY ASN THR VAL LEU HIS ALA
SEQRES 15 B 260 LEU VAL ALA ILE ALA ASP ASN THR ARG GLU ASN THR LYS
SEQRES 16 B 260 PHE VAL THR LYS MET TYR ASP LEU LEU LEU ILE LYS CYS
SEQRES 17 B 260 ALA LYS LEU PHE PRO ASP THR ASN LEU GLU ALA LEU LEU
SEQRES 18 B 260 ASN ASN ASP GLY LEU SER PRO LEU MET MET ALA ALA LYS
SEQRES 19 B 260 THR GLY LYS ILE GLY ILE PHE GLN HIS ILE ILE ARG ARG
SEQRES 20 B 260 GLU ILE ALA ASP ALA ALA ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 C 260 MET LYS VAL PHE ASN ARG PRO ILE LEU PHE ASP ILE VAL
SEQRES 2 C 260 SER ARG GLY SER PRO ASP GLY LEU GLU GLY LEU LEU SER
SEQRES 3 C 260 PHE LEU LEU THR HIS LYS LYS ARG LEU THR ASP GLU GLU
SEQRES 4 C 260 PHE ARG GLU PRO SER THR GLY LYS THR CYS LEU PRO LYS
SEQRES 5 C 260 ALA LEU LEU ASN LEU SER ALA GLY ARG ASN ASP THR ILE
SEQRES 6 C 260 PRO ILE LEU LEU ASP ILE ALA GLU LYS THR GLY ASN MET
SEQRES 7 C 260 ARG GLU PHE ILE ASN SER PRO PHE ARG ASP VAL TYR TYR
SEQRES 8 C 260 ARG GLY GLN THR ALA LEU HIS ILE ALA ILE GLU ARG ARG
SEQRES 9 C 260 CYS LYS HIS TYR VAL GLU LEU LEU VAL GLU LYS GLY ALA
SEQRES 10 C 260 ASP VAL HIS ALA GLN ALA ARG GLY ARG PHE PHE GLN PRO
SEQRES 11 C 260 LYS ASP GLU GLY GLY TYR PHE TYR PHE GLY GLU LEU PRO
SEQRES 12 C 260 LEU SER LEU ALA ALA CYS THR ASN GLN PRO HIS ILE VAL
SEQRES 13 C 260 HIS TYR LEU THR GLU ASN GLY HIS LYS GLN ALA ASP LEU
SEQRES 14 C 260 ARG ARG GLN ASP SER ARG GLY ASN THR VAL LEU HIS ALA
SEQRES 15 C 260 LEU VAL ALA ILE ALA ASP ASN THR ARG GLU ASN THR LYS
SEQRES 16 C 260 PHE VAL THR LYS MET TYR ASP LEU LEU LEU ILE LYS CYS
SEQRES 17 C 260 ALA LYS LEU PHE PRO ASP THR ASN LEU GLU ALA LEU LEU
SEQRES 18 C 260 ASN ASN ASP GLY LEU SER PRO LEU MET MET ALA ALA LYS
SEQRES 19 C 260 THR GLY LYS ILE GLY ILE PHE GLN HIS ILE ILE ARG ARG
SEQRES 20 C 260 GLU ILE ALA ASP ALA ALA ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 D 260 MET LYS VAL PHE ASN ARG PRO ILE LEU PHE ASP ILE VAL
SEQRES 2 D 260 SER ARG GLY SER PRO ASP GLY LEU GLU GLY LEU LEU SER
SEQRES 3 D 260 PHE LEU LEU THR HIS LYS LYS ARG LEU THR ASP GLU GLU
SEQRES 4 D 260 PHE ARG GLU PRO SER THR GLY LYS THR CYS LEU PRO LYS
SEQRES 5 D 260 ALA LEU LEU ASN LEU SER ALA GLY ARG ASN ASP THR ILE
SEQRES 6 D 260 PRO ILE LEU LEU ASP ILE ALA GLU LYS THR GLY ASN MET
SEQRES 7 D 260 ARG GLU PHE ILE ASN SER PRO PHE ARG ASP VAL TYR TYR
SEQRES 8 D 260 ARG GLY GLN THR ALA LEU HIS ILE ALA ILE GLU ARG ARG
SEQRES 9 D 260 CYS LYS HIS TYR VAL GLU LEU LEU VAL GLU LYS GLY ALA
SEQRES 10 D 260 ASP VAL HIS ALA GLN ALA ARG GLY ARG PHE PHE GLN PRO
SEQRES 11 D 260 LYS ASP GLU GLY GLY TYR PHE TYR PHE GLY GLU LEU PRO
SEQRES 12 D 260 LEU SER LEU ALA ALA CYS THR ASN GLN PRO HIS ILE VAL
SEQRES 13 D 260 HIS TYR LEU THR GLU ASN GLY HIS LYS GLN ALA ASP LEU
SEQRES 14 D 260 ARG ARG GLN ASP SER ARG GLY ASN THR VAL LEU HIS ALA
SEQRES 15 D 260 LEU VAL ALA ILE ALA ASP ASN THR ARG GLU ASN THR LYS
SEQRES 16 D 260 PHE VAL THR LYS MET TYR ASP LEU LEU LEU ILE LYS CYS
SEQRES 17 D 260 ALA LYS LEU PHE PRO ASP THR ASN LEU GLU ALA LEU LEU
SEQRES 18 D 260 ASN ASN ASP GLY LEU SER PRO LEU MET MET ALA ALA LYS
SEQRES 19 D 260 THR GLY LYS ILE GLY ILE PHE GLN HIS ILE ILE ARG ARG
SEQRES 20 D 260 GLU ILE ALA ASP ALA ALA ALA HIS HIS HIS HIS HIS HIS
FORMUL 5 HOH *534(H2 O)
HELIX 1 1 ASN A 136 GLY A 147 1 12
HELIX 2 2 SER A 148 GLU A 153 5 6
HELIX 3 3 GLY A 154 LYS A 163 1 10
HELIX 4 4 ASP A 168 ARG A 172 5 5
HELIX 5 5 THR A 179 LEU A 186 1 8
HELIX 6 6 ASP A 194 THR A 206 1 13
HELIX 7 7 ASN A 208 ASN A 214 1 7
HELIX 8 8 THR A 226 ARG A 234 1 9
HELIX 9 9 CYS A 236 LYS A 246 1 11
HELIX 10 10 LEU A 273 THR A 281 1 9
HELIX 11 11 GLN A 283 ASN A 293 1 11
HELIX 12 12 THR A 309 ALA A 318 1 10
HELIX 13 13 THR A 321 PHE A 343 1 23
HELIX 14 14 ASN A 347 LEU A 351 5 5
HELIX 15 15 SER A 358 THR A 366 1 9
HELIX 16 16 LYS A 368 ALA A 384 1 17
HELIX 17 17 ASN B 136 GLY B 147 1 12
HELIX 18 18 PRO B 149 GLU B 153 5 5
HELIX 19 19 GLY B 154 LYS B 163 1 10
HELIX 20 20 ASP B 168 ARG B 172 5 5
HELIX 21 21 THR B 179 LEU B 186 1 8
HELIX 22 22 ASP B 194 THR B 206 1 13
HELIX 23 23 ASN B 208 SER B 215 1 8
HELIX 24 24 THR B 226 ARG B 234 1 9
HELIX 25 25 CYS B 236 LYS B 246 1 11
HELIX 26 26 LEU B 273 THR B 281 1 9
HELIX 27 27 GLN B 283 ASN B 293 1 11
HELIX 28 28 THR B 309 ALA B 318 1 10
HELIX 29 29 THR B 321 PHE B 343 1 23
HELIX 30 30 ASN B 347 LEU B 351 5 5
HELIX 31 31 SER B 358 THR B 366 1 9
HELIX 32 32 LYS B 368 HIS B 387 1 20
HELIX 33 33 ASN C 136 GLY C 147 1 12
HELIX 34 34 GLY C 154 LYS C 163 1 10
HELIX 35 35 ASP C 168 ARG C 172 5 5
HELIX 36 36 THR C 179 LEU C 186 1 8
HELIX 37 37 THR C 195 THR C 206 1 12
HELIX 38 38 ASN C 208 SER C 215 1 8
HELIX 39 39 THR C 226 ARG C 234 1 9
HELIX 40 40 CYS C 236 LYS C 246 1 11
HELIX 41 41 LEU C 273 THR C 281 1 9
HELIX 42 42 GLN C 283 ASN C 293 1 11
HELIX 43 43 THR C 309 ALA C 318 1 10
HELIX 44 44 THR C 321 PHE C 343 1 23
HELIX 45 45 ASN C 347 LEU C 351 5 5
HELIX 46 46 SER C 358 GLY C 367 1 10
HELIX 47 47 LYS C 368 HIS C 387 1 20
HELIX 48 48 ASN D 136 GLY D 147 1 12
HELIX 49 49 GLY D 154 HIS D 162 1 9
HELIX 50 50 ASP D 168 ARG D 172 5 5
HELIX 51 51 THR D 179 LEU D 186 1 8
HELIX 52 52 THR D 195 THR D 206 1 12
HELIX 53 53 MET D 209 ASN D 214 1 6
HELIX 54 54 THR D 226 ARG D 234 1 9
HELIX 55 55 CYS D 236 LYS D 246 1 11
HELIX 56 56 LEU D 273 THR D 281 1 9
HELIX 57 57 GLN D 283 ASN D 293 1 11
HELIX 58 58 THR D 309 ALA D 318 1 10
HELIX 59 59 THR D 321 PHE D 343 1 23
HELIX 60 60 SER D 358 THR D 366 1 9
HELIX 61 61 LYS D 368 HIS D 387 1 20
SHEET 1 A 2 TYR A 222 ARG A 223 0
SHEET 2 A 2 ARG A 255 GLY A 256 -1 O ARG A 255 N ARG A 223
SHEET 1 B 2 TYR B 222 ARG B 223 0
SHEET 2 B 2 ARG B 255 GLY B 256 -1 O ARG B 255 N ARG B 223
SHEET 1 C 2 TYR C 222 ARG C 223 0
SHEET 2 C 2 ARG C 255 GLY C 256 -1 O ARG C 255 N ARG C 223
SHEET 1 D 3 PHE D 217 ARG D 218 0
SHEET 2 D 3 TYR D 222 GLN D 225 -1 O GLY D 224 N PHE D 217
SHEET 3 D 3 ARG D 255 GLY D 256 -1 O ARG D 255 N ARG D 223
CRYST1 105.259 48.119 133.891 90.00 101.89 90.00 P 1 21 1 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 0.009500 0.000000 0.002000 0.00000
SCALE2 0.000000 0.020782 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007633 0.00000
(ATOM LINES ARE NOT SHOWN.)
END