HEADER METAL TRANSPORT 15-SEP-14 4WFG
TITLE HUMAN TRAAK K+ CHANNEL IN A TL+ BOUND CONDUCTIVE CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM CHANNEL SUBFAMILY K MEMBER 4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TWIK-RELATED ARACHIDONIC ACID-STIMULATED POTASSIUM CHANNEL
COMPND 5 PROTEIN,TRAAK,TWO PORE POTASSIUM CHANNEL KT4.1,TWO PORE K(+) CHANNEL
COMPND 6 KT4.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: ANTI-TRAAK ANTIBODY 13E9 FAB FRAGMENT LIGHT CHAIN;
COMPND 11 CHAIN: D, F;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: ANTI-TRAAK ANTIBODY 13E9 FAB FRAGMENT HEAVY CHAIN;
COMPND 15 CHAIN: E, G;
COMPND 16 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: KCNK4, TRAAK;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_COMMON: MOUSE;
SOURCE 11 ORGANISM_TAXID: 10090;
SOURCE 12 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 10090;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 16 ORGANISM_COMMON: MOUSE;
SOURCE 17 ORGANISM_TAXID: 10090;
SOURCE 18 EXPRESSION_SYSTEM: MUS MUSCULUS;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10090
KEYWDS MECHANOSENSITIVE ION CHANNEL, TWO-PORE DOMAIN POTASSIUM ION CHANNEL,
KEYWDS 2 MEMBRANE PROTEIN, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR S.G.BROHAWN,R.MACKINNON
REVDAT 3 27-SEP-23 4WFG 1 SOURCE KEYWDS JRNL REMARK
REVDAT 3 2 1 LINK
REVDAT 2 17-DEC-14 4WFG 1 JRNL
REVDAT 1 03-DEC-14 4WFG 0
JRNL AUTH S.G.BROHAWN,E.B.CAMPBELL,R.MACKINNON
JRNL TITL PHYSICAL MECHANISM FOR GATING AND MECHANOSENSITIVITY OF THE
JRNL TITL 2 HUMAN TRAAK K+ CHANNEL.
JRNL REF NATURE V. 516 126 2014
JRNL REFN ESSN 1476-4687
JRNL PMID 25471887
JRNL DOI 10.1038/NATURE14013
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 40099
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) : 0.202
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2130
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2940
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.3860
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.3790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10398
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 11
REMARK 3 SOLVENT ATOMS : 190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 108.7
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.97000
REMARK 3 B22 (A**2) : -3.86000
REMARK 3 B33 (A**2) : 4.32000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.89000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.371
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.376
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 43.040
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.910
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10670 ; 0.006 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 9942 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14534 ; 0.898 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 22938 ; 0.611 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1341 ; 6.614 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 405 ;33.162 ;23.704
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1692 ;15.275 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;18.281 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1661 ; 0.055 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11903 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2417 ; 0.002 ; 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): 5394 ; 3.946 ; 5.232
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5393 ; 3.946 ; 5.232
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6725 ; 6.020 ; 7.850
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6726 ; 6.020 ; 7.850
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5276 ; 4.474 ; 5.599
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5277 ; 4.473 ; 5.600
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 7810 ; 6.880 ; 8.254
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 44033 ;10.525 ;50.417
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 43965 ;10.515 ;50.371
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 3
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 28 286 B 28 286 12887 0.15 0.05
REMARK 3 2 D 1 211 F 1 211 10978 0.12 0.05
REMARK 3 3 E 1 215 G 1 215 11345 0.11 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
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 28 A 148
REMARK 3 ORIGIN FOR THE GROUP (A): 44.2640 -5.8350 10.0950
REMARK 3 T TENSOR
REMARK 3 T11: 0.5513 T22: 0.3256
REMARK 3 T33: 0.6008 T12: -0.0489
REMARK 3 T13: 0.1909 T23: 0.0815
REMARK 3 L TENSOR
REMARK 3 L11: 4.2915 L22: 0.3471
REMARK 3 L33: 5.1726 L12: -1.1235
REMARK 3 L13: -3.7239 L23: 0.7346
REMARK 3 S TENSOR
REMARK 3 S11: 0.4151 S12: 0.4098 S13: 0.1537
REMARK 3 S21: -0.1270 S22: -0.1425 S23: 0.0644
REMARK 3 S31: -0.5110 S32: 0.3281 S33: -0.2726
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 149 A 219
REMARK 3 ORIGIN FOR THE GROUP (A): 49.9510 -20.4150 -20.7750
REMARK 3 T TENSOR
REMARK 3 T11: 1.5530 T22: 1.1377
REMARK 3 T33: 0.9076 T12: 0.0758
REMARK 3 T13: 0.1229 T23: -0.2229
REMARK 3 L TENSOR
REMARK 3 L11: 0.5369 L22: 0.2791
REMARK 3 L33: 11.1008 L12: -0.3237
REMARK 3 L13: 0.3128 L23: -0.9466
REMARK 3 S TENSOR
REMARK 3 S11: 0.1260 S12: 0.7721 S13: -0.2249
REMARK 3 S21: -0.3153 S22: -0.4534 S23: 0.1776
REMARK 3 S31: 0.9828 S32: 0.5889 S33: 0.3274
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 220 A 286
REMARK 3 ORIGIN FOR THE GROUP (A): 45.6680 -16.7530 -6.5940
REMARK 3 T TENSOR
REMARK 3 T11: 0.8071 T22: 0.7405
REMARK 3 T33: 0.5816 T12: 0.0511
REMARK 3 T13: -0.0544 T23: -0.1023
REMARK 3 L TENSOR
REMARK 3 L11: 7.3772 L22: 7.7051
REMARK 3 L33: 5.5835 L12: -0.8321
REMARK 3 L13: -1.6433 L23: -1.3747
REMARK 3 S TENSOR
REMARK 3 S11: -0.2576 S12: 0.8010 S13: -0.8072
REMARK 3 S21: -0.7418 S22: 0.1161 S23: 0.1273
REMARK 3 S31: 0.9860 S32: -0.5867 S33: 0.1415
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 : B 28 B 175
REMARK 3 ORIGIN FOR THE GROUP (A): 47.8750 -10.1550 7.3270
REMARK 3 T TENSOR
REMARK 3 T11: 0.4675 T22: 0.4712
REMARK 3 T33: 0.4840 T12: -0.0700
REMARK 3 T13: 0.1208 T23: -0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 4.2062 L22: 1.1668
REMARK 3 L33: 5.8726 L12: -0.5715
REMARK 3 L13: -3.5920 L23: -0.9029
REMARK 3 S TENSOR
REMARK 3 S11: 0.4473 S12: 0.4573 S13: 0.2438
REMARK 3 S21: -0.2544 S22: -0.1785 S23: -0.0069
REMARK 3 S31: -0.5321 S32: 0.3732 S33: -0.2688
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 : B 176 B 197
REMARK 3 ORIGIN FOR THE GROUP (A): 92.1490 -4.5590 -4.8010
REMARK 3 T TENSOR
REMARK 3 T11: 1.3127 T22: 1.5139
REMARK 3 T33: 1.4456 T12: 0.0685
REMARK 3 T13: 0.0626 T23: -0.1381
REMARK 3 L TENSOR
REMARK 3 L11: 2.7900 L22: 8.1678
REMARK 3 L33: 3.1981 L12: -1.4140
REMARK 3 L13: 2.4654 L23: -3.9800
REMARK 3 S TENSOR
REMARK 3 S11: -0.5098 S12: 0.0033 S13: -0.0658
REMARK 3 S21: 0.2011 S22: 0.7452 S23: 0.1257
REMARK 3 S31: -0.3719 S32: -0.3023 S33: -0.2355
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 : B 198 B 286
REMARK 3 ORIGIN FOR THE GROUP (A): 64.3700 -2.7270 5.5240
REMARK 3 T TENSOR
REMARK 3 T11: 0.7989 T22: 0.9136
REMARK 3 T33: 0.8877 T12: -0.1381
REMARK 3 T13: 0.1922 T23: 0.0854
REMARK 3 L TENSOR
REMARK 3 L11: 7.8051 L22: 4.6078
REMARK 3 L33: 6.6046 L12: 2.0643
REMARK 3 L13: 0.7468 L23: -2.3005
REMARK 3 S TENSOR
REMARK 3 S11: 0.4954 S12: 0.0804 S13: 0.8497
REMARK 3 S21: -0.0344 S22: -0.2391 S23: -1.0600
REMARK 3 S31: -0.9038 S32: 1.2097 S33: -0.2563
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 : D 1 D 105
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1780 16.4760 27.0640
REMARK 3 T TENSOR
REMARK 3 T11: 0.3970 T22: 0.0771
REMARK 3 T33: 0.3855 T12: 0.0541
REMARK 3 T13: -0.0807 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 4.4083 L22: 5.8656
REMARK 3 L33: 6.8217 L12: -1.4975
REMARK 3 L13: 0.7015 L23: 0.2457
REMARK 3 S TENSOR
REMARK 3 S11: -0.1675 S12: 0.3709 S13: 0.3609
REMARK 3 S21: -0.8357 S22: -0.4002 S23: 0.2766
REMARK 3 S31: -0.9592 S32: -0.3429 S33: 0.5677
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 : D 106 D 157
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9270 46.3870 46.1370
REMARK 3 T TENSOR
REMARK 3 T11: 0.5771 T22: 0.1931
REMARK 3 T33: 0.6288 T12: 0.1023
REMARK 3 T13: -0.0243 T23: 0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 6.0968 L22: 5.8882
REMARK 3 L33: 9.1882 L12: 3.2539
REMARK 3 L13: 6.1701 L23: 5.3152
REMARK 3 S TENSOR
REMARK 3 S11: -0.0382 S12: 0.6044 S13: 0.1561
REMARK 3 S21: -1.0939 S22: -0.0852 S23: -0.0468
REMARK 3 S31: -0.7314 S32: 0.8283 S33: 0.1234
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 : D 158 D 211
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4110 47.4600 46.1140
REMARK 3 T TENSOR
REMARK 3 T11: 0.6138 T22: 0.1715
REMARK 3 T33: 0.6461 T12: 0.0123
REMARK 3 T13: 0.0619 T23: 0.0502
REMARK 3 L TENSOR
REMARK 3 L11: 5.2532 L22: 6.6416
REMARK 3 L33: 7.9362 L12: 1.5577
REMARK 3 L13: 4.1440 L23: 5.1708
REMARK 3 S TENSOR
REMARK 3 S11: 0.0639 S12: 0.6582 S13: 0.4101
REMARK 3 S21: -0.5866 S22: -0.1503 S23: 0.0161
REMARK 3 S31: -0.7061 S32: 0.5501 S33: 0.0864
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 : E 1 E 80
REMARK 3 ORIGIN FOR THE GROUP (A): 24.9360 6.5270 45.2740
REMARK 3 T TENSOR
REMARK 3 T11: 0.1066 T22: 0.0673
REMARK 3 T33: 0.3541 T12: 0.0148
REMARK 3 T13: 0.1014 T23: 0.0424
REMARK 3 L TENSOR
REMARK 3 L11: 3.7908 L22: 6.2133
REMARK 3 L33: 7.0208 L12: -0.8106
REMARK 3 L13: 0.4644 L23: 3.7005
REMARK 3 S TENSOR
REMARK 3 S11: -0.1900 S12: -0.1204 S13: 0.1782
REMARK 3 S21: 0.3498 S22: -0.0452 S23: 0.2633
REMARK 3 S31: -0.1052 S32: 0.3674 S33: 0.2353
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 : E 81 E 137
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3250 22.1370 49.2690
REMARK 3 T TENSOR
REMARK 3 T11: 0.2398 T22: 0.2230
REMARK 3 T33: 0.3404 T12: 0.0359
REMARK 3 T13: 0.0282 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 1.3972 L22: 6.8867
REMARK 3 L33: 2.6437 L12: -1.8229
REMARK 3 L13: -1.7867 L23: 3.5792
REMARK 3 S TENSOR
REMARK 3 S11: 0.1806 S12: -0.3448 S13: 0.0303
REMARK 3 S21: -0.3040 S22: -0.2578 S23: 0.1880
REMARK 3 S31: -0.2767 S32: 0.2439 S33: 0.0771
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 : E 138 E 217
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3200 37.1270 58.2600
REMARK 3 T TENSOR
REMARK 3 T11: 0.3039 T22: 0.1272
REMARK 3 T33: 0.6124 T12: -0.0659
REMARK 3 T13: 0.0295 T23: -0.0608
REMARK 3 L TENSOR
REMARK 3 L11: 9.5398 L22: 6.0617
REMARK 3 L33: 2.1218 L12: -4.7834
REMARK 3 L13: -0.0673 L23: 0.8805
REMARK 3 S TENSOR
REMARK 3 S11: 0.0679 S12: -0.5066 S13: 0.1082
REMARK 3 S21: 0.0423 S22: -0.0022 S23: 0.4759
REMARK 3 S31: -0.1055 S32: -0.0904 S33: -0.0657
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 : F 1 F 105
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7280 -34.9840 42.2410
REMARK 3 T TENSOR
REMARK 3 T11: 0.1012 T22: 0.0274
REMARK 3 T33: 0.4867 T12: 0.0212
REMARK 3 T13: 0.0714 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 6.3499 L22: 6.0538
REMARK 3 L33: 3.2788 L12: -0.1711
REMARK 3 L13: 0.0291 L23: -2.2867
REMARK 3 S TENSOR
REMARK 3 S11: 0.0890 S12: -0.2120 S13: -0.4868
REMARK 3 S21: 0.2840 S22: -0.0617 S23: -0.3335
REMARK 3 S31: 0.0088 S32: 0.0959 S33: -0.0273
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 : F 106 F 188
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7950 -63.2070 43.9360
REMARK 3 T TENSOR
REMARK 3 T11: 0.4770 T22: 0.1068
REMARK 3 T33: 1.0959 T12: 0.0845
REMARK 3 T13: -0.0287 T23: 0.1515
REMARK 3 L TENSOR
REMARK 3 L11: 13.3180 L22: 5.4432
REMARK 3 L33: 6.0560 L12: 5.5032
REMARK 3 L13: 6.1924 L23: 2.4838
REMARK 3 S TENSOR
REMARK 3 S11: 0.2926 S12: 0.5880 S13: -1.0705
REMARK 3 S21: -0.5295 S22: 0.0979 S23: -0.2011
REMARK 3 S31: 0.6497 S32: 0.0936 S33: -0.3904
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 : F 189 F 211
REMARK 3 ORIGIN FOR THE GROUP (A): 11.8760 -72.0560 46.6510
REMARK 3 T TENSOR
REMARK 3 T11: 0.9643 T22: 0.3668
REMARK 3 T33: 1.5131 T12: -0.1182
REMARK 3 T13: -0.0949 T23: 0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 0.1351 L22: 3.9355
REMARK 3 L33: 2.7905 L12: -0.6954
REMARK 3 L13: 0.1942 L23: -0.8479
REMARK 3 S TENSOR
REMARK 3 S11: 0.0867 S12: -0.0438 S13: -0.1538
REMARK 3 S21: -0.0348 S22: 0.0106 S23: 0.7506
REMARK 3 S31: 1.2945 S32: -0.0222 S33: -0.0973
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 : G 1 G 80
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7730 -25.2400 31.1340
REMARK 3 T TENSOR
REMARK 3 T11: 0.1178 T22: 0.0771
REMARK 3 T33: 0.2876 T12: 0.0420
REMARK 3 T13: 0.0535 T23: 0.0524
REMARK 3 L TENSOR
REMARK 3 L11: 6.5590 L22: 7.3212
REMARK 3 L33: 3.4697 L12: 2.6453
REMARK 3 L13: -0.2578 L23: -1.3303
REMARK 3 S TENSOR
REMARK 3 S11: -0.0507 S12: 0.2953 S13: -0.0828
REMARK 3 S21: -0.0195 S22: 0.2011 S23: 0.5403
REMARK 3 S31: -0.0038 S32: -0.1772 S33: -0.1504
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 : G 81 G 172
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0050 -45.0850 42.0350
REMARK 3 T TENSOR
REMARK 3 T11: 0.0653 T22: 0.0997
REMARK 3 T33: 0.7504 T12: -0.0253
REMARK 3 T13: 0.0416 T23: 0.0693
REMARK 3 L TENSOR
REMARK 3 L11: 3.7808 L22: 5.6402
REMARK 3 L33: 1.1374 L12: 2.6455
REMARK 3 L13: -1.3556 L23: -1.1870
REMARK 3 S TENSOR
REMARK 3 S11: -0.0479 S12: -0.0535 S13: -0.8174
REMARK 3 S21: 0.0043 S22: 0.0020 S23: 0.0299
REMARK 3 S31: 0.1353 S32: -0.2132 S33: 0.0459
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 : G 173 G 216
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5390 -55.6170 50.5200
REMARK 3 T TENSOR
REMARK 3 T11: 0.3378 T22: 0.4265
REMARK 3 T33: 0.7016 T12: -0.0268
REMARK 3 T13: -0.0003 T23: 0.0454
REMARK 3 L TENSOR
REMARK 3 L11: 2.4311 L22: 4.1774
REMARK 3 L33: 6.6182 L12: -0.5567
REMARK 3 L13: 1.5845 L23: -4.2615
REMARK 3 S TENSOR
REMARK 3 S11: -0.1623 S12: -0.3031 S13: -0.1036
REMARK 3 S21: 0.0077 S22: 0.2615 S23: 0.2216
REMARK 3 S31: 0.3745 S32: -0.4602 S33: -0.0992
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 4WFG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-14.
REMARK 100 THE DEPOSITION ID IS D_1000203724.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8-9
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) : 0.9781
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40099
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 48.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 4I9W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS PH 8.8, 200 MM CA(NO3)2, 27
REMARK 280 -30%(VOL/VOL) PEG400, 52 MM TRICHLOROETHANOL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, 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 69.38000
REMARK 290 SMTRY3 2 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: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E, F, G
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 THR A 2
REMARK 465 THR A 3
REMARK 465 ALA A 4
REMARK 465 PRO A 5
REMARK 465 GLN A 6
REMARK 465 GLU A 7
REMARK 465 PRO A 8
REMARK 465 PRO A 9
REMARK 465 ALA A 10
REMARK 465 ARG A 11
REMARK 465 PRO A 12
REMARK 465 LEU A 13
REMARK 465 GLN A 14
REMARK 465 ALA A 15
REMARK 465 GLY A 16
REMARK 465 SER A 17
REMARK 465 GLY A 18
REMARK 465 ALA A 19
REMARK 465 GLY A 20
REMARK 465 PRO A 21
REMARK 465 ALA A 22
REMARK 465 PRO A 23
REMARK 465 GLY A 24
REMARK 465 ARG A 25
REMARK 465 ALA A 26
REMARK 465 MET A 27
REMARK 465 GLN A 104
REMARK 465 SER A 105
REMARK 465 THR A 106
REMARK 465 SER A 107
REMARK 465 GLN A 108
REMARK 465 SER A 109
REMARK 465 SER A 287
REMARK 465 ARG A 288
REMARK 465 ARG A 289
REMARK 465 THR A 290
REMARK 465 SER A 291
REMARK 465 ASN A 292
REMARK 465 SER A 293
REMARK 465 LEU A 294
REMARK 465 GLU A 295
REMARK 465 VAL A 296
REMARK 465 LEU A 297
REMARK 465 PHE A 298
REMARK 465 GLN A 299
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 THR B 3
REMARK 465 ALA B 4
REMARK 465 PRO B 5
REMARK 465 GLN B 6
REMARK 465 GLU B 7
REMARK 465 PRO B 8
REMARK 465 PRO B 9
REMARK 465 ALA B 10
REMARK 465 ARG B 11
REMARK 465 PRO B 12
REMARK 465 LEU B 13
REMARK 465 GLN B 14
REMARK 465 ALA B 15
REMARK 465 GLY B 16
REMARK 465 SER B 17
REMARK 465 GLY B 18
REMARK 465 ALA B 19
REMARK 465 GLY B 20
REMARK 465 PRO B 21
REMARK 465 ALA B 22
REMARK 465 PRO B 23
REMARK 465 GLY B 24
REMARK 465 ARG B 25
REMARK 465 ALA B 26
REMARK 465 MET B 27
REMARK 465 THR B 106
REMARK 465 SER B 107
REMARK 465 GLN B 108
REMARK 465 SER B 109
REMARK 465 SER B 287
REMARK 465 ARG B 288
REMARK 465 ARG B 289
REMARK 465 THR B 290
REMARK 465 SER B 291
REMARK 465 ASN B 292
REMARK 465 SER B 293
REMARK 465 LEU B 294
REMARK 465 GLU B 295
REMARK 465 VAL B 296
REMARK 465 LEU B 297
REMARK 465 PHE B 298
REMARK 465 GLN B 299
REMARK 465 GLY E 130
REMARK 465 SER E 131
REMARK 465 ALA E 132
REMARK 465 ALA E 133
REMARK 465 GLN E 134
REMARK 465 THR E 135
REMARK 465 GLY G 130
REMARK 465 SER G 131
REMARK 465 ALA G 132
REMARK 465 ALA G 133
REMARK 465 GLN G 134
REMARK 465 THR G 135
REMARK 465 ASP G 217
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 SER A 110 OG
REMARK 470 HIS A 111 CG ND1 CD2 CE1 NE2
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 ND2 ASN D 189 OD1 ASN D 211 2.09
REMARK 500 O GLY F 98 O HOH F 305 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU E 194 OE1 GLU G 10 2556 2.14
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 CYS B 78 CA - CB - SG ANGL. DEV. = 6.8 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 VAL A 210 -62.43 -101.19
REMARK 500 ASP A 253 2.48 85.81
REMARK 500 SER A 254 85.69 -161.08
REMARK 500 HIS B 111 137.82 77.96
REMARK 500 VAL B 210 -62.94 -101.40
REMARK 500 ASP B 253 6.02 82.16
REMARK 500 SER B 254 79.71 -157.21
REMARK 500 ASP D 49 53.85 39.65
REMARK 500 THR D 50 -50.22 74.35
REMARK 500 ALA D 83 -179.83 -178.37
REMARK 500 TRP D 90 46.13 -146.61
REMARK 500 HIS E 41 84.82 -15.44
REMARK 500 LYS E 43 -146.68 -131.84
REMARK 500 SER E 77 60.74 29.42
REMARK 500 ALA E 92 -176.81 -172.52
REMARK 500 TYR E 101 -39.90 -144.29
REMARK 500 THR F 50 -50.54 74.13
REMARK 500 ALA F 83 -179.11 -176.85
REMARK 500 TRP F 90 44.71 -146.95
REMARK 500 PRO F 203 153.54 -48.11
REMARK 500 HIS G 41 81.79 -9.28
REMARK 500 LYS G 43 -154.15 -130.54
REMARK 500 SER G 77 58.95 31.34
REMARK 500 SER G 85 65.56 36.78
REMARK 500 ALA G 92 -177.97 -171.33
REMARK 500 TYR G 101 -41.00 -143.21
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 306 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 98 O
REMARK 620 2 ASP A 100 OD1 106.0
REMARK 620 3 HOH A 419 O 58.3 93.2
REMARK 620 4 GLU B 58 OE2 99.7 140.3 75.1
REMARK 620 5 HOH B 418 O 93.2 122.7 140.5 84.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 305 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 112 O
REMARK 620 2 ASP A 115 OD1 68.5
REMARK 620 3 ASP A 115 OD2 79.8 49.1
REMARK 620 4 SER A 118 OG 79.4 67.0 116.1
REMARK 620 5 ASP A 249 OD1 119.2 125.2 158.4 62.6
REMARK 620 6 ASP A 249 OD2 110.0 167.2 143.7 100.2 43.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 TL A 301 TL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 129 O
REMARK 620 2 THR A 129 OG1 57.7
REMARK 620 3 THR A 238 O 72.5 107.0
REMARK 620 4 THR A 238 OG1 106.4 83.8 62.2
REMARK 620 5 THR B 129 O 105.3 163.0 64.8 103.6
REMARK 620 6 THR B 129 OG1 162.3 137.5 104.6 86.5 59.1
REMARK 620 7 THR B 238 O 61.6 97.3 102.2 163.7 71.3 103.0
REMARK 620 8 THR B 238 OG1 95.9 80.8 157.7 140.1 101.8 80.6 55.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 TL A 307 TL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 129 O
REMARK 620 2 ILE A 130 O 70.9
REMARK 620 3 THR A 238 O 72.4 85.0
REMARK 620 4 VAL A 239 O 137.9 78.3 77.2
REMARK 620 5 THR B 129 O 107.4 146.5 63.7 83.3
REMARK 620 6 ILE B 130 O 143.5 130.6 130.5 78.6 71.1
REMARK 620 7 THR B 238 O 62.6 128.8 99.7 152.7 71.4 83.6
REMARK 620 8 VAL B 239 O 79.5 78.1 150.7 121.6 135.2 77.9 73.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 TL A 302 TL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 130 O
REMARK 620 2 GLY A 131 O 72.5
REMARK 620 3 VAL A 239 O 67.4 133.0
REMARK 620 4 GLY A 240 O 79.5 77.9 71.7
REMARK 620 5 ILE B 130 O 100.0 146.4 66.3 134.1
REMARK 620 6 GLY B 131 O 145.4 132.5 78.8 83.5 71.3
REMARK 620 7 VAL B 239 O 66.9 81.8 103.4 144.8 65.5 130.8
REMARK 620 8 GLY B 240 O 133.8 84.4 142.0 134.5 77.7 78.3 70.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 TL A 303 TL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 131 O
REMARK 620 2 TYR A 132 O 62.5
REMARK 620 3 GLY A 240 O 61.9 78.5
REMARK 620 4 PHE A 241 O 117.1 71.6 68.9
REMARK 620 5 GLY B 131 O 103.4 147.2 68.9 92.6
REMARK 620 6 TYR B 132 O 145.6 142.1 131.9 96.6 66.2
REMARK 620 7 GLY B 240 O 65.6 124.3 94.4 155.4 63.9 80.9
REMARK 620 8 PHE B 241 O 84.4 90.0 146.0 137.3 119.3 74.5 65.9
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 TL A 304 TL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 218 O
REMARK 620 2 ASP A 222 OD1 90.3
REMARK 620 3 TRP A 223 O 73.8 114.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 TL B 303 TL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 218 O
REMARK 620 2 TRP B 223 O 70.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 194 OE2
REMARK 620 2 GLU G 10 OE1 77.6
REMARK 620 3 GLU G 10 OE2 77.1 0.9
REMARK 620 4 LYS G 19 O 76.1 1.9 2.1
REMARK 620 5 HOH G 407 O 74.9 2.8 2.2 2.2
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TL A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue TL B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WFE RELATED DB: PDB
REMARK 900 RELATED ID: 4WFF RELATED DB: PDB
REMARK 900 RELATED ID: 4WFH RELATED DB: PDB
DBREF 4WFG A 1 290 UNP Q9NYG8 KCNK4_HUMAN 1 290
DBREF 4WFG B 1 290 UNP Q9NYG8 KCNK4_HUMAN 1 290
DBREF 4WFG D 1 211 PDB 4WFG 4WFG 1 211
DBREF 4WFG E 1 217 PDB 4WFG 4WFG 1 217
DBREF 4WFG F 1 211 PDB 4WFG 4WFG 1 211
DBREF 4WFG G 1 217 PDB 4WFG 4WFG 1 217
SEQADV 4WFG GLN A 104 UNP Q9NYG8 ASN 104 ENGINEERED MUTATION
SEQADV 4WFG GLN A 108 UNP Q9NYG8 ASN 108 ENGINEERED MUTATION
SEQADV 4WFG SER A 291 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG ASN A 292 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG SER A 293 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG LEU A 294 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG GLU A 295 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG VAL A 296 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG LEU A 297 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG PHE A 298 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG GLN A 299 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG GLN B 104 UNP Q9NYG8 ASN 104 ENGINEERED MUTATION
SEQADV 4WFG GLN B 108 UNP Q9NYG8 ASN 108 ENGINEERED MUTATION
SEQADV 4WFG SER B 291 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG ASN B 292 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG SER B 293 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG LEU B 294 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG GLU B 295 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG VAL B 296 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG LEU B 297 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG PHE B 298 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4WFG GLN B 299 UNP Q9NYG8 EXPRESSION TAG
SEQRES 1 A 299 MET THR THR ALA PRO GLN GLU PRO PRO ALA ARG PRO LEU
SEQRES 2 A 299 GLN ALA GLY SER GLY ALA GLY PRO ALA PRO GLY ARG ALA
SEQRES 3 A 299 MET ARG SER THR THR LEU LEU ALA LEU LEU ALA LEU VAL
SEQRES 4 A 299 LEU LEU TYR LEU VAL SER GLY ALA LEU VAL PHE ARG ALA
SEQRES 5 A 299 LEU GLU GLN PRO HIS GLU GLN GLN ALA GLN ARG GLU LEU
SEQRES 6 A 299 GLY GLU VAL ARG GLU LYS PHE LEU ARG ALA HIS PRO CYS
SEQRES 7 A 299 VAL SER ASP GLN GLU LEU GLY LEU LEU ILE LYS GLU VAL
SEQRES 8 A 299 ALA ASP ALA LEU GLY GLY GLY ALA ASP PRO GLU THR GLN
SEQRES 9 A 299 SER THR SER GLN SER SER HIS SER ALA TRP ASP LEU GLY
SEQRES 10 A 299 SER ALA PHE PHE PHE SER GLY THR ILE ILE THR THR ILE
SEQRES 11 A 299 GLY TYR GLY ASN VAL ALA LEU ARG THR ASP ALA GLY ARG
SEQRES 12 A 299 LEU PHE CYS ILE PHE TYR ALA LEU VAL GLY ILE PRO LEU
SEQRES 13 A 299 PHE GLY ILE LEU LEU ALA GLY VAL GLY ASP ARG LEU GLY
SEQRES 14 A 299 SER SER LEU ARG HIS GLY ILE GLY HIS ILE GLU ALA ILE
SEQRES 15 A 299 PHE LEU LYS TRP HIS VAL PRO PRO GLU LEU VAL ARG VAL
SEQRES 16 A 299 LEU SER ALA MET LEU PHE LEU LEU ILE GLY CYS LEU LEU
SEQRES 17 A 299 PHE VAL LEU THR PRO THR PHE VAL PHE CYS TYR MET GLU
SEQRES 18 A 299 ASP TRP SER LYS LEU GLU ALA ILE TYR PHE VAL ILE VAL
SEQRES 19 A 299 THR LEU THR THR VAL GLY PHE GLY ASP TYR VAL ALA GLY
SEQRES 20 A 299 ALA ASP PRO ARG GLN ASP SER PRO ALA TYR GLN PRO LEU
SEQRES 21 A 299 VAL TRP PHE TRP ILE LEU LEU GLY LEU ALA TYR PHE ALA
SEQRES 22 A 299 SER VAL LEU THR THR ILE GLY ASN TRP LEU ARG VAL VAL
SEQRES 23 A 299 SER ARG ARG THR SER ASN SER LEU GLU VAL LEU PHE GLN
SEQRES 1 B 299 MET THR THR ALA PRO GLN GLU PRO PRO ALA ARG PRO LEU
SEQRES 2 B 299 GLN ALA GLY SER GLY ALA GLY PRO ALA PRO GLY ARG ALA
SEQRES 3 B 299 MET ARG SER THR THR LEU LEU ALA LEU LEU ALA LEU VAL
SEQRES 4 B 299 LEU LEU TYR LEU VAL SER GLY ALA LEU VAL PHE ARG ALA
SEQRES 5 B 299 LEU GLU GLN PRO HIS GLU GLN GLN ALA GLN ARG GLU LEU
SEQRES 6 B 299 GLY GLU VAL ARG GLU LYS PHE LEU ARG ALA HIS PRO CYS
SEQRES 7 B 299 VAL SER ASP GLN GLU LEU GLY LEU LEU ILE LYS GLU VAL
SEQRES 8 B 299 ALA ASP ALA LEU GLY GLY GLY ALA ASP PRO GLU THR GLN
SEQRES 9 B 299 SER THR SER GLN SER SER HIS SER ALA TRP ASP LEU GLY
SEQRES 10 B 299 SER ALA PHE PHE PHE SER GLY THR ILE ILE THR THR ILE
SEQRES 11 B 299 GLY TYR GLY ASN VAL ALA LEU ARG THR ASP ALA GLY ARG
SEQRES 12 B 299 LEU PHE CYS ILE PHE TYR ALA LEU VAL GLY ILE PRO LEU
SEQRES 13 B 299 PHE GLY ILE LEU LEU ALA GLY VAL GLY ASP ARG LEU GLY
SEQRES 14 B 299 SER SER LEU ARG HIS GLY ILE GLY HIS ILE GLU ALA ILE
SEQRES 15 B 299 PHE LEU LYS TRP HIS VAL PRO PRO GLU LEU VAL ARG VAL
SEQRES 16 B 299 LEU SER ALA MET LEU PHE LEU LEU ILE GLY CYS LEU LEU
SEQRES 17 B 299 PHE VAL LEU THR PRO THR PHE VAL PHE CYS TYR MET GLU
SEQRES 18 B 299 ASP TRP SER LYS LEU GLU ALA ILE TYR PHE VAL ILE VAL
SEQRES 19 B 299 THR LEU THR THR VAL GLY PHE GLY ASP TYR VAL ALA GLY
SEQRES 20 B 299 ALA ASP PRO ARG GLN ASP SER PRO ALA TYR GLN PRO LEU
SEQRES 21 B 299 VAL TRP PHE TRP ILE LEU LEU GLY LEU ALA TYR PHE ALA
SEQRES 22 B 299 SER VAL LEU THR THR ILE GLY ASN TRP LEU ARG VAL VAL
SEQRES 23 B 299 SER ARG ARG THR SER ASN SER LEU GLU VAL LEU PHE GLN
SEQRES 1 D 211 GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA
SEQRES 2 D 211 SER PRO GLY GLU LYS VAL THR MET THR CYS SER ALA SER
SEQRES 3 D 211 SER SER VAL SER TYR MET HIS TRP TYR GLN GLN LYS SER
SEQRES 4 D 211 GLY THR SER PRO LYS ARG TRP ILE TYR ASP THR SER LYS
SEQRES 5 D 211 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY
SEQRES 6 D 211 SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU
SEQRES 7 D 211 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TRP SER
SEQRES 8 D 211 ASN SER PRO PRO THR PHE GLY ALA GLY ALA LYS LEU GLU
SEQRES 9 D 211 LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE
SEQRES 10 D 211 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER
SEQRES 11 D 211 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE
SEQRES 12 D 211 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN
SEQRES 13 D 211 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP
SEQRES 14 D 211 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS
SEQRES 15 D 211 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA
SEQRES 16 D 211 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE
SEQRES 17 D 211 ASN ARG ASN
SEQRES 1 E 217 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS
SEQRES 2 E 217 PRO GLY ALA SER MET LYS THR SER CYS LYS VAL SER GLY
SEQRES 3 E 217 TYR SER PHE THR GLY TYR ILE MET ASN TRP VAL LYS GLN
SEQRES 4 E 217 ARG HIS GLY LYS ASN LEU GLU TRP ILE GLY LEU ILE ASN
SEQRES 5 E 217 PRO ASN THR GLY TYR THR THR TYR ASN GLN LYS PHE LYS
SEQRES 6 E 217 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR
SEQRES 7 E 217 ALA TYR MET GLU LEU LEU SER LEU THR SER GLU ASP SER
SEQRES 8 E 217 ALA ILE TYR TYR CYS THR ARG GLY ASN TYR VAL PHE ASP
SEQRES 9 E 217 TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER ALA
SEQRES 10 E 217 LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY
SEQRES 11 E 217 SER ALA ALA GLN THR ASN SER MET VAL THR LEU GLY CYS
SEQRES 12 E 217 LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR
SEQRES 13 E 217 TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE
SEQRES 14 E 217 PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER
SEQRES 15 E 217 SER VAL THR VAL PRO SER SER SER TRP PRO SER GLU THR
SEQRES 16 E 217 VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS
SEQRES 17 E 217 VAL ASP LYS LYS ILE VAL PRO ARG ASP
SEQRES 1 F 211 GLN ILE VAL LEU THR GLN SER PRO ALA ILE MET SER ALA
SEQRES 2 F 211 SER PRO GLY GLU LYS VAL THR MET THR CYS SER ALA SER
SEQRES 3 F 211 SER SER VAL SER TYR MET HIS TRP TYR GLN GLN LYS SER
SEQRES 4 F 211 GLY THR SER PRO LYS ARG TRP ILE TYR ASP THR SER LYS
SEQRES 5 F 211 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY
SEQRES 6 F 211 SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU
SEQRES 7 F 211 ALA GLU ASP ALA ALA THR TYR TYR CYS GLN GLN TRP SER
SEQRES 8 F 211 ASN SER PRO PRO THR PHE GLY ALA GLY ALA LYS LEU GLU
SEQRES 9 F 211 LEU LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE PHE
SEQRES 10 F 211 PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA SER
SEQRES 11 F 211 VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE
SEQRES 12 F 211 ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN ASN
SEQRES 13 F 211 GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS ASP
SEQRES 14 F 211 SER THR TYR SER MET SER SER THR LEU THR LEU THR LYS
SEQRES 15 F 211 ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU ALA
SEQRES 16 F 211 THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER PHE
SEQRES 17 F 211 ASN ARG ASN
SEQRES 1 G 217 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU VAL LYS
SEQRES 2 G 217 PRO GLY ALA SER MET LYS THR SER CYS LYS VAL SER GLY
SEQRES 3 G 217 TYR SER PHE THR GLY TYR ILE MET ASN TRP VAL LYS GLN
SEQRES 4 G 217 ARG HIS GLY LYS ASN LEU GLU TRP ILE GLY LEU ILE ASN
SEQRES 5 G 217 PRO ASN THR GLY TYR THR THR TYR ASN GLN LYS PHE LYS
SEQRES 6 G 217 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR
SEQRES 7 G 217 ALA TYR MET GLU LEU LEU SER LEU THR SER GLU ASP SER
SEQRES 8 G 217 ALA ILE TYR TYR CYS THR ARG GLY ASN TYR VAL PHE ASP
SEQRES 9 G 217 TYR TRP GLY GLN GLY THR THR LEU THR VAL SER SER ALA
SEQRES 10 G 217 LYS THR THR PRO PRO SER VAL TYR PRO LEU ALA PRO GLY
SEQRES 11 G 217 SER ALA ALA GLN THR ASN SER MET VAL THR LEU GLY CYS
SEQRES 12 G 217 LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL THR VAL THR
SEQRES 13 G 217 TRP ASN SER GLY SER LEU SER SER GLY VAL HIS THR PHE
SEQRES 14 G 217 PRO ALA VAL LEU GLN SER ASP LEU TYR THR LEU SER SER
SEQRES 15 G 217 SER VAL THR VAL PRO SER SER SER TRP PRO SER GLU THR
SEQRES 16 G 217 VAL THR CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS
SEQRES 17 G 217 VAL ASP LYS LYS ILE VAL PRO ARG ASP
HET TL A 301 1
HET TL A 302 1
HET TL A 303 1
HET TL A 304 1
HET CA A 305 1
HET CA A 306 1
HET TL A 307 1
HET TL B 301 1
HET TL B 302 1
HET TL B 303 1
HET CA G 301 1
HETNAM TL THALLIUM (I) ION
HETNAM CA CALCIUM ION
FORMUL 7 TL 8(TL 1+)
FORMUL 11 CA 3(CA 2+)
FORMUL 18 HOH *190(H2 O)
HELIX 1 AA1 ARG A 28 GLN A 55 1 28
HELIX 2 AA2 PRO A 56 GLU A 58 5 3
HELIX 3 AA3 GLN A 59 HIS A 76 1 18
HELIX 4 AA4 SER A 80 GLY A 97 1 18
HELIX 5 AA5 ASP A 115 THR A 128 1 14
HELIX 6 AA6 THR A 139 TRP A 186 1 48
HELIX 7 AA7 PRO A 189 VAL A 210 1 22
HELIX 8 AA8 VAL A 210 ASP A 222 1 13
HELIX 9 AA9 SER A 224 THR A 237 1 14
HELIX 10 AB1 ALA A 256 VAL A 286 1 31
HELIX 11 AB2 SER B 29 HIS B 76 1 48
HELIX 12 AB3 SER B 80 GLY B 97 1 18
HELIX 13 AB4 ASP B 115 THR B 128 1 14
HELIX 14 AB5 THR B 139 TRP B 186 1 48
HELIX 15 AB6 PRO B 189 VAL B 210 1 22
HELIX 16 AB7 VAL B 210 ASP B 222 1 13
HELIX 17 AB8 SER B 224 THR B 237 1 14
HELIX 18 AB9 ALA B 256 VAL B 286 1 31
HELIX 19 AC1 GLU D 78 ALA D 82 5 5
HELIX 20 AC2 SER D 120 SER D 126 1 7
HELIX 21 AC3 LYS D 182 HIS D 188 1 7
HELIX 22 AC4 SER E 28 TYR E 32 5 5
HELIX 23 AC5 GLN E 62 LYS E 65 5 4
HELIX 24 AC6 THR E 87 SER E 91 5 5
HELIX 25 AC7 SER E 159 SER E 161 5 3
HELIX 26 AC8 PRO E 203 SER E 206 5 4
HELIX 27 AC9 GLU F 78 ALA F 82 5 5
HELIX 28 AD1 SER F 120 SER F 126 1 7
HELIX 29 AD2 LYS F 182 HIS F 188 1 7
HELIX 30 AD3 SER G 28 TYR G 32 5 5
HELIX 31 AD4 GLN G 62 LYS G 65 5 4
HELIX 32 AD5 THR G 87 SER G 91 5 5
HELIX 33 AD6 SER G 159 SER G 161 5 3
HELIX 34 AD7 PRO G 203 SER G 206 5 4
SHEET 1 AA1 4 LEU D 4 THR D 5 0
SHEET 2 AA1 4 VAL D 19 ALA D 25 -1 O SER D 24 N THR D 5
SHEET 3 AA1 4 SER D 69 ILE D 74 -1 O ILE D 74 N VAL D 19
SHEET 4 AA1 4 PHE D 61 SER D 66 -1 N SER D 64 O SER D 71
SHEET 1 AA2 6 ILE D 10 ALA D 13 0
SHEET 2 AA2 6 ALA D 101 LEU D 105 1 O GLU D 104 N MET D 11
SHEET 3 AA2 6 ALA D 83 GLN D 89 -1 N ALA D 83 O LEU D 103
SHEET 4 AA2 6 HIS D 33 GLN D 37 -1 N HIS D 33 O GLN D 88
SHEET 5 AA2 6 LYS D 44 TYR D 48 -1 O ILE D 47 N TRP D 34
SHEET 6 AA2 6 LYS D 52 LEU D 53 -1 O LYS D 52 N TYR D 48
SHEET 1 AA3 4 ILE D 10 ALA D 13 0
SHEET 2 AA3 4 ALA D 101 LEU D 105 1 O GLU D 104 N MET D 11
SHEET 3 AA3 4 ALA D 83 GLN D 89 -1 N ALA D 83 O LEU D 103
SHEET 4 AA3 4 THR D 96 PHE D 97 -1 O THR D 96 N GLN D 89
SHEET 1 AA4 4 THR D 113 PHE D 117 0
SHEET 2 AA4 4 GLY D 128 PHE D 138 -1 O ASN D 136 N THR D 113
SHEET 3 AA4 4 TYR D 172 THR D 181 -1 O LEU D 178 N VAL D 131
SHEET 4 AA4 4 VAL D 158 TRP D 162 -1 N LEU D 159 O THR D 177
SHEET 1 AA5 4 SER D 152 ARG D 154 0
SHEET 2 AA5 4 ILE D 143 ILE D 149 -1 N ILE D 149 O SER D 152
SHEET 3 AA5 4 SER D 190 HIS D 197 -1 O THR D 196 N ASN D 144
SHEET 4 AA5 4 ILE D 204 ASN D 209 -1 O ILE D 204 N ALA D 195
SHEET 1 AA6 4 GLN E 3 GLN E 6 0
SHEET 2 AA6 4 MET E 18 SER E 25 -1 O LYS E 23 N GLN E 5
SHEET 3 AA6 4 THR E 78 LEU E 83 -1 O LEU E 83 N MET E 18
SHEET 4 AA6 4 ALA E 68 ASP E 73 -1 N THR E 71 O TYR E 80
SHEET 1 AA7 6 GLU E 10 VAL E 12 0
SHEET 2 AA7 6 THR E 110 VAL E 114 1 O THR E 113 N GLU E 10
SHEET 3 AA7 6 ALA E 92 ARG E 98 -1 N ALA E 92 O LEU E 112
SHEET 4 AA7 6 MET E 34 GLN E 39 -1 N ASN E 35 O THR E 97
SHEET 5 AA7 6 LEU E 45 ILE E 51 -1 O ILE E 48 N TRP E 36
SHEET 6 AA7 6 THR E 58 TYR E 60 -1 O THR E 59 N LEU E 50
SHEET 1 AA8 4 GLU E 10 VAL E 12 0
SHEET 2 AA8 4 THR E 110 VAL E 114 1 O THR E 113 N GLU E 10
SHEET 3 AA8 4 ALA E 92 ARG E 98 -1 N ALA E 92 O LEU E 112
SHEET 4 AA8 4 TYR E 105 TRP E 106 -1 O TYR E 105 N ARG E 98
SHEET 1 AA9 4 SER E 123 LEU E 127 0
SHEET 2 AA9 4 MET E 138 TYR E 148 -1 O LEU E 144 N TYR E 125
SHEET 3 AA9 4 LEU E 177 PRO E 187 -1 O VAL E 186 N VAL E 139
SHEET 4 AA9 4 VAL E 166 THR E 168 -1 N HIS E 167 O SER E 183
SHEET 1 AB1 4 SER E 123 LEU E 127 0
SHEET 2 AB1 4 MET E 138 TYR E 148 -1 O LEU E 144 N TYR E 125
SHEET 3 AB1 4 LEU E 177 PRO E 187 -1 O VAL E 186 N VAL E 139
SHEET 4 AB1 4 VAL E 172 GLN E 174 -1 N GLN E 174 O LEU E 177
SHEET 1 AB2 3 THR E 154 TRP E 157 0
SHEET 2 AB2 3 THR E 197 HIS E 202 -1 O ASN E 199 N THR E 156
SHEET 3 AB2 3 THR E 207 LYS E 212 -1 O VAL E 209 N VAL E 200
SHEET 1 AB3 4 LEU F 4 THR F 5 0
SHEET 2 AB3 4 VAL F 19 ALA F 25 -1 O SER F 24 N THR F 5
SHEET 3 AB3 4 SER F 69 ILE F 74 -1 O ILE F 74 N VAL F 19
SHEET 4 AB3 4 PHE F 61 SER F 66 -1 N SER F 64 O SER F 71
SHEET 1 AB4 6 ILE F 10 ALA F 13 0
SHEET 2 AB4 6 ALA F 101 LEU F 105 1 O LYS F 102 N MET F 11
SHEET 3 AB4 6 ALA F 83 GLN F 89 -1 N ALA F 83 O LEU F 103
SHEET 4 AB4 6 HIS F 33 GLN F 37 -1 N HIS F 33 O GLN F 88
SHEET 5 AB4 6 LYS F 44 TYR F 48 -1 O ILE F 47 N TRP F 34
SHEET 6 AB4 6 LYS F 52 LEU F 53 -1 O LYS F 52 N TYR F 48
SHEET 1 AB5 4 ILE F 10 ALA F 13 0
SHEET 2 AB5 4 ALA F 101 LEU F 105 1 O LYS F 102 N MET F 11
SHEET 3 AB5 4 ALA F 83 GLN F 89 -1 N ALA F 83 O LEU F 103
SHEET 4 AB5 4 THR F 96 PHE F 97 -1 O THR F 96 N GLN F 89
SHEET 1 AB6 4 THR F 113 PHE F 117 0
SHEET 2 AB6 4 GLY F 128 PHE F 138 -1 O VAL F 132 N PHE F 117
SHEET 3 AB6 4 TYR F 172 THR F 181 -1 O LEU F 178 N VAL F 131
SHEET 4 AB6 4 VAL F 158 TRP F 162 -1 N LEU F 159 O THR F 177
SHEET 1 AB7 4 SER F 152 ARG F 154 0
SHEET 2 AB7 4 ASN F 144 ILE F 149 -1 N ILE F 149 O SER F 152
SHEET 3 AB7 4 SER F 190 THR F 196 -1 O THR F 196 N ASN F 144
SHEET 4 AB7 4 ILE F 204 ASN F 209 -1 O ILE F 204 N ALA F 195
SHEET 1 AB8 4 GLN G 3 GLN G 6 0
SHEET 2 AB8 4 MET G 18 SER G 25 -1 O LYS G 23 N GLN G 5
SHEET 3 AB8 4 THR G 78 LEU G 83 -1 O LEU G 83 N MET G 18
SHEET 4 AB8 4 ALA G 68 ASP G 73 -1 N THR G 71 O TYR G 80
SHEET 1 AB9 6 GLU G 10 VAL G 12 0
SHEET 2 AB9 6 THR G 110 VAL G 114 1 O THR G 113 N GLU G 10
SHEET 3 AB9 6 ALA G 92 ARG G 98 -1 N ALA G 92 O LEU G 112
SHEET 4 AB9 6 MET G 34 GLN G 39 -1 N GLN G 39 O ILE G 93
SHEET 5 AB9 6 LEU G 45 ILE G 51 -1 O ILE G 48 N TRP G 36
SHEET 6 AB9 6 THR G 58 TYR G 60 -1 O THR G 59 N LEU G 50
SHEET 1 AC1 4 GLU G 10 VAL G 12 0
SHEET 2 AC1 4 THR G 110 VAL G 114 1 O THR G 113 N GLU G 10
SHEET 3 AC1 4 ALA G 92 ARG G 98 -1 N ALA G 92 O LEU G 112
SHEET 4 AC1 4 TYR G 105 TRP G 106 -1 O TYR G 105 N ARG G 98
SHEET 1 AC2 4 SER G 123 LEU G 127 0
SHEET 2 AC2 4 MET G 138 TYR G 148 -1 O LEU G 144 N TYR G 125
SHEET 3 AC2 4 LEU G 177 PRO G 187 -1 O VAL G 186 N VAL G 139
SHEET 4 AC2 4 VAL G 166 THR G 168 -1 N HIS G 167 O SER G 183
SHEET 1 AC3 4 SER G 123 LEU G 127 0
SHEET 2 AC3 4 MET G 138 TYR G 148 -1 O LEU G 144 N TYR G 125
SHEET 3 AC3 4 LEU G 177 PRO G 187 -1 O VAL G 186 N VAL G 139
SHEET 4 AC3 4 VAL G 172 GLN G 174 -1 N GLN G 174 O LEU G 177
SHEET 1 AC4 3 THR G 154 TRP G 157 0
SHEET 2 AC4 3 THR G 197 HIS G 202 -1 O ASN G 199 N THR G 156
SHEET 3 AC4 3 THR G 207 LYS G 212 -1 O VAL G 209 N VAL G 200
SSBOND 1 CYS A 78 CYS B 78 1555 1555 2.07
SSBOND 2 CYS D 23 CYS D 87 1555 1555 2.04
SSBOND 3 CYS D 133 CYS D 193 1555 1555 2.02
SSBOND 4 CYS E 22 CYS E 96 1555 1555 2.04
SSBOND 5 CYS E 143 CYS E 198 1555 1555 2.02
SSBOND 6 CYS F 23 CYS F 87 1555 1555 2.05
SSBOND 7 CYS F 133 CYS F 193 1555 1555 2.02
SSBOND 8 CYS G 22 CYS G 96 1555 1555 2.04
SSBOND 9 CYS G 143 CYS G 198 1555 1555 2.02
LINK O GLY A 98 CA CA A 306 1555 1555 2.39
LINK OD1 ASP A 100 CA CA A 306 1555 1555 3.00
LINK O SER A 112 CA CA A 305 1555 1555 2.42
LINK OD1 ASP A 115 CA CA A 305 1555 1555 2.80
LINK OD2 ASP A 115 CA CA A 305 1555 1555 2.37
LINK OG SER A 118 CA CA A 305 1555 1555 2.71
LINK O THR A 129 TL TL A 301 1555 1555 3.06
LINK OG1 THR A 129 TL TL A 301 1555 1555 2.90
LINK O THR A 129 TL TL A 307 1555 1555 2.99
LINK O ILE A 130 TL TL A 302 1555 1555 3.13
LINK O ILE A 130 TL TL A 307 1555 1555 2.69
LINK O GLY A 131 TL TL A 302 1555 1555 2.71
LINK O GLY A 131 TL TL A 303 1555 1555 3.27
LINK O TYR A 132 TL TL A 303 1555 1555 2.84
LINK O CYS A 218 TL TL A 304 1555 1555 3.06
LINK OD1 ASP A 222 TL TL A 304 1555 1555 3.52
LINK O TRP A 223 TL TL A 304 1555 1555 2.67
LINK O THR A 238 TL TL A 301 1555 1555 2.69
LINK OG1 THR A 238 TL TL A 301 1555 1555 2.38
LINK O THR A 238 TL TL A 307 1555 1555 2.79
LINK O VAL A 239 TL TL A 302 1555 1555 2.95
LINK O VAL A 239 TL TL A 307 1555 1555 2.66
LINK O GLY A 240 TL TL A 302 1555 1555 2.48
LINK O GLY A 240 TL TL A 303 1555 1555 3.07
LINK O PHE A 241 TL TL A 303 1555 1555 2.58
LINK OD1 ASP A 249 CA CA A 305 1555 1555 2.43
LINK OD2 ASP A 249 CA CA A 305 1555 1555 3.18
LINK TL TL A 301 O THR B 129 1555 1555 2.97
LINK TL TL A 301 OG1 THR B 129 1555 1555 2.83
LINK TL TL A 301 O THR B 238 1555 1555 2.90
LINK TL TL A 301 OG1 THR B 238 1555 1555 2.67
LINK TL TL A 302 O ILE B 130 1555 1555 3.21
LINK TL TL A 302 O GLY B 131 1555 1555 2.76
LINK TL TL A 302 O VAL B 239 1555 1555 3.01
LINK TL TL A 302 O GLY B 240 1555 1555 2.48
LINK TL TL A 303 O GLY B 131 1555 1555 3.10
LINK TL TL A 303 O TYR B 132 1555 1555 2.63
LINK TL TL A 303 O GLY B 240 1555 1555 3.17
LINK TL TL A 303 O PHE B 241 1555 1555 2.68
LINK CA CA A 306 O HOH A 419 1555 1555 2.65
LINK CA CA A 306 OE2 GLU B 58 1555 1555 2.88
LINK CA CA A 306 O HOH B 418 1555 1555 2.74
LINK TL TL A 307 O THR B 129 1555 1555 2.97
LINK TL TL A 307 O ILE B 130 1555 1555 2.66
LINK TL TL A 307 O THR B 238 1555 1555 2.90
LINK TL TL A 307 O VAL B 239 1555 1555 2.70
LINK O CYS B 218 TL TL B 303 1555 1555 3.27
LINK O TRP B 223 TL TL B 303 1555 1555 2.67
LINK OE2 GLU E 194 CA CA G 301 1555 2556 1.98
LINK OE1 GLU G 10 CA CA G 301 1555 1555 2.40
LINK OE2 GLU G 10 CA CA G 301 1555 1555 2.83
LINK O LYS G 19 CA CA G 301 1555 1555 2.64
LINK CA CA G 301 O HOH G 407 1555 1555 2.42
CISPEP 1 SER D 7 PRO D 8 0 -0.04
CISPEP 2 SER D 93 PRO D 94 0 2.11
CISPEP 3 TYR D 139 PRO D 140 0 8.01
CISPEP 4 PHE E 149 PRO E 150 0 -0.86
CISPEP 5 GLU E 151 PRO E 152 0 4.61
CISPEP 6 TRP E 191 PRO E 192 0 14.59
CISPEP 7 SER F 7 PRO F 8 0 -2.99
CISPEP 8 SER F 93 PRO F 94 0 1.82
CISPEP 9 TYR F 139 PRO F 140 0 8.52
CISPEP 10 PHE G 149 PRO G 150 0 -3.77
CISPEP 11 GLU G 151 PRO G 152 0 5.11
CISPEP 12 TRP G 191 PRO G 192 0 13.62
SITE 1 AC1 5 THR A 129 THR A 238 TL A 307 THR B 129
SITE 2 AC1 5 THR B 238
SITE 1 AC2 10 ILE A 130 GLY A 131 VAL A 239 GLY A 240
SITE 2 AC2 10 TL A 303 TL A 307 ILE B 130 GLY B 131
SITE 3 AC2 10 VAL B 239 GLY B 240
SITE 1 AC3 9 GLY A 131 TYR A 132 GLY A 240 PHE A 241
SITE 2 AC3 9 TL A 302 GLY B 131 TYR B 132 GLY B 240
SITE 3 AC3 9 PHE B 241
SITE 1 AC4 3 CYS A 218 ASP A 222 TRP A 223
SITE 1 AC5 4 SER A 112 ASP A 115 SER A 118 ASP A 249
SITE 1 AC6 6 GLY A 98 ASP A 100 HIS A 111 HOH A 419
SITE 2 AC6 6 GLU B 58 HOH B 418
SITE 1 AC7 10 THR A 129 ILE A 130 THR A 238 VAL A 239
SITE 2 AC7 10 TL A 301 TL A 302 THR B 129 ILE B 130
SITE 3 AC7 10 THR B 238 VAL B 239
SITE 1 AC8 2 CYS B 218 TRP B 223
SITE 1 AC9 3 GLU G 10 LYS G 19 HOH G 407
CRYST1 80.798 138.760 96.317 90.00 94.52 90.00 P 1 21 1 4
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 0.012377 0.000000 0.000978 0.00000
SCALE2 0.000000 0.007207 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010415 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
