HEADER OXIDOREDUCTASE 02-DEC-15 5F2S
TITLE CRYSTAL STRUCTURE OF HUMAN KDM4A IN COMPLEX WITH COMPOUND 15
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 4A;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 3A,
COMPND 5 JUMONJI DOMAIN-CONTAINING PROTEIN 2A;
COMPND 6 EC: 1.14.11.-;
COMPND 7 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: KDM4A, JHDM3A, JMJD2, JMJD2A, KIAA0677;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28
KEYWDS EPIGENETICS, DEMETHYLASE, INHIBITOR, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-V.LE BIHAN,S.DEMPSTER,I.M.WESTWOOD,R.L.M.VAN MONTFORT
REVDAT 3 10-JAN-24 5F2S 1 LINK
REVDAT 2 09-MAR-16 5F2S 1 JRNL
REVDAT 1 20-JAN-16 5F2S 0
JRNL AUTH V.BAVETSIAS,R.M.LANIGAN,G.F.RUDA,B.ATRASH,M.G.MCLAUGHLIN,
JRNL AUTH 2 A.TUMBER,N.Y.MOK,Y.V.LE BIHAN,S.DEMPSTER,K.J.BOXALL,
JRNL AUTH 3 F.JEGANATHAN,S.B.HATCH,P.SAVITSKY,S.VELUPILLAI,T.KROJER,
JRNL AUTH 4 K.S.ENGLAND,J.SEJBERG,C.THAI,A.DONOVAN,A.PAL,G.SCOZZAFAVA,
JRNL AUTH 5 J.M.BENNETT,A.KAWAMURA,C.JOHANSSON,A.SZYKOWSKA,C.GILEADI,
JRNL AUTH 6 N.A.BURGESS-BROWN,F.VON DELFT,U.OPPERMANN,Z.WALTERS,
JRNL AUTH 7 J.SHIPLEY,F.I.RAYNAUD,S.M.WESTAWAY,R.K.PRINJHA,O.FEDOROV,
JRNL AUTH 8 R.BURKE,C.J.SCHOFIELD,I.M.WESTWOOD,C.BOUNTRA,S.MULLER,
JRNL AUTH 9 R.L.VAN MONTFORT,P.E.BRENNAN,J.BLAGG
JRNL TITL 8-SUBSTITUTED PYRIDO[3,4-D]PYRIMIDIN-4(3H)-ONE DERIVATIVES
JRNL TITL 2 AS POTENT, CELL PERMEABLE, KDM4 (JMJD2) AND KDM5 (JARID1)
JRNL TITL 3 HISTONE LYSINE DEMETHYLASE INHIBITORS.
JRNL REF J.MED.CHEM. V. 59 1388 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 26741168
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01635
REMARK 2
REMARK 2 RESOLUTION. 2.08 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.08
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.61
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 95754
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4799
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.08
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.92
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 7152
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1964
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6773
REMARK 3 BIN R VALUE (WORKING SET) : 0.1942
REMARK 3 BIN FREE R VALUE : 0.2348
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 379
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11030
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 233
REMARK 3 SOLVENT ATOMS : 939
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.41
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.18140
REMARK 3 B22 (A**2) : -0.62540
REMARK 3 B33 (A**2) : 0.44410
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.84180
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.209
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.180
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.143
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.175
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.143
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 11686 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 15827 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3804 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 231 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1773 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 11686 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 4 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1480 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : 11 ; 1.000 ; HARMONIC
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 13970 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.98
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.35
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.38
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 22
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|9 - 102}
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7786 -108.0480 53.0193
REMARK 3 T TENSOR
REMARK 3 T11: -0.1280 T22: -0.0560
REMARK 3 T33: -0.1087 T12: -0.0072
REMARK 3 T13: -0.0656 T23: 0.0359
REMARK 3 L TENSOR
REMARK 3 L11: 2.0387 L22: 1.9440
REMARK 3 L33: 1.6727 L12: -0.2480
REMARK 3 L13: -0.2076 L23: -0.0907
REMARK 3 S TENSOR
REMARK 3 S11: -0.1171 S12: 0.0236 S13: 0.1114
REMARK 3 S21: -0.0331 S22: 0.1447 S23: -0.1222
REMARK 3 S31: 0.1833 S32: 0.2374 S33: -0.0276
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|103 - 124}
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7798 -96.4193 67.3470
REMARK 3 T TENSOR
REMARK 3 T11: -0.0491 T22: -0.0107
REMARK 3 T33: 0.0554 T12: -0.0016
REMARK 3 T13: -0.1245 T23: -0.0244
REMARK 3 L TENSOR
REMARK 3 L11: 1.0468 L22: 1.3624
REMARK 3 L33: 1.5310 L12: 2.3717
REMARK 3 L13: 0.4125 L23: 2.5743
REMARK 3 S TENSOR
REMARK 3 S11: -0.0366 S12: -0.2626 S13: 0.1103
REMARK 3 S21: 0.1768 S22: 0.0678 S23: 0.0018
REMARK 3 S31: -0.0965 S32: 0.2240 S33: -0.0311
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|125 - 144}
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7770 -99.6938 50.1854
REMARK 3 T TENSOR
REMARK 3 T11: -0.0610 T22: -0.0384
REMARK 3 T33: 0.0767 T12: -0.0463
REMARK 3 T13: -0.0541 T23: 0.0888
REMARK 3 L TENSOR
REMARK 3 L11: 2.3691 L22: 1.4808
REMARK 3 L33: 0.6641 L12: -0.5785
REMARK 3 L13: 0.3480 L23: -0.2221
REMARK 3 S TENSOR
REMARK 3 S11: -0.1284 S12: 0.2469 S13: 0.3952
REMARK 3 S21: -0.2133 S22: -0.0377 S23: -0.0097
REMARK 3 S31: -0.0051 S32: 0.2195 S33: 0.1661
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|145 - 226}
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7922 -111.8840 50.8700
REMARK 3 T TENSOR
REMARK 3 T11: -0.0711 T22: -0.0364
REMARK 3 T33: -0.0396 T12: -0.0074
REMARK 3 T13: -0.0285 T23: 0.0593
REMARK 3 L TENSOR
REMARK 3 L11: 1.5878 L22: 1.2870
REMARK 3 L33: 1.2557 L12: -0.7288
REMARK 3 L13: 0.0186 L23: 0.2891
REMARK 3 S TENSOR
REMARK 3 S11: -0.0437 S12: 0.0667 S13: -0.0716
REMARK 3 S21: -0.0863 S22: -0.0143 S23: 0.1652
REMARK 3 S31: 0.1815 S32: 0.0731 S33: 0.0580
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {A|227 - 252}
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4689 -106.8980 61.7126
REMARK 3 T TENSOR
REMARK 3 T11: -0.0535 T22: -0.0118
REMARK 3 T33: 0.0806 T12: 0.0054
REMARK 3 T13: 0.0184 T23: 0.0401
REMARK 3 L TENSOR
REMARK 3 L11: 1.7672 L22: 0.5360
REMARK 3 L33: 1.3596 L12: -0.3803
REMARK 3 L13: -0.6678 L23: -1.1080
REMARK 3 S TENSOR
REMARK 3 S11: -0.0467 S12: 0.0546 S13: 0.0167
REMARK 3 S21: 0.1437 S22: 0.0293 S23: 0.3570
REMARK 3 S31: 0.0698 S32: -0.1548 S33: 0.0174
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {A|253 - 293}
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6136 -111.1440 57.8088
REMARK 3 T TENSOR
REMARK 3 T11: -0.0666 T22: -0.0423
REMARK 3 T33: -0.0613 T12: 0.0167
REMARK 3 T13: -0.0240 T23: 0.0489
REMARK 3 L TENSOR
REMARK 3 L11: 1.8872 L22: 1.4167
REMARK 3 L33: 2.0799 L12: -1.0407
REMARK 3 L13: -0.0375 L23: 0.7781
REMARK 3 S TENSOR
REMARK 3 S11: -0.1338 S12: -0.0961 S13: 0.0604
REMARK 3 S21: 0.0873 S22: 0.0801 S23: 0.1250
REMARK 3 S31: 0.1867 S32: 0.1849 S33: 0.0537
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {A|294 - 354}
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0611 -128.2670 48.1756
REMARK 3 T TENSOR
REMARK 3 T11: 0.0246 T22: -0.1737
REMARK 3 T33: 0.0871 T12: -0.1466
REMARK 3 T13: -0.0276 T23: -0.0361
REMARK 3 L TENSOR
REMARK 3 L11: 2.9886 L22: 1.3347
REMARK 3 L33: 2.7852 L12: 1.7871
REMARK 3 L13: 0.1358 L23: 1.1748
REMARK 3 S TENSOR
REMARK 3 S11: -0.0912 S12: 0.2611 S13: -0.4626
REMARK 3 S21: -0.0668 S22: -0.0825 S23: 0.4940
REMARK 3 S31: 0.4848 S32: -0.2615 S33: 0.1737
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: {B|1 - 26}
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6103 -163.2770 7.8585
REMARK 3 T TENSOR
REMARK 3 T11: 0.0225 T22: -0.0781
REMARK 3 T33: -0.0241 T12: -0.0675
REMARK 3 T13: -0.0360 T23: 0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 1.8582 L22: 3.3104
REMARK 3 L33: 1.2130 L12: 0.1334
REMARK 3 L13: 1.0158 L23: 1.2411
REMARK 3 S TENSOR
REMARK 3 S11: 0.1362 S12: -0.0565 S13: -0.4332
REMARK 3 S21: 0.1281 S22: -0.0411 S23: 0.1974
REMARK 3 S31: 0.4957 S32: -0.2791 S33: -0.0951
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: {B|27 - 70}
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1765 -152.1550 18.7152
REMARK 3 T TENSOR
REMARK 3 T11: -0.0390 T22: -0.0116
REMARK 3 T33: -0.0849 T12: -0.0228
REMARK 3 T13: 0.0267 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 1.3563 L22: 2.8858
REMARK 3 L33: 2.0052 L12: 0.0540
REMARK 3 L13: -0.0807 L23: 1.1924
REMARK 3 S TENSOR
REMARK 3 S11: 0.0409 S12: -0.1672 S13: -0.0267
REMARK 3 S21: 0.4313 S22: -0.1072 S23: 0.3471
REMARK 3 S31: 0.3552 S32: -0.4720 S33: 0.0663
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: {B|71 - 124}
REMARK 3 ORIGIN FOR THE GROUP (A): 30.7272 -132.2050 11.1285
REMARK 3 T TENSOR
REMARK 3 T11: -0.0224 T22: -0.1369
REMARK 3 T33: -0.0071 T12: 0.0540
REMARK 3 T13: 0.0007 T23: -0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 2.5502 L22: 2.1674
REMARK 3 L33: 2.8876 L12: -0.0884
REMARK 3 L13: -0.5281 L23: 0.6580
REMARK 3 S TENSOR
REMARK 3 S11: 0.0404 S12: 0.0031 S13: 0.3005
REMARK 3 S21: -0.2225 S22: -0.0327 S23: 0.0217
REMARK 3 S31: -0.4973 S32: -0.1535 S33: -0.0077
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: {B|125 - 226}
REMARK 3 ORIGIN FOR THE GROUP (A): 31.5240 -148.4670 18.5571
REMARK 3 T TENSOR
REMARK 3 T11: -0.0080 T22: -0.0528
REMARK 3 T33: -0.0673 T12: 0.0103
REMARK 3 T13: -0.0182 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 1.0528 L22: 1.5907
REMARK 3 L33: 1.0461 L12: -0.1999
REMARK 3 L13: 0.2497 L23: 0.3936
REMARK 3 S TENSOR
REMARK 3 S11: 0.0307 S12: -0.1425 S13: 0.0572
REMARK 3 S21: 0.2580 S22: 0.0539 S23: -0.1268
REMARK 3 S31: 0.1144 S32: -0.1071 S33: -0.0846
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: {B|227 - 252}
REMARK 3 ORIGIN FOR THE GROUP (A): 45.4799 -144.8160 7.2971
REMARK 3 T TENSOR
REMARK 3 T11: -0.0356 T22: -0.0729
REMARK 3 T33: 0.0887 T12: -0.0185
REMARK 3 T13: 0.0053 T23: -0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 1.9363 L22: 1.1706
REMARK 3 L33: 3.7021 L12: 0.0860
REMARK 3 L13: -0.2885 L23: 1.8397
REMARK 3 S TENSOR
REMARK 3 S11: 0.0212 S12: -0.0860 S13: 0.0285
REMARK 3 S21: -0.0807 S22: 0.1015 S23: -0.4049
REMARK 3 S31: -0.1327 S32: 0.2016 S33: -0.1227
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: {B|253 - 317}
REMARK 3 ORIGIN FOR THE GROUP (A): 34.2763 -152.7430 14.6016
REMARK 3 T TENSOR
REMARK 3 T11: -0.0353 T22: -0.0894
REMARK 3 T33: -0.0589 T12: 0.0049
REMARK 3 T13: -0.0370 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 1.0439 L22: 1.8355
REMARK 3 L33: 1.9826 L12: 0.0718
REMARK 3 L13: 0.0566 L23: 0.0718
REMARK 3 S TENSOR
REMARK 3 S11: 0.0373 S12: -0.0948 S13: -0.0358
REMARK 3 S21: 0.1968 S22: 0.0267 S23: -0.2842
REMARK 3 S31: 0.2552 S32: 0.0887 S33: -0.0640
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: {B|318 - 354}
REMARK 3 ORIGIN FOR THE GROUP (A): 39.7951 -171.0720 19.3463
REMARK 3 T TENSOR
REMARK 3 T11: 0.1953 T22: -0.2061
REMARK 3 T33: -0.0066 T12: 0.1007
REMARK 3 T13: -0.1204 T23: 0.0658
REMARK 3 L TENSOR
REMARK 3 L11: 2.5391 L22: 1.0828
REMARK 3 L33: 3.7967 L12: -1.2182
REMARK 3 L13: -0.5532 L23: -1.4832
REMARK 3 S TENSOR
REMARK 3 S11: -0.0964 S12: -0.1718 S13: -0.4481
REMARK 3 S21: 0.3260 S22: -0.0172 S23: -0.1858
REMARK 3 S31: 0.4859 S32: 0.4076 S33: 0.1137
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: {C|7 - 53}
REMARK 3 ORIGIN FOR THE GROUP (A): 41.2901 -159.5580 58.3199
REMARK 3 T TENSOR
REMARK 3 T11: 0.0182 T22: -0.0977
REMARK 3 T33: -0.0355 T12: -0.0017
REMARK 3 T13: 0.0430 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 3.5410 L22: 3.6522
REMARK 3 L33: 3.5595 L12: 0.1183
REMARK 3 L13: 0.7950 L23: 0.9180
REMARK 3 S TENSOR
REMARK 3 S11: 0.0387 S12: 0.0130 S13: 0.4269
REMARK 3 S21: -0.0318 S22: -0.0426 S23: 0.3702
REMARK 3 S31: -0.5288 S32: -0.1660 S33: 0.0039
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: {C|54 - 102}
REMARK 3 ORIGIN FOR THE GROUP (A): 46.1625 -187.8620 51.8900
REMARK 3 T TENSOR
REMARK 3 T11: -0.0297 T22: -0.0533
REMARK 3 T33: -0.0409 T12: -0.0085
REMARK 3 T13: -0.0385 T23: -0.0469
REMARK 3 L TENSOR
REMARK 3 L11: 2.6573 L22: 1.5130
REMARK 3 L33: 2.2268 L12: -0.3157
REMARK 3 L13: 1.3714 L23: 0.0410
REMARK 3 S TENSOR
REMARK 3 S11: 0.0324 S12: 0.2416 S13: -0.1591
REMARK 3 S21: 0.1313 S22: 0.0268 S23: 0.0382
REMARK 3 S31: 0.1905 S32: 0.1982 S33: -0.0592
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: {C|103 - 124}
REMARK 3 ORIGIN FOR THE GROUP (A): 46.0013 -186.2680 69.1589
REMARK 3 T TENSOR
REMARK 3 T11: 0.0611 T22: -0.0282
REMARK 3 T33: -0.1133 T12: -0.0310
REMARK 3 T13: -0.0116 T23: 0.0372
REMARK 3 L TENSOR
REMARK 3 L11: 3.6597 L22: 1.3096
REMARK 3 L33: 2.8280 L12: -0.1637
REMARK 3 L13: -0.4336 L23: 0.0704
REMARK 3 S TENSOR
REMARK 3 S11: 0.0221 S12: -0.4255 S13: -0.1023
REMARK 3 S21: 0.2637 S22: 0.0634 S23: 0.1235
REMARK 3 S31: 0.0398 S32: -0.0266 S33: -0.0856
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: {C|125 - 293}
REMARK 3 ORIGIN FOR THE GROUP (A): 51.3786 -173.2340 54.5382
REMARK 3 T TENSOR
REMARK 3 T11: -0.0296 T22: -0.0183
REMARK 3 T33: -0.1106 T12: -0.0412
REMARK 3 T13: 0.0155 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 1.5155 L22: 1.3671
REMARK 3 L33: 1.1995 L12: 0.0877
REMARK 3 L13: 0.3975 L23: 0.5388
REMARK 3 S TENSOR
REMARK 3 S11: 0.0273 S12: 0.1598 S13: 0.0392
REMARK 3 S21: -0.0983 S22: 0.0910 S23: -0.0804
REMARK 3 S31: -0.0909 S32: 0.1662 S33: -0.1183
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: {C|294 - 355}
REMARK 3 ORIGIN FOR THE GROUP (A): 60.0403 -157.1460 46.0605
REMARK 3 T TENSOR
REMARK 3 T11: 0.0168 T22: -0.0355
REMARK 3 T33: -0.1489 T12: -0.1640
REMARK 3 T13: 0.1173 T23: 0.0564
REMARK 3 L TENSOR
REMARK 3 L11: 4.1137 L22: 2.0509
REMARK 3 L33: 4.1001 L12: 1.5539
REMARK 3 L13: -1.2262 L23: 0.0652
REMARK 3 S TENSOR
REMARK 3 S11: -0.0299 S12: 0.4504 S13: 0.4689
REMARK 3 S21: -0.4235 S22: 0.1884 S23: -0.3647
REMARK 3 S31: -0.4413 S32: 0.5220 S33: -0.1584
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: {D|6 - 53}
REMARK 3 ORIGIN FOR THE GROUP (A): 61.6476 -94.5944 13.5292
REMARK 3 T TENSOR
REMARK 3 T11: -0.0264 T22: -0.0840
REMARK 3 T33: 0.0279 T12: -0.0798
REMARK 3 T13: -0.0202 T23: 0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 2.2271 L22: 2.2529
REMARK 3 L33: 2.4780 L12: -0.6190
REMARK 3 L13: -0.7557 L23: -1.1649
REMARK 3 S TENSOR
REMARK 3 S11: 0.0766 S12: 0.0273 S13: 0.3977
REMARK 3 S21: 0.0966 S22: -0.1156 S23: -0.3718
REMARK 3 S31: -0.4928 S32: 0.4640 S33: 0.0390
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: {D|54 - 293}
REMARK 3 ORIGIN FOR THE GROUP (A): 53.6615 -113.2870 15.0471
REMARK 3 T TENSOR
REMARK 3 T11: -0.0470 T22: -0.0536
REMARK 3 T33: -0.0463 T12: 0.0209
REMARK 3 T13: -0.0121 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 1.5210 L22: 0.8765
REMARK 3 L33: 0.7953 L12: -0.1034
REMARK 3 L13: 0.3182 L23: -0.1726
REMARK 3 S TENSOR
REMARK 3 S11: 0.0516 S12: -0.0198 S13: -0.0912
REMARK 3 S21: -0.0239 S22: -0.0292 S23: -0.0881
REMARK 3 S31: 0.0594 S32: 0.1106 S33: -0.0224
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: {D|294 - 354}
REMARK 3 ORIGIN FOR THE GROUP (A): 42.9923 -93.7281 27.2539
REMARK 3 T TENSOR
REMARK 3 T11: -0.0014 T22: -0.0486
REMARK 3 T33: -0.0306 T12: 0.0224
REMARK 3 T13: -0.0295 T23: -0.0507
REMARK 3 L TENSOR
REMARK 3 L11: 1.4234 L22: 0.5295
REMARK 3 L33: 2.9458 L12: -0.7445
REMARK 3 L13: -0.4964 L23: 1.0199
REMARK 3 S TENSOR
REMARK 3 S11: 0.1182 S12: -0.3289 S13: 0.2150
REMARK 3 S21: 0.0416 S22: -0.0698 S23: -0.1122
REMARK 3 S31: -0.2808 S32: -0.2403 S33: -0.0483
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5F2S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000215456.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-FEB-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9200
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95776
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
REMARK 200 RESOLUTION RANGE LOW (A) : 57.820
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.48700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2OQ7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.61
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLISATION SOLUTION IS 0.1M BIS
REMARK 280 -TRIS-PROPANE PH7.5, 12-16% PEG-4000. INHIBITOR IS SOAKED IN
REMARK 280 CRYSTALS BY ADDITION DIRECTLY TO THE DROPS OF DMSO DISSOLVED
REMARK 280 COMPOUND, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 51.16000
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 SER A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLU A 4
REMARK 465 SER A 5
REMARK 465 GLU A 6
REMARK 465 THR A 7
REMARK 465 LEU A 8
REMARK 465 ARG A 309
REMARK 465 LYS A 310
REMARK 465 ASP A 311
REMARK 465 MET A 312
REMARK 465 LYS A 355
REMARK 465 GLU A 356
REMARK 465 SER A 357
REMARK 465 GLU A 358
REMARK 465 LEU A 359
REMARK 465 SER B 0
REMARK 465 LYS B 310
REMARK 465 ASP B 311
REMARK 465 LYS B 355
REMARK 465 GLU B 356
REMARK 465 SER B 357
REMARK 465 GLU B 358
REMARK 465 LEU B 359
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 SER C 3
REMARK 465 GLU C 4
REMARK 465 SER C 5
REMARK 465 GLU C 6
REMARK 465 LEU C 354
REMARK 465 LYS C 355
REMARK 465 GLU C 356
REMARK 465 SER C 357
REMARK 465 GLU C 358
REMARK 465 LEU C 359
REMARK 465 SER D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 SER D 3
REMARK 465 GLU D 4
REMARK 465 SER D 5
REMARK 465 LYS D 355
REMARK 465 GLU D 356
REMARK 465 SER D 357
REMARK 465 GLU D 358
REMARK 465 LEU D 359
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU A 22 CG CD OE1 OE2
REMARK 470 LYS A 51 CG CD CE NZ
REMARK 470 LYS A 54 CG CD CE NZ
REMARK 470 LYS A 89 CE NZ
REMARK 470 LYS A 90 CG CD CE NZ
REMARK 470 LYS A 99 CG CD CE NZ
REMARK 470 ASP A 104 CG OD1 OD2
REMARK 470 LYS A 105 CD CE NZ
REMARK 470 ARG A 110 CG CD NE CZ NH1 NH2
REMARK 470 SER A 112 OG
REMARK 470 GLU A 113 CD OE1 OE2
REMARK 470 GLU A 115 CG CD OE1 OE2
REMARK 470 LYS A 120 CE NZ
REMARK 470 LYS A 123 CG CD CE NZ
REMARK 470 LYS A 143 CG CD CE NZ
REMARK 470 ARG A 154 NE CZ NH1 NH2
REMARK 470 ARG A 218 CZ NH1 NH2
REMARK 470 ARG A 221 NE CZ NH1 NH2
REMARK 470 LYS A 224 CE NZ
REMARK 470 GLN A 232 CG CD OE1 NE2
REMARK 470 GLU A 235 CG CD OE1 OE2
REMARK 470 LYS A 251 CD CE NZ
REMARK 470 LYS A 252 NZ
REMARK 470 LYS A 314 CD CE NZ
REMARK 470 SER A 316 OG
REMARK 470 ASP A 318 CG OD1 OD2
REMARK 470 VAL A 319 CG1 CG2
REMARK 470 ARG A 322 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 323 CG CD CE NZ
REMARK 470 ARG A 328 CZ NH1 NH2
REMARK 470 TYR A 329 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 330 CG CD CE NZ
REMARK 470 LYS A 333 CG CD CE NZ
REMARK 470 LYS A 336 CG CD CE NZ
REMARK 470 ASN A 338 CG OD1 ND2
REMARK 470 VAL A 340 CG1 CG2
REMARK 470 GLU B 4 CD OE1 OE2
REMARK 470 GLU B 22 CG CD OE1 OE2
REMARK 470 LYS B 51 CG CD CE NZ
REMARK 470 LYS B 54 CE NZ
REMARK 470 ASP B 61 CG OD1 OD2
REMARK 470 LYS B 90 CD CE NZ
REMARK 470 ARG B 110 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 113 CG CD OE1 OE2
REMARK 470 GLU B 115 CG CD OE1 OE2
REMARK 470 LYS B 123 CE NZ
REMARK 470 LYS B 143 CG CD CE NZ
REMARK 470 ARG B 154 NE CZ NH1 NH2
REMARK 470 ARG B 218 NH1 NH2
REMARK 470 LYS B 224 CD CE NZ
REMARK 470 GLN B 232 CG CD OE1 NE2
REMARK 470 GLU B 235 CD OE1 OE2
REMARK 470 LYS B 241 CD CE NZ
REMARK 470 LYS B 251 CD CE NZ
REMARK 470 LYS B 314 CE NZ
REMARK 470 LYS B 330 CG CD CE NZ
REMARK 470 LEU B 331 CD1 CD2
REMARK 470 LYS B 333 CE NZ
REMARK 470 LYS B 336 CG CD CE NZ
REMARK 470 ASN B 338 CG OD1 ND2
REMARK 470 THR C 7 OG1 CG2
REMARK 470 GLU C 22 CD OE1 OE2
REMARK 470 ARG C 29 CZ NH1 NH2
REMARK 470 LYS C 51 CG CD CE NZ
REMARK 470 LYS C 54 CD CE NZ
REMARK 470 SER C 79 OG
REMARK 470 LYS C 89 CE NZ
REMARK 470 LYS C 90 NZ
REMARK 470 LYS C 105 NZ
REMARK 470 ARG C 110 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 113 CG CD OE1 OE2
REMARK 470 GLU C 115 CG CD OE1 OE2
REMARK 470 LYS C 123 CE NZ
REMARK 470 LYS C 143 CG CD CE NZ
REMARK 470 GLU C 163 CG CD OE1 OE2
REMARK 470 ARG C 221 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 232 CG CD OE1 NE2
REMARK 470 SER C 233 OG
REMARK 470 GLU C 235 CG CD OE1 OE2
REMARK 470 LYS C 252 CE NZ
REMARK 470 ARG C 294 NH1 NH2
REMARK 470 ARG C 309 NE CZ NH1 NH2
REMARK 470 LYS C 310 CG CD CE NZ
REMARK 470 MET C 312 CE
REMARK 470 LYS C 314 CG CD CE NZ
REMARK 470 ARG C 322 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 327 CG CD OE1 OE2
REMARK 470 ARG C 328 CG CD NE CZ NH1 NH2
REMARK 470 TYR C 329 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS C 330 NZ
REMARK 470 LEU C 331 CD1 CD2
REMARK 470 LYS C 333 CE NZ
REMARK 470 LYS C 336 CG CD CE NZ
REMARK 470 ASN C 338 CG OD1 ND2
REMARK 470 GLU D 6 CG CD OE1 OE2
REMARK 470 THR D 7 OG1 CG2
REMARK 470 LYS D 51 CG CD CE NZ
REMARK 470 LYS D 54 CD CE NZ
REMARK 470 LYS D 90 CG CD CE NZ
REMARK 470 LYS D 99 NZ
REMARK 470 ARG D 110 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 113 CG CD OE1 OE2
REMARK 470 GLU D 115 CG CD OE1 OE2
REMARK 470 LYS D 123 CG CD CE NZ
REMARK 470 LYS D 143 NZ
REMARK 470 LEU D 159 CD1 CD2
REMARK 470 GLU D 161 CG CD OE1 OE2
REMARK 470 LYS D 162 NZ
REMARK 470 GLU D 163 CG CD OE1 OE2
REMARK 470 ILE D 166 CG1 CD1
REMARK 470 THR D 167 OG1 CG2
REMARK 470 GLN D 232 CG CD OE1 NE2
REMARK 470 LYS D 241 CD CE NZ
REMARK 470 LYS D 310 CG CD CE NZ
REMARK 470 ASP D 311 CG OD1 OD2
REMARK 470 LYS D 314 CE NZ
REMARK 470 LYS D 323 NZ
REMARK 470 LYS D 336 CE NZ
REMARK 470 LEU D 354 CG CD1 CD2
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 ARG A 152 75.70 -152.17
REMARK 500 MET A 192 17.08 59.97
REMARK 500 ASN A 338 38.14 -97.08
REMARK 500 ARG B 152 70.03 -155.67
REMARK 500 SER C 112 -67.37 -93.23
REMARK 500 ARG C 152 74.77 -161.10
REMARK 500 MET C 192 19.76 58.05
REMARK 500 ARG D 152 68.04 -159.51
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 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 188 NE2
REMARK 620 2 GLU A 190 OE2 102.2
REMARK 620 3 HIS A 276 NE2 84.4 92.1
REMARK 620 4 5TZ A 403 N1 80.9 96.1 164.4
REMARK 620 5 5TZ A 403 N2 95.5 160.1 98.6 77.7
REMARK 620 6 HOH A 526 O 177.0 80.7 96.5 97.9 81.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 234 SG
REMARK 620 2 HIS A 240 NE2 112.3
REMARK 620 3 CYS A 306 SG 117.7 109.6
REMARK 620 4 CYS A 308 SG 108.7 91.6 114.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 188 NE2
REMARK 620 2 GLU B 190 OE2 96.7
REMARK 620 3 HIS B 276 NE2 84.6 88.4
REMARK 620 4 5TZ B 403 N2 96.1 165.0 100.5
REMARK 620 5 5TZ B 403 N1 82.3 95.8 166.6 78.2
REMARK 620 6 HOH B 574 O 177.8 85.4 94.8 81.9 98.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 234 SG
REMARK 620 2 HIS B 240 NE2 110.7
REMARK 620 3 CYS B 306 SG 119.9 113.2
REMARK 620 4 CYS B 308 SG 110.3 88.9 109.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 188 NE2
REMARK 620 2 GLU C 190 OE2 100.5
REMARK 620 3 HIS C 276 NE2 83.4 86.4
REMARK 620 4 5TZ C 403 N1 79.5 97.5 162.9
REMARK 620 5 5TZ C 403 N2 92.8 165.2 101.7 78.5
REMARK 620 6 HOH C 583 O 172.4 85.1 91.9 105.0 82.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 234 SG
REMARK 620 2 HIS C 240 NE2 111.6
REMARK 620 3 CYS C 306 SG 114.8 110.8
REMARK 620 4 CYS C 308 SG 115.8 91.0 110.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 188 NE2
REMARK 620 2 GLU D 190 OE2 93.4
REMARK 620 3 HIS D 276 NE2 86.3 90.7
REMARK 620 4 5TZ D 403 N2 98.8 165.1 98.6
REMARK 620 5 5TZ D 403 N1 79.6 97.5 164.0 76.4
REMARK 620 6 HOH D 629 O 174.6 88.1 98.9 79.0 95.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 234 SG
REMARK 620 2 HIS D 240 NE2 115.1
REMARK 620 3 CYS D 306 SG 117.1 109.9
REMARK 620 4 CYS D 308 SG 112.1 90.3 109.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5TZ A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5TZ B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5TZ C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS C 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5TZ D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS D 415
DBREF 5F2S A 1 359 UNP O75164 KDM4A_HUMAN 1 359
DBREF 5F2S B 1 359 UNP O75164 KDM4A_HUMAN 1 359
DBREF 5F2S C 1 359 UNP O75164 KDM4A_HUMAN 1 359
DBREF 5F2S D 1 359 UNP O75164 KDM4A_HUMAN 1 359
SEQADV 5F2S SER A 0 UNP O75164 EXPRESSION TAG
SEQADV 5F2S SER B 0 UNP O75164 EXPRESSION TAG
SEQADV 5F2S SER C 0 UNP O75164 EXPRESSION TAG
SEQADV 5F2S SER D 0 UNP O75164 EXPRESSION TAG
SEQRES 1 A 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 A 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 A 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 A 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 A 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 A 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 A 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 A 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 A 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 A 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 A 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 A 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 A 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 A 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 A 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 A 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 A 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 A 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 A 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 A 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 A 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 A 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 A 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 A 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 A 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 A 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 A 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 A 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
SEQRES 1 B 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 B 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 B 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 B 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 B 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 B 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 B 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 B 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 B 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 B 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 B 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 B 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 B 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 B 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 B 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 B 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 B 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 B 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 B 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 B 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 B 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 B 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 B 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 B 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 B 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 B 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 B 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 B 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
SEQRES 1 C 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 C 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 C 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 C 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 C 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 C 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 C 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 C 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 C 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 C 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 C 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 C 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 C 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 C 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 C 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 C 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 C 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 C 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 C 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 C 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 C 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 C 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 C 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 C 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 C 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 C 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 C 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 C 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
SEQRES 1 D 360 SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER ALA
SEQRES 2 D 360 ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE ARG
SEQRES 3 D 360 ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN GLY
SEQRES 4 D 360 ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO LYS
SEQRES 5 D 360 GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP ASP
SEQRES 6 D 360 LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR GLY
SEQRES 7 D 360 GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS LYS
SEQRES 8 D 360 ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN SER
SEQRES 9 D 360 ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU GLU
SEQRES 10 D 360 LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN PRO
SEQRES 11 D 360 PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR GLU
SEQRES 12 D 360 LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG THR
SEQRES 13 D 360 ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR ILE
SEQRES 14 D 360 GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP
SEQRES 15 D 360 LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP LEU
SEQRES 16 D 360 TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS SER
SEQRES 17 D 360 TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU GLU
SEQRES 18 D 360 ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN SER
SEQRES 19 D 360 CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE SER
SEQRES 20 D 360 PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP LYS
SEQRES 21 D 360 VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE PRO
SEQRES 22 D 360 TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS
SEQRES 23 D 360 ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE GLU
SEQRES 24 D 360 TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS ASP
SEQRES 25 D 360 MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS PHE
SEQRES 26 D 360 GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS ASP
SEQRES 27 D 360 ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU ALA
SEQRES 28 D 360 ALA GLU PHE LEU LYS GLU SER GLU LEU
HET ZN A 401 1
HET ZN A 402 1
HET 5TZ A 403 15
HET EDO A 404 4
HET EDO A 405 4
HET EDO A 406 4
HET EDO A 407 4
HET EDO A 408 4
HET EDO A 409 4
HET EDO A 410 4
HET DMS A 411 4
HET DMS A 412 4
HET ZN B 401 1
HET ZN B 402 1
HET 5TZ B 403 15
HET EDO B 404 4
HET EDO B 405 4
HET EDO B 406 4
HET EDO B 407 4
HET EDO B 408 4
HET EDO B 409 4
HET EDO B 410 4
HET EDO B 411 4
HET EDO B 412 4
HET EDO B 413 4
HET EDO B 414 4
HET ZN C 401 1
HET ZN C 402 1
HET 5TZ C 403 15
HET EDO C 404 4
HET EDO C 405 4
HET EDO C 406 4
HET EDO C 407 4
HET EDO C 408 4
HET EDO C 409 4
HET EDO C 410 4
HET EDO C 411 4
HET EDO C 412 4
HET DMS C 413 4
HET ZN D 401 1
HET ZN D 402 1
HET 5TZ D 403 15
HET CL D 404 1
HET EDO D 405 4
HET EDO D 406 4
HET EDO D 407 4
HET EDO D 408 4
HET EDO D 409 4
HET EDO D 410 4
HET EDO D 411 4
HET EDO D 412 4
HET EDO D 413 4
HET EDO D 414 4
HET DMS D 415 4
HETNAM ZN ZINC ION
HETNAM 5TZ 2-(2-AZANYL-1,3-THIAZOL-4-YL)PYRIDINE-4-CARBOXYLIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM CL CHLORIDE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 ZN 8(ZN 2+)
FORMUL 7 5TZ 4(C9 H7 N3 O2 S)
FORMUL 8 EDO 37(C2 H6 O2)
FORMUL 15 DMS 4(C2 H6 O S)
FORMUL 47 CL CL 1-
FORMUL 59 HOH *939(H2 O)
HELIX 1 AA1 THR A 20 ARG A 25 1 6
HELIX 2 AA2 ASN A 26 GLN A 37 1 12
HELIX 3 AA3 GLY A 38 ALA A 42 5 5
HELIX 4 AA4 VAL A 94 ASN A 102 1 9
HELIX 5 AA5 GLU A 113 LEU A 125 1 13
HELIX 6 AA6 THR A 155 LEU A 157 5 3
HELIX 7 AA7 ASP A 158 GLY A 165 1 8
HELIX 8 AA8 GLU A 190 LEU A 194 5 5
HELIX 9 AA9 PRO A 212 GLU A 214 5 3
HELIX 10 AB1 HIS A 215 PHE A 227 1 13
HELIX 11 AB2 PHE A 227 CYS A 234 1 8
HELIX 12 AB3 ALA A 236 LYS A 241 5 6
HELIX 13 AB4 SER A 246 TYR A 253 1 8
HELIX 14 AB5 ARG A 295 ALA A 303 1 9
HELIX 15 AB6 MET A 317 GLN A 325 1 9
HELIX 16 AB7 ARG A 328 ALA A 334 1 7
HELIX 17 AB8 THR A 347 LEU A 354 5 8
HELIX 18 AB9 SER B 3 LEU B 8 1 6
HELIX 19 AC1 ASN B 26 GLN B 37 1 12
HELIX 20 AC2 GLY B 38 ALA B 42 5 5
HELIX 21 AC3 VAL B 94 SER B 103 1 10
HELIX 22 AC4 GLU B 113 LEU B 125 1 13
HELIX 23 AC5 THR B 155 LEU B 157 5 3
HELIX 24 AC6 ASP B 158 GLY B 165 1 8
HELIX 25 AC7 GLU B 190 LEU B 194 5 5
HELIX 26 AC8 PRO B 212 GLU B 214 5 3
HELIX 27 AC9 HIS B 215 PHE B 227 1 13
HELIX 28 AD1 PHE B 227 CYS B 234 1 8
HELIX 29 AD2 ALA B 236 LYS B 241 5 6
HELIX 30 AD3 SER B 246 TYR B 253 1 8
HELIX 31 AD4 ARG B 295 ALA B 303 1 9
HELIX 32 AD5 MET B 317 GLN B 325 1 9
HELIX 33 AD6 ARG B 328 ALA B 334 1 7
HELIX 34 AD7 THR B 347 LEU B 354 5 8
HELIX 35 AD8 THR C 20 ARG C 25 1 6
HELIX 36 AD9 ASN C 26 GLN C 37 1 12
HELIX 37 AE1 GLY C 38 ALA C 42 5 5
HELIX 38 AE2 VAL C 94 SER C 103 1 10
HELIX 39 AE3 GLU C 113 LEU C 125 1 13
HELIX 40 AE4 THR C 155 LEU C 157 5 3
HELIX 41 AE5 ASP C 158 GLU C 163 1 6
HELIX 42 AE6 GLU C 190 LEU C 194 5 5
HELIX 43 AE7 PRO C 212 GLU C 214 5 3
HELIX 44 AE8 HIS C 215 PHE C 227 1 13
HELIX 45 AE9 PHE C 227 CYS C 234 1 8
HELIX 46 AF1 ALA C 236 LYS C 241 5 6
HELIX 47 AF2 SER C 246 TYR C 253 1 8
HELIX 48 AF3 ARG C 295 ALA C 303 1 9
HELIX 49 AF4 MET C 317 GLN C 325 1 9
HELIX 50 AF5 ARG C 328 ALA C 334 1 7
HELIX 51 AF6 THR C 347 PHE C 353 5 7
HELIX 52 AF7 THR D 20 ARG D 25 1 6
HELIX 53 AF8 ASN D 26 GLN D 37 1 12
HELIX 54 AF9 GLY D 38 ALA D 42 5 5
HELIX 55 AG1 VAL D 94 SER D 103 1 10
HELIX 56 AG2 GLU D 113 LEU D 125 1 13
HELIX 57 AG3 THR D 155 LEU D 157 5 3
HELIX 58 AG4 ASP D 158 GLU D 163 1 6
HELIX 59 AG5 GLU D 190 LEU D 194 5 5
HELIX 60 AG6 PRO D 212 GLU D 214 5 3
HELIX 61 AG7 HIS D 215 PHE D 227 1 13
HELIX 62 AG8 PHE D 227 CYS D 234 1 8
HELIX 63 AG9 ALA D 236 LYS D 241 5 6
HELIX 64 AH1 SER D 246 TYR D 253 1 8
HELIX 65 AH2 ARG D 295 ALA D 303 1 9
HELIX 66 AH3 MET D 317 GLN D 325 1 9
HELIX 67 AH4 ARG D 328 ALA D 334 1 7
HELIX 68 AH5 THR D 347 LEU D 354 5 8
SHEET 1 AA110 MET A 15 PHE A 17 0
SHEET 2 AA110 LEU A 44 VAL A 47 1 O LYS A 46 N MET A 15
SHEET 3 AA110 PHE A 267 THR A 270 -1 O ILE A 269 N ALA A 45
SHEET 4 AA110 TYR A 195 GLY A 203 -1 N ASN A 198 O MET A 268
SHEET 5 AA110 ASN A 284 PHE A 291 -1 O GLU A 287 N TYR A 199
SHEET 6 AA110 TYR A 175 GLY A 179 -1 N TYR A 177 O ALA A 286
SHEET 7 AA110 ILE A 131 ASN A 137 -1 N GLY A 133 O PHE A 178
SHEET 8 AA110 ILE A 71 GLN A 78 -1 N ILE A 71 O TYR A 132
SHEET 9 AA110 LEU A 81 GLN A 88 -1 O TYR A 85 N LEU A 74
SHEET 10 AA110 THR A 243 ILE A 245 -1 O LEU A 244 N PHE A 82
SHEET 1 AA2 2 VAL A 66 ILE A 67 0
SHEET 2 AA2 2 MET A 92 THR A 93 -1 O MET A 92 N ILE A 67
SHEET 1 AA3 4 SER A 184 HIS A 188 0
SHEET 2 AA3 4 TYR A 275 ASN A 280 -1 O HIS A 276 N HIS A 188
SHEET 3 AA3 4 LYS A 206 VAL A 211 -1 N TYR A 209 O ALA A 277
SHEET 4 AA3 4 ASP A 258 GLN A 262 -1 O GLN A 262 N LYS A 206
SHEET 1 AA410 MET B 15 PHE B 17 0
SHEET 2 AA410 LEU B 44 VAL B 47 1 O LYS B 46 N MET B 15
SHEET 3 AA410 PHE B 267 THR B 270 -1 O ILE B 269 N ALA B 45
SHEET 4 AA410 TYR B 195 GLY B 203 -1 N ASN B 198 O MET B 268
SHEET 5 AA410 ASN B 284 PHE B 291 -1 O GLU B 287 N TYR B 199
SHEET 6 AA410 TYR B 175 GLY B 179 -1 N TYR B 175 O SER B 288
SHEET 7 AA410 ILE B 131 ASN B 137 -1 N GLY B 133 O PHE B 178
SHEET 8 AA410 ILE B 71 GLN B 78 -1 N ILE B 71 O TYR B 132
SHEET 9 AA410 LEU B 81 GLN B 88 -1 O TYR B 85 N LEU B 74
SHEET 10 AA410 THR B 243 ILE B 245 -1 O LEU B 244 N PHE B 82
SHEET 1 AA5 2 VAL B 66 ILE B 67 0
SHEET 2 AA5 2 MET B 92 THR B 93 -1 O MET B 92 N ILE B 67
SHEET 1 AA6 4 SER B 184 HIS B 188 0
SHEET 2 AA6 4 TYR B 275 ASN B 280 -1 O GLY B 278 N PHE B 185
SHEET 3 AA6 4 LYS B 206 VAL B 211 -1 N TYR B 209 O ALA B 277
SHEET 4 AA6 4 ASP B 258 GLN B 262 -1 O GLN B 262 N LYS B 206
SHEET 1 AA710 MET C 15 PHE C 17 0
SHEET 2 AA710 LEU C 44 VAL C 47 1 O LYS C 46 N MET C 15
SHEET 3 AA710 PHE C 267 THR C 270 -1 O ILE C 269 N ALA C 45
SHEET 4 AA710 TYR C 195 GLY C 203 -1 N ASN C 198 O MET C 268
SHEET 5 AA710 ASN C 284 PHE C 291 -1 O GLU C 287 N TYR C 199
SHEET 6 AA710 TYR C 175 GLY C 179 -1 N TYR C 177 O ALA C 286
SHEET 7 AA710 ILE C 131 ASN C 137 -1 N GLY C 133 O PHE C 178
SHEET 8 AA710 ILE C 71 GLN C 78 -1 N ILE C 71 O TYR C 132
SHEET 9 AA710 LEU C 81 GLN C 88 -1 O TYR C 85 N LEU C 74
SHEET 10 AA710 THR C 243 ILE C 245 -1 O LEU C 244 N PHE C 82
SHEET 1 AA8 2 VAL C 66 ILE C 67 0
SHEET 2 AA8 2 MET C 92 THR C 93 -1 O MET C 92 N ILE C 67
SHEET 1 AA9 4 SER C 184 HIS C 188 0
SHEET 2 AA9 4 TYR C 275 ASN C 280 -1 O GLY C 278 N PHE C 185
SHEET 3 AA9 4 LYS C 206 VAL C 211 -1 N SER C 207 O PHE C 279
SHEET 4 AA9 4 ASP C 258 GLN C 262 -1 O VAL C 260 N TRP C 208
SHEET 1 AB110 THR D 16 PHE D 17 0
SHEET 2 AB110 LEU D 44 VAL D 47 1 O LYS D 46 N PHE D 17
SHEET 3 AB110 PHE D 267 THR D 270 -1 O ILE D 269 N ALA D 45
SHEET 4 AB110 TYR D 195 GLY D 203 -1 N SER D 196 O THR D 270
SHEET 5 AB110 ASN D 284 PHE D 291 -1 O GLU D 287 N TYR D 199
SHEET 6 AB110 TYR D 175 GLY D 179 -1 N TYR D 177 O ALA D 286
SHEET 7 AB110 ILE D 131 ASN D 137 -1 N GLY D 133 O PHE D 178
SHEET 8 AB110 ILE D 71 GLN D 78 -1 N ILE D 71 O TYR D 132
SHEET 9 AB110 LEU D 81 GLN D 88 -1 O TYR D 85 N LEU D 74
SHEET 10 AB110 THR D 243 ILE D 245 -1 O LEU D 244 N PHE D 82
SHEET 1 AB2 2 VAL D 66 ILE D 67 0
SHEET 2 AB2 2 MET D 92 THR D 93 -1 O MET D 92 N ILE D 67
SHEET 1 AB3 4 SER D 184 HIS D 188 0
SHEET 2 AB3 4 TYR D 275 ASN D 280 -1 O HIS D 276 N HIS D 188
SHEET 3 AB3 4 LYS D 206 VAL D 211 -1 N TYR D 209 O ALA D 277
SHEET 4 AB3 4 ASP D 258 GLN D 262 -1 O GLN D 262 N LYS D 206
LINK NE2 HIS A 188 ZN ZN A 401 1555 1555 2.17
LINK OE2 GLU A 190 ZN ZN A 401 1555 1555 2.08
LINK SG CYS A 234 ZN ZN A 402 1555 1555 2.17
LINK NE2 HIS A 240 ZN ZN A 402 1555 1555 2.14
LINK NE2 HIS A 276 ZN ZN A 401 1555 1555 2.24
LINK SG CYS A 306 ZN ZN A 402 1555 1555 2.17
LINK SG CYS A 308 ZN ZN A 402 1555 1555 2.70
LINK ZN ZN A 401 N1 5TZ A 403 1555 1555 2.27
LINK ZN ZN A 401 N2 5TZ A 403 1555 1555 2.15
LINK ZN ZN A 401 O HOH A 526 1555 1555 2.10
LINK NE2 HIS B 188 ZN ZN B 401 1555 1555 2.18
LINK OE2 GLU B 190 ZN ZN B 401 1555 1555 2.11
LINK SG CYS B 234 ZN ZN B 402 1555 1555 2.20
LINK NE2 HIS B 240 ZN ZN B 402 1555 1555 2.15
LINK NE2 HIS B 276 ZN ZN B 401 1555 1555 2.26
LINK SG CYS B 306 ZN ZN B 402 1555 1555 2.16
LINK SG CYS B 308 ZN ZN B 402 1555 1555 2.52
LINK ZN ZN B 401 N2 5TZ B 403 1555 1555 2.14
LINK ZN ZN B 401 N1 5TZ B 403 1555 1555 2.25
LINK ZN ZN B 401 O HOH B 574 1555 1555 2.10
LINK NE2 HIS C 188 ZN ZN C 401 1555 1555 2.24
LINK OE2 GLU C 190 ZN ZN C 401 1555 1555 2.13
LINK SG CYS C 234 ZN ZN C 402 1555 1555 2.20
LINK NE2 HIS C 240 ZN ZN C 402 1555 1555 2.06
LINK NE2 HIS C 276 ZN ZN C 401 1555 1555 2.27
LINK SG CYS C 306 ZN ZN C 402 1555 1555 2.17
LINK SG CYS C 308 ZN ZN C 402 1555 1555 2.39
LINK ZN ZN C 401 N1 5TZ C 403 1555 1555 2.23
LINK ZN ZN C 401 N2 5TZ C 403 1555 1555 2.17
LINK ZN ZN C 401 O HOH C 583 1555 1555 2.03
LINK NE2 HIS D 188 ZN ZN D 401 1555 1555 2.17
LINK OE2 GLU D 190 ZN ZN D 401 1555 1555 2.11
LINK SG CYS D 234 ZN ZN D 402 1555 1555 2.29
LINK NE2 HIS D 240 ZN ZN D 402 1555 1555 2.06
LINK NE2 HIS D 276 ZN ZN D 401 1555 1555 2.23
LINK SG CYS D 306 ZN ZN D 402 1555 1555 2.22
LINK SG CYS D 308 ZN ZN D 402 1555 1555 2.44
LINK ZN ZN D 401 N2 5TZ D 403 1555 1555 2.21
LINK ZN ZN D 401 N1 5TZ D 403 1555 1555 2.28
LINK ZN ZN D 401 O HOH D 629 1555 1555 2.23
SITE 1 AC1 5 HIS A 188 GLU A 190 HIS A 276 5TZ A 403
SITE 2 AC1 5 HOH A 526
SITE 1 AC2 4 CYS A 234 HIS A 240 CYS A 306 CYS A 308
SITE 1 AC3 14 TYR A 132 TYR A 177 PHE A 185 HIS A 188
SITE 2 AC3 14 GLU A 190 LYS A 206 TRP A 208 LYS A 241
SITE 3 AC3 14 HIS A 276 ZN A 401 HOH A 502 HOH A 526
SITE 4 AC3 14 HOH A 533 HOH A 614
SITE 1 AC4 7 GLY A 170 TYR A 177 GLU A 190 SER A 196
SITE 2 AC4 7 SER A 288 THR A 289 ASN A 290
SITE 1 AC5 4 THR A 83 PHE A 227 SER A 230 THR A 243
SITE 1 AC6 2 PRO A 247 LEU A 248
SITE 1 AC7 3 LEU A 65 GLY A 138 THR A 139
SITE 1 AC8 6 ILE A 150 GLY A 151 ARG A 152 LEU A 153
SITE 2 AC8 6 ASN A 290 HOH A 534
SITE 1 AC9 5 ASN A 9 PRO A 10 SER A 11 ALA A 12
SITE 2 AC9 5 ARG A 13
SITE 1 AD1 5 SER A 11 ALA A 12 ARG A 13 PHE A 257
SITE 2 AD1 5 ASP A 258
SITE 1 AD2 4 TYR A 59 ARG A 98 PHE A 202 PHE A 283
SITE 1 AD3 2 LYS A 217 TYR A 273
SITE 1 AD4 5 HIS B 188 GLU B 190 HIS B 276 5TZ B 403
SITE 2 AD4 5 HOH B 574
SITE 1 AD5 4 CYS B 234 HIS B 240 CYS B 306 CYS B 308
SITE 1 AD6 14 TYR B 132 TYR B 177 PHE B 185 HIS B 188
SITE 2 AD6 14 GLU B 190 LYS B 206 TRP B 208 HIS B 276
SITE 3 AD6 14 ZN B 401 HOH B 501 HOH B 550 HOH B 561
SITE 4 AD6 14 HOH B 574 HOH B 666
SITE 1 AD7 5 GLY B 170 TYR B 177 GLU B 190 SER B 288
SITE 2 AD7 5 ASN B 290
SITE 1 AD8 4 ASN B 9 PRO B 10 SER B 11 HOH B 603
SITE 1 AD9 5 PRO B 10 ALA B 12 GLU B 214 HIS B 215
SITE 2 AD9 5 HOH B 559
SITE 1 AE1 7 SER B 11 ALA B 12 ARG B 13 PRO B 212
SITE 2 AE1 7 PHE B 257 ASP B 258 HOH B 539
SITE 1 AE2 3 PRO B 256 PHE B 257 HOH B 527
SITE 1 AE3 3 LEU B 65 GLY B 138 THR B 139
SITE 1 AE4 4 THR B 83 PHE B 227 SER B 230 THR B 243
SITE 1 AE5 2 TRP B 122 LEU B 248
SITE 1 AE6 6 ILE B 150 GLY B 151 ARG B 152 LEU B 153
SITE 2 AE6 6 ASN B 290 HOH B 507
SITE 1 AE7 3 ASN B 9 GLN B 37 HOH B 512
SITE 1 AE8 5 GLU B 23 ARG B 29 TYR B 33 PHE B 353
SITE 2 AE8 5 HOH B 635
SITE 1 AE9 5 HIS C 188 GLU C 190 HIS C 276 5TZ C 403
SITE 2 AE9 5 HOH C 583
SITE 1 AF1 4 CYS C 234 HIS C 240 CYS C 306 CYS C 308
SITE 1 AF2 15 TYR C 132 TYR C 177 PHE C 185 HIS C 188
SITE 2 AF2 15 GLU C 190 LYS C 206 TRP C 208 LYS C 241
SITE 3 AF2 15 HIS C 276 ZN C 401 EDO C 404 HOH C 503
SITE 4 AF2 15 HOH C 571 HOH C 581 HOH C 583
SITE 1 AF3 7 GLY C 170 TYR C 177 GLU C 190 SER C 288
SITE 2 AF3 7 THR C 289 ASN C 290 5TZ C 403
SITE 1 AF4 4 THR C 83 PHE C 227 THR C 243 HOH C 616
SITE 1 AF5 2 HOH C 552 HOH C 559
SITE 1 AF6 3 LEU C 65 GLY C 138 THR C 139
SITE 1 AF7 7 SER C 11 ALA C 12 ARG C 13 PRO C 212
SITE 2 AF7 7 PHE C 257 ASP C 258 HOH C 539
SITE 1 AF8 4 GLU C 23 TYR C 30 TYR C 33 HOH C 531
SITE 1 AF9 4 LYS C 105 TYR C 106 CYS C 107 HOH C 592
SITE 1 AG1 6 ILE C 150 ARG C 152 LEU C 153 ASP C 158
SITE 2 AG1 6 ASN C 290 HOH C 525
SITE 1 AG2 5 GLU C 298 THR C 339 VAL C 340 ASP C 342
SITE 2 AG2 5 HOH C 585
SITE 1 AG3 2 TYR C 59 ARG C 98
SITE 1 AG4 5 HIS D 188 GLU D 190 HIS D 276 5TZ D 403
SITE 2 AG4 5 HOH D 629
SITE 1 AG5 4 CYS D 234 HIS D 240 CYS D 306 CYS D 308
SITE 1 AG6 12 TYR D 132 TYR D 177 PHE D 185 HIS D 188
SITE 2 AG6 12 GLU D 190 LYS D 206 TRP D 208 HIS D 276
SITE 3 AG6 12 ZN D 401 HOH D 628 HOH D 629 HOH D 660
SITE 1 AG7 6 GLY D 170 TYR D 177 GLU D 190 SER D 288
SITE 2 AG7 6 THR D 289 ASN D 290
SITE 1 AG8 8 GLU D 220 LYS D 224 ALA D 236 PHE D 237
SITE 2 AG8 8 LEU D 238 TYR D 275 HOH D 520 HOH D 590
SITE 1 AG9 2 HIS D 201 PHE D 202
SITE 1 AH1 4 THR D 83 SER D 230 PHE D 237 THR D 243
SITE 1 AH2 4 GLU D 118 TRP D 122 LEU D 248 HOH D 563
SITE 1 AH3 7 SER D 11 ALA D 12 ARG D 13 PRO D 212
SITE 2 AH3 7 PHE D 257 ASP D 258 HOH D 517
SITE 1 AH4 4 SER D 11 ALA D 12 GLU D 214 HIS D 215
SITE 1 AH5 5 LYS D 251 GLY D 254 ILE D 255 PHE D 257
SITE 2 AH5 5 EDO D 414
SITE 1 AH6 5 GLU A 161 LYS A 162 ARG D 56 ASP D 61
SITE 2 AH6 5 LEU D 65
SITE 1 AH7 3 PRO D 256 PHE D 257 EDO D 412
SITE 1 AH8 2 TYR D 59 ARG D 98
CRYST1 57.450 102.320 142.250 90.00 99.82 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 0.017406 0.000000 0.003013 0.00000
SCALE2 0.000000 0.009773 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007134 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
