HEADER TRANSFERASE 31-JAN-11 2Y7J
TITLE STRUCTURE OF HUMAN PHOSPHORYLASE KINASE, GAMMA 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHORYLASE B KINASE GAMMA CATALYTIC CHAIN, TESTIS/LIVER
COMPND 3 ISOFORM;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 FRAGMENT: RESIDUES 6-293;
COMPND 6 SYNONYM: PHOSPHORYLASE KINASE GAMMA 2, PHK-GAMMA-T, PSK-C3,
COMPND 7 PHOSPHORYLASE KINASE SUBUNIT GAMMA-2;
COMPND 8 EC: 2.7.11.19;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: R-LA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PNIC-ZB
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.C.MUNIZ,A.SHRESTHA,P.SAVITSKY,J.WANG,P.RELLOS,O.FEDOROV,
AUTHOR 2 N.BURGESS-BROWN,B.BRENNER,G.BERRIDGE,J.M.ELKINS,T.KROJER,M.VOLLMAR,
AUTHOR 3 K.H.CHE,F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,J.WEIGELT,C.BOUNTRA,
AUTHOR 4 S.KNAPP
REVDAT 3 24-JAN-18 2Y7J 1 JRNL
REVDAT 2 12-OCT-11 2Y7J 1 SOURCE REMARK HETATM VERSN
REVDAT 1 09-FEB-11 2Y7J 0
JRNL AUTH J.R.C.MUNIZ,A.SHRESTHA,P.SAVITSKY,J.WANG,P.RELLOS,O.FEDOROV,
JRNL AUTH 2 N.BURGESS-BROWN,B.BRENNER,G.BERRIDGE,J.M.ELKINS,T.KROJER,
JRNL AUTH 3 M.VOLLMAR,K.H.CHE,F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,
JRNL AUTH 4 J.WEIGELT,C.BOUNTRA,S.KNAPP
JRNL TITL STRUCTURE OF HUMAN PHOSPHORYLASE KINASE, GAMMA 2
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.8.0
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 46353
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.182
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 2343
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.56
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3283
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2166
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3100
REMARK 3 BIN R VALUE (WORKING SET) : 0.2133
REMARK 3 BIN FREE R VALUE : 0.2722
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.57
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 183
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 : 8940
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 116
REMARK 3 SOLVENT ATOMS : 283
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 56.58
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.37820
REMARK 3 B22 (A**2) : -2.91620
REMARK 3 B33 (A**2) : 3.29430
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.306
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 9318 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 12635 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 4273 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 248 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1386 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 9318 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1188 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
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 : 10788 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.08
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.20
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.89
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 10 - 118)
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5224 -3.1174 47.2739
REMARK 3 T TENSOR
REMARK 3 T11: -0.0810 T22: 0.0140
REMARK 3 T33: -0.0961 T12: 0.0178
REMARK 3 T13: 0.0010 T23: 0.0348
REMARK 3 L TENSOR
REMARK 3 L11: 0.5490 L22: 2.3057
REMARK 3 L33: 2.4548 L12: 0.1333
REMARK 3 L13: 0.1551 L23: 0.8495
REMARK 3 S TENSOR
REMARK 3 S11: -0.1063 S12: 0.0740 S13: 0.0532
REMARK 3 S21: 0.0745 S22: 0.0161 S23: 0.2650
REMARK 3 S31: -0.2144 S32: -0.0373 S33: 0.0902
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 119 - 131)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.0438 -24.7278 33.1752
REMARK 3 T TENSOR
REMARK 3 T11: -0.0303 T22: 0.1951
REMARK 3 T33: -0.0943 T12: 0.1520
REMARK 3 T13: 0.0258 T23: -0.0389
REMARK 3 L TENSOR
REMARK 3 L11: 2.0918 L22: 0.6875
REMARK 3 L33: 0.0000 L12: -2.9002
REMARK 3 L13: 2.0709 L23: 1.1794
REMARK 3 S TENSOR
REMARK 3 S11: 0.0137 S12: -0.0505 S13: -0.1750
REMARK 3 S21: 0.0190 S22: 0.1030 S23: -0.1399
REMARK 3 S31: -0.0245 S32: 0.2315 S33: -0.1167
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 132 - 178)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.2961 -19.9314 41.7306
REMARK 3 T TENSOR
REMARK 3 T11: -0.0438 T22: -0.0669
REMARK 3 T33: -0.1138 T12: 0.0116
REMARK 3 T13: -0.0414 T23: -0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 0.6004 L22: 2.2751
REMARK 3 L33: 2.9994 L12: -0.6737
REMARK 3 L13: 0.3588 L23: 0.1994
REMARK 3 S TENSOR
REMARK 3 S11: 0.0502 S12: -0.0220 S13: 0.1798
REMARK 3 S21: 0.2210 S22: -0.0470 S23: 0.1868
REMARK 3 S31: 0.4079 S32: 0.1184 S33: -0.0033
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 179 - 186)
REMARK 3 ORIGIN FOR THE GROUP (A): -43.4873 -20.7281 36.8591
REMARK 3 T TENSOR
REMARK 3 T11: -0.1272 T22: -0.0112
REMARK 3 T33: 0.2985 T12: -0.1009
REMARK 3 T13: -0.1152 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 3.0857 L22: 0.8666
REMARK 3 L33: 0.0000 L12: 0.6114
REMARK 3 L13: 0.3025 L23: -0.1809
REMARK 3 S TENSOR
REMARK 3 S11: 0.0168 S12: 0.0382 S13: 0.0288
REMARK 3 S21: 0.1774 S22: -0.1072 S23: 0.0401
REMARK 3 S31: 0.0701 S32: -0.1287 S33: 0.0904
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 187 - 232)
REMARK 3 ORIGIN FOR THE GROUP (A): -31.2986 -22.4086 28.2363
REMARK 3 T TENSOR
REMARK 3 T11: 0.0219 T22: -0.0282
REMARK 3 T33: -0.0983 T12: -0.0146
REMARK 3 T13: -0.0812 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 4.3493
REMARK 3 L33: 3.5009 L12: -1.3302
REMARK 3 L13: 0.0251 L23: 1.1135
REMARK 3 S TENSOR
REMARK 3 S11: 0.0656 S12: 0.1161 S13: -0.0252
REMARK 3 S21: -0.4808 S22: -0.0907 S23: 0.5442
REMARK 3 S31: 0.4256 S32: -0.0588 S33: 0.0250
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 233 - 292)
REMARK 3 ORIGIN FOR THE GROUP (A): -24.6404 -29.9401 26.2073
REMARK 3 T TENSOR
REMARK 3 T11: 0.0585 T22: -0.1380
REMARK 3 T33: -0.2295 T12: 0.0456
REMARK 3 T13: -0.0655 T23: -0.1211
REMARK 3 L TENSOR
REMARK 3 L11: 3.3249 L22: 2.9897
REMARK 3 L33: 6.4938 L12: -1.2141
REMARK 3 L13: 1.0540 L23: -0.9141
REMARK 3 S TENSOR
REMARK 3 S11: -0.0227 S12: 0.4148 S13: -0.3923
REMARK 3 S21: -0.0840 S22: -0.0377 S23: 0.0355
REMARK 3 S31: 0.5442 S32: 0.5083 S33: 0.0604
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 11 - 55)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0360 -3.2267 -6.7566
REMARK 3 T TENSOR
REMARK 3 T11: -0.0599 T22: -0.1043
REMARK 3 T33: -0.0695 T12: -0.0098
REMARK 3 T13: 0.0108 T23: -0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 2.3497 L22: 1.1648
REMARK 3 L33: 2.5747 L12: -0.4532
REMARK 3 L13: 1.5748 L23: -0.5183
REMARK 3 S TENSOR
REMARK 3 S11: 0.1458 S12: -0.0184 S13: 0.0357
REMARK 3 S21: 0.0796 S22: -0.0549 S23: -0.3538
REMARK 3 S31: -0.1084 S32: 0.1848 S33: -0.0909
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 56 - 82)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1159 14.1691 -3.9376
REMARK 3 T TENSOR
REMARK 3 T11: 0.1789 T22: 0.0391
REMARK 3 T33: -0.0088 T12: -0.1520
REMARK 3 T13: 0.0049 T23: -0.1414
REMARK 3 L TENSOR
REMARK 3 L11: 1.2060 L22: 1.9945
REMARK 3 L33: 0.9978 L12: -2.9104
REMARK 3 L13: 2.7320 L23: -2.9104
REMARK 3 S TENSOR
REMARK 3 S11: -0.0248 S12: 0.0161 S13: 0.1956
REMARK 3 S21: -0.2038 S22: -0.0851 S23: 0.2739
REMARK 3 S31: -0.2393 S32: 0.1440 S33: 0.1099
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 83 - 110)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2251 0.9966 -2.8629
REMARK 3 T TENSOR
REMARK 3 T11: 0.0032 T22: -0.0230
REMARK 3 T33: -0.0245 T12: -0.0337
REMARK 3 T13: 0.0051 T23: -0.0576
REMARK 3 L TENSOR
REMARK 3 L11: 2.2240 L22: 0.0000
REMARK 3 L33: 2.8570 L12: 2.9104
REMARK 3 L13: 2.1676 L23: 2.8478
REMARK 3 S TENSOR
REMARK 3 S11: -0.0128 S12: -0.1330 S13: 0.1808
REMARK 3 S21: -0.2134 S22: 0.1116 S23: -0.0957
REMARK 3 S31: -0.0628 S32: 0.2266 S33: -0.0988
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 111 - 183)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7813 1.1243 12.7587
REMARK 3 T TENSOR
REMARK 3 T11: -0.0736 T22: -0.0344
REMARK 3 T33: -0.0413 T12: -0.0425
REMARK 3 T13: -0.0281 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.9018 L22: 4.3122
REMARK 3 L33: 2.2577 L12: 0.3679
REMARK 3 L13: 1.1381 L23: 1.7724
REMARK 3 S TENSOR
REMARK 3 S11: -0.0064 S12: 0.2091 S13: -0.3028
REMARK 3 S21: -0.4253 S22: 0.4113 S23: -0.3430
REMARK 3 S31: 0.4388 S32: 0.1757 S33: -0.4050
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN B AND RESID 184 - 229)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.6413 15.3745 18.5428
REMARK 3 T TENSOR
REMARK 3 T11: -0.0447 T22: 0.0163
REMARK 3 T33: -0.1135 T12: -0.0662
REMARK 3 T13: -0.0214 T23: 0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 0.1286 L22: 7.0637
REMARK 3 L33: 0.0000 L12: 1.4167
REMARK 3 L13: -0.1977 L23: 2.2715
REMARK 3 S TENSOR
REMARK 3 S11: 0.0943 S12: 0.0756 S13: 0.0545
REMARK 3 S21: 0.3661 S22: 0.1660 S23: 0.0143
REMARK 3 S31: -0.1648 S32: 0.0612 S33: -0.2603
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN B AND RESID 230 - 293)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5938 6.4037 27.6853
REMARK 3 T TENSOR
REMARK 3 T11: -0.0285 T22: -0.1337
REMARK 3 T33: -0.2131 T12: -0.1084
REMARK 3 T13: -0.1520 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 3.2538 L22: 7.2407
REMARK 3 L33: 8.2135 L12: 1.8735
REMARK 3 L13: -0.3743 L23: -0.4479
REMARK 3 S TENSOR
REMARK 3 S11: 0.0112 S12: -0.5065 S13: -0.4714
REMARK 3 S21: 0.5442 S22: 0.0935 S23: -0.3617
REMARK 3 S31: -0.1597 S32: 0.3735 S33: -0.1047
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN C AND RESID 10 - 111)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2557 -1.0067 -10.6763
REMARK 3 T TENSOR
REMARK 3 T11: 0.0069 T22: -0.0608
REMARK 3 T33: -0.0833 T12: 0.0144
REMARK 3 T13: -0.0745 T23: -0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 1.9222 L22: 0.5961
REMARK 3 L33: 2.3247 L12: 0.0511
REMARK 3 L13: -0.3002 L23: -0.3424
REMARK 3 S TENSOR
REMARK 3 S11: 0.0592 S12: 0.0601 S13: -0.0353
REMARK 3 S21: 0.0666 S22: -0.0516 S23: -0.0689
REMARK 3 S31: 0.0735 S32: -0.0664 S33: -0.0076
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN C AND RESID 112 - 178)
REMARK 3 ORIGIN FOR THE GROUP (A): -38.2396 3.1254 -1.4931
REMARK 3 T TENSOR
REMARK 3 T11: -0.0507 T22: -0.0043
REMARK 3 T33: -0.1076 T12: 0.0782
REMARK 3 T13: -0.0347 T23: 0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 2.3568 L22: 3.3277
REMARK 3 L33: 3.0768 L12: 0.6995
REMARK 3 L13: 0.0428 L23: -0.0240
REMARK 3 S TENSOR
REMARK 3 S11: 0.1151 S12: 0.1016 S13: 0.2923
REMARK 3 S21: 0.2187 S22: 0.0252 S23: 0.1800
REMARK 3 S31: -0.2195 S32: -0.4897 S33: -0.1402
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN C AND RESID 179 - 186)
REMARK 3 ORIGIN FOR THE GROUP (A): -39.4227 -20.0129 -1.7411
REMARK 3 T TENSOR
REMARK 3 T11: 0.1574 T22: -0.1085
REMARK 3 T33: 0.0981 T12: -0.1520
REMARK 3 T13: -0.1511 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 1.1118 L22: 2.7507
REMARK 3 L33: 0.8239 L12: 1.8381
REMARK 3 L13: -2.1376 L23: -0.9891
REMARK 3 S TENSOR
REMARK 3 S11: -0.0230 S12: 0.0619 S13: 0.0422
REMARK 3 S21: 0.0134 S22: 0.0800 S23: 0.0301
REMARK 3 S31: 0.0436 S32: -0.0678 S33: -0.0570
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN C AND RESID 187 - 246)
REMARK 3 ORIGIN FOR THE GROUP (A): -39.5436 -8.2769 11.4855
REMARK 3 T TENSOR
REMARK 3 T11: 0.0360 T22: -0.0531
REMARK 3 T33: -0.0723 T12: 0.0459
REMARK 3 T13: -0.0097 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 0.5306 L22: 1.1984
REMARK 3 L33: 1.1888 L12: 0.1108
REMARK 3 L13: 0.0622 L23: -2.6265
REMARK 3 S TENSOR
REMARK 3 S11: 0.0121 S12: 0.0189 S13: 0.0179
REMARK 3 S21: 0.4965 S22: 0.2688 S23: 0.4756
REMARK 3 S31: -0.2185 S32: -0.5442 S33: -0.2808
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN C AND RESID 247 - 257)
REMARK 3 ORIGIN FOR THE GROUP (A): -48.3382 1.8129 18.0980
REMARK 3 T TENSOR
REMARK 3 T11: 0.0538 T22: 0.0433
REMARK 3 T33: -0.0449 T12: 0.1024
REMARK 3 T13: 0.1520 T23: 0.1520
REMARK 3 L TENSOR
REMARK 3 L11: 2.8807 L22: 0.0000
REMARK 3 L33: 2.2666 L12: -1.1365
REMARK 3 L13: -0.4917 L23: -1.0062
REMARK 3 S TENSOR
REMARK 3 S11: -0.0225 S12: -0.0383 S13: 0.1146
REMARK 3 S21: 0.0429 S22: -0.0598 S23: -0.0124
REMARK 3 S31: -0.0644 S32: 0.0056 S33: 0.0822
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN C AND RESID 258 - 292)
REMARK 3 ORIGIN FOR THE GROUP (A): -52.8069 -0.7229 4.6583
REMARK 3 T TENSOR
REMARK 3 T11: -0.2212 T22: 0.1627
REMARK 3 T33: -0.0060 T12: 0.0708
REMARK 3 T13: 0.0496 T23: 0.1059
REMARK 3 L TENSOR
REMARK 3 L11: 3.2495 L22: 1.5165
REMARK 3 L33: 2.7522 L12: -2.9104
REMARK 3 L13: -1.2829 L23: 0.9907
REMARK 3 S TENSOR
REMARK 3 S11: 0.0054 S12: 0.1323 S13: 0.0552
REMARK 3 S21: 0.1775 S22: 0.0974 S23: 0.4286
REMARK 3 S31: -0.1689 S32: -0.5423 S33: -0.1028
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN D AND RESID 11 - 55)
REMARK 3 ORIGIN FOR THE GROUP (A): -26.6932 15.9233 45.2118
REMARK 3 T TENSOR
REMARK 3 T11: -0.1578 T22: 0.0195
REMARK 3 T33: -0.1145 T12: 0.0380
REMARK 3 T13: 0.0180 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 0.2669 L22: 4.8411
REMARK 3 L33: 3.7281 L12: 0.9278
REMARK 3 L13: -0.0875 L23: -0.3621
REMARK 3 S TENSOR
REMARK 3 S11: 0.0366 S12: 0.3491 S13: -0.0594
REMARK 3 S21: 0.0698 S22: 0.1661 S23: -0.0949
REMARK 3 S31: -0.1686 S32: 0.3721 S33: -0.2027
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN D AND RESID 56 - 72)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8567 15.3474 45.9389
REMARK 3 T TENSOR
REMARK 3 T11: -0.0400 T22: 0.1312
REMARK 3 T33: 0.2247 T12: 0.0302
REMARK 3 T13: -0.0433 T23: 0.0755
REMARK 3 L TENSOR
REMARK 3 L11: 1.7555 L22: 2.4302
REMARK 3 L33: 1.4543 L12: -1.9173
REMARK 3 L13: -0.1909 L23: 0.3748
REMARK 3 S TENSOR
REMARK 3 S11: 0.0050 S12: 0.0469 S13: -0.0267
REMARK 3 S21: 0.0255 S22: -0.0018 S23: 0.0493
REMARK 3 S31: -0.0255 S32: -0.0133 S33: -0.0032
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN D AND RESID 73 - 111)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.8356 25.7850 42.6683
REMARK 3 T TENSOR
REMARK 3 T11: -0.1273 T22: 0.0500
REMARK 3 T33: -0.1236 T12: -0.0701
REMARK 3 T13: -0.0025 T23: -0.0322
REMARK 3 L TENSOR
REMARK 3 L11: 1.3729 L22: 0.9147
REMARK 3 L33: 3.2483 L12: 0.5868
REMARK 3 L13: -2.9104 L23: -1.1745
REMARK 3 S TENSOR
REMARK 3 S11: 0.1081 S12: -0.2461 S13: 0.2101
REMARK 3 S21: 0.0082 S22: 0.1626 S23: 0.1006
REMARK 3 S31: -0.3901 S32: 0.4210 S33: -0.2707
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN D AND RESID 112 - 183)
REMARK 3 ORIGIN FOR THE GROUP (A): -19.4548 30.9288 27.3812
REMARK 3 T TENSOR
REMARK 3 T11: -0.1851 T22: -0.0131
REMARK 3 T33: -0.1184 T12: -0.0229
REMARK 3 T13: 0.0249 T23: 0.0708
REMARK 3 L TENSOR
REMARK 3 L11: 8.3155 L22: 2.1522
REMARK 3 L33: 4.1445 L12: 0.3133
REMARK 3 L13: -0.9866 L23: -0.2099
REMARK 3 S TENSOR
REMARK 3 S11: 0.2466 S12: 0.4758 S13: 0.5442
REMARK 3 S21: -0.1090 S22: 0.0511 S23: 0.3700
REMARK 3 S31: -0.2527 S32: -0.5442 S33: -0.2977
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN D AND RESID 184 - 231)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.2456 30.5557 23.1368
REMARK 3 T TENSOR
REMARK 3 T11: -0.0828 T22: 0.1403
REMARK 3 T33: -0.1128 T12: -0.0142
REMARK 3 T13: -0.0388 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 8.3155 L22: 0.5254
REMARK 3 L33: 0.0261 L12: 2.6403
REMARK 3 L13: -2.3055 L23: 0.1159
REMARK 3 S TENSOR
REMARK 3 S11: 0.1226 S12: 0.5299 S13: 0.1525
REMARK 3 S21: -0.1127 S22: 0.0960 S23: 0.0360
REMARK 3 S31: -0.1449 S32: -0.1316 S33: -0.2186
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN D AND RESID 232 - 293)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.9287 33.5418 13.5590
REMARK 3 T TENSOR
REMARK 3 T11: -0.3040 T22: 0.1526
REMARK 3 T33: -0.2687 T12: 0.0095
REMARK 3 T13: -0.0083 T23: 0.1520
REMARK 3 L TENSOR
REMARK 3 L11: 7.8335 L22: 4.3395
REMARK 3 L33: 8.3155 L12: -0.4026
REMARK 3 L13: -2.9104 L23: -1.1665
REMARK 3 S TENSOR
REMARK 3 S11: 0.1222 S12: 0.5442 S13: 0.5217
REMARK 3 S21: -0.2560 S22: 0.0227 S23: 0.2824
REMARK 3 S31: -0.2240 S32: -0.0795 S33: -0.1448
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2Y7J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JAN-11.
REMARK 100 THE DEPOSITION ID IS D_1290047206.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46408
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 63.320
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.56000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350; 0.1 M BIS-TRIS 5.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 43.89500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.24000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.71000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.24000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 43.89500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.71000
REMARK 290 SMTRY3 4 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 MET A -71
REMARK 465 HIS A -70
REMARK 465 HIS A -69
REMARK 465 HIS A -68
REMARK 465 HIS A -67
REMARK 465 HIS A -66
REMARK 465 HIS A -65
REMARK 465 SER A -64
REMARK 465 SER A -63
REMARK 465 GLY A -62
REMARK 465 VAL A -61
REMARK 465 ASP A -60
REMARK 465 ASN A -59
REMARK 465 LYS A -58
REMARK 465 PHE A -57
REMARK 465 ASN A -56
REMARK 465 LYS A -55
REMARK 465 GLU A -54
REMARK 465 ARG A -53
REMARK 465 ARG A -52
REMARK 465 ARG A -51
REMARK 465 ALA A -50
REMARK 465 ARG A -49
REMARK 465 ARG A -48
REMARK 465 GLU A -47
REMARK 465 ILE A -46
REMARK 465 ARG A -45
REMARK 465 HIS A -44
REMARK 465 LEU A -43
REMARK 465 PRO A -42
REMARK 465 ASN A -41
REMARK 465 LEU A -40
REMARK 465 ASN A -39
REMARK 465 ARG A -38
REMARK 465 GLU A -37
REMARK 465 GLN A -36
REMARK 465 ARG A -35
REMARK 465 ARG A -34
REMARK 465 ALA A -33
REMARK 465 PHE A -32
REMARK 465 ILE A -31
REMARK 465 ARG A -30
REMARK 465 SER A -29
REMARK 465 LEU A -28
REMARK 465 ARG A -27
REMARK 465 ASP A -26
REMARK 465 ASP A -25
REMARK 465 PRO A -24
REMARK 465 SER A -23
REMARK 465 GLN A -22
REMARK 465 SER A -21
REMARK 465 ALA A -20
REMARK 465 ASN A -19
REMARK 465 LEU A -18
REMARK 465 LEU A -17
REMARK 465 ALA A -16
REMARK 465 GLU A -15
REMARK 465 ALA A -14
REMARK 465 LYS A -13
REMARK 465 LYS A -12
REMARK 465 LEU A -11
REMARK 465 ASN A -10
REMARK 465 ASP A -9
REMARK 465 ALA A -8
REMARK 465 GLN A -7
REMARK 465 PRO A -6
REMARK 465 LYS A -5
REMARK 465 GLY A -4
REMARK 465 THR A -3
REMARK 465 GLU A -2
REMARK 465 ASN A -1
REMARK 465 LEU A 0
REMARK 465 TYR A 1
REMARK 465 PHE A 2
REMARK 465 GLN A 3
REMARK 465 SER A 4
REMARK 465 MET A 5
REMARK 465 GLY A 6
REMARK 465 PRO A 7
REMARK 465 GLU A 8
REMARK 465 ASP A 9
REMARK 465 MET B -71
REMARK 465 HIS B -70
REMARK 465 HIS B -69
REMARK 465 HIS B -68
REMARK 465 HIS B -67
REMARK 465 HIS B -66
REMARK 465 HIS B -65
REMARK 465 SER B -64
REMARK 465 SER B -63
REMARK 465 GLY B -62
REMARK 465 VAL B -61
REMARK 465 ASP B -60
REMARK 465 ASN B -59
REMARK 465 LYS B -58
REMARK 465 PHE B -57
REMARK 465 ASN B -56
REMARK 465 LYS B -55
REMARK 465 GLU B -54
REMARK 465 ARG B -53
REMARK 465 ARG B -52
REMARK 465 ARG B -51
REMARK 465 ALA B -50
REMARK 465 ARG B -49
REMARK 465 ARG B -48
REMARK 465 GLU B -47
REMARK 465 ILE B -46
REMARK 465 ARG B -45
REMARK 465 HIS B -44
REMARK 465 LEU B -43
REMARK 465 PRO B -42
REMARK 465 ASN B -41
REMARK 465 LEU B -40
REMARK 465 ASN B -39
REMARK 465 ARG B -38
REMARK 465 GLU B -37
REMARK 465 GLN B -36
REMARK 465 ARG B -35
REMARK 465 ARG B -34
REMARK 465 ALA B -33
REMARK 465 PHE B -32
REMARK 465 ILE B -31
REMARK 465 ARG B -30
REMARK 465 SER B -29
REMARK 465 LEU B -28
REMARK 465 ARG B -27
REMARK 465 ASP B -26
REMARK 465 ASP B -25
REMARK 465 PRO B -24
REMARK 465 SER B -23
REMARK 465 GLN B -22
REMARK 465 SER B -21
REMARK 465 ALA B -20
REMARK 465 ASN B -19
REMARK 465 LEU B -18
REMARK 465 LEU B -17
REMARK 465 ALA B -16
REMARK 465 GLU B -15
REMARK 465 ALA B -14
REMARK 465 LYS B -13
REMARK 465 LYS B -12
REMARK 465 LEU B -11
REMARK 465 ASN B -10
REMARK 465 ASP B -9
REMARK 465 ALA B -8
REMARK 465 GLN B -7
REMARK 465 PRO B -6
REMARK 465 LYS B -5
REMARK 465 GLY B -4
REMARK 465 THR B -3
REMARK 465 GLU B -2
REMARK 465 ASN B -1
REMARK 465 LEU B 0
REMARK 465 TYR B 1
REMARK 465 PHE B 2
REMARK 465 GLN B 3
REMARK 465 SER B 4
REMARK 465 MET B 5
REMARK 465 GLY B 6
REMARK 465 PRO B 7
REMARK 465 GLU B 8
REMARK 465 ASP B 9
REMARK 465 GLU B 60
REMARK 465 ARG B 61
REMARK 465 LEU B 62
REMARK 465 MET C -71
REMARK 465 HIS C -70
REMARK 465 HIS C -69
REMARK 465 HIS C -68
REMARK 465 HIS C -67
REMARK 465 HIS C -66
REMARK 465 HIS C -65
REMARK 465 SER C -64
REMARK 465 SER C -63
REMARK 465 GLY C -62
REMARK 465 VAL C -61
REMARK 465 ASP C -60
REMARK 465 ASN C -59
REMARK 465 LYS C -58
REMARK 465 PHE C -57
REMARK 465 ASN C -56
REMARK 465 LYS C -55
REMARK 465 GLU C -54
REMARK 465 ARG C -53
REMARK 465 ARG C -52
REMARK 465 ARG C -51
REMARK 465 ALA C -50
REMARK 465 ARG C -49
REMARK 465 ARG C -48
REMARK 465 GLU C -47
REMARK 465 ILE C -46
REMARK 465 ARG C -45
REMARK 465 HIS C -44
REMARK 465 LEU C -43
REMARK 465 PRO C -42
REMARK 465 ASN C -41
REMARK 465 LEU C -40
REMARK 465 ASN C -39
REMARK 465 ARG C -38
REMARK 465 GLU C -37
REMARK 465 GLN C -36
REMARK 465 ARG C -35
REMARK 465 ARG C -34
REMARK 465 ALA C -33
REMARK 465 PHE C -32
REMARK 465 ILE C -31
REMARK 465 ARG C -30
REMARK 465 SER C -29
REMARK 465 LEU C -28
REMARK 465 ARG C -27
REMARK 465 ASP C -26
REMARK 465 ASP C -25
REMARK 465 PRO C -24
REMARK 465 SER C -23
REMARK 465 GLN C -22
REMARK 465 SER C -21
REMARK 465 ALA C -20
REMARK 465 ASN C -19
REMARK 465 LEU C -18
REMARK 465 LEU C -17
REMARK 465 ALA C -16
REMARK 465 GLU C -15
REMARK 465 ALA C -14
REMARK 465 LYS C -13
REMARK 465 LYS C -12
REMARK 465 LEU C -11
REMARK 465 ASN C -10
REMARK 465 ASP C -9
REMARK 465 ALA C -8
REMARK 465 GLN C -7
REMARK 465 PRO C -6
REMARK 465 LYS C -5
REMARK 465 GLY C -4
REMARK 465 THR C -3
REMARK 465 GLU C -2
REMARK 465 ASN C -1
REMARK 465 LEU C 0
REMARK 465 TYR C 1
REMARK 465 PHE C 2
REMARK 465 GLN C 3
REMARK 465 SER C 4
REMARK 465 MET C 5
REMARK 465 GLY C 6
REMARK 465 PRO C 7
REMARK 465 GLU C 8
REMARK 465 ASP C 9
REMARK 465 MET D -71
REMARK 465 HIS D -70
REMARK 465 HIS D -69
REMARK 465 HIS D -68
REMARK 465 HIS D -67
REMARK 465 HIS D -66
REMARK 465 HIS D -65
REMARK 465 SER D -64
REMARK 465 SER D -63
REMARK 465 GLY D -62
REMARK 465 VAL D -61
REMARK 465 ASP D -60
REMARK 465 ASN D -59
REMARK 465 LYS D -58
REMARK 465 PHE D -57
REMARK 465 ASN D -56
REMARK 465 LYS D -55
REMARK 465 GLU D -54
REMARK 465 ARG D -53
REMARK 465 ARG D -52
REMARK 465 ARG D -51
REMARK 465 ALA D -50
REMARK 465 ARG D -49
REMARK 465 ARG D -48
REMARK 465 GLU D -47
REMARK 465 ILE D -46
REMARK 465 ARG D -45
REMARK 465 HIS D -44
REMARK 465 LEU D -43
REMARK 465 PRO D -42
REMARK 465 ASN D -41
REMARK 465 LEU D -40
REMARK 465 ASN D -39
REMARK 465 ARG D -38
REMARK 465 GLU D -37
REMARK 465 GLN D -36
REMARK 465 ARG D -35
REMARK 465 ARG D -34
REMARK 465 ALA D -33
REMARK 465 PHE D -32
REMARK 465 ILE D -31
REMARK 465 ARG D -30
REMARK 465 SER D -29
REMARK 465 LEU D -28
REMARK 465 ARG D -27
REMARK 465 ASP D -26
REMARK 465 ASP D -25
REMARK 465 PRO D -24
REMARK 465 SER D -23
REMARK 465 GLN D -22
REMARK 465 SER D -21
REMARK 465 ALA D -20
REMARK 465 ASN D -19
REMARK 465 LEU D -18
REMARK 465 LEU D -17
REMARK 465 ALA D -16
REMARK 465 GLU D -15
REMARK 465 ALA D -14
REMARK 465 LYS D -13
REMARK 465 LYS D -12
REMARK 465 LEU D -11
REMARK 465 ASN D -10
REMARK 465 ASP D -9
REMARK 465 ALA D -8
REMARK 465 GLN D -7
REMARK 465 PRO D -6
REMARK 465 LYS D -5
REMARK 465 GLY D -4
REMARK 465 THR D -3
REMARK 465 GLU D -2
REMARK 465 ASN D -1
REMARK 465 LEU D 0
REMARK 465 TYR D 1
REMARK 465 PHE D 2
REMARK 465 GLN D 3
REMARK 465 SER D 4
REMARK 465 MET D 5
REMARK 465 GLY D 6
REMARK 465 PRO D 7
REMARK 465 GLU D 8
REMARK 465 ASP D 9
REMARK 465 THR D 58
REMARK 465 ALA D 59
REMARK 465 GLU D 60
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 61 CG CD NE CZ NH1 NH2
REMARK 470 SER A 63 OG
REMARK 470 LYS A 128 CG CD CE NZ
REMARK 470 ASP A 204 CG OD1 OD2
REMARK 470 ARG A 236 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 256 CG CD OE1 OE2
REMARK 470 ASP A 258 CG OD1 OD2
REMARK 470 ASP A 259 CG OD1 OD2
REMARK 470 SER A 269 OG
REMARK 470 GLU A 292 CD OE1 OE2
REMARK 470 ARG A 293 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 10 CG CD OE1 OE2
REMARK 470 LEU B 11 CG CD1 CD2
REMARK 470 VAL B 34 CG1 CG2
REMARK 470 GLN B 66 CG CD OE1 NE2
REMARK 470 LEU B 67 CG CD1 CD2
REMARK 470 ARG B 71 CG CD NE CZ NH1 NH2
REMARK 470 MET B 103 CG SD CE
REMARK 470 GLU B 179 CG CD OE1 OE2
REMARK 470 HIS B 235 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 236 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 237 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 238 CG CD OE1 NE2
REMARK 470 ILE B 239 CG1 CG2 CD1
REMARK 470 LEU B 240 CG CD1 CD2
REMARK 470 ARG B 243 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 249 CG CD OE1 NE2
REMARK 470 SER B 254 OG
REMARK 470 SER B 269 OG
REMARK 470 LYS C 18 CE NZ
REMARK 470 ARG C 61 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 65 CG CD OE1 OE2
REMARK 470 LYS C 200 CD CE NZ
REMARK 470 ARG C 236 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 243 NE CZ NH1 NH2
REMARK 470 GLN C 251 CG CD OE1 NE2
REMARK 470 GLU C 256 CG CD OE1 OE2
REMARK 470 ASP C 258 CG OD1 OD2
REMARK 470 SER C 269 OG
REMARK 470 GLU C 277 CD OE1 OE2
REMARK 470 ARG C 293 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 10 CG CD OE1 OE2
REMARK 470 VAL D 57 CG1 CG2
REMARK 470 ARG D 61 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 62 CG CD1 CD2
REMARK 470 GLU D 65 CG CD OE1 OE2
REMARK 470 GLN D 66 CG CD OE1 NE2
REMARK 470 SER D 100 OG
REMARK 470 LYS D 122 CG CD CE NZ
REMARK 470 ARG D 236 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 238 CG CD OE1 NE2
REMARK 470 LEU D 240 CG CD1 CD2
REMARK 470 ARG D 243 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 247 CG CD OE1 OE2
REMARK 470 GLN D 249 CD OE1 NE2
REMARK 470 SER D 254 OG
REMARK 470 ASP D 258 CG OD1 OD2
REMARK 470 LYS D 265 CG CD CE NZ
REMARK 470 SER D 269 OG
REMARK 470 GLU D 292 CG CD OE1 OE2
REMARK 470 ARG D 293 CG CD NE CZ NH1 NH2
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 O PRO A 208 O ALA D 45 3445 2.11
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 LYS A 27 -140.21 -117.67
REMARK 500 VAL A 123 -58.44 75.12
REMARK 500 ASP A 153 44.98 -164.47
REMARK 500 ASP A 171 70.88 54.75
REMARK 500 MET A 203 -19.62 -151.54
REMARK 500 LYS B 27 -145.15 -123.81
REMARK 500 VAL B 57 54.54 -96.24
REMARK 500 THR B 58 1.91 -163.59
REMARK 500 VAL B 123 -60.32 75.52
REMARK 500 ASP B 153 41.00 -150.42
REMARK 500 ASP B 171 72.46 48.31
REMARK 500 MET B 203 -74.71 -90.05
REMARK 500 PRO B 289 -8.34 -57.36
REMARK 500 LYS C 27 -139.62 -119.23
REMARK 500 VAL C 123 -59.15 74.37
REMARK 500 ASP C 153 41.54 -158.82
REMARK 500 SER C 170 -166.61 -128.01
REMARK 500 ASP C 171 75.18 49.58
REMARK 500 LYS D 27 -150.10 -117.63
REMARK 500 VAL D 123 -58.90 74.87
REMARK 500 ASP D 153 41.93 -149.06
REMARK 500 ASP D 171 74.24 54.45
REMARK 500 ASP D 259 45.46 -95.80
REMARK 500 LEU D 272 55.08 -93.24
REMARK 500 PRO D 289 -7.01 -58.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B49 A 1294
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B49 B 1294
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B49 C 1294
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE B49 D 1294
DBREF 2Y7J A 6 293 UNP P15735 PHKG2_HUMAN 6 293
DBREF 2Y7J B 6 293 UNP P15735 PHKG2_HUMAN 6 293
DBREF 2Y7J C 6 293 UNP P15735 PHKG2_HUMAN 6 293
DBREF 2Y7J D 6 293 UNP P15735 PHKG2_HUMAN 6 293
SEQADV 2Y7J MET A -71 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS A -70 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS A -69 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS A -68 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS A -67 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS A -66 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS A -65 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER A -64 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER A -63 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLY A -62 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J VAL A -61 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP A -60 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN A -59 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS A -58 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PHE A -57 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN A -56 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS A -55 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU A -54 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG A -53 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG A -52 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG A -51 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA A -50 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG A -49 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG A -48 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU A -47 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ILE A -46 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG A -45 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS A -44 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU A -43 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PRO A -42 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN A -41 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU A -40 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN A -39 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG A -38 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU A -37 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN A -36 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG A -35 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG A -34 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA A -33 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PHE A -32 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ILE A -31 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG A -30 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER A -29 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU A -28 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG A -27 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP A -26 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP A -25 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PRO A -24 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER A -23 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN A -22 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER A -21 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA A -20 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN A -19 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU A -18 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU A -17 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA A -16 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU A -15 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA A -14 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS A -13 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS A -12 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU A -11 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN A -10 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP A -9 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA A -8 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN A -7 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PRO A -6 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS A -5 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLY A -4 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J THR A -3 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU A -2 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN A -1 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU A 0 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J TYR A 1 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PHE A 2 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN A 3 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER A 4 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J MET A 5 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J MET B -71 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS B -70 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS B -69 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS B -68 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS B -67 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS B -66 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS B -65 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER B -64 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER B -63 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLY B -62 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J VAL B -61 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP B -60 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN B -59 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS B -58 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PHE B -57 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN B -56 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS B -55 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU B -54 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG B -53 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG B -52 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG B -51 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA B -50 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG B -49 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG B -48 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU B -47 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ILE B -46 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG B -45 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS B -44 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU B -43 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PRO B -42 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN B -41 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU B -40 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN B -39 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG B -38 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU B -37 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN B -36 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG B -35 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG B -34 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA B -33 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PHE B -32 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ILE B -31 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG B -30 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER B -29 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU B -28 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG B -27 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP B -26 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP B -25 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PRO B -24 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER B -23 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN B -22 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER B -21 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA B -20 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN B -19 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU B -18 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU B -17 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA B -16 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU B -15 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA B -14 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS B -13 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS B -12 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU B -11 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN B -10 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP B -9 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA B -8 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN B -7 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PRO B -6 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS B -5 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLY B -4 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J THR B -3 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU B -2 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN B -1 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU B 0 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J TYR B 1 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PHE B 2 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN B 3 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER B 4 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J MET B 5 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J MET C -71 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS C -70 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS C -69 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS C -68 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS C -67 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS C -66 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS C -65 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER C -64 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER C -63 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLY C -62 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J VAL C -61 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP C -60 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN C -59 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS C -58 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PHE C -57 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN C -56 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS C -55 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU C -54 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG C -53 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG C -52 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG C -51 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA C -50 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG C -49 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG C -48 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU C -47 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ILE C -46 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG C -45 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS C -44 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU C -43 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PRO C -42 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN C -41 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU C -40 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN C -39 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG C -38 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU C -37 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN C -36 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG C -35 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG C -34 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA C -33 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PHE C -32 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ILE C -31 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG C -30 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER C -29 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU C -28 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG C -27 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP C -26 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP C -25 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PRO C -24 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER C -23 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN C -22 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER C -21 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA C -20 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN C -19 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU C -18 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU C -17 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA C -16 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU C -15 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA C -14 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS C -13 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS C -12 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU C -11 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN C -10 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP C -9 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA C -8 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN C -7 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PRO C -6 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS C -5 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLY C -4 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J THR C -3 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU C -2 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN C -1 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU C 0 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J TYR C 1 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PHE C 2 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN C 3 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER C 4 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J MET C 5 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J MET D -71 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS D -70 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS D -69 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS D -68 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS D -67 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS D -66 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS D -65 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER D -64 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER D -63 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLY D -62 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J VAL D -61 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP D -60 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN D -59 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS D -58 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PHE D -57 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN D -56 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS D -55 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU D -54 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG D -53 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG D -52 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG D -51 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA D -50 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG D -49 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG D -48 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU D -47 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ILE D -46 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG D -45 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J HIS D -44 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU D -43 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PRO D -42 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN D -41 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU D -40 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN D -39 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG D -38 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU D -37 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN D -36 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG D -35 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG D -34 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA D -33 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PHE D -32 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ILE D -31 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG D -30 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER D -29 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU D -28 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ARG D -27 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP D -26 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP D -25 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PRO D -24 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER D -23 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN D -22 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER D -21 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA D -20 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN D -19 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU D -18 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU D -17 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA D -16 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU D -15 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA D -14 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS D -13 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS D -12 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU D -11 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN D -10 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASP D -9 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ALA D -8 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN D -7 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PRO D -6 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LYS D -5 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLY D -4 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J THR D -3 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLU D -2 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J ASN D -1 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J LEU D 0 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J TYR D 1 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J PHE D 2 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J GLN D 3 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J SER D 4 UNP P15735 EXPRESSION TAG
SEQADV 2Y7J MET D 5 UNP P15735 EXPRESSION TAG
SEQRES 1 A 365 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP ASN
SEQRES 2 A 365 LYS PHE ASN LYS GLU ARG ARG ARG ALA ARG ARG GLU ILE
SEQRES 3 A 365 ARG HIS LEU PRO ASN LEU ASN ARG GLU GLN ARG ARG ALA
SEQRES 4 A 365 PHE ILE ARG SER LEU ARG ASP ASP PRO SER GLN SER ALA
SEQRES 5 A 365 ASN LEU LEU ALA GLU ALA LYS LYS LEU ASN ASP ALA GLN
SEQRES 6 A 365 PRO LYS GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY
SEQRES 7 A 365 PRO GLU ASP GLU LEU PRO ASP TRP ALA ALA ALA LYS GLU
SEQRES 8 A 365 PHE TYR GLN LYS TYR ASP PRO LYS ASP VAL ILE GLY ARG
SEQRES 9 A 365 GLY VAL SER SER VAL VAL ARG ARG CYS VAL HIS ARG ALA
SEQRES 10 A 365 THR GLY HIS GLU PHE ALA VAL LYS ILE MET GLU VAL THR
SEQRES 11 A 365 ALA GLU ARG LEU SER PRO GLU GLN LEU GLU GLU VAL ARG
SEQRES 12 A 365 GLU ALA THR ARG ARG GLU THR HIS ILE LEU ARG GLN VAL
SEQRES 13 A 365 ALA GLY HIS PRO HIS ILE ILE THR LEU ILE ASP SER TYR
SEQRES 14 A 365 GLU SER SER SER PHE MET PHE LEU VAL PHE ASP LEU MET
SEQRES 15 A 365 ARG LYS GLY GLU LEU PHE ASP TYR LEU THR GLU LYS VAL
SEQRES 16 A 365 ALA LEU SER GLU LYS GLU THR ARG SER ILE MET ARG SER
SEQRES 17 A 365 LEU LEU GLU ALA VAL SER PHE LEU HIS ALA ASN ASN ILE
SEQRES 18 A 365 VAL HIS ARG ASP LEU LYS PRO GLU ASN ILE LEU LEU ASP
SEQRES 19 A 365 ASP ASN MET GLN ILE ARG LEU SER ASP PHE GLY PHE SER
SEQRES 20 A 365 CYS HIS LEU GLU PRO GLY GLU LYS LEU ARG GLU LEU CYS
SEQRES 21 A 365 GLY THR PRO GLY TYR LEU ALA PRO GLU ILE LEU LYS CYS
SEQRES 22 A 365 SER MET ASP GLU THR HIS PRO GLY TYR GLY LYS GLU VAL
SEQRES 23 A 365 ASP LEU TRP ALA CYS GLY VAL ILE LEU PHE THR LEU LEU
SEQRES 24 A 365 ALA GLY SER PRO PRO PHE TRP HIS ARG ARG GLN ILE LEU
SEQRES 25 A 365 MET LEU ARG MET ILE MET GLU GLY GLN TYR GLN PHE SER
SEQRES 26 A 365 SER PRO GLU TRP ASP ASP ARG SER SER THR VAL LYS ASP
SEQRES 27 A 365 LEU ILE SER ARG LEU LEU GLN VAL ASP PRO GLU ALA ARG
SEQRES 28 A 365 LEU THR ALA GLU GLN ALA LEU GLN HIS PRO PHE PHE GLU
SEQRES 29 A 365 ARG
SEQRES 1 B 365 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP ASN
SEQRES 2 B 365 LYS PHE ASN LYS GLU ARG ARG ARG ALA ARG ARG GLU ILE
SEQRES 3 B 365 ARG HIS LEU PRO ASN LEU ASN ARG GLU GLN ARG ARG ALA
SEQRES 4 B 365 PHE ILE ARG SER LEU ARG ASP ASP PRO SER GLN SER ALA
SEQRES 5 B 365 ASN LEU LEU ALA GLU ALA LYS LYS LEU ASN ASP ALA GLN
SEQRES 6 B 365 PRO LYS GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY
SEQRES 7 B 365 PRO GLU ASP GLU LEU PRO ASP TRP ALA ALA ALA LYS GLU
SEQRES 8 B 365 PHE TYR GLN LYS TYR ASP PRO LYS ASP VAL ILE GLY ARG
SEQRES 9 B 365 GLY VAL SER SER VAL VAL ARG ARG CYS VAL HIS ARG ALA
SEQRES 10 B 365 THR GLY HIS GLU PHE ALA VAL LYS ILE MET GLU VAL THR
SEQRES 11 B 365 ALA GLU ARG LEU SER PRO GLU GLN LEU GLU GLU VAL ARG
SEQRES 12 B 365 GLU ALA THR ARG ARG GLU THR HIS ILE LEU ARG GLN VAL
SEQRES 13 B 365 ALA GLY HIS PRO HIS ILE ILE THR LEU ILE ASP SER TYR
SEQRES 14 B 365 GLU SER SER SER PHE MET PHE LEU VAL PHE ASP LEU MET
SEQRES 15 B 365 ARG LYS GLY GLU LEU PHE ASP TYR LEU THR GLU LYS VAL
SEQRES 16 B 365 ALA LEU SER GLU LYS GLU THR ARG SER ILE MET ARG SER
SEQRES 17 B 365 LEU LEU GLU ALA VAL SER PHE LEU HIS ALA ASN ASN ILE
SEQRES 18 B 365 VAL HIS ARG ASP LEU LYS PRO GLU ASN ILE LEU LEU ASP
SEQRES 19 B 365 ASP ASN MET GLN ILE ARG LEU SER ASP PHE GLY PHE SER
SEQRES 20 B 365 CYS HIS LEU GLU PRO GLY GLU LYS LEU ARG GLU LEU CYS
SEQRES 21 B 365 GLY THR PRO GLY TYR LEU ALA PRO GLU ILE LEU LYS CYS
SEQRES 22 B 365 SER MET ASP GLU THR HIS PRO GLY TYR GLY LYS GLU VAL
SEQRES 23 B 365 ASP LEU TRP ALA CYS GLY VAL ILE LEU PHE THR LEU LEU
SEQRES 24 B 365 ALA GLY SER PRO PRO PHE TRP HIS ARG ARG GLN ILE LEU
SEQRES 25 B 365 MET LEU ARG MET ILE MET GLU GLY GLN TYR GLN PHE SER
SEQRES 26 B 365 SER PRO GLU TRP ASP ASP ARG SER SER THR VAL LYS ASP
SEQRES 27 B 365 LEU ILE SER ARG LEU LEU GLN VAL ASP PRO GLU ALA ARG
SEQRES 28 B 365 LEU THR ALA GLU GLN ALA LEU GLN HIS PRO PHE PHE GLU
SEQRES 29 B 365 ARG
SEQRES 1 C 365 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP ASN
SEQRES 2 C 365 LYS PHE ASN LYS GLU ARG ARG ARG ALA ARG ARG GLU ILE
SEQRES 3 C 365 ARG HIS LEU PRO ASN LEU ASN ARG GLU GLN ARG ARG ALA
SEQRES 4 C 365 PHE ILE ARG SER LEU ARG ASP ASP PRO SER GLN SER ALA
SEQRES 5 C 365 ASN LEU LEU ALA GLU ALA LYS LYS LEU ASN ASP ALA GLN
SEQRES 6 C 365 PRO LYS GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY
SEQRES 7 C 365 PRO GLU ASP GLU LEU PRO ASP TRP ALA ALA ALA LYS GLU
SEQRES 8 C 365 PHE TYR GLN LYS TYR ASP PRO LYS ASP VAL ILE GLY ARG
SEQRES 9 C 365 GLY VAL SER SER VAL VAL ARG ARG CYS VAL HIS ARG ALA
SEQRES 10 C 365 THR GLY HIS GLU PHE ALA VAL LYS ILE MET GLU VAL THR
SEQRES 11 C 365 ALA GLU ARG LEU SER PRO GLU GLN LEU GLU GLU VAL ARG
SEQRES 12 C 365 GLU ALA THR ARG ARG GLU THR HIS ILE LEU ARG GLN VAL
SEQRES 13 C 365 ALA GLY HIS PRO HIS ILE ILE THR LEU ILE ASP SER TYR
SEQRES 14 C 365 GLU SER SER SER PHE MET PHE LEU VAL PHE ASP LEU MET
SEQRES 15 C 365 ARG LYS GLY GLU LEU PHE ASP TYR LEU THR GLU LYS VAL
SEQRES 16 C 365 ALA LEU SER GLU LYS GLU THR ARG SER ILE MET ARG SER
SEQRES 17 C 365 LEU LEU GLU ALA VAL SER PHE LEU HIS ALA ASN ASN ILE
SEQRES 18 C 365 VAL HIS ARG ASP LEU LYS PRO GLU ASN ILE LEU LEU ASP
SEQRES 19 C 365 ASP ASN MET GLN ILE ARG LEU SER ASP PHE GLY PHE SER
SEQRES 20 C 365 CYS HIS LEU GLU PRO GLY GLU LYS LEU ARG GLU LEU CYS
SEQRES 21 C 365 GLY THR PRO GLY TYR LEU ALA PRO GLU ILE LEU LYS CYS
SEQRES 22 C 365 SER MET ASP GLU THR HIS PRO GLY TYR GLY LYS GLU VAL
SEQRES 23 C 365 ASP LEU TRP ALA CYS GLY VAL ILE LEU PHE THR LEU LEU
SEQRES 24 C 365 ALA GLY SER PRO PRO PHE TRP HIS ARG ARG GLN ILE LEU
SEQRES 25 C 365 MET LEU ARG MET ILE MET GLU GLY GLN TYR GLN PHE SER
SEQRES 26 C 365 SER PRO GLU TRP ASP ASP ARG SER SER THR VAL LYS ASP
SEQRES 27 C 365 LEU ILE SER ARG LEU LEU GLN VAL ASP PRO GLU ALA ARG
SEQRES 28 C 365 LEU THR ALA GLU GLN ALA LEU GLN HIS PRO PHE PHE GLU
SEQRES 29 C 365 ARG
SEQRES 1 D 365 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP ASN
SEQRES 2 D 365 LYS PHE ASN LYS GLU ARG ARG ARG ALA ARG ARG GLU ILE
SEQRES 3 D 365 ARG HIS LEU PRO ASN LEU ASN ARG GLU GLN ARG ARG ALA
SEQRES 4 D 365 PHE ILE ARG SER LEU ARG ASP ASP PRO SER GLN SER ALA
SEQRES 5 D 365 ASN LEU LEU ALA GLU ALA LYS LYS LEU ASN ASP ALA GLN
SEQRES 6 D 365 PRO LYS GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY
SEQRES 7 D 365 PRO GLU ASP GLU LEU PRO ASP TRP ALA ALA ALA LYS GLU
SEQRES 8 D 365 PHE TYR GLN LYS TYR ASP PRO LYS ASP VAL ILE GLY ARG
SEQRES 9 D 365 GLY VAL SER SER VAL VAL ARG ARG CYS VAL HIS ARG ALA
SEQRES 10 D 365 THR GLY HIS GLU PHE ALA VAL LYS ILE MET GLU VAL THR
SEQRES 11 D 365 ALA GLU ARG LEU SER PRO GLU GLN LEU GLU GLU VAL ARG
SEQRES 12 D 365 GLU ALA THR ARG ARG GLU THR HIS ILE LEU ARG GLN VAL
SEQRES 13 D 365 ALA GLY HIS PRO HIS ILE ILE THR LEU ILE ASP SER TYR
SEQRES 14 D 365 GLU SER SER SER PHE MET PHE LEU VAL PHE ASP LEU MET
SEQRES 15 D 365 ARG LYS GLY GLU LEU PHE ASP TYR LEU THR GLU LYS VAL
SEQRES 16 D 365 ALA LEU SER GLU LYS GLU THR ARG SER ILE MET ARG SER
SEQRES 17 D 365 LEU LEU GLU ALA VAL SER PHE LEU HIS ALA ASN ASN ILE
SEQRES 18 D 365 VAL HIS ARG ASP LEU LYS PRO GLU ASN ILE LEU LEU ASP
SEQRES 19 D 365 ASP ASN MET GLN ILE ARG LEU SER ASP PHE GLY PHE SER
SEQRES 20 D 365 CYS HIS LEU GLU PRO GLY GLU LYS LEU ARG GLU LEU CYS
SEQRES 21 D 365 GLY THR PRO GLY TYR LEU ALA PRO GLU ILE LEU LYS CYS
SEQRES 22 D 365 SER MET ASP GLU THR HIS PRO GLY TYR GLY LYS GLU VAL
SEQRES 23 D 365 ASP LEU TRP ALA CYS GLY VAL ILE LEU PHE THR LEU LEU
SEQRES 24 D 365 ALA GLY SER PRO PRO PHE TRP HIS ARG ARG GLN ILE LEU
SEQRES 25 D 365 MET LEU ARG MET ILE MET GLU GLY GLN TYR GLN PHE SER
SEQRES 26 D 365 SER PRO GLU TRP ASP ASP ARG SER SER THR VAL LYS ASP
SEQRES 27 D 365 LEU ILE SER ARG LEU LEU GLN VAL ASP PRO GLU ALA ARG
SEQRES 28 D 365 LEU THR ALA GLU GLN ALA LEU GLN HIS PRO PHE PHE GLU
SEQRES 29 D 365 ARG
HET B49 A1294 29
HET B49 B1294 29
HET B49 C1294 29
HET B49 D1294 29
HETNAM B49 N-[2-(DIETHYLAMINO)ETHYL]-5-[(Z)-(5-FLUORO-2-OXO-1,2-
HETNAM 2 B49 DIHYDRO-3H-INDOL-3-YLIDENE)METHYL]-2,4-DIMETHYL-1H-
HETNAM 3 B49 PYRROLE-3-CARBOXAMIDE
HETSYN B49 SUNITINIB
FORMUL 5 B49 4(C22 H27 F N4 O2)
FORMUL 9 HOH *283(H2 O)
HELIX 1 1 PRO A 12 LYS A 23 1 12
HELIX 2 2 SER A 63 ALA A 85 1 23
HELIX 3 3 GLU A 114 VAL A 123 1 10
HELIX 4 4 SER A 126 ASN A 147 1 22
HELIX 5 5 LYS A 155 GLU A 157 5 3
HELIX 6 6 THR A 190 LEU A 194 5 5
HELIX 7 7 ALA A 195 SER A 202 1 8
HELIX 8 8 GLU A 213 GLY A 229 1 17
HELIX 9 9 ARG A 237 GLY A 248 1 12
HELIX 10 10 SER A 253 ASP A 258 1 6
HELIX 11 11 SER A 261 LEU A 272 1 12
HELIX 12 12 THR A 281 HIS A 288 1 8
HELIX 13 13 PRO A 289 GLU A 292 5 4
HELIX 14 14 PRO B 12 LYS B 23 1 12
HELIX 15 15 SER B 63 ALA B 85 1 23
HELIX 16 16 LEU B 115 VAL B 123 1 9
HELIX 17 17 SER B 126 ASN B 147 1 22
HELIX 18 18 LYS B 155 GLU B 157 5 3
HELIX 19 19 THR B 190 LEU B 194 5 5
HELIX 20 20 ALA B 195 ASP B 204 1 10
HELIX 21 21 LYS B 212 GLY B 229 1 18
HELIX 22 22 ARG B 237 GLY B 248 1 12
HELIX 23 23 SER B 253 ASP B 258 1 6
HELIX 24 24 SER B 261 LEU B 272 1 12
HELIX 25 25 THR B 281 GLN B 287 1 7
HELIX 26 26 HIS B 288 GLU B 292 5 5
HELIX 27 27 PRO C 12 LYS C 23 1 12
HELIX 28 28 SER C 63 ALA C 85 1 23
HELIX 29 29 LEU C 115 VAL C 123 1 9
HELIX 30 30 SER C 126 ASN C 147 1 22
HELIX 31 31 LYS C 155 GLU C 157 5 3
HELIX 32 32 THR C 190 LEU C 194 5 5
HELIX 33 33 ALA C 195 ASP C 204 1 10
HELIX 34 34 LYS C 212 GLY C 229 1 18
HELIX 35 35 ARG C 237 GLU C 247 1 11
HELIX 36 36 SER C 253 ASP C 258 1 6
HELIX 37 37 SER C 261 LEU C 272 1 12
HELIX 38 38 THR C 281 GLN C 287 1 7
HELIX 39 39 HIS C 288 GLU C 292 5 5
HELIX 40 40 PRO D 12 LYS D 23 1 12
HELIX 41 41 SER D 63 ALA D 85 1 23
HELIX 42 42 LEU D 115 VAL D 123 1 9
HELIX 43 43 SER D 126 ASN D 147 1 22
HELIX 44 44 LYS D 155 GLU D 157 5 3
HELIX 45 45 THR D 190 LEU D 194 5 5
HELIX 46 46 ALA D 195 ASP D 204 1 10
HELIX 47 47 GLU D 213 GLY D 229 1 17
HELIX 48 48 ARG D 237 GLY D 248 1 12
HELIX 49 49 SER D 253 ASP D 258 1 6
HELIX 50 50 SER D 261 LEU D 272 1 12
HELIX 51 51 THR D 281 GLN D 287 1 7
SHEET 1 AA 5 TYR A 24 ARG A 32 0
SHEET 2 AA 5 SER A 36 HIS A 43 -1 O VAL A 38 N ILE A 30
SHEET 3 AA 5 GLU A 49 GLU A 56 -1 O PHE A 50 N CYS A 41
SHEET 4 AA 5 PHE A 102 PHE A 107 -1 O MET A 103 N MET A 55
SHEET 5 AA 5 LEU A 93 GLU A 98 -1 N ILE A 94 O VAL A 106
SHEET 1 AB 2 ILE A 149 VAL A 150 0
SHEET 2 AB 2 CYS A 176 HIS A 177 -1 O CYS A 176 N VAL A 150
SHEET 1 AC 2 ILE A 159 LEU A 161 0
SHEET 2 AC 2 ILE A 167 LEU A 169 -1 O ARG A 168 N LEU A 160
SHEET 1 BA 5 TYR B 24 ARG B 32 0
SHEET 2 BA 5 SER B 36 HIS B 43 -1 O VAL B 38 N ILE B 30
SHEET 3 BA 5 GLU B 49 GLU B 56 -1 O PHE B 50 N CYS B 41
SHEET 4 BA 5 PHE B 102 PHE B 107 -1 O MET B 103 N MET B 55
SHEET 5 BA 5 LEU B 93 GLU B 98 -1 N ILE B 94 O VAL B 106
SHEET 1 BB 3 GLY B 113 GLU B 114 0
SHEET 2 BB 3 ILE B 159 LEU B 161 -1 N LEU B 161 O GLY B 113
SHEET 3 BB 3 ILE B 167 LEU B 169 -1 O ARG B 168 N LEU B 160
SHEET 1 BC 2 ILE B 149 VAL B 150 0
SHEET 2 BC 2 CYS B 176 HIS B 177 -1 O CYS B 176 N VAL B 150
SHEET 1 CA 5 TYR C 24 ARG C 32 0
SHEET 2 CA 5 SER C 36 HIS C 43 -1 O VAL C 38 N ILE C 30
SHEET 3 CA 5 GLU C 49 GLU C 56 -1 O PHE C 50 N CYS C 41
SHEET 4 CA 5 PHE C 102 PHE C 107 -1 O MET C 103 N MET C 55
SHEET 5 CA 5 LEU C 93 GLU C 98 -1 N ILE C 94 O VAL C 106
SHEET 1 CB 3 GLY C 113 GLU C 114 0
SHEET 2 CB 3 ILE C 159 LEU C 161 -1 N LEU C 161 O GLY C 113
SHEET 3 CB 3 ILE C 167 LEU C 169 -1 O ARG C 168 N LEU C 160
SHEET 1 CC 2 ILE C 149 VAL C 150 0
SHEET 2 CC 2 CYS C 176 HIS C 177 -1 O CYS C 176 N VAL C 150
SHEET 1 DA 5 TYR D 24 ARG D 32 0
SHEET 2 DA 5 SER D 36 HIS D 43 -1 O VAL D 38 N ILE D 30
SHEET 3 DA 5 GLU D 49 GLU D 56 -1 O PHE D 50 N CYS D 41
SHEET 4 DA 5 PHE D 102 ASP D 108 -1 O MET D 103 N MET D 55
SHEET 5 DA 5 LEU D 93 GLU D 98 -1 N ILE D 94 O VAL D 106
SHEET 1 DB 3 GLY D 113 GLU D 114 0
SHEET 2 DB 3 ILE D 159 LEU D 161 -1 N LEU D 161 O GLY D 113
SHEET 3 DB 3 ILE D 167 LEU D 169 -1 O ARG D 168 N LEU D 160
SHEET 1 DC 2 ILE D 149 VAL D 150 0
SHEET 2 DC 2 CYS D 176 HIS D 177 -1 O CYS D 176 N VAL D 150
SITE 1 AC1 13 VAL A 29 ILE A 30 GLY A 31 ARG A 32
SITE 2 AC1 13 ALA A 51 PHE A 107 ASP A 108 MET A 110
SITE 3 AC1 13 ARG A 111 GLY A 113 LEU A 160 ASP A 171
SITE 4 AC1 13 HOH A2063
SITE 1 AC2 11 VAL B 29 ILE B 30 ALA B 51 ILE B 91
SITE 2 AC2 11 PHE B 107 ASP B 108 MET B 110 ARG B 111
SITE 3 AC2 11 GLY B 113 LEU B 160 HOH B2036
SITE 1 AC3 10 ILE C 30 ALA C 51 ILE C 91 PHE C 107
SITE 2 AC3 10 ASP C 108 MET C 110 ARG C 111 GLY C 113
SITE 3 AC3 10 ASP C 117 LEU C 160
SITE 1 AC4 10 ILE D 30 ALA D 51 PHE D 107 ASP D 108
SITE 2 AC4 10 LEU D 109 MET D 110 ARG D 111 GLY D 113
SITE 3 AC4 10 LEU D 160 HOH D2028
CRYST1 87.790 91.420 164.480 90.00 90.00 90.00 P 21 21 21 16
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 0.011391 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010939 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006080 0.00000
MTRIX1 1 -0.334400 -0.896600 0.290400 9.41390 1
MTRIX2 1 -0.817800 0.122900 -0.562200 5.16780 1
MTRIX3 1 0.468400 -0.425500 -0.774300 12.33360 1
(ATOM LINES ARE NOT SHOWN.)
END