HEADER UNKNOWN FUNCTION 23-AUG-12 4GQO
TITLE 2.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF UNCHARACTERIZED PROTEIN
TITLE 2 LMO0859 FROM LISTERIA MONOCYTOGENES EGD-E
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LMO0859 PROTEIN;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 31-439;
COMPND 5 SYNONYM: UNCHARACTERIZED PROTEIN LMO0859;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LISTERIA MONOCYTOGENES;
SOURCE 3 ORGANISM_TAXID: 169963;
SOURCE 4 STRAIN: ATCC BAA-679 / EGD-E;
SOURCE 5 GENE: LMO0859;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21/MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS VIRULENCE, PATHOGENESIS, VACCINE CANDIDATE, CENTER FOR STRUCTURAL
KEYWDS 2 GENOMICS OF INFECTIOUS DISEASES, CSGID, NIAID, NATIONAL INSTITUTE OF
KEYWDS 3 ALLERGY AND INFECTIOUS DISEASES, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.S.HALAVATY,E.V.FILIPPOVA,G.MINASOV,I.DUBROVSKA,J.WINSOR,
AUTHOR 2 L.SHUVALOVA,S.N.PETERSON,W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS
AUTHOR 3 OF INFECTIOUS DISEASES (CSGID)
REVDAT 2 15-NOV-17 4GQO 1 REMARK
REVDAT 1 19-SEP-12 4GQO 0
JRNL AUTH A.S.HALAVATY,E.V.FILIPPOVA,G.MINASOV,I.DUBROVSKA,J.WINSOR,
JRNL AUTH 2 L.SHUVALOVA,S.N.PETERSON,W.F.ANDERSON,
JRNL AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 4 (CSGID)
JRNL TITL 2.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF UNCHARACTERIZED
JRNL TITL 2 PROTEIN LMO0859 FROM LISTERIA MONOCYTOGENES EGD-E
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 67299
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) : 0.167
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3581
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4790
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.37
REMARK 3 BIN R VALUE (WORKING SET) : 0.1910
REMARK 3 BIN FREE R VALUE SET COUNT : 247
REMARK 3 BIN FREE R VALUE : 0.2540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9624
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 585
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.48000
REMARK 3 B22 (A**2) : 1.09000
REMARK 3 B33 (A**2) : -1.56000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.231
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.180
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.118
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.798
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10304 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 6918 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14058 ; 1.554 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17067 ; 0.895 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1298 ; 1.794 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 481 ;28.876 ;26.341
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1784 ; 8.335 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;13.132 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1498 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11669 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1937 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 6367 ; 0.908 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2482 ; 0.279 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10357 ; 1.643 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3937 ; 3.089 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3701 ; 4.819 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 35 A 84
REMARK 3 ORIGIN FOR THE GROUP (A): -6.0878 -13.1888 33.7739
REMARK 3 T TENSOR
REMARK 3 T11: 0.0762 T22: 0.1087
REMARK 3 T33: 0.1860 T12: -0.0458
REMARK 3 T13: 0.0200 T23: -0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 2.4188 L22: 3.5996
REMARK 3 L33: 2.9146 L12: -0.2779
REMARK 3 L13: -0.1435 L23: 0.2879
REMARK 3 S TENSOR
REMARK 3 S11: 0.0264 S12: -0.0740 S13: 0.1863
REMARK 3 S21: -0.0591 S22: 0.0913 S23: -0.2794
REMARK 3 S31: -0.1112 S32: 0.1510 S33: -0.1176
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 85 A 150
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0679 -11.2036 38.3112
REMARK 3 T TENSOR
REMARK 3 T11: 0.1028 T22: 0.0943
REMARK 3 T33: 0.1219 T12: 0.0214
REMARK 3 T13: -0.0222 T23: 0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 2.0099 L22: 2.7891
REMARK 3 L33: 1.7365 L12: 0.0665
REMARK 3 L13: -0.7099 L23: 0.4476
REMARK 3 S TENSOR
REMARK 3 S11: 0.1266 S12: 0.0780 S13: 0.1246
REMARK 3 S21: -0.1000 S22: -0.0909 S23: 0.2033
REMARK 3 S31: -0.3730 S32: -0.2390 S33: -0.0357
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 151 A 245
REMARK 3 ORIGIN FOR THE GROUP (A): -22.6112 -25.7190 64.8323
REMARK 3 T TENSOR
REMARK 3 T11: 0.0573 T22: 0.1028
REMARK 3 T33: 0.0916 T12: -0.0100
REMARK 3 T13: -0.0051 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.9576 L22: 1.7864
REMARK 3 L33: 3.0465 L12: -0.1582
REMARK 3 L13: 0.0053 L23: -0.5230
REMARK 3 S TENSOR
REMARK 3 S11: -0.0194 S12: -0.0882 S13: -0.0180
REMARK 3 S21: 0.2280 S22: 0.0969 S23: 0.0988
REMARK 3 S31: 0.0402 S32: -0.1107 S33: -0.0775
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 246 A 305
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0989 -29.9893 64.0041
REMARK 3 T TENSOR
REMARK 3 T11: 0.1369 T22: 0.1338
REMARK 3 T33: 0.1259 T12: 0.0030
REMARK 3 T13: -0.0338 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 2.2867 L22: 1.6449
REMARK 3 L33: 3.2999 L12: -0.5103
REMARK 3 L13: -0.9855 L23: 0.6553
REMARK 3 S TENSOR
REMARK 3 S11: 0.0078 S12: -0.0918 S13: 0.0261
REMARK 3 S21: 0.2077 S22: 0.0632 S23: -0.1593
REMARK 3 S31: 0.0731 S32: 0.3174 S33: -0.0711
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 306 A 404
REMARK 3 ORIGIN FOR THE GROUP (A): -18.2709 -23.4507 41.5341
REMARK 3 T TENSOR
REMARK 3 T11: 0.0074 T22: 0.0891
REMARK 3 T33: 0.1128 T12: -0.0056
REMARK 3 T13: -0.0156 T23: -0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.7621 L22: 1.2929
REMARK 3 L33: 1.9390 L12: 0.0237
REMARK 3 L13: -0.2777 L23: 0.2329
REMARK 3 S TENSOR
REMARK 3 S11: 0.0193 S12: 0.0269 S13: 0.0054
REMARK 3 S21: -0.0057 S22: -0.0289 S23: 0.0039
REMARK 3 S31: -0.0868 S32: -0.0762 S33: 0.0096
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 405 A 438
REMARK 3 ORIGIN FOR THE GROUP (A): -27.8215 -9.7602 69.5479
REMARK 3 T TENSOR
REMARK 3 T11: 0.3498 T22: 0.1336
REMARK 3 T33: 0.1430 T12: 0.0740
REMARK 3 T13: 0.0749 T23: -0.0583
REMARK 3 L TENSOR
REMARK 3 L11: 2.9977 L22: 4.4768
REMARK 3 L33: 7.9013 L12: -0.3757
REMARK 3 L13: 1.2939 L23: -2.6371
REMARK 3 S TENSOR
REMARK 3 S11: -0.0391 S12: -0.2038 S13: 0.2412
REMARK 3 S21: 0.6485 S22: 0.0348 S23: 0.2427
REMARK 3 S31: -1.0291 S32: -0.5307 S33: 0.0043
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 35 B 93
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1417 -51.9346 41.7017
REMARK 3 T TENSOR
REMARK 3 T11: 0.0691 T22: 0.1573
REMARK 3 T33: 0.2150 T12: 0.0587
REMARK 3 T13: -0.0456 T23: 0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 1.8456 L22: 4.1154
REMARK 3 L33: 3.0606 L12: 0.8352
REMARK 3 L13: 0.9334 L23: 1.0286
REMARK 3 S TENSOR
REMARK 3 S11: 0.0444 S12: -0.0804 S13: -0.1657
REMARK 3 S21: 0.0785 S22: 0.1493 S23: -0.2321
REMARK 3 S31: 0.2651 S32: 0.2774 S33: -0.1937
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 94 B 194
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5688 -39.8727 24.7462
REMARK 3 T TENSOR
REMARK 3 T11: 0.0332 T22: 0.0803
REMARK 3 T33: 0.1239 T12: -0.0248
REMARK 3 T13: -0.0061 T23: -0.0564
REMARK 3 L TENSOR
REMARK 3 L11: 0.8897 L22: 0.7424
REMARK 3 L33: 2.1209 L12: -0.1951
REMARK 3 L13: 0.3402 L23: -0.1845
REMARK 3 S TENSOR
REMARK 3 S11: 0.0270 S12: 0.0358 S13: -0.0867
REMARK 3 S21: -0.0913 S22: 0.0475 S23: 0.0528
REMARK 3 S31: -0.0022 S32: 0.0203 S33: -0.0746
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 195 B 252
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6052 -44.3553 12.8687
REMARK 3 T TENSOR
REMARK 3 T11: 0.1631 T22: 0.0614
REMARK 3 T33: 0.1530 T12: 0.0012
REMARK 3 T13: -0.0640 T23: -0.0728
REMARK 3 L TENSOR
REMARK 3 L11: 2.0306 L22: 2.8148
REMARK 3 L33: 5.8084 L12: 0.0079
REMARK 3 L13: 0.5447 L23: -1.5875
REMARK 3 S TENSOR
REMARK 3 S11: 0.1389 S12: 0.0358 S13: -0.1941
REMARK 3 S21: -0.3591 S22: 0.0411 S23: 0.1979
REMARK 3 S31: 0.4998 S32: 0.2208 S33: -0.1800
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 253 B 305
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0637 -31.4350 14.0259
REMARK 3 T TENSOR
REMARK 3 T11: 0.1857 T22: 0.2922
REMARK 3 T33: 0.1651 T12: -0.0912
REMARK 3 T13: 0.0225 T23: -0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 2.2461 L22: 1.4431
REMARK 3 L33: 4.0949 L12: -0.6684
REMARK 3 L13: -0.0380 L23: -0.5868
REMARK 3 S TENSOR
REMARK 3 S11: 0.0477 S12: 0.1891 S13: -0.1304
REMARK 3 S21: -0.1046 S22: -0.0857 S23: -0.3111
REMARK 3 S31: -0.1569 S32: 0.8611 S33: 0.0381
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 306 B 379
REMARK 3 ORIGIN FOR THE GROUP (A): 5.4525 -38.6158 38.2001
REMARK 3 T TENSOR
REMARK 3 T11: 0.0035 T22: 0.1115
REMARK 3 T33: 0.1012 T12: -0.0124
REMARK 3 T13: -0.0042 T23: -0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 1.2249 L22: 1.5094
REMARK 3 L33: 2.0858 L12: -0.5335
REMARK 3 L13: 0.5001 L23: 0.1399
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: -0.0861 S13: -0.0364
REMARK 3 S21: 0.0494 S22: 0.0232 S23: -0.0557
REMARK 3 S31: 0.0078 S32: -0.0119 S33: -0.0248
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 380 B 438
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3610 -48.8650 14.2163
REMARK 3 T TENSOR
REMARK 3 T11: 0.2803 T22: 0.0926
REMARK 3 T33: 0.1666 T12: 0.0333
REMARK 3 T13: -0.0838 T23: -0.0617
REMARK 3 L TENSOR
REMARK 3 L11: 0.8309 L22: 1.7608
REMARK 3 L33: 3.6768 L12: 0.0556
REMARK 3 L13: 0.6772 L23: -0.2671
REMARK 3 S TENSOR
REMARK 3 S11: 0.1184 S12: 0.0961 S13: -0.1664
REMARK 3 S21: -0.5281 S22: 0.0079 S23: 0.2142
REMARK 3 S31: 0.7273 S32: 0.0757 S33: -0.1263
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 35 C 84
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2498 14.9107 -11.8924
REMARK 3 T TENSOR
REMARK 3 T11: 0.1228 T22: 0.1318
REMARK 3 T33: 0.2419 T12: -0.0256
REMARK 3 T13: -0.1118 T23: -0.0459
REMARK 3 L TENSOR
REMARK 3 L11: 4.0146 L22: 6.2474
REMARK 3 L33: 2.4309 L12: -1.5586
REMARK 3 L13: -0.1017 L23: -1.4991
REMARK 3 S TENSOR
REMARK 3 S11: 0.2041 S12: 0.0998 S13: -0.4514
REMARK 3 S21: -0.4163 S22: -0.0363 S23: 0.6017
REMARK 3 S31: 0.1614 S32: -0.1135 S33: -0.1678
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 85 C 164
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4001 13.5013 -3.0213
REMARK 3 T TENSOR
REMARK 3 T11: 0.0798 T22: 0.0558
REMARK 3 T33: 0.1462 T12: 0.0137
REMARK 3 T13: -0.0055 T23: -0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 0.8120 L22: 1.5403
REMARK 3 L33: 1.2368 L12: -0.1241
REMARK 3 L13: 0.3182 L23: 0.1976
REMARK 3 S TENSOR
REMARK 3 S11: 0.0458 S12: 0.1705 S13: -0.1157
REMARK 3 S21: -0.1877 S22: -0.0054 S23: -0.0278
REMARK 3 S31: 0.2107 S32: 0.1555 S33: -0.0404
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 165 C 253
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9957 12.2142 23.3837
REMARK 3 T TENSOR
REMARK 3 T11: 0.1416 T22: 0.0370
REMARK 3 T33: 0.1013 T12: -0.0107
REMARK 3 T13: -0.0099 T23: 0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 1.4693 L22: 1.8065
REMARK 3 L33: 3.6523 L12: -0.0690
REMARK 3 L13: -0.2309 L23: 0.4510
REMARK 3 S TENSOR
REMARK 3 S11: 0.0258 S12: -0.1334 S13: -0.0517
REMARK 3 S21: 0.1660 S22: 0.0406 S23: 0.0304
REMARK 3 S31: 0.1215 S32: 0.0914 S33: -0.0664
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 254 C 305
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3855 20.1267 21.5772
REMARK 3 T TENSOR
REMARK 3 T11: 0.1730 T22: 0.1445
REMARK 3 T33: 0.1593 T12: -0.0128
REMARK 3 T13: 0.0484 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 2.3166 L22: 1.6630
REMARK 3 L33: 3.2939 L12: -0.4415
REMARK 3 L13: 0.6410 L23: -0.3535
REMARK 3 S TENSOR
REMARK 3 S11: -0.0129 S12: -0.0296 S13: -0.0223
REMARK 3 S21: 0.1516 S22: 0.1508 S23: 0.3722
REMARK 3 S31: -0.0805 S32: -0.5080 S33: -0.1379
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 306 C 398
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2819 22.9408 -0.9404
REMARK 3 T TENSOR
REMARK 3 T11: 0.0344 T22: 0.0592
REMARK 3 T33: 0.0913 T12: -0.0078
REMARK 3 T13: 0.0159 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.9579 L22: 1.7375
REMARK 3 L33: 1.8795 L12: -0.1496
REMARK 3 L13: 0.4672 L23: -0.3877
REMARK 3 S TENSOR
REMARK 3 S11: 0.0493 S12: 0.0962 S13: 0.0103
REMARK 3 S21: -0.0827 S22: -0.0499 S23: 0.0513
REMARK 3 S31: 0.0491 S32: 0.0196 S33: 0.0006
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 399 C 438
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1544 -2.2303 17.5694
REMARK 3 T TENSOR
REMARK 3 T11: 0.3073 T22: 0.0280
REMARK 3 T33: 0.1880 T12: 0.0448
REMARK 3 T13: -0.0122 T23: 0.0394
REMARK 3 L TENSOR
REMARK 3 L11: 2.2246 L22: 2.1490
REMARK 3 L33: 11.1447 L12: 0.1156
REMARK 3 L13: -0.9783 L23: 1.8468
REMARK 3 S TENSOR
REMARK 3 S11: -0.0784 S12: -0.0830 S13: -0.3353
REMARK 3 S21: 0.1393 S22: 0.0157 S23: -0.0015
REMARK 3 S31: 0.9297 S32: 0.4484 S33: 0.0627
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4GQO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000074517.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : DIAMOND(111)
REMARK 200 OPTICS : BE LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70880
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.09800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.7200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.54000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.760
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 7.1 MG/ML IN 10 MM TRIS-HCL,
REMARK 280 PH 8.3, 250 MM SODIUM CHLORIDE, 5 MM BME, CRYSTALLIZED WITH THE
REMARK 280 PACT SUITE (B1: 0.1 M MIB BUFFER, PH 4, 25% W/V PEG1500), VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K, PH 4.0
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 22.43250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 110.72400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 60.01650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 110.72400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.43250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 60.01650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 MSE A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 HIS A 13
REMARK 465 SER A 14
REMARK 465 SER A 15
REMARK 465 GLY A 16
REMARK 465 VAL A 17
REMARK 465 ASP A 18
REMARK 465 LEU A 19
REMARK 465 GLY A 20
REMARK 465 THR A 21
REMARK 465 GLU A 22
REMARK 465 ASN A 23
REMARK 465 LEU A 24
REMARK 465 TYR A 25
REMARK 465 PHE A 26
REMARK 465 GLN A 27
REMARK 465 SER A 28
REMARK 465 ASN A 29
REMARK 465 ALA A 30
REMARK 465 ASP A 31
REMARK 465 ASP A 32
REMARK 465 ASN A 33
REMARK 465 GLY A 34
REMARK 465 GLU A 439
REMARK 465 MSE B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 HIS B 11
REMARK 465 HIS B 12
REMARK 465 HIS B 13
REMARK 465 SER B 14
REMARK 465 SER B 15
REMARK 465 GLY B 16
REMARK 465 VAL B 17
REMARK 465 ASP B 18
REMARK 465 LEU B 19
REMARK 465 GLY B 20
REMARK 465 THR B 21
REMARK 465 GLU B 22
REMARK 465 ASN B 23
REMARK 465 LEU B 24
REMARK 465 TYR B 25
REMARK 465 PHE B 26
REMARK 465 GLN B 27
REMARK 465 SER B 28
REMARK 465 ASN B 29
REMARK 465 ALA B 30
REMARK 465 ASP B 31
REMARK 465 ASP B 32
REMARK 465 ASN B 33
REMARK 465 GLY B 34
REMARK 465 GLU B 439
REMARK 465 MSE C 7
REMARK 465 HIS C 8
REMARK 465 HIS C 9
REMARK 465 HIS C 10
REMARK 465 HIS C 11
REMARK 465 HIS C 12
REMARK 465 HIS C 13
REMARK 465 SER C 14
REMARK 465 SER C 15
REMARK 465 GLY C 16
REMARK 465 VAL C 17
REMARK 465 ASP C 18
REMARK 465 LEU C 19
REMARK 465 GLY C 20
REMARK 465 THR C 21
REMARK 465 GLU C 22
REMARK 465 ASN C 23
REMARK 465 LEU C 24
REMARK 465 TYR C 25
REMARK 465 PHE C 26
REMARK 465 GLN C 27
REMARK 465 SER C 28
REMARK 465 ASN C 29
REMARK 465 ALA C 30
REMARK 465 ASP C 31
REMARK 465 ASP C 32
REMARK 465 ASN C 33
REMARK 465 GLY C 34
REMARK 465 GLU C 439
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 362 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 362 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 97 -157.95 -105.35
REMARK 500 ASP A 212 -72.37 -138.87
REMARK 500 PHE A 226 -58.44 68.71
REMARK 500 ASN A 311 46.72 71.28
REMARK 500 ALA A 411 -52.49 -124.73
REMARK 500 GLU B 97 -161.49 -108.68
REMARK 500 LYS B 139 124.14 -33.81
REMARK 500 ASP B 212 -66.06 -141.94
REMARK 500 PHE B 226 -61.20 72.10
REMARK 500 ALA B 257 39.15 -99.22
REMARK 500 ALA B 260 145.70 -35.29
REMARK 500 ASN B 292 16.20 59.72
REMARK 500 GLU C 97 -161.55 -107.95
REMARK 500 ASP C 212 -69.06 -142.06
REMARK 500 PHE C 226 -60.48 74.92
REMARK 500 ALA C 257 61.89 -112.38
REMARK 500 ASP C 262 61.28 36.59
REMARK 500 ASN C 292 14.85 58.29
REMARK 500 GLU C 293 -70.41 -113.06
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 PGE C 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CSGID-IDP05674 RELATED DB: TARGETTRACK
DBREF 4GQO A 31 439 UNP Q8Y8N7 Q8Y8N7_LISMO 31 439
DBREF 4GQO B 31 439 UNP Q8Y8N7 Q8Y8N7_LISMO 31 439
DBREF 4GQO C 31 439 UNP Q8Y8N7 Q8Y8N7_LISMO 31 439
SEQADV 4GQO MSE A 7 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS A 8 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS A 9 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS A 10 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS A 11 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS A 12 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS A 13 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO SER A 14 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO SER A 15 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO GLY A 16 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO VAL A 17 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO ASP A 18 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO LEU A 19 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO GLY A 20 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO THR A 21 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO GLU A 22 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO ASN A 23 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO LEU A 24 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO TYR A 25 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO PHE A 26 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO GLN A 27 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO SER A 28 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO ASN A 29 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO ALA A 30 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO MSE B 7 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS B 8 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS B 9 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS B 10 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS B 11 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS B 12 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS B 13 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO SER B 14 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO SER B 15 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO GLY B 16 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO VAL B 17 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO ASP B 18 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO LEU B 19 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO GLY B 20 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO THR B 21 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO GLU B 22 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO ASN B 23 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO LEU B 24 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO TYR B 25 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO PHE B 26 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO GLN B 27 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO SER B 28 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO ASN B 29 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO ALA B 30 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO MSE C 7 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS C 8 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS C 9 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS C 10 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS C 11 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS C 12 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO HIS C 13 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO SER C 14 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO SER C 15 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO GLY C 16 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO VAL C 17 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO ASP C 18 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO LEU C 19 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO GLY C 20 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO THR C 21 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO GLU C 22 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO ASN C 23 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO LEU C 24 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO TYR C 25 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO PHE C 26 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO GLN C 27 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO SER C 28 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO ASN C 29 UNP Q8Y8N7 EXPRESSION TAG
SEQADV 4GQO ALA C 30 UNP Q8Y8N7 EXPRESSION TAG
SEQRES 1 A 433 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 433 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA ASP ASP
SEQRES 3 A 433 ASN GLY LYS THR LYS VAL THR PHE TRP ALA ALA PRO ASN
SEQRES 4 A 433 PRO THR GLN VAL LYS TYR TRP ASP GLU MSE ALA LYS ALA
SEQRES 5 A 433 TYR GLU LYS GLU ASN PRO ASP VAL THR ILE GLU VAL SER
SEQRES 6 A 433 GLN MSE LYS GLU SER PRO SER SER GLU ALA THR ILE GLN
SEQRES 7 A 433 SER ALA ILE ALA SER LYS THR ALA PRO THR MSE SER GLU
SEQRES 8 A 433 ASN ILE ASN ARG SER PHE ALA ALA GLN LEU ALA ASP SER
SEQRES 9 A 433 LYS ALA ILE VAL PRO LEU ASN ASP VAL LYS GLY LEU ASP
SEQRES 10 A 433 ASP VAL VAL LYS GLU ARG ASN MSE SER GLU THR MSE ASP
SEQRES 11 A 433 SER TRP LYS PHE SER ASP GLY ASN GLN TYR VAL LEU PRO
SEQRES 12 A 433 VAL TYR SER ASN PRO ILE LEU PHE ALA TRP ARG LEU ASP
SEQRES 13 A 433 THR LEU LYS GLU LEU GLY TYR ASP ALA PRO PRO LYS THR
SEQRES 14 A 433 TYR SER GLU ALA LEU GLU VAL GLY LYS LYS LEU LYS ALA
SEQRES 15 A 433 LYS TYR PRO ASP LYS VAL LEU TRP ALA LYS GLY ASP LEU
SEQRES 16 A 433 SER ASP PRO THR ALA TRP MSE ARG TRP PHE ASP PHE PHE
SEQRES 17 A 433 PRO LEU TYR ASP ALA ALA SER LYS GLY ASN ALA PHE VAL
SEQRES 18 A 433 GLU ASP GLY LYS LEU VAL ALA ASP ASP LYS ALA GLY THR
SEQRES 19 A 433 GLU LEU LEU THR PHE MSE SER GLU LEU GLN LYS ASN LYS
SEQRES 20 A 433 LEU LEU LEU ALA SER LYS ALA THR ASP PRO PHE GLU THR
SEQRES 21 A 433 GLY THR SER ILE MSE ALA ASP ASN GLY PRO TRP THR PHE
SEQRES 22 A 433 PRO ASN TRP ASP GLU LYS PHE PRO GLU LEU LYS TYR ASN
SEQRES 23 A 433 GLU ASN TYR ALA ILE THR ALA PRO LEU VAL PRO ASP SER
SEQRES 24 A 433 MSE VAL ASN GLU GLU ASN VAL ALA THR TYR ALA ASP SER
SEQRES 25 A 433 LYS GLY VAL VAL MSE TYR ALA GLN ALA THR ASP LYS GLU
SEQRES 26 A 433 LYS GLU ALA ALA MSE ASP PHE LEU LYS PHE VAL TYR ASN
SEQRES 27 A 433 ASP ASP LYS ASN ASP LEU LYS PHE LEU GLU THR THR ASN
SEQRES 28 A 433 LEU ILE PRO ALA ARG ASP ASP ALA THR GLU ASN GLU THR
SEQRES 29 A 433 PHE THR ALA PHE PHE LYS GLU ASN PRO GLU LEU GLU VAL
SEQRES 30 A 433 TYR ALA ALA ASN VAL PRO TYR SER ILE PRO ALA MSE ASP
SEQRES 31 A 433 ASP ALA LYS TYR ASN ASP ILE GLN GLN ILE ILE GLY GLU
SEQRES 32 A 433 GLU ALA TRP ASN PRO ILE VAL ARG GLY GLU LYS LYS PRO
SEQRES 33 A 433 THR LYS ALA TRP SER ASP MSE LYS LYS ALA GLU ASP GLY
SEQRES 34 A 433 VAL LEU GLN GLU
SEQRES 1 B 433 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 433 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA ASP ASP
SEQRES 3 B 433 ASN GLY LYS THR LYS VAL THR PHE TRP ALA ALA PRO ASN
SEQRES 4 B 433 PRO THR GLN VAL LYS TYR TRP ASP GLU MSE ALA LYS ALA
SEQRES 5 B 433 TYR GLU LYS GLU ASN PRO ASP VAL THR ILE GLU VAL SER
SEQRES 6 B 433 GLN MSE LYS GLU SER PRO SER SER GLU ALA THR ILE GLN
SEQRES 7 B 433 SER ALA ILE ALA SER LYS THR ALA PRO THR MSE SER GLU
SEQRES 8 B 433 ASN ILE ASN ARG SER PHE ALA ALA GLN LEU ALA ASP SER
SEQRES 9 B 433 LYS ALA ILE VAL PRO LEU ASN ASP VAL LYS GLY LEU ASP
SEQRES 10 B 433 ASP VAL VAL LYS GLU ARG ASN MSE SER GLU THR MSE ASP
SEQRES 11 B 433 SER TRP LYS PHE SER ASP GLY ASN GLN TYR VAL LEU PRO
SEQRES 12 B 433 VAL TYR SER ASN PRO ILE LEU PHE ALA TRP ARG LEU ASP
SEQRES 13 B 433 THR LEU LYS GLU LEU GLY TYR ASP ALA PRO PRO LYS THR
SEQRES 14 B 433 TYR SER GLU ALA LEU GLU VAL GLY LYS LYS LEU LYS ALA
SEQRES 15 B 433 LYS TYR PRO ASP LYS VAL LEU TRP ALA LYS GLY ASP LEU
SEQRES 16 B 433 SER ASP PRO THR ALA TRP MSE ARG TRP PHE ASP PHE PHE
SEQRES 17 B 433 PRO LEU TYR ASP ALA ALA SER LYS GLY ASN ALA PHE VAL
SEQRES 18 B 433 GLU ASP GLY LYS LEU VAL ALA ASP ASP LYS ALA GLY THR
SEQRES 19 B 433 GLU LEU LEU THR PHE MSE SER GLU LEU GLN LYS ASN LYS
SEQRES 20 B 433 LEU LEU LEU ALA SER LYS ALA THR ASP PRO PHE GLU THR
SEQRES 21 B 433 GLY THR SER ILE MSE ALA ASP ASN GLY PRO TRP THR PHE
SEQRES 22 B 433 PRO ASN TRP ASP GLU LYS PHE PRO GLU LEU LYS TYR ASN
SEQRES 23 B 433 GLU ASN TYR ALA ILE THR ALA PRO LEU VAL PRO ASP SER
SEQRES 24 B 433 MSE VAL ASN GLU GLU ASN VAL ALA THR TYR ALA ASP SER
SEQRES 25 B 433 LYS GLY VAL VAL MSE TYR ALA GLN ALA THR ASP LYS GLU
SEQRES 26 B 433 LYS GLU ALA ALA MSE ASP PHE LEU LYS PHE VAL TYR ASN
SEQRES 27 B 433 ASP ASP LYS ASN ASP LEU LYS PHE LEU GLU THR THR ASN
SEQRES 28 B 433 LEU ILE PRO ALA ARG ASP ASP ALA THR GLU ASN GLU THR
SEQRES 29 B 433 PHE THR ALA PHE PHE LYS GLU ASN PRO GLU LEU GLU VAL
SEQRES 30 B 433 TYR ALA ALA ASN VAL PRO TYR SER ILE PRO ALA MSE ASP
SEQRES 31 B 433 ASP ALA LYS TYR ASN ASP ILE GLN GLN ILE ILE GLY GLU
SEQRES 32 B 433 GLU ALA TRP ASN PRO ILE VAL ARG GLY GLU LYS LYS PRO
SEQRES 33 B 433 THR LYS ALA TRP SER ASP MSE LYS LYS ALA GLU ASP GLY
SEQRES 34 B 433 VAL LEU GLN GLU
SEQRES 1 C 433 MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 433 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA ASP ASP
SEQRES 3 C 433 ASN GLY LYS THR LYS VAL THR PHE TRP ALA ALA PRO ASN
SEQRES 4 C 433 PRO THR GLN VAL LYS TYR TRP ASP GLU MSE ALA LYS ALA
SEQRES 5 C 433 TYR GLU LYS GLU ASN PRO ASP VAL THR ILE GLU VAL SER
SEQRES 6 C 433 GLN MSE LYS GLU SER PRO SER SER GLU ALA THR ILE GLN
SEQRES 7 C 433 SER ALA ILE ALA SER LYS THR ALA PRO THR MSE SER GLU
SEQRES 8 C 433 ASN ILE ASN ARG SER PHE ALA ALA GLN LEU ALA ASP SER
SEQRES 9 C 433 LYS ALA ILE VAL PRO LEU ASN ASP VAL LYS GLY LEU ASP
SEQRES 10 C 433 ASP VAL VAL LYS GLU ARG ASN MSE SER GLU THR MSE ASP
SEQRES 11 C 433 SER TRP LYS PHE SER ASP GLY ASN GLN TYR VAL LEU PRO
SEQRES 12 C 433 VAL TYR SER ASN PRO ILE LEU PHE ALA TRP ARG LEU ASP
SEQRES 13 C 433 THR LEU LYS GLU LEU GLY TYR ASP ALA PRO PRO LYS THR
SEQRES 14 C 433 TYR SER GLU ALA LEU GLU VAL GLY LYS LYS LEU LYS ALA
SEQRES 15 C 433 LYS TYR PRO ASP LYS VAL LEU TRP ALA LYS GLY ASP LEU
SEQRES 16 C 433 SER ASP PRO THR ALA TRP MSE ARG TRP PHE ASP PHE PHE
SEQRES 17 C 433 PRO LEU TYR ASP ALA ALA SER LYS GLY ASN ALA PHE VAL
SEQRES 18 C 433 GLU ASP GLY LYS LEU VAL ALA ASP ASP LYS ALA GLY THR
SEQRES 19 C 433 GLU LEU LEU THR PHE MSE SER GLU LEU GLN LYS ASN LYS
SEQRES 20 C 433 LEU LEU LEU ALA SER LYS ALA THR ASP PRO PHE GLU THR
SEQRES 21 C 433 GLY THR SER ILE MSE ALA ASP ASN GLY PRO TRP THR PHE
SEQRES 22 C 433 PRO ASN TRP ASP GLU LYS PHE PRO GLU LEU LYS TYR ASN
SEQRES 23 C 433 GLU ASN TYR ALA ILE THR ALA PRO LEU VAL PRO ASP SER
SEQRES 24 C 433 MSE VAL ASN GLU GLU ASN VAL ALA THR TYR ALA ASP SER
SEQRES 25 C 433 LYS GLY VAL VAL MSE TYR ALA GLN ALA THR ASP LYS GLU
SEQRES 26 C 433 LYS GLU ALA ALA MSE ASP PHE LEU LYS PHE VAL TYR ASN
SEQRES 27 C 433 ASP ASP LYS ASN ASP LEU LYS PHE LEU GLU THR THR ASN
SEQRES 28 C 433 LEU ILE PRO ALA ARG ASP ASP ALA THR GLU ASN GLU THR
SEQRES 29 C 433 PHE THR ALA PHE PHE LYS GLU ASN PRO GLU LEU GLU VAL
SEQRES 30 C 433 TYR ALA ALA ASN VAL PRO TYR SER ILE PRO ALA MSE ASP
SEQRES 31 C 433 ASP ALA LYS TYR ASN ASP ILE GLN GLN ILE ILE GLY GLU
SEQRES 32 C 433 GLU ALA TRP ASN PRO ILE VAL ARG GLY GLU LYS LYS PRO
SEQRES 33 C 433 THR LYS ALA TRP SER ASP MSE LYS LYS ALA GLU ASP GLY
SEQRES 34 C 433 VAL LEU GLN GLU
MODRES 4GQO MSE A 55 MET SELENOMETHIONINE
MODRES 4GQO MSE A 73 MET SELENOMETHIONINE
MODRES 4GQO MSE A 95 MET SELENOMETHIONINE
MODRES 4GQO MSE A 131 MET SELENOMETHIONINE
MODRES 4GQO MSE A 135 MET SELENOMETHIONINE
MODRES 4GQO MSE A 208 MET SELENOMETHIONINE
MODRES 4GQO MSE A 246 MET SELENOMETHIONINE
MODRES 4GQO MSE A 271 MET SELENOMETHIONINE
MODRES 4GQO MSE A 306 MET SELENOMETHIONINE
MODRES 4GQO MSE A 323 MET SELENOMETHIONINE
MODRES 4GQO MSE A 336 MET SELENOMETHIONINE
MODRES 4GQO MSE A 395 MET SELENOMETHIONINE
MODRES 4GQO MSE A 429 MET SELENOMETHIONINE
MODRES 4GQO MSE B 55 MET SELENOMETHIONINE
MODRES 4GQO MSE B 73 MET SELENOMETHIONINE
MODRES 4GQO MSE B 95 MET SELENOMETHIONINE
MODRES 4GQO MSE B 131 MET SELENOMETHIONINE
MODRES 4GQO MSE B 135 MET SELENOMETHIONINE
MODRES 4GQO MSE B 208 MET SELENOMETHIONINE
MODRES 4GQO MSE B 246 MET SELENOMETHIONINE
MODRES 4GQO MSE B 271 MET SELENOMETHIONINE
MODRES 4GQO MSE B 306 MET SELENOMETHIONINE
MODRES 4GQO MSE B 323 MET SELENOMETHIONINE
MODRES 4GQO MSE B 336 MET SELENOMETHIONINE
MODRES 4GQO MSE B 395 MET SELENOMETHIONINE
MODRES 4GQO MSE B 429 MET SELENOMETHIONINE
MODRES 4GQO MSE C 55 MET SELENOMETHIONINE
MODRES 4GQO MSE C 73 MET SELENOMETHIONINE
MODRES 4GQO MSE C 95 MET SELENOMETHIONINE
MODRES 4GQO MSE C 131 MET SELENOMETHIONINE
MODRES 4GQO MSE C 135 MET SELENOMETHIONINE
MODRES 4GQO MSE C 208 MET SELENOMETHIONINE
MODRES 4GQO MSE C 246 MET SELENOMETHIONINE
MODRES 4GQO MSE C 271 MET SELENOMETHIONINE
MODRES 4GQO MSE C 306 MET SELENOMETHIONINE
MODRES 4GQO MSE C 323 MET SELENOMETHIONINE
MODRES 4GQO MSE C 336 MET SELENOMETHIONINE
MODRES 4GQO MSE C 395 MET SELENOMETHIONINE
MODRES 4GQO MSE C 429 MET SELENOMETHIONINE
HET MSE A 55 8
HET MSE A 73 8
HET MSE A 95 16
HET MSE A 131 8
HET MSE A 135 8
HET MSE A 208 8
HET MSE A 246 8
HET MSE A 271 8
HET MSE A 306 8
HET MSE A 323 8
HET MSE A 336 8
HET MSE A 395 8
HET MSE A 429 8
HET MSE B 55 8
HET MSE B 73 8
HET MSE B 95 8
HET MSE B 131 8
HET MSE B 135 8
HET MSE B 208 8
HET MSE B 246 8
HET MSE B 271 8
HET MSE B 306 8
HET MSE B 323 8
HET MSE B 336 8
HET MSE B 395 16
HET MSE B 429 8
HET MSE C 55 8
HET MSE C 73 8
HET MSE C 95 16
HET MSE C 131 8
HET MSE C 135 8
HET MSE C 208 8
HET MSE C 246 8
HET MSE C 271 8
HET MSE C 306 8
HET MSE C 323 8
HET MSE C 336 8
HET MSE C 395 8
HET MSE C 429 8
HET PGE C 501 10
HETNAM MSE SELENOMETHIONINE
HETNAM PGE TRIETHYLENE GLYCOL
FORMUL 1 MSE 39(C5 H11 N O2 SE)
FORMUL 4 PGE C6 H14 O4
FORMUL 5 HOH *585(H2 O)
HELIX 1 1 ASN A 45 ASN A 63 1 19
HELIX 2 2 SER A 78 SER A 89 1 12
HELIX 3 3 ASN A 100 SER A 110 1 11
HELIX 4 4 PRO A 115 VAL A 119 5 5
HELIX 5 5 GLY A 121 ARG A 129 1 9
HELIX 6 6 MSE A 131 TRP A 138 1 8
HELIX 7 7 ARG A 160 LEU A 167 1 8
HELIX 8 8 THR A 175 TYR A 190 1 16
HELIX 9 9 GLY A 199 ASP A 203 5 5
HELIX 10 10 THR A 205 PHE A 211 5 7
HELIX 11 11 ASP A 212 SER A 221 1 10
HELIX 12 12 ASP A 235 ASN A 252 1 18
HELIX 13 13 TRP A 277 PHE A 286 1 10
HELIX 14 14 PRO A 303 VAL A 307 5 5
HELIX 15 15 THR A 328 TYR A 343 1 16
HELIX 16 16 ASP A 345 ASN A 357 1 13
HELIX 17 17 ASN A 368 THR A 370 5 3
HELIX 18 18 PHE A 371 ASN A 378 1 8
HELIX 19 19 ASN A 378 VAL A 388 1 11
HELIX 20 20 LYS A 399 ALA A 411 1 13
HELIX 21 21 ALA A 411 ARG A 417 1 7
HELIX 22 22 LYS A 421 LEU A 437 1 17
HELIX 23 23 ASN B 45 ASN B 63 1 19
HELIX 24 24 SER B 78 SER B 89 1 12
HELIX 25 25 ASN B 100 SER B 110 1 11
HELIX 26 26 PRO B 115 VAL B 119 5 5
HELIX 27 27 GLY B 121 ARG B 129 1 9
HELIX 28 28 MSE B 131 SER B 137 1 7
HELIX 29 29 LEU B 161 LEU B 167 1 7
HELIX 30 30 THR B 175 TYR B 190 1 16
HELIX 31 31 GLY B 199 ASP B 203 5 5
HELIX 32 32 THR B 205 PHE B 211 5 7
HELIX 33 33 ASP B 212 SER B 221 1 10
HELIX 34 34 ASP B 235 ASN B 252 1 18
HELIX 35 35 TRP B 277 PHE B 286 1 10
HELIX 36 36 PRO B 303 VAL B 307 5 5
HELIX 37 37 THR B 328 TYR B 343 1 16
HELIX 38 38 ASP B 345 ASN B 357 1 13
HELIX 39 39 ASN B 368 THR B 370 5 3
HELIX 40 40 PHE B 371 ASN B 378 1 8
HELIX 41 41 ASN B 378 VAL B 388 1 11
HELIX 42 42 LYS B 399 ALA B 411 1 13
HELIX 43 43 ALA B 411 ARG B 417 1 7
HELIX 44 44 LYS B 421 GLN B 438 1 18
HELIX 45 45 ASN C 45 ASN C 63 1 19
HELIX 46 46 SER C 78 LYS C 90 1 13
HELIX 47 47 ASN C 100 SER C 110 1 11
HELIX 48 48 PRO C 115 VAL C 119 5 5
HELIX 49 49 GLY C 121 ASN C 130 1 10
HELIX 50 50 MSE C 131 SER C 137 1 7
HELIX 51 51 LEU C 161 LEU C 167 1 7
HELIX 52 52 THR C 175 TYR C 190 1 16
HELIX 53 53 GLY C 199 ASP C 203 5 5
HELIX 54 54 THR C 205 PHE C 211 5 7
HELIX 55 55 ASP C 212 SER C 221 1 10
HELIX 56 56 ASP C 235 ASN C 252 1 18
HELIX 57 57 TRP C 277 PHE C 286 1 10
HELIX 58 58 PRO C 303 VAL C 307 5 5
HELIX 59 59 THR C 328 ASN C 344 1 17
HELIX 60 60 ASP C 345 ASN C 357 1 13
HELIX 61 61 ASN C 368 THR C 370 5 3
HELIX 62 62 PHE C 371 ASN C 378 1 8
HELIX 63 63 ASN C 378 VAL C 388 1 11
HELIX 64 64 LYS C 399 ALA C 411 1 13
HELIX 65 65 ALA C 411 GLY C 418 1 8
HELIX 66 66 LYS C 421 GLN C 438 1 18
SHEET 1 A 5 VAL A 66 GLN A 72 0
SHEET 2 A 5 THR A 36 ALA A 42 1 N PHE A 40 O GLU A 69
SHEET 3 A 5 MSE A 95 ILE A 99 1 O MSE A 95 N TRP A 41
SHEET 4 A 5 THR A 314 MSE A 323 -1 O VAL A 322 N SER A 96
SHEET 5 A 5 LEU A 148 PRO A 154 -1 N ASN A 153 O ASP A 317
SHEET 1 B 5 VAL A 66 GLN A 72 0
SHEET 2 B 5 THR A 36 ALA A 42 1 N PHE A 40 O GLU A 69
SHEET 3 B 5 MSE A 95 ILE A 99 1 O MSE A 95 N TRP A 41
SHEET 4 B 5 THR A 314 MSE A 323 -1 O VAL A 322 N SER A 96
SHEET 5 B 5 SER A 391 ILE A 392 1 O ILE A 392 N ALA A 316
SHEET 1 C 5 LEU A 255 LEU A 256 0
SHEET 2 C 5 VAL A 194 ALA A 197 1 N TRP A 196 O LEU A 256
SHEET 3 C 5 SER A 269 ASN A 274 1 O MSE A 271 N LEU A 195
SHEET 4 C 5 LEU A 156 TRP A 159 -1 N LEU A 156 O ASN A 274
SHEET 5 C 5 ALA A 296 THR A 298 -1 O THR A 298 N PHE A 157
SHEET 1 D 2 VAL A 227 GLU A 228 0
SHEET 2 D 2 LYS A 231 LEU A 232 -1 O LYS A 231 N GLU A 228
SHEET 1 E 5 VAL B 66 GLN B 72 0
SHEET 2 E 5 THR B 36 ALA B 42 1 N PHE B 40 O GLU B 69
SHEET 3 E 5 MSE B 95 ILE B 99 1 O MSE B 95 N TRP B 41
SHEET 4 E 5 THR B 314 MSE B 323 -1 O VAL B 322 N SER B 96
SHEET 5 E 5 LEU B 148 PRO B 154 -1 N ASN B 153 O ASP B 317
SHEET 1 F 5 VAL B 66 GLN B 72 0
SHEET 2 F 5 THR B 36 ALA B 42 1 N PHE B 40 O GLU B 69
SHEET 3 F 5 MSE B 95 ILE B 99 1 O MSE B 95 N TRP B 41
SHEET 4 F 5 THR B 314 MSE B 323 -1 O VAL B 322 N SER B 96
SHEET 5 F 5 SER B 391 ILE B 392 1 O ILE B 392 N THR B 314
SHEET 1 G 3 MSE B 271 ASN B 274 0
SHEET 2 G 3 LEU B 156 ARG B 160 -1 N LEU B 156 O ASN B 274
SHEET 3 G 3 TYR B 295 THR B 298 -1 O THR B 298 N PHE B 157
SHEET 1 H 2 TRP B 196 ALA B 197 0
SHEET 2 H 2 LEU B 255 LEU B 256 1 O LEU B 256 N TRP B 196
SHEET 1 I 2 VAL B 227 GLU B 228 0
SHEET 2 I 2 LYS B 231 LEU B 232 -1 O LYS B 231 N GLU B 228
SHEET 1 J 5 VAL C 66 GLN C 72 0
SHEET 2 J 5 THR C 36 ALA C 42 1 N ALA C 42 O SER C 71
SHEET 3 J 5 MSE C 95 ILE C 99 1 O MSE C 95 N TRP C 41
SHEET 4 J 5 THR C 314 MSE C 323 -1 O GLY C 320 N ILE C 99
SHEET 5 J 5 LEU C 148 PRO C 154 -1 N ASN C 153 O ASP C 317
SHEET 1 K 5 VAL C 66 GLN C 72 0
SHEET 2 K 5 THR C 36 ALA C 42 1 N ALA C 42 O SER C 71
SHEET 3 K 5 MSE C 95 ILE C 99 1 O MSE C 95 N TRP C 41
SHEET 4 K 5 THR C 314 MSE C 323 -1 O GLY C 320 N ILE C 99
SHEET 5 K 5 SER C 391 ILE C 392 1 O ILE C 392 N THR C 314
SHEET 1 L 3 MSE C 271 ASN C 274 0
SHEET 2 L 3 LEU C 156 ARG C 160 -1 N ALA C 158 O ALA C 272
SHEET 3 L 3 TYR C 295 THR C 298 -1 O THR C 298 N PHE C 157
SHEET 1 M 2 TRP C 196 ALA C 197 0
SHEET 2 M 2 LEU C 255 LEU C 256 1 O LEU C 256 N TRP C 196
SHEET 1 N 2 VAL C 227 GLU C 228 0
SHEET 2 N 2 LYS C 231 LEU C 232 -1 O LYS C 231 N GLU C 228
LINK C GLU A 54 N MSE A 55 1555 1555 1.34
LINK C MSE A 55 N ALA A 56 1555 1555 1.34
LINK C GLN A 72 N MSE A 73 1555 1555 1.32
LINK C MSE A 73 N LYS A 74 1555 1555 1.33
LINK C THR A 94 N AMSE A 95 1555 1555 1.33
LINK C THR A 94 N BMSE A 95 1555 1555 1.33
LINK C AMSE A 95 N SER A 96 1555 1555 1.33
LINK C BMSE A 95 N SER A 96 1555 1555 1.34
LINK C ASN A 130 N MSE A 131 1555 1555 1.33
LINK C MSE A 131 N SER A 132 1555 1555 1.33
LINK C THR A 134 N MSE A 135 1555 1555 1.33
LINK C MSE A 135 N ASP A 136 1555 1555 1.33
LINK C TRP A 207 N MSE A 208 1555 1555 1.32
LINK C MSE A 208 N ARG A 209 1555 1555 1.33
LINK C PHE A 245 N MSE A 246 1555 1555 1.32
LINK C MSE A 246 N SER A 247 1555 1555 1.34
LINK C ILE A 270 N MSE A 271 1555 1555 1.33
LINK C MSE A 271 N ALA A 272 1555 1555 1.32
LINK C SER A 305 N MSE A 306 1555 1555 1.33
LINK C MSE A 306 N VAL A 307 1555 1555 1.33
LINK C VAL A 322 N MSE A 323 1555 1555 1.33
LINK C MSE A 323 N TYR A 324 1555 1555 1.33
LINK C ALA A 335 N MSE A 336 1555 1555 1.33
LINK C MSE A 336 N ASP A 337 1555 1555 1.34
LINK C ALA A 394 N MSE A 395 1555 1555 1.32
LINK C MSE A 395 N ASP A 396 1555 1555 1.34
LINK C ASP A 428 N MSE A 429 1555 1555 1.33
LINK C MSE A 429 N LYS A 430 1555 1555 1.33
LINK C GLU B 54 N MSE B 55 1555 1555 1.34
LINK C MSE B 55 N ALA B 56 1555 1555 1.33
LINK C GLN B 72 N MSE B 73 1555 1555 1.33
LINK C MSE B 73 N LYS B 74 1555 1555 1.33
LINK C THR B 94 N MSE B 95 1555 1555 1.33
LINK C MSE B 95 N SER B 96 1555 1555 1.33
LINK C ASN B 130 N MSE B 131 1555 1555 1.33
LINK C MSE B 131 N SER B 132 1555 1555 1.33
LINK C THR B 134 N MSE B 135 1555 1555 1.33
LINK C MSE B 135 N ASP B 136 1555 1555 1.33
LINK C TRP B 207 N MSE B 208 1555 1555 1.33
LINK C MSE B 208 N ARG B 209 1555 1555 1.32
LINK C PHE B 245 N MSE B 246 1555 1555 1.33
LINK C MSE B 246 N ASER B 247 1555 1555 1.33
LINK C MSE B 246 N BSER B 247 1555 1555 1.33
LINK C ILE B 270 N MSE B 271 1555 1555 1.33
LINK C MSE B 271 N ALA B 272 1555 1555 1.33
LINK C SER B 305 N MSE B 306 1555 1555 1.33
LINK C MSE B 306 N VAL B 307 1555 1555 1.33
LINK C VAL B 322 N MSE B 323 1555 1555 1.33
LINK C MSE B 323 N TYR B 324 1555 1555 1.33
LINK C ALA B 335 N MSE B 336 1555 1555 1.32
LINK C MSE B 336 N ASP B 337 1555 1555 1.33
LINK C ALA B 394 N AMSE B 395 1555 1555 1.33
LINK C ALA B 394 N BMSE B 395 1555 1555 1.33
LINK C AMSE B 395 N ASP B 396 1555 1555 1.33
LINK C BMSE B 395 N ASP B 396 1555 1555 1.33
LINK C ASP B 428 N MSE B 429 1555 1555 1.33
LINK C MSE B 429 N LYS B 430 1555 1555 1.34
LINK C GLU C 54 N MSE C 55 1555 1555 1.33
LINK C MSE C 55 N ALA C 56 1555 1555 1.32
LINK C GLN C 72 N MSE C 73 1555 1555 1.32
LINK C MSE C 73 N LYS C 74 1555 1555 1.33
LINK C THR C 94 N AMSE C 95 1555 1555 1.33
LINK C THR C 94 N BMSE C 95 1555 1555 1.33
LINK C AMSE C 95 N SER C 96 1555 1555 1.33
LINK C BMSE C 95 N SER C 96 1555 1555 1.34
LINK C ASN C 130 N MSE C 131 1555 1555 1.33
LINK C MSE C 131 N SER C 132 1555 1555 1.33
LINK C THR C 134 N MSE C 135 1555 1555 1.33
LINK C MSE C 135 N ASP C 136 1555 1555 1.33
LINK C TRP C 207 N MSE C 208 1555 1555 1.33
LINK C MSE C 208 N ARG C 209 1555 1555 1.33
LINK C PHE C 245 N MSE C 246 1555 1555 1.32
LINK C MSE C 246 N ASER C 247 1555 1555 1.33
LINK C MSE C 246 N BSER C 247 1555 1555 1.33
LINK C ILE C 270 N MSE C 271 1555 1555 1.33
LINK C MSE C 271 N ALA C 272 1555 1555 1.32
LINK C SER C 305 N MSE C 306 1555 1555 1.33
LINK C MSE C 306 N VAL C 307 1555 1555 1.33
LINK C VAL C 322 N MSE C 323 1555 1555 1.33
LINK C MSE C 323 N TYR C 324 1555 1555 1.33
LINK C ALA C 335 N MSE C 336 1555 1555 1.33
LINK C MSE C 336 N ASP C 337 1555 1555 1.33
LINK C ALA C 394 N MSE C 395 1555 1555 1.32
LINK C MSE C 395 N ASP C 396 1555 1555 1.34
LINK C ASP C 428 N MSE C 429 1555 1555 1.33
LINK C MSE C 429 N LYS C 430 1555 1555 1.34
CISPEP 1 SER A 76 PRO A 77 0 0.65
CISPEP 2 SER B 76 PRO B 77 0 0.44
CISPEP 3 SER C 76 PRO C 77 0 -0.33
SITE 1 AC1 1 TRP C 207
CRYST1 44.865 120.033 221.448 90.00 90.00 90.00 P 21 21 21 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.022289 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008331 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004516 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
