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HEADER HYDROLASE 14-DEC-06 2JBW
TITLE CRYSTAL STRUCTURE OF THE 2,6-DIHYDROXY-PSEUDO-OXYNICOTINE
TITLE 2 HYDROLASE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2,6-DIHYDROXY-PSEUDO-OXYNICOTINE HYDROLASE;
COMPND 3 SYNONYM: DHPON-HYDROLASE;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 EC: 3.7.1.-;
COMPND 6 FRAGMENT: RESIDUES 1-365;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 3 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: PH6EX3.DHPONH;
SOURCE 5 ORGANISM_SCIENTIFIC: ARTHROBACTER NICOTINOVORANS
KEYWDS ALPHA/BETA HYDROLASE, META-CLEAVAGE PATHWAY,
KEYWDS 2 RETRO- FRIEDEL-CRAFTS ACYLATION,
KEYWDS 3 NICOTINE DEGRADATION, HYPOTHETICAL PROTEIN,
KEYWDS 4 PLASMID, CATALYTIC TRIAD, C-C BOND CLEAVAGE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.SCHLEBERGER,P.SACHELARU,R.BRANDSCH,G.E.SCHULZ
REVDAT 1 04-JAN-07 2JBW 0
JRNL AUTH C.SCHLEBERGER,P.SACHELARU,R.BRANDSCH,G.E.SCHULZ
JRNL TITL STRUCTURE AND ACTION OF A C-C BOND CLEAVING
JRNL TITL 2 ALPHABETA-HYDROLASE INVOLVED IN NICOTINE
JRNL TITL 3 DEGRADATION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.1 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.87
REMARK 3 NUMBER OF REFLECTIONS : 86393
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) : 0.18303
REMARK 3 R VALUE (WORKING SET) : 0.18140
REMARK 3 FREE R VALUE : 0.23791
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.9
REMARK 3 FREE R VALUE TEST SET COUNT : 2580
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) : 2.100
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.154
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6256
REMARK 3 BIN R VALUE (WORKING SET) : 0.208
REMARK 3 BIN FREE R VALUE SET COUNT : 186
REMARK 3 BIN FREE R VALUE : 0.265
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10898
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 348
REMARK 3 SOLVENT ATOMS : 964
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 33.2
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.893
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.53
REMARK 3 B22 (A**2) : 0.18
REMARK 3 B33 (A**2) : -0.40
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -1.63
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.219
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.190
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.136
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.260
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 11517 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED (DEGREES): 15652 ; 1.527 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1425 ; 5.919 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 525 ;33.240 ;24.133
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1927 ;16.836 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 72 ;17.916 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1699 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED (A): 8820 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED (A): 5855 ; 0.214 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED (A): 7767 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED (A): 1068 ; 0.164 ; 0.200
REMARK 3 SYMMETRY VDW REFINED (A): 73 ; 0.182 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED (A): 17 ; 0.160 ; 0.200
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): 7116 ; 0.754 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): 11417 ; 1.333 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): 4637 ; 2.405 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): 4235 ; 3.328 ; 4.500
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 139 A 384 5
REMARK 3 1 B 139 B 384 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 904 ; 0.16 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 850 ; 0.46 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 904 ; 1.40 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 850 ; 2.12 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 40 A 111 5
REMARK 3 1 B 40 B 111 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 288 ; 0.10 ; 0.50
REMARK 3 LOOSE POSITIONAL 2 A (A): 302 ; 0.45 ; 5.00
REMARK 3 MEDIUM THERMAL 2 A (A**2): 288 ; 0.73 ; 2.00
REMARK 3 LOOSE THERMAL 2 A (A**2): 302 ; 1.44 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 30
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 8 A 28
REMARK 3 ORIGIN FOR THE GROUP (A): 84.7520 27.2414 132.3267
REMARK 3 T TENSOR
REMARK 3 T11: -0.0502 T22: 0.0065
REMARK 3 T33: -0.1287 T12: -0.0415
REMARK 3 T13: 0.0084 T23: 0.0303
REMARK 3 L TENSOR
REMARK 3 L11: 2.0628 L22: 3.7311
REMARK 3 L33: 4.3453 L12: -0.3222
REMARK 3 L13: 2.6548 L23: 1.9958
REMARK 3 S TENSOR
REMARK 3 S11: 0.0268 S12: 0.0910 S13: -0.0464
REMARK 3 S21: -0.2393 S22: -0.0620 S23: -0.5312
REMARK 3 S31: -0.2023 S32: 0.1388 S33: 0.0352
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 29 A 35
REMARK 3 ORIGIN FOR THE GROUP (A): 86.2240 33.6607 125.7500
REMARK 3 T TENSOR
REMARK 3 T11: -0.0528 T22: 0.0885
REMARK 3 T33: -0.1573 T12: -0.0485
REMARK 3 T13: -0.0260 T23: 0.0539
REMARK 3 L TENSOR
REMARK 3 L11: 24.3292 L22: 19.7423
REMARK 3 L33: 7.8610 L12: 4.7310
REMARK 3 L13: -3.6790 L23: 16.4392
REMARK 3 S TENSOR
REMARK 3 S11: -0.7001 S12: 0.0366 S13: 0.7685
REMARK 3 S21: 0.2533 S22: 0.7954 S23: -0.6688
REMARK 3 S31: 0.5226 S32: 0.8039 S33: -0.0953
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 36 A 60
REMARK 3 ORIGIN FOR THE GROUP (A): 79.2784 41.4957 133.7179
REMARK 3 T TENSOR
REMARK 3 T11: 0.1700 T22: -0.1038
REMARK 3 T33: -0.1860 T12: 0.0177
REMARK 3 T13: -0.1121 T23: -0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 15.3801 L22: 2.9060
REMARK 3 L33: 4.8527 L12: 0.3647
REMARK 3 L13: -1.4259 L23: 0.1500
REMARK 3 S TENSOR
REMARK 3 S11: -0.0945 S12: 0.4224 S13: 1.2259
REMARK 3 S21: -0.2057 S22: -0.0803 S23: -0.4096
REMARK 3 S31: -1.1259 S32: -0.0102 S33: 0.1748
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 61 A 89
REMARK 3 ORIGIN FOR THE GROUP (A): 76.9604 36.0452 139.5102
REMARK 3 T TENSOR
REMARK 3 T11: 0.1386 T22: 0.0615
REMARK 3 T33: -0.1598 T12: 0.0908
REMARK 3 T13: -0.0895 T23: -0.1463
REMARK 3 L TENSOR
REMARK 3 L11: 8.7295 L22: 1.2063
REMARK 3 L33: 2.9805 L12: -1.2168
REMARK 3 L13: 3.6017 L23: -1.1064
REMARK 3 S TENSOR
REMARK 3 S11: 0.1776 S12: -0.5142 S13: 0.1282
REMARK 3 S21: 0.0620 S22: -0.2648 S23: -0.1117
REMARK 3 S31: -0.4284 S32: -0.4634 S33: 0.0872
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 90 A 100
REMARK 3 ORIGIN FOR THE GROUP (A): 83.6863 39.9627 146.0872
REMARK 3 T TENSOR
REMARK 3 T11: 0.1222 T22: -0.0627
REMARK 3 T33: -0.1088 T12: -0.0284
REMARK 3 T13: -0.1114 T23: -0.0953
REMARK 3 L TENSOR
REMARK 3 L11: 17.1142 L22: 1.1501
REMARK 3 L33: 9.7074 L12: -2.0592
REMARK 3 L13: -1.3794 L23: -0.4021
REMARK 3 S TENSOR
REMARK 3 S11: -0.0879 S12: -0.1882 S13: 1.6104
REMARK 3 S21: -0.1018 S22: -0.1291 S23: -0.3698
REMARK 3 S31: -1.1102 S32: 0.5859 S33: 0.2170
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 101 A 122
REMARK 3 ORIGIN FOR THE GROUP (A): 69.6351 33.6623 152.5738
REMARK 3 T TENSOR
REMARK 3 T11: -0.0797 T22: 0.2098
REMARK 3 T33: -0.2291 T12: 0.0927
REMARK 3 T13: 0.0235 T23: -0.1734
REMARK 3 L TENSOR
REMARK 3 L11: 2.2272 L22: 2.7884
REMARK 3 L33: 9.6638 L12: -0.2232
REMARK 3 L13: 1.3444 L23: -0.6170
REMARK 3 S TENSOR
REMARK 3 S11: -0.0246 S12: -0.6747 S13: 0.1841
REMARK 3 S21: 0.4501 S22: -0.2518 S23: 0.2771
REMARK 3 S31: -0.8848 S32: -1.3492 S33: 0.2764
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 : A 123 A 149
REMARK 3 ORIGIN FOR THE GROUP (A): 70.2872 24.5040 152.6217
REMARK 3 T TENSOR
REMARK 3 T11: -0.0569 T22: 0.3390
REMARK 3 T33: -0.2601 T12: -0.1013
REMARK 3 T13: 0.0899 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 1.5496 L22: 3.3327
REMARK 3 L33: 4.0338 L12: -1.4441
REMARK 3 L13: 1.1086 L23: 1.2403
REMARK 3 S TENSOR
REMARK 3 S11: -0.0530 S12: -0.4549 S13: 0.0092
REMARK 3 S21: 0.3697 S22: -0.1128 S23: 0.3949
REMARK 3 S31: 0.2657 S32: -1.0078 S33: 0.1658
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 : A 150 A 176
REMARK 3 ORIGIN FOR THE GROUP (A): 72.8052 23.9128 147.4054
REMARK 3 T TENSOR
REMARK 3 T11: -0.0387 T22: 0.1983
REMARK 3 T33: -0.2278 T12: -0.0134
REMARK 3 T13: 0.0550 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 3.0923 L22: 3.4720
REMARK 3 L33: 3.9869 L12: 2.3216
REMARK 3 L13: 2.2820 L23: 2.0980
REMARK 3 S TENSOR
REMARK 3 S11: -0.0893 S12: -0.3601 S13: -0.0571
REMARK 3 S21: 0.2275 S22: -0.0627 S23: 0.2354
REMARK 3 S31: 0.0513 S32: -0.6867 S33: 0.1520
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 : A 177 A 208
REMARK 3 ORIGIN FOR THE GROUP (A): 77.1445 25.0766 160.5712
REMARK 3 T TENSOR
REMARK 3 T11: 0.0736 T22: 0.3617
REMARK 3 T33: -0.3438 T12: -0.0442
REMARK 3 T13: 0.0481 T23: 0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.0498 L22: 1.3484
REMARK 3 L33: 1.5240 L12: -0.9013
REMARK 3 L13: -0.1420 L23: 1.6469
REMARK 3 S TENSOR
REMARK 3 S11: -0.1923 S12: -0.6439 S13: -0.0084
REMARK 3 S21: 0.6948 S22: -0.0488 S23: 0.0418
REMARK 3 S31: 0.1263 S32: -0.6001 S33: 0.2411
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 : A 209 A 237
REMARK 3 ORIGIN FOR THE GROUP (A): 78.2425 14.9043 155.9425
REMARK 3 T TENSOR
REMARK 3 T11: 0.1115 T22: 0.1631
REMARK 3 T33: -0.2928 T12: -0.1703
REMARK 3 T13: 0.0204 T23: 0.1235
REMARK 3 L TENSOR
REMARK 3 L11: 4.7870 L22: 1.1727
REMARK 3 L33: 1.9946 L12: 1.4285
REMARK 3 L13: -1.0557 L23: 2.6321
REMARK 3 S TENSOR
REMARK 3 S11: -0.0858 S12: -0.7077 S13: -0.3401
REMARK 3 S21: 0.5390 S22: -0.0097 S23: -0.1500
REMARK 3 S31: 0.9164 S32: -0.6536 S33: 0.0955
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 : A 238 A 272
REMARK 3 ORIGIN FOR THE GROUP (A): 96.4881 22.5207 149.2701
REMARK 3 T TENSOR
REMARK 3 T11: -0.0400 T22: -0.0551
REMARK 3 T33: -0.0890 T12: 0.0174
REMARK 3 T13: -0.1188 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 3.7040 L22: 2.4818
REMARK 3 L33: 3.9016 L12: 0.5265
REMARK 3 L13: 0.7170 L23: 0.6221
REMARK 3 S TENSOR
REMARK 3 S11: -0.0359 S12: -0.1994 S13: -0.0450
REMARK 3 S21: 0.3256 S22: 0.1996 S23: -0.6722
REMARK 3 S31: 0.1344 S32: 0.4081 S33: -0.1637
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 : A 273 A 306
REMARK 3 ORIGIN FOR THE GROUP (A): 88.8449 11.1438 151.8790
REMARK 3 T TENSOR
REMARK 3 T11: 0.1166 T22: -0.0495
REMARK 3 T33: -0.2133 T12: 0.0294
REMARK 3 T13: -0.0838 T23: 0.0831
REMARK 3 L TENSOR
REMARK 3 L11: 2.9063 L22: 2.5805
REMARK 3 L33: 4.9452 L12: -0.0670
REMARK 3 L13: 2.3491 L23: 1.0520
REMARK 3 S TENSOR
REMARK 3 S11: 0.2131 S12: -0.3664 S13: -0.3045
REMARK 3 S21: 0.5735 S22: 0.1293 S23: -0.3164
REMARK 3 S31: 0.9062 S32: 0.0127 S33: -0.3423
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 : A 307 A 336
REMARK 3 ORIGIN FOR THE GROUP (A): 83.9705 7.0061 144.5282
REMARK 3 T TENSOR
REMARK 3 T11: 0.1394 T22: -0.1078
REMARK 3 T33: -0.1553 T12: -0.0781
REMARK 3 T13: -0.0561 T23: 0.0975
REMARK 3 L TENSOR
REMARK 3 L11: 3.5908 L22: 3.3322
REMARK 3 L33: 5.5298 L12: -1.4705
REMARK 3 L13: 2.3935 L23: -2.1275
REMARK 3 S TENSOR
REMARK 3 S11: 0.3110 S12: -0.2742 S13: -0.6396
REMARK 3 S21: 0.3372 S22: -0.0814 S23: -0.1232
REMARK 3 S31: 1.0084 S32: -0.2103 S33: -0.2297
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 : A 337 A 350
REMARK 3 ORIGIN FOR THE GROUP (A): 70.9594 10.5045 143.4769
REMARK 3 T TENSOR
REMARK 3 T11: 0.0144 T22: 0.0492
REMARK 3 T33: -0.1780 T12: -0.1931
REMARK 3 T13: 0.0570 T23: 0.0793
REMARK 3 L TENSOR
REMARK 3 L11: 9.6956 L22: 5.0748
REMARK 3 L33: 11.2777 L12: 4.8333
REMARK 3 L13: -3.2579 L23: -4.2781
REMARK 3 S TENSOR
REMARK 3 S11: 0.2279 S12: -0.1155 S13: -0.7705
REMARK 3 S21: 0.3597 S22: -0.2156 S23: 0.0502
REMARK 3 S31: 0.8865 S32: -0.6730 S33: -0.0123
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 : A 351 A 366
REMARK 3 ORIGIN FOR THE GROUP (A): 77.4760 0.2110 144.9677
REMARK 3 T TENSOR
REMARK 3 T11: 0.2516 T22: -0.3287
REMARK 3 T33: -0.1036 T12: -0.3034
REMARK 3 T13: -0.1485 T23: 0.0828
REMARK 3 L TENSOR
REMARK 3 L11: 51.2325 L22: 14.5749
REMARK 3 L33: 9.0092 L12: -18.6466
REMARK 3 L13: -17.6795 L23: 5.8692
REMARK 3 S TENSOR
REMARK 3 S11: -1.0619 S12: -1.9183 S13: -2.3055
REMARK 3 S21: 0.6002 S22: 0.7554 S23: 0.3855
REMARK 3 S31: 1.2957 S32: 0.0936 S33: 0.3066
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 : B 6 B 28
REMARK 3 ORIGIN FOR THE GROUP (A): 76.5553 22.7097 117.3385
REMARK 3 T TENSOR
REMARK 3 T11: -0.1134 T22: 0.0582
REMARK 3 T33: -0.0838 T12: 0.0709
REMARK 3 T13: 0.0269 T23: -0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 3.1838 L22: 2.0808
REMARK 3 L33: 5.3872 L12: 1.8041
REMARK 3 L13: 5.0378 L23: 0.1324
REMARK 3 S TENSOR
REMARK 3 S11: 0.0111 S12: 0.3190 S13: 0.1072
REMARK 3 S21: -0.0415 S22: -0.0686 S23: -0.1627
REMARK 3 S31: -0.0051 S32: 0.6141 S33: 0.0575
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 : B 29 B 55
REMARK 3 ORIGIN FOR THE GROUP (A): 77.8648 10.3788 119.0301
REMARK 3 T TENSOR
REMARK 3 T11: -0.0110 T22: -0.0228
REMARK 3 T33: -0.0694 T12: 0.0670
REMARK 3 T13: -0.0513 T23: -0.0969
REMARK 3 L TENSOR
REMARK 3 L11: 7.5428 L22: 2.9476
REMARK 3 L33: 3.8200 L12: 2.6637
REMARK 3 L13: 0.6896 L23: 0.6571
REMARK 3 S TENSOR
REMARK 3 S11: 0.0138 S12: 0.1782 S13: -0.1783
REMARK 3 S21: -0.3058 S22: 0.1085 S23: -0.1717
REMARK 3 S31: 0.9392 S32: 0.4693 S33: -0.1223
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 : B 56 B 66
REMARK 3 ORIGIN FOR THE GROUP (A): 64.7786 4.8101 135.9422
REMARK 3 T TENSOR
REMARK 3 T11: 0.0186 T22: 0.0788
REMARK 3 T33: -0.1412 T12: -0.2800
REMARK 3 T13: 0.0280 T23: 0.0433
REMARK 3 L TENSOR
REMARK 3 L11: -3.2840 L22: 20.6794
REMARK 3 L33: 32.9756 L12: 11.1727
REMARK 3 L13: -1.7515 L23: 4.1487
REMARK 3 S TENSOR
REMARK 3 S11: 0.5785 S12: -0.2887 S13: -0.3047
REMARK 3 S21: -0.1221 S22: 0.3293 S23: 1.0834
REMARK 3 S31: 2.0331 S32: -0.6500 S33: -0.9078
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 67 B 89
REMARK 3 ORIGIN FOR THE GROUP (A): 68.5750 13.6844 117.4541
REMARK 3 T TENSOR
REMARK 3 T11: -0.0179 T22: 0.0119
REMARK 3 T33: -0.0950 T12: -0.0774
REMARK 3 T13: -0.0301 T23: -0.0836
REMARK 3 L TENSOR
REMARK 3 L11: 1.8039 L22: 1.3206
REMARK 3 L33: 12.7344 L12: 0.6360
REMARK 3 L13: 0.2805 L23: -2.9766
REMARK 3 S TENSOR
REMARK 3 S11: 0.2046 S12: -0.0139 S13: -0.2095
REMARK 3 S21: -0.1161 S22: -0.1972 S23: 0.0811
REMARK 3 S31: 0.6344 S32: -0.4818 S33: -0.0074
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 90 B 108
REMARK 3 ORIGIN FOR THE GROUP (A): 62.2834 9.1374 117.6898
REMARK 3 T TENSOR
REMARK 3 T11: -0.0626 T22: 0.0616
REMARK 3 T33: -0.1054 T12: -0.1850
REMARK 3 T13: -0.0532 T23: -0.0441
REMARK 3 L TENSOR
REMARK 3 L11: 1.9259 L22: 4.2988
REMARK 3 L33: 16.3563 L12: 0.1586
REMARK 3 L13: -2.9327 L23: 0.9388
REMARK 3 S TENSOR
REMARK 3 S11: 0.1301 S12: -0.0512 S13: -0.6408
REMARK 3 S21: 0.1497 S22: -0.1785 S23: -0.0039
REMARK 3 S31: 1.7634 S32: -0.8002 S33: 0.0484
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 109 B 120
REMARK 3 ORIGIN FOR THE GROUP (A): 49.5768 14.9102 122.9940
REMARK 3 T TENSOR
REMARK 3 T11: -0.3766 T22: 0.6868
REMARK 3 T33: -0.2178 T12: -0.1740
REMARK 3 T13: 0.1751 T23: -0.0871
REMARK 3 L TENSOR
REMARK 3 L11: 8.3874 L22: 5.3886
REMARK 3 L33: 31.9881 L12: -1.5935
REMARK 3 L13: 12.3867 L23: -2.9248
REMARK 3 S TENSOR
REMARK 3 S11: 0.1937 S12: -0.9989 S13: -0.9023
REMARK 3 S21: 0.2045 S22: -0.1967 S23: 0.4905
REMARK 3 S31: 1.1346 S32: -2.2785 S33: 0.0030
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 121 B 137
REMARK 3 ORIGIN FOR THE GROUP (A): 48.5459 19.1857 123.4101
REMARK 3 T TENSOR
REMARK 3 T11: -0.3935 T22: 0.6453
REMARK 3 T33: -0.1324 T12: -0.1080
REMARK 3 T13: 0.0818 T23: -0.1066
REMARK 3 L TENSOR
REMARK 3 L11: 2.8604 L22: 8.1453
REMARK 3 L33: 15.2395 L12: 0.6847
REMARK 3 L13: -0.5923 L23: 4.6258
REMARK 3 S TENSOR
REMARK 3 S11: 0.0362 S12: -0.7206 S13: -0.0132
REMARK 3 S21: 0.4761 S22: -0.5085 S23: 0.8129
REMARK 3 S31: 0.5342 S32: -1.7400 S33: 0.4722
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 138 B 158
REMARK 3 ORIGIN FOR THE GROUP (A): 58.0178 23.7433 120.5573
REMARK 3 T TENSOR
REMARK 3 T11: -0.1940 T22: 0.3236
REMARK 3 T33: -0.1582 T12: 0.0197
REMARK 3 T13: 0.0155 T23: -0.1056
REMARK 3 L TENSOR
REMARK 3 L11: 2.1594 L22: 2.1886
REMARK 3 L33: 4.4517 L12: -1.0237
REMARK 3 L13: -0.1097 L23: -0.0103
REMARK 3 S TENSOR
REMARK 3 S11: 0.0570 S12: -0.3640 S13: -0.1104
REMARK 3 S21: 0.2031 S22: -0.3800 S23: 0.0767
REMARK 3 S31: -0.0546 S32: -0.8460 S33: 0.3230
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 159 B 178
REMARK 3 ORIGIN FOR THE GROUP (A): 55.3877 23.5874 121.9382
REMARK 3 T TENSOR
REMARK 3 T11: -0.1931 T22: 0.3088
REMARK 3 T33: -0.1724 T12: 0.0027
REMARK 3 T13: 0.0799 T23: -0.0609
REMARK 3 L TENSOR
REMARK 3 L11: 2.8281 L22: 3.0476
REMARK 3 L33: 7.1457 L12: -1.3070
REMARK 3 L13: 1.1277 L23: 3.1592
REMARK 3 S TENSOR
REMARK 3 S11: -0.0188 S12: -0.5260 S13: -0.1760
REMARK 3 S21: 0.2297 S22: -0.2582 S23: 0.4669
REMARK 3 S31: 0.1641 S32: -1.1430 S33: 0.2770
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 179 B 203
REMARK 3 ORIGIN FOR THE GROUP (A): 48.2497 21.3882 110.3458
REMARK 3 T TENSOR
REMARK 3 T11: -0.2808 T22: 0.4832
REMARK 3 T33: -0.0997 T12: 0.0373
REMARK 3 T13: -0.0627 T23: -0.1513
REMARK 3 L TENSOR
REMARK 3 L11: 1.1618 L22: 2.7795
REMARK 3 L33: 7.1906 L12: -0.5352
REMARK 3 L13: -1.3440 L23: 0.6611
REMARK 3 S TENSOR
REMARK 3 S11: 0.1275 S12: -0.5111 S13: -0.2617
REMARK 3 S21: -0.1405 S22: -0.1732 S23: 0.5935
REMARK 3 S31: 0.3219 S32: -1.5172 S33: 0.0457
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 204 B 221
REMARK 3 ORIGIN FOR THE GROUP (A): 49.9321 29.5449 120.3021
REMARK 3 T TENSOR
REMARK 3 T11: -0.1985 T22: 0.4814
REMARK 3 T33: -0.1625 T12: 0.1809
REMARK 3 T13: 0.0223 T23: -0.1587
REMARK 3 L TENSOR
REMARK 3 L11: -0.9716 L22: 3.0813
REMARK 3 L33: 5.1189 L12: 0.8726
REMARK 3 L13: 0.1667 L23: -1.0296
REMARK 3 S TENSOR
REMARK 3 S11: 0.2424 S12: -0.4858 S13: -0.1248
REMARK 3 S21: 0.2474 S22: -0.2658 S23: 0.5582
REMARK 3 S31: -0.1760 S32: -0.9715 S33: 0.0234
REMARK 3
REMARK 3 TLS GROUP : 27
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 222 B 245
REMARK 3 ORIGIN FOR THE GROUP (A): 52.9937 33.9200 111.8985
REMARK 3 T TENSOR
REMARK 3 T11: -0.0865 T22: 0.2395
REMARK 3 T33: -0.1422 T12: 0.2850
REMARK 3 T13: -0.0608 T23: -0.2509
REMARK 3 L TENSOR
REMARK 3 L11: 4.4774 L22: 1.0520
REMARK 3 L33: 3.0610 L12: -0.5446
REMARK 3 L13: 0.5644 L23: -1.8486
REMARK 3 S TENSOR
REMARK 3 S11: 0.0018 S12: -0.5102 S13: 0.1979
REMARK 3 S21: -0.1122 S22: -0.0401 S23: 0.3029
REMARK 3 S31: -0.4701 S32: -0.8709 S33: 0.0383
REMARK 3
REMARK 3 TLS GROUP : 28
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 246 B 309
REMARK 3 ORIGIN FOR THE GROUP (A): 62.4111 32.5120 103.3612
REMARK 3 T TENSOR
REMARK 3 T11: -0.0439 T22: 0.0131
REMARK 3 T33: -0.1456 T12: 0.1507
REMARK 3 T13: -0.0554 T23: -0.0993
REMARK 3 L TENSOR
REMARK 3 L11: 1.4686 L22: 1.4666
REMARK 3 L33: 3.7584 L12: -0.0602
REMARK 3 L13: 1.3025 L23: 1.0861
REMARK 3 S TENSOR
REMARK 3 S11: -0.2334 S12: 0.0494 S13: 0.1335
REMARK 3 S21: -0.1527 S22: -0.0225 S23: 0.0692
REMARK 3 S31: -0.5602 S32: -0.0953 S33: 0.2559
REMARK 3
REMARK 3 TLS GROUP : 29
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 310 B 351
REMARK 3 ORIGIN FOR THE GROUP (A): 61.2089 39.4149 120.3773
REMARK 3 T TENSOR
REMARK 3 T11: 0.0895 T22: 0.1323
REMARK 3 T33: -0.1103 T12: 0.2654
REMARK 3 T13: -0.0851 T23: -0.2130
REMARK 3 L TENSOR
REMARK 3 L11: 1.3197 L22: 0.5227
REMARK 3 L33: 3.4226 L12: 0.4173
REMARK 3 L13: 1.5565 L23: -1.4950
REMARK 3 S TENSOR
REMARK 3 S11: -0.4074 S12: -0.4328 S13: 0.4879
REMARK 3 S21: 0.1674 S22: -0.0238 S23: -0.1422
REMARK 3 S31: -1.0468 S32: -0.4799 S33: 0.4313
REMARK 3
REMARK 3 TLS GROUP : 30
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 352 B 365
REMARK 3 ORIGIN FOR THE GROUP (A): 59.1130 47.7920 120.9040
REMARK 3 T TENSOR
REMARK 3 T11: 0.3768 T22: -0.0434
REMARK 3 T33: -0.2318 T12: 0.3995
REMARK 3 T13: -0.1536 T23: -0.3919
REMARK 3 L TENSOR
REMARK 3 L11: 44.0339 L22: 8.9936
REMARK 3 L33: 33.6313 L12: 13.3557
REMARK 3 L13: -35.8968 L23: -14.5303
REMARK 3 S TENSOR
REMARK 3 S11: -0.5950 S12: -0.0238 S13: 2.2368
REMARK 3 S21: 0.2575 S22: 0.6834 S23: 0.8967
REMARK 3 S31: -0.8680 S32: -1.7511 S33: -0.0885
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: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2JBW COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 14-DEC-2006.
REMARK 100 THE EBI ID CODE IS EBI-30821.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY BEAMLINE PX-BL14.1
REMARK 200 BEAMLINE : PX-BL14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91841
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 172409
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.10
REMARK 200 RESOLUTION RANGE LOW (A) : 35.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 1.9
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.50
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.09
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.25
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.30
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD, SHARP
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEINSOLUTION: 50 MM TRIS-HCL
REMARK 280 PH 7.4, 200 MM NACL, 0.5 M TCEP RESERVOIR: 35% PEG 10000,
REMARK 280 O.1 M TRIS-HCL PH 8.8 HANGING DROP, MIXED 1:1,
REMARK 280 MICROSEEDING
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 28.51000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 295
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS
REMARK 295 IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.
REMARK 295
REMARK 295 APPLIED TO TRANSFORMED TO
REMARK 295 TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD
REMARK 295 M 1 B 8 .. 365 A 8 .. 365 0.342
REMARK 295 M 2 D 15 .. 365 C 15 .. 365 0.429
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: DIMERIC
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A, 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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ALA A -13
REMARK 465 SER A -12
REMARK 465 MSE A -11
REMARK 465 THR A -10
REMARK 465 GLY A -9
REMARK 465 GLY A -8
REMARK 465 GLN A -7
REMARK 465 GLN A -6
REMARK 465 MSE A -5
REMARK 465 GLY A -4
REMARK 465 ARG A -3
REMARK 465 ASP A -2
REMARK 465 PRO A -1
REMARK 465 GLY A 0
REMARK 465 MSE A 1
REMARK 465 THR A 2
REMARK 465 VAL A 3
REMARK 465 THR A 4
REMARK 465 SER A 5
REMARK 465 GLN A 6
REMARK 465 VAL A 7
REMARK 465 HIS A 368
REMARK 465 HIS A 369
REMARK 465 HIS A 370
REMARK 465 HIS A 371
REMARK 465 HIS A 372
REMARK 465 ALA B -13
REMARK 465 SER B -12
REMARK 465 MSE B -11
REMARK 465 THR B -10
REMARK 465 GLY B -9
REMARK 465 GLY B -8
REMARK 465 GLN B -7
REMARK 465 GLN B -6
REMARK 465 MSE B -5
REMARK 465 GLY B -4
REMARK 465 ARG B -3
REMARK 465 ASP B -2
REMARK 465 PRO B -1
REMARK 465 GLY B 0
REMARK 465 MSE B 1
REMARK 465 THR B 2
REMARK 465 VAL B 3
REMARK 465 THR B 4
REMARK 465 SER B 5
REMARK 465 HIS B 367
REMARK 465 HIS B 368
REMARK 465 HIS B 369
REMARK 465 HIS B 370
REMARK 465 HIS B 371
REMARK 465 HIS B 372
REMARK 465 ALA C -13
REMARK 465 SER C -12
REMARK 465 MSE C -11
REMARK 465 THR C -10
REMARK 465 GLY C -9
REMARK 465 GLY C -8
REMARK 465 GLN C -7
REMARK 465 GLN C -6
REMARK 465 MSE C -5
REMARK 465 GLY C -4
REMARK 465 ARG C -3
REMARK 465 ASP C -2
REMARK 465 PRO C -1
REMARK 465 GLY C 0
REMARK 465 MSE C 1
REMARK 465 THR C 2
REMARK 465 VAL C 3
REMARK 465 THR C 4
REMARK 465 SER C 5
REMARK 465 GLN C 6
REMARK 465 VAL C 7
REMARK 465 LYS C 8
REMARK 465 PRO C 9
REMARK 465 GLU C 10
REMARK 465 ASP C 11
REMARK 465 GLU C 12
REMARK 465 MSE C 13
REMARK 465 ASP C 14
REMARK 465 HIS C 367
REMARK 465 HIS C 368
REMARK 465 HIS C 369
REMARK 465 HIS C 370
REMARK 465 HIS C 371
REMARK 465 HIS C 372
REMARK 465 ALA D -13
REMARK 465 SER D -12
REMARK 465 MSE D -11
REMARK 465 THR D -10
REMARK 465 GLY D -9
REMARK 465 GLY D -8
REMARK 465 GLN D -7
REMARK 465 GLN D -6
REMARK 465 MSE D -5
REMARK 465 GLY D -4
REMARK 465 ARG D -3
REMARK 465 ASP D -2
REMARK 465 PRO D -1
REMARK 465 GLY D 0
REMARK 465 MSE D 1
REMARK 465 THR D 2
REMARK 465 VAL D 3
REMARK 465 THR D 4
REMARK 465 SER D 5
REMARK 465 GLN D 6
REMARK 465 HIS D 367
REMARK 465 HIS D 368
REMARK 465 HIS D 369
REMARK 465 HIS D 370
REMARK 465 HIS D 371
REMARK 465 HIS D 372
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 HIS A 367 CA C O CB CG ND1 CD2 CE1 NE2
REMARK 470 GLN B 6 CG CD OE1 NE2
REMARK 470 LYS B 355 CG CD CE NZ
REMARK 470 GLU B 366 CA C O CB CG CD OE1 OE2
REMARK 470 GLU C 366 CA C O CB CG CD OE1 OE2
REMARK 470 GLU D 366 CA C O CB CG CD OE1 OE2
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ALA B 352 N - CA - C ANGL. DEV. = 9.6 DEGREES
REMARK 500 LYS B 354 CB - CA - C ANGL. DEV. = -10.6 DEGREES
REMARK 500 LYS B 354 CG - CD - CE ANGL. DEV. = 9.5 DEGREES
REMARK 500 LEU C 268 CA - CB - CG ANGL. DEV. = 9.4 DEGREES
REMARK 500 LEU D 48 CA - CB - CG ANGL. DEV. = 10.2 DEGREES
REMARK 500 LEU D 72 CA - CB - CG ANGL. DEV. = 9.3 DEGREES
REMARK 500 LEU D 72 CB - CG - CD1 ANGL. DEV. = 11.5 DEGREES
REMARK 500 LEU D 85 CB - CG - CD1 ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG D 97 CG - CD - NE ANGL. DEV. = -10.5 DEGREES
REMARK 500 LYS D 260 CD - CE - NZ ANGL. DEV. = -10.0 DEGREES
REMARK 500 LEU D 321 CA - CB - CG ANGL. DEV. = 9.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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 AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 198 CB ASP A 198 CG 0.308
REMARK 500 GLU A 204 CD GLU A 204 OE2 0.186
REMARK 500 ASP A 209 CB ASP A 209 CG 0.202
REMARK 500 ASP A 209 CG ASP A 209 OD2 0.169
REMARK 500 PRO A 231 C PRO A 231 O 0.153
REMARK 500 LEU A 233 C LEU A 233 O 0.201
REMARK 500 LEU A 233 C ALA A 234 N 0.154
REMARK 500 GLU B 114 CD GLU B 114 OE2 0.158
REMARK 500 LYS B 202 CE LYS B 202 NZ 0.167
REMARK 500 ASN B 208 CG ASN B 208 ND2 0.156
REMARK 500 ALA B 234 CA ALA B 234 CB 0.160
REMARK 500 VAL B 351 C VAL B 351 O 0.220
REMARK 500 ALA B 352 C ALA B 352 O 0.157
REMARK 500 GLY B 353 N GLY B 353 CA 0.355
REMARK 500 LYS B 354 C LYS B 354 O 0.214
REMARK 500 LYS B 354 CD LYS B 354 CE 0.927
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CE MSE A 13 O HOH Z 17 2.11
REMARK 500 OE2 GLU C 53 NZ LYS C 104 2.13
REMARK 500 CD2 HIS C 138 O HOH X 168 2.09
REMARK 500 OD1 ASP D 11 O HOH W 8 2.17
REMARK 500 NE2 GLN D 54 O HOH W 70 1.98
REMARK 500 CD2 HIS D 138 O HOH W 188 2.19
REMARK 500 O HOH W 50 O HOH W 120 2.15
REMARK 500 O HOH Z 6 O HOH Z 10 2.09
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 525 B Y
REMARK 525 C X
REMARK 525 D W
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 FOR METAL ATOM NA NA A1368 THE COORDINATION ANGLES ARE:
REMARK 600 1 LEU 203A O
REMARK 600 2 ILE 206A O 104.4
REMARK 600 3 ASN 208A OD1 164.4 88.4
REMARK 600 1 2
REMARK 600
REMARK 600 FOR METAL ATOM NA NA B1367 THE COORDINATION ANGLES ARE:
REMARK 600 1 LEU 203B O
REMARK 600 2 ASN 208B OD1 162.9
REMARK 600 1
REMARK 600
REMARK 600 FOR METAL ATOM NA NA C1367 THE COORDINATION ANGLES ARE:
REMARK 600 1 LEU 203C O
REMARK 600 2 HOH 169X O 96.8
REMARK 600 3 LEU 200C O 91.8 160.9
REMARK 600 4 ILE 206C O 98.6 82.8 112.8
REMARK 600 1 2 3
REMARK 600
REMARK 600 FOR METAL ATOM NA NA D1367 THE COORDINATION ANGLES ARE:
REMARK 600 1 ILE 206D O
REMARK 600 2 ASN 208D OD1 90.0
REMARK 600 3 LEU 203D O 95.5 171.3
REMARK 600 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: TRI
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIADS
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS1
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE RESIDUES CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS2
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE RESIDUES CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS3
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE RESIDUES CHAIN C
REMARK 800
REMARK 800 SITE_IDENTIFIER: AS4
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE RESIDUES CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: NA BINDING SITE FOR CHAIN D
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: NA BINDING SITE FOR CHAIN B
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: NA BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: NA BINDING SITE FOR CHAIN C
DBREF 2JBW A -13 0 PDB 2JBW 2JBW -13 0
DBREF 2JBW A 1 365 UNP Q93NG6 Q93NG6_ARTNI 1 365
DBREF 2JBW A 366 372 PDB 2JBW 2JBW 366 372
DBREF 2JBW B -13 0 PDB 2JBW 2JBW -13 0
DBREF 2JBW B 1 365 UNP Q93NG6 Q93NG6_ARTNI 1 365
DBREF 2JBW B 366 372 PDB 2JBW 2JBW 366 372
DBREF 2JBW C -13 0 PDB 2JBW 2JBW -13 0
DBREF 2JBW C 1 365 UNP Q93NG6 Q93NG6_ARTNI 1 365
DBREF 2JBW C 366 372 PDB 2JBW 2JBW 366 372
DBREF 2JBW D -13 0 PDB 2JBW 2JBW -13 0
DBREF 2JBW D 1 365 UNP Q93NG6 Q93NG6_ARTNI 1 365
DBREF 2JBW D 366 372 PDB 2JBW 2JBW 366 372
SEQADV 2JBW ASP A 14 UNP Q93NG6 LEU 14 CONFLICT
SEQADV 2JBW ASP B 14 UNP Q93NG6 LEU 14 CONFLICT
SEQADV 2JBW ASP C 14 UNP Q93NG6 LEU 14 CONFLICT
SEQADV 2JBW ASP D 14 UNP Q93NG6 LEU 14 CONFLICT
SEQRES 1 A 386 ALA SER MSE THR GLY GLY GLN GLN MSE GLY ARG ASP PRO
SEQRES 2 A 386 GLY MSE THR VAL THR SER GLN VAL LYS PRO GLU ASP GLU
SEQRES 3 A 386 MSE ASP ASN TRP GLY ARG LEU ILE LEU ASP GLY VAL SER
SEQRES 4 A 386 TYR SER ASP MSE VAL GLY ALA ARG ASP ARG PRO LYS GLU
SEQRES 5 A 386 ILE THR TRP PHE ASP TYR TRP MSE SER LEU ALA ASN GLU
SEQRES 6 A 386 TYR GLU GLN GLU ALA GLU ARG LYS VAL ALA LEU GLY HIS
SEQRES 7 A 386 ASP LEU SER ALA GLY GLU LEU LEU MSE SER ALA ALA LEU
SEQRES 8 A 386 CYS ALA GLN TYR ALA GLN PHE LEU TRP PHE ASP GLU ARG
SEQRES 9 A 386 ARG GLN LYS GLY GLN ALA ARG LYS VAL GLU LEU TYR GLN
SEQRES 10 A 386 LYS ALA ALA PRO LEU LEU SER PRO PRO ALA GLU ARG HIS
SEQRES 11 A 386 GLU LEU VAL VAL ASP GLY ILE PRO MSE PRO VAL TYR VAL
SEQRES 12 A 386 ARG ILE PRO GLU GLY PRO GLY PRO HIS PRO ALA VAL ILE
SEQRES 13 A 386 MSE LEU GLY GLY LEU GLU SER THR LYS GLU GLU SER PHE
SEQRES 14 A 386 GLN MSE GLU ASN LEU VAL LEU ASP ARG GLY MSE ALA THR
SEQRES 15 A 386 ALA THR PHE ASP GLY PRO GLY GLN GLY GLU MSE PHE GLU
SEQRES 16 A 386 TYR LYS ARG ILE ALA GLY ASP TYR GLU LYS TYR THR SER
SEQRES 17 A 386 ALA VAL VAL ASP LEU LEU THR LYS LEU GLU ALA ILE ARG
SEQRES 18 A 386 ASN ASP ALA ILE GLY VAL LEU GLY ARG SER LEU GLY GLY
SEQRES 19 A 386 ASN TYR ALA LEU LYS SER ALA ALA CYS GLU PRO ARG LEU
SEQRES 20 A 386 ALA ALA CYS ILE SER TRP GLY GLY PHE SER ASP LEU ASP
SEQRES 21 A 386 TYR TRP ASP LEU GLU THR PRO LEU THR LYS GLU SER TRP
SEQRES 22 A 386 LYS TYR VAL SER LYS VAL ASP THR LEU GLU GLU ALA ARG
SEQRES 23 A 386 LEU HIS VAL HIS ALA ALA LEU GLU THR ARG ASP VAL LEU
SEQRES 24 A 386 SER GLN ILE ALA CYS PRO THR TYR ILE LEU HIS GLY VAL
SEQRES 25 A 386 HIS ASP GLU VAL PRO LEU SER PHE VAL ASP THR VAL LEU
SEQRES 26 A 386 GLU LEU VAL PRO ALA GLU HIS LEU ASN LEU VAL VAL GLU
SEQRES 27 A 386 LYS ASP GLY ASP HIS CYS CYS HIS ASN LEU GLY ILE ARG
SEQRES 28 A 386 PRO ARG LEU GLU MSE ALA ASP TRP LEU TYR ASP VAL LEU
SEQRES 29 A 386 VAL ALA GLY LYS LYS VAL ALA PRO THR MSE LYS GLY TRP
SEQRES 30 A 386 PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 386 ALA SER MSE THR GLY GLY GLN GLN MSE GLY ARG ASP PRO
SEQRES 2 B 386 GLY MSE THR VAL THR SER GLN VAL LYS PRO GLU ASP GLU
SEQRES 3 B 386 MSE ASP ASN TRP GLY ARG LEU ILE LEU ASP GLY VAL SER
SEQRES 4 B 386 TYR SER ASP MSE VAL GLY ALA ARG ASP ARG PRO LYS GLU
SEQRES 5 B 386 ILE THR TRP PHE ASP TYR TRP MSE SER LEU ALA ASN GLU
SEQRES 6 B 386 TYR GLU GLN GLU ALA GLU ARG LYS VAL ALA LEU GLY HIS
SEQRES 7 B 386 ASP LEU SER ALA GLY GLU LEU LEU MSE SER ALA ALA LEU
SEQRES 8 B 386 CYS ALA GLN TYR ALA GLN PHE LEU TRP PHE ASP GLU ARG
SEQRES 9 B 386 ARG GLN LYS GLY GLN ALA ARG LYS VAL GLU LEU TYR GLN
SEQRES 10 B 386 LYS ALA ALA PRO LEU LEU SER PRO PRO ALA GLU ARG HIS
SEQRES 11 B 386 GLU LEU VAL VAL ASP GLY ILE PRO MSE PRO VAL TYR VAL
SEQRES 12 B 386 ARG ILE PRO GLU GLY PRO GLY PRO HIS PRO ALA VAL ILE
SEQRES 13 B 386 MSE LEU GLY GLY LEU GLU SER THR LYS GLU GLU SER PHE
SEQRES 14 B 386 GLN MSE GLU ASN LEU VAL LEU ASP ARG GLY MSE ALA THR
SEQRES 15 B 386 ALA THR PHE ASP GLY PRO GLY GLN GLY GLU MSE PHE GLU
SEQRES 16 B 386 TYR LYS ARG ILE ALA GLY ASP TYR GLU LYS TYR THR SER
SEQRES 17 B 386 ALA VAL VAL ASP LEU LEU THR LYS LEU GLU ALA ILE ARG
SEQRES 18 B 386 ASN ASP ALA ILE GLY VAL LEU GLY ARG SER LEU GLY GLY
SEQRES 19 B 386 ASN TYR ALA LEU LYS SER ALA ALA CYS GLU PRO ARG LEU
SEQRES 20 B 386 ALA ALA CYS ILE SER TRP GLY GLY PHE SER ASP LEU ASP
SEQRES 21 B 386 TYR TRP ASP LEU GLU THR PRO LEU THR LYS GLU SER TRP
SEQRES 22 B 386 LYS TYR VAL SER LYS VAL ASP THR LEU GLU GLU ALA ARG
SEQRES 23 B 386 LEU HIS VAL HIS ALA ALA LEU GLU THR ARG ASP VAL LEU
SEQRES 24 B 386 SER GLN ILE ALA CYS PRO THR TYR ILE LEU HIS GLY VAL
SEQRES 25 B 386 HIS ASP GLU VAL PRO LEU SER PHE VAL ASP THR VAL LEU
SEQRES 26 B 386 GLU LEU VAL PRO ALA GLU HIS LEU ASN LEU VAL VAL GLU
SEQRES 27 B 386 LYS ASP GLY ASP HIS CYS CYS HIS ASN LEU GLY ILE ARG
SEQRES 28 B 386 PRO ARG LEU GLU MSE ALA ASP TRP LEU TYR ASP VAL LEU
SEQRES 29 B 386 VAL ALA GLY LYS LYS VAL ALA PRO THR MSE LYS GLY TRP
SEQRES 30 B 386 PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 386 ALA SER MSE THR GLY GLY GLN GLN MSE GLY ARG ASP PRO
SEQRES 2 C 386 GLY MSE THR VAL THR SER GLN VAL LYS PRO GLU ASP GLU
SEQRES 3 C 386 MSE ASP ASN TRP GLY ARG LEU ILE LEU ASP GLY VAL SER
SEQRES 4 C 386 TYR SER ASP MSE VAL GLY ALA ARG ASP ARG PRO LYS GLU
SEQRES 5 C 386 ILE THR TRP PHE ASP TYR TRP MSE SER LEU ALA ASN GLU
SEQRES 6 C 386 TYR GLU GLN GLU ALA GLU ARG LYS VAL ALA LEU GLY HIS
SEQRES 7 C 386 ASP LEU SER ALA GLY GLU LEU LEU MSE SER ALA ALA LEU
SEQRES 8 C 386 CYS ALA GLN TYR ALA GLN PHE LEU TRP PHE ASP GLU ARG
SEQRES 9 C 386 ARG GLN LYS GLY GLN ALA ARG LYS VAL GLU LEU TYR GLN
SEQRES 10 C 386 LYS ALA ALA PRO LEU LEU SER PRO PRO ALA GLU ARG HIS
SEQRES 11 C 386 GLU LEU VAL VAL ASP GLY ILE PRO MSE PRO VAL TYR VAL
SEQRES 12 C 386 ARG ILE PRO GLU GLY PRO GLY PRO HIS PRO ALA VAL ILE
SEQRES 13 C 386 MSE LEU GLY GLY LEU GLU SER THR LYS GLU GLU SER PHE
SEQRES 14 C 386 GLN MSE GLU ASN LEU VAL LEU ASP ARG GLY MSE ALA THR
SEQRES 15 C 386 ALA THR PHE ASP GLY PRO GLY GLN GLY GLU MSE PHE GLU
SEQRES 16 C 386 TYR LYS ARG ILE ALA GLY ASP TYR GLU LYS TYR THR SER
SEQRES 17 C 386 ALA VAL VAL ASP LEU LEU THR LYS LEU GLU ALA ILE ARG
SEQRES 18 C 386 ASN ASP ALA ILE GLY VAL LEU GLY ARG SER LEU GLY GLY
SEQRES 19 C 386 ASN TYR ALA LEU LYS SER ALA ALA CYS GLU PRO ARG LEU
SEQRES 20 C 386 ALA ALA CYS ILE SER TRP GLY GLY PHE SER ASP LEU ASP
SEQRES 21 C 386 TYR TRP ASP LEU GLU THR PRO LEU THR LYS GLU SER TRP
SEQRES 22 C 386 LYS TYR VAL SER LYS VAL ASP THR LEU GLU GLU ALA ARG
SEQRES 23 C 386 LEU HIS VAL HIS ALA ALA LEU GLU THR ARG ASP VAL LEU
SEQRES 24 C 386 SER GLN ILE ALA CYS PRO THR TYR ILE LEU HIS GLY VAL
SEQRES 25 C 386 HIS ASP GLU VAL PRO LEU SER PHE VAL ASP THR VAL LEU
SEQRES 26 C 386 GLU LEU VAL PRO ALA GLU HIS LEU ASN LEU VAL VAL GLU
SEQRES 27 C 386 LYS ASP GLY ASP HIS CYS CYS HIS ASN LEU GLY ILE ARG
SEQRES 28 C 386 PRO ARG LEU GLU MSE ALA ASP TRP LEU TYR ASP VAL LEU
SEQRES 29 C 386 VAL ALA GLY LYS LYS VAL ALA PRO THR MSE LYS GLY TRP
SEQRES 30 C 386 PRO LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 D 386 ALA SER MSE THR GLY GLY GLN GLN MSE GLY ARG ASP PRO
SEQRES 2 D 386 GLY MSE THR VAL THR SER GLN VAL LYS PRO GLU ASP GLU
SEQRES 3 D 386 MSE ASP ASN TRP GLY ARG LEU ILE LEU ASP GLY VAL SER
SEQRES 4 D 386 TYR SER ASP MSE VAL GLY ALA ARG ASP ARG PRO LYS GLU
SEQRES 5 D 386 ILE THR TRP PHE ASP TYR TRP MSE SER LEU ALA ASN GLU
SEQRES 6 D 386 TYR GLU GLN GLU ALA GLU ARG LYS VAL ALA LEU GLY HIS
SEQRES 7 D 386 ASP LEU SER ALA GLY GLU LEU LEU MSE SER ALA ALA LEU
SEQRES 8 D 386 CYS ALA GLN TYR ALA GLN PHE LEU TRP PHE ASP GLU ARG
SEQRES 9 D 386 ARG GLN LYS GLY GLN ALA ARG LYS VAL GLU LEU TYR GLN
SEQRES 10 D 386 LYS ALA ALA PRO LEU LEU SER PRO PRO ALA GLU ARG HIS
SEQRES 11 D 386 GLU LEU VAL VAL ASP GLY ILE PRO MSE PRO VAL TYR VAL
SEQRES 12 D 386 ARG ILE PRO GLU GLY PRO GLY PRO HIS PRO ALA VAL ILE
SEQRES 13 D 386 MSE LEU GLY GLY LEU GLU SER THR LYS GLU GLU SER PHE
SEQRES 14 D 386 GLN MSE GLU ASN LEU VAL LEU ASP ARG GLY MSE ALA THR
SEQRES 15 D 386 ALA THR PHE ASP GLY PRO GLY GLN GLY GLU MSE PHE GLU
SEQRES 16 D 386 TYR LYS ARG ILE ALA GLY ASP TYR GLU LYS TYR THR SER
SEQRES 17 D 386 ALA VAL VAL ASP LEU LEU THR LYS LEU GLU ALA ILE ARG
SEQRES 18 D 386 ASN ASP ALA ILE GLY VAL LEU GLY ARG SER LEU GLY GLY
SEQRES 19 D 386 ASN TYR ALA LEU LYS SER ALA ALA CYS GLU PRO ARG LEU
SEQRES 20 D 386 ALA ALA CYS ILE SER TRP GLY GLY PHE SER ASP LEU ASP
SEQRES 21 D 386 TYR TRP ASP LEU GLU THR PRO LEU THR LYS GLU SER TRP
SEQRES 22 D 386 LYS TYR VAL SER LYS VAL ASP THR LEU GLU GLU ALA ARG
SEQRES 23 D 386 LEU HIS VAL HIS ALA ALA LEU GLU THR ARG ASP VAL LEU
SEQRES 24 D 386 SER GLN ILE ALA CYS PRO THR TYR ILE LEU HIS GLY VAL
SEQRES 25 D 386 HIS ASP GLU VAL PRO LEU SER PHE VAL ASP THR VAL LEU
SEQRES 26 D 386 GLU LEU VAL PRO ALA GLU HIS LEU ASN LEU VAL VAL GLU
SEQRES 27 D 386 LYS ASP GLY ASP HIS CYS CYS HIS ASN LEU GLY ILE ARG
SEQRES 28 D 386 PRO ARG LEU GLU MSE ALA ASP TRP LEU TYR ASP VAL LEU
SEQRES 29 D 386 VAL ALA GLY LYS LYS VAL ALA PRO THR MSE LYS GLY TRP
SEQRES 30 D 386 PRO LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 2JBW MSE A 13 MET SELENOMETHIONINE
MODRES 2JBW MSE A 29 MET SELENOMETHIONINE
MODRES 2JBW MSE A 46 MET SELENOMETHIONINE
MODRES 2JBW MSE A 73 MET SELENOMETHIONINE
MODRES 2JBW MSE A 125 MET SELENOMETHIONINE
MODRES 2JBW MSE A 143 MET SELENOMETHIONINE
MODRES 2JBW MSE A 157 MET SELENOMETHIONINE
MODRES 2JBW MSE A 166 MET SELENOMETHIONINE
MODRES 2JBW MSE A 179 MET SELENOMETHIONINE
MODRES 2JBW MSE A 342 MET SELENOMETHIONINE
MODRES 2JBW MSE A 360 MET SELENOMETHIONINE
MODRES 2JBW MSE B 13 MET SELENOMETHIONINE
MODRES 2JBW MSE B 29 MET SELENOMETHIONINE
MODRES 2JBW MSE B 46 MET SELENOMETHIONINE
MODRES 2JBW MSE B 73 MET SELENOMETHIONINE
MODRES 2JBW MSE B 125 MET SELENOMETHIONINE
MODRES 2JBW MSE B 143 MET SELENOMETHIONINE
MODRES 2JBW MSE B 157 MET SELENOMETHIONINE
MODRES 2JBW MSE B 166 MET SELENOMETHIONINE
MODRES 2JBW MSE B 179 MET SELENOMETHIONINE
MODRES 2JBW MSE B 342 MET SELENOMETHIONINE
MODRES 2JBW MSE B 360 MET SELENOMETHIONINE
MODRES 2JBW MSE C 29 MET SELENOMETHIONINE
MODRES 2JBW MSE C 46 MET SELENOMETHIONINE
MODRES 2JBW MSE C 73 MET SELENOMETHIONINE
MODRES 2JBW MSE C 125 MET SELENOMETHIONINE
MODRES 2JBW MSE C 143 MET SELENOMETHIONINE
MODRES 2JBW MSE C 157 MET SELENOMETHIONINE
MODRES 2JBW MSE C 166 MET SELENOMETHIONINE
MODRES 2JBW MSE C 179 MET SELENOMETHIONINE
MODRES 2JBW MSE C 342 MET SELENOMETHIONINE
MODRES 2JBW MSE C 360 MET SELENOMETHIONINE
MODRES 2JBW MSE D 13 MET SELENOMETHIONINE
MODRES 2JBW MSE D 29 MET SELENOMETHIONINE
MODRES 2JBW MSE D 46 MET SELENOMETHIONINE
MODRES 2JBW MSE D 73 MET SELENOMETHIONINE
MODRES 2JBW MSE D 125 MET SELENOMETHIONINE
MODRES 2JBW MSE D 143 MET SELENOMETHIONINE
MODRES 2JBW MSE D 157 MET SELENOMETHIONINE
MODRES 2JBW MSE D 166 MET SELENOMETHIONINE
MODRES 2JBW MSE D 179 MET SELENOMETHIONINE
MODRES 2JBW MSE D 342 MET SELENOMETHIONINE
MODRES 2JBW MSE D 360 MET SELENOMETHIONINE
HET MSE A 13 8
HET MSE A 29 8
HET MSE A 46 8
HET MSE A 73 8
HET MSE A 125 8
HET MSE A 143 8
HET MSE A 157 8
HET MSE A 166 8
HET MSE A 179 8
HET MSE A 342 8
HET MSE A 360 8
HET MSE B 13 8
HET MSE B 29 8
HET MSE B 46 8
HET MSE B 73 8
HET MSE B 125 8
HET MSE B 143 8
HET MSE B 157 8
HET MSE B 166 8
HET MSE B 179 8
HET MSE B 342 8
HET MSE B 360 8
HET MSE C 29 8
HET MSE C 46 8
HET MSE C 73 8
HET MSE C 125 8
HET MSE C 143 8
HET MSE C 157 8
HET MSE C 166 8
HET MSE C 179 8
HET MSE C 342 8
HET MSE C 360 8
HET MSE D 13 8
HET MSE D 29 8
HET MSE D 46 8
HET MSE D 73 8
HET MSE D 125 8
HET MSE D 143 8
HET MSE D 157 8
HET MSE D 166 8
HET MSE D 179 8
HET MSE D 342 8
HET MSE D 360 8
HET NA D1367 1
HET NA B1367 1
HET NA A1368 1
HET NA C1367 1
HETNAM NA SODIUM ION
HETNAM MSE SELENOMETHIONINE
FORMUL 5 NA 4(NA1 1+)
FORMUL 6 MSE 43(C5 H11 N1 O2 SE1)
FORMUL 7 HOH *964(H2 O1)
HELIX 1 1 LYS A 8 ASP A 14 1 7
HELIX 2 2 ASN A 15 GLY A 23 1 9
HELIX 3 3 SER A 25 ASP A 34 1 10
HELIX 4 4 THR A 40 LEU A 62 1 23
HELIX 5 5 HIS A 64 PHE A 84 1 21
HELIX 6 6 GLU A 89 ALA A 106 1 18
HELIX 7 7 PRO A 107 LEU A 109 5 3
HELIX 8 8 SER A 154 ARG A 164 1 11
HELIX 9 9 GLN A 176 PHE A 180 5 5
HELIX 10 10 ASP A 188 LEU A 203 1 16
HELIX 11 11 SER A 217 GLU A 230 1 14
HELIX 12 12 TYR A 247 GLU A 251 5 5
HELIX 13 13 THR A 252 SER A 263 1 12
HELIX 14 14 THR A 267 LEU A 279 1 13
HELIX 15 15 VAL A 284 ILE A 288 5 5
HELIX 16 16 LEU A 304 VAL A 314 1 11
HELIX 17 17 PRO A 315 GLU A 317 5 3
HELIX 18 18 ASP A 328 GLY A 335 5 8
HELIX 19 19 ILE A 336 VAL A 351 1 16
HELIX 20 20 LYS B 8 ASP B 14 1 7
HELIX 21 21 ASN B 15 ASP B 22 1 8
HELIX 22 22 SER B 25 ASP B 34 1 10
HELIX 23 23 THR B 40 LEU B 62 1 23
HELIX 24 24 HIS B 64 PHE B 84 1 21
HELIX 25 25 ARG B 90 ALA B 106 1 17
HELIX 26 26 PRO B 107 LEU B 109 5 3
HELIX 27 27 THR B 150 GLU B 153 5 4
HELIX 28 28 SER B 154 ASP B 163 1 10
HELIX 29 29 TYR B 189 LEU B 203 1 15
HELIX 30 30 SER B 217 CYS B 229 1 13
HELIX 31 31 TYR B 247 GLU B 251 5 5
HELIX 32 32 THR B 252 LYS B 264 1 13
HELIX 33 33 THR B 267 LEU B 279 1 13
HELIX 34 34 VAL B 284 ILE B 288 5 5
HELIX 35 35 LEU B 304 VAL B 314 1 11
HELIX 36 36 ASP B 328 GLY B 335 5 8
HELIX 37 37 ILE B 336 VAL B 351 1 16
HELIX 38 38 ASN C 15 GLY C 23 1 9
HELIX 39 39 SER C 25 ASP C 34 1 10
HELIX 40 40 THR C 40 LEU C 62 1 23
HELIX 41 41 HIS C 64 GLN C 83 1 20
HELIX 42 42 ASP C 88 ALA C 106 1 19
HELIX 43 43 PRO C 107 LEU C 109 5 3
HELIX 44 44 THR C 150 GLU C 153 5 4
HELIX 45 45 SER C 154 ARG C 164 1 11
HELIX 46 46 GLN C 176 LYS C 183 5 8
HELIX 47 47 ASP C 188 LEU C 203 1 16
HELIX 48 48 SER C 217 GLU C 230 1 14
HELIX 49 49 TYR C 247 GLU C 251 5 5
HELIX 50 50 THR C 252 LYS C 264 1 13
HELIX 51 51 THR C 267 LEU C 279 1 13
HELIX 52 52 VAL C 284 ILE C 288 5 5
HELIX 53 53 LEU C 304 VAL C 314 1 11
HELIX 54 54 ASP C 328 GLY C 335 5 8
HELIX 55 55 ILE C 336 VAL C 351 1 16
HELIX 56 56 LYS D 8 GLU D 12 5 5
HELIX 57 57 ASN D 15 GLY D 23 1 9
HELIX 58 58 SER D 25 ASP D 34 1 10
HELIX 59 59 THR D 40 LEU D 62 1 23
HELIX 60 60 HIS D 64 GLN D 83 1 20
HELIX 61 61 ASP D 88 ALA D 106 1 19
HELIX 62 62 PRO D 107 LEU D 109 5 3
HELIX 63 63 THR D 150 GLU D 153 5 4
HELIX 64 64 SER D 154 ARG D 164 1 11
HELIX 65 65 GLN D 176 PHE D 180 5 5
HELIX 66 66 ASP D 188 THR D 201 1 14
HELIX 67 67 SER D 217 GLU D 230 1 14
HELIX 68 68 TYR D 247 GLU D 251 5 5
HELIX 69 69 THR D 252 LYS D 264 1 13
HELIX 70 70 THR D 267 LEU D 279 1 13
HELIX 71 71 VAL D 284 ILE D 288 5 5
HELIX 72 72 LEU D 304 VAL D 314 1 11
HELIX 73 73 ASP D 328 GLY D 335 5 8
HELIX 74 74 ILE D 336 VAL D 351 1 16
SHEET 1 AA 9 ALA A 113 VAL A 120 0
SHEET 2 AA 9 ILE A 123 ARG A 130 -1 O ILE A 123 N VAL A 120
SHEET 3 AA 9 ALA A 167 PHE A 171 -1 O THR A 168 N ARG A 130
SHEET 4 AA 9 HIS A 138 LEU A 144 1 O PRO A 139 N ALA A 167
SHEET 5 AA 9 ILE A 206 ARG A 216 1 N ARG A 207 O HIS A 138
SHEET 6 AA 9 ALA A 235 TRP A 239 1 O ALA A 235 N VAL A 213
SHEET 7 AA 9 THR A 292 GLY A 297 1 O TYR A 293 N SER A 238
SHEET 8 AA 9 LEU A 319 GLU A 324 1 O ASN A 320 N ILE A 294
SHEET 9 AA 9 MSE A 360 LYS A 361 1 O LYS A 361 N VAL A 323
SHEET 1 BA 9 ALA B 113 VAL B 120 0
SHEET 2 BA 9 ILE B 123 ARG B 130 -1 O ILE B 123 N VAL B 120
SHEET 3 BA 9 ALA B 167 PHE B 171 -1 O THR B 168 N ARG B 130
SHEET 4 BA 9 HIS B 138 LEU B 144 1 O PRO B 139 N ALA B 167
SHEET 5 BA 9 ILE B 206 ARG B 216 1 N ARG B 207 O HIS B 138
SHEET 6 BA 9 CYS B 236 TRP B 239 1 O ILE B 237 N GLY B 215
SHEET 7 BA 9 THR B 292 GLY B 297 1 O TYR B 293 N SER B 238
SHEET 8 BA 9 LEU B 319 GLU B 324 1 O ASN B 320 N ILE B 294
SHEET 9 BA 9 THR B 359 LYS B 361 1 O THR B 359 N LEU B 321
SHEET 1 CA 9 ALA C 113 VAL C 120 0
SHEET 2 CA 9 ILE C 123 ARG C 130 -1 O ILE C 123 N VAL C 120
SHEET 3 CA 9 ALA C 167 PHE C 171 -1 O THR C 168 N ARG C 130
SHEET 4 CA 9 HIS C 138 LEU C 144 1 O PRO C 139 N ALA C 167
SHEET 5 CA 9 ILE C 206 ARG C 216 1 N ARG C 207 O HIS C 138
SHEET 6 CA 9 CYS C 236 TRP C 239 1 O ILE C 237 N GLY C 215
SHEET 7 CA 9 THR C 292 GLY C 297 1 O TYR C 293 N SER C 238
SHEET 8 CA 9 LEU C 319 GLU C 324 1 O ASN C 320 N ILE C 294
SHEET 9 CA 9 THR C 359 LYS C 361 1 O THR C 359 N LEU C 321
SHEET 1 DA 9 ALA D 113 VAL D 120 0
SHEET 2 DA 9 ILE D 123 ARG D 130 -1 O ILE D 123 N VAL D 120
SHEET 3 DA 9 ALA D 167 PHE D 171 -1 O THR D 168 N ARG D 130
SHEET 4 DA 9 HIS D 138 LEU D 144 1 O PRO D 139 N ALA D 167
SHEET 5 DA 9 ILE D 206 ARG D 216 1 N ARG D 207 O HIS D 138
SHEET 6 DA 9 CYS D 236 TRP D 239 1 O ILE D 237 N GLY D 215
SHEET 7 DA 9 THR D 292 GLY D 297 1 O TYR D 293 N SER D 238
SHEET 8 DA 9 LEU D 319 GLU D 324 1 O ASN D 320 N ILE D 294
SHEET 9 DA 9 THR D 359 LYS D 361 1 O THR D 359 N LEU D 321
LINK C GLU A 12 N MSE A 13 1555 1555
LINK C MSE A 13 N ASP A 14 1555 1555
LINK C ASP A 28 N MSE A 29 1555 1555
LINK C MSE A 29 N VAL A 30 1555 1555
LINK C TRP A 45 N MSE A 46 1555 1555
LINK C MSE A 46 N SER A 47 1555 1555
LINK C LEU A 72 N MSE A 73 1555 1555
LINK C MSE A 73 N SER A 74 1555 1555
LINK C PRO A 124 N MSE A 125 1555 1555
LINK C MSE A 125 N PRO A 126 1555 1555
LINK C ILE A 142 N MSE A 143 1555 1555
LINK C MSE A 143 N LEU A 144 1555 1555
LINK C GLN A 156 N MSE A 157 1555 1555
LINK C MSE A 157 N GLU A 158 1555 1555
LINK C GLY A 165 N MSE A 166 1555 1555
LINK C MSE A 166 N ALA A 167 1555 1555
LINK C GLU A 178 N MSE A 179 1555 1555
LINK C MSE A 179 N PHE A 180 1555 1555
LINK C GLU A 341 N MSE A 342 1555 1555
LINK C MSE A 342 N ALA A 343 1555 1555
LINK C THR A 359 N MSE A 360 1555 1555
LINK C MSE A 360 N LYS A 361 1555 1555
LINK NA NA A1368 O LEU A 203 1555 1555
LINK NA NA A1368 O ILE A 206 1555 1555
LINK NA NA A1368 OD1 ASN A 208 1555 1555
LINK C GLU B 12 N MSE B 13 1555 1555
LINK C MSE B 13 N ASP B 14 1555 1555
LINK C ASP B 28 N MSE B 29 1555 1555
LINK C MSE B 29 N VAL B 30 1555 1555
LINK C TRP B 45 N MSE B 46 1555 1555
LINK C MSE B 46 N SER B 47 1555 1555
LINK C LEU B 72 N MSE B 73 1555 1555
LINK C MSE B 73 N SER B 74 1555 1555
LINK C PRO B 124 N MSE B 125 1555 1555
LINK C MSE B 125 N PRO B 126 1555 1555
LINK C ILE B 142 N MSE B 143 1555 1555
LINK C MSE B 143 N LEU B 144 1555 1555
LINK C GLN B 156 N MSE B 157 1555 1555
LINK C MSE B 157 N GLU B 158 1555 1555
LINK C GLY B 165 N MSE B 166 1555 1555
LINK C MSE B 166 N ALA B 167 1555 1555
LINK C GLU B 178 N MSE B 179 1555 1555
LINK C MSE B 179 N PHE B 180 1555 1555
LINK C GLU B 341 N MSE B 342 1555 1555
LINK C MSE B 342 N ALA B 343 1555 1555
LINK C THR B 359 N MSE B 360 1555 1555
LINK C MSE B 360 N LYS B 361 1555 1555
LINK NA NA B1367 O LEU B 203 1555 1555
LINK NA NA B1367 OD1 ASN B 208 1555 1555
LINK C ASP C 28 N MSE C 29 1555 1555
LINK C MSE C 29 N VAL C 30 1555 1555
LINK C TRP C 45 N MSE C 46 1555 1555
LINK C MSE C 46 N SER C 47 1555 1555
LINK C LEU C 72 N MSE C 73 1555 1555
LINK C MSE C 73 N SER C 74 1555 1555
LINK C PRO C 124 N MSE C 125 1555 1555
LINK C MSE C 125 N PRO C 126 1555 1555
LINK C ILE C 142 N MSE C 143 1555 1555
LINK C MSE C 143 N LEU C 144 1555 1555
LINK C GLN C 156 N MSE C 157 1555 1555
LINK C MSE C 157 N GLU C 158 1555 1555
LINK C GLY C 165 N MSE C 166 1555 1555
LINK C MSE C 166 N ALA C 167 1555 1555
LINK C GLU C 178 N MSE C 179 1555 1555
LINK C MSE C 179 N PHE C 180 1555 1555
LINK C GLU C 341 N MSE C 342 1555 1555
LINK C MSE C 342 N ALA C 343 1555 1555
LINK C THR C 359 N MSE C 360 1555 1555
LINK C MSE C 360 N LYS C 361 1555 1555
LINK NA NA C1367 O ILE C 206 1555 1555
LINK NA NA C1367 O LEU C 200 1555 1555
LINK NA NA C1367 O HOH X 169 1555 1555
LINK NA NA C1367 O LEU C 203 1555 1555
LINK C GLU D 12 N MSE D 13 1555 1555
LINK C MSE D 13 N ASP D 14 1555 1555
LINK C ASP D 28 N MSE D 29 1555 1555
LINK C MSE D 29 N VAL D 30 1555 1555
LINK C TRP D 45 N MSE D 46 1555 1555
LINK C MSE D 46 N SER D 47 1555 1555
LINK C LEU D 72 N MSE D 73 1555 1555
LINK C MSE D 73 N SER D 74 1555 1555
LINK C PRO D 124 N MSE D 125 1555 1555
LINK C MSE D 125 N PRO D 126 1555 1555
LINK C ILE D 142 N MSE D 143 1555 1555
LINK C MSE D 143 N LEU D 144 1555 1555
LINK C GLN D 156 N MSE D 157 1555 1555
LINK C MSE D 157 N GLU D 158 1555 1555
LINK C GLY D 165 N MSE D 166 1555 1555
LINK C MSE D 166 N ALA D 167 1555 1555
LINK C GLU D 178 N MSE D 179 1555 1555
LINK C MSE D 179 N PHE D 180 1555 1555
LINK C GLU D 341 N MSE D 342 1555 1555
LINK C MSE D 342 N ALA D 343 1555 1555
LINK C THR D 359 N MSE D 360 1555 1555
LINK C MSE D 360 N LYS D 361 1555 1555
LINK NA NA D1367 O LEU D 203 1555 1555
LINK NA NA D1367 OD1 ASN D 208 1555 1555
LINK NA NA D1367 O ILE D 206 1555 1555
CISPEP 1 SER A 110 PRO A 111 0 0.46
CISPEP 2 GLY A 136 PRO A 137 0 -1.62
CISPEP 3 TRP A 363 PRO A 364 0 1.53
CISPEP 4 SER B 110 PRO B 111 0 -4.74
CISPEP 5 GLY B 136 PRO B 137 0 -9.84
CISPEP 6 TRP B 363 PRO B 364 0 -3.69
CISPEP 7 SER C 110 PRO C 111 0 -1.38
CISPEP 8 GLY C 136 PRO C 137 0 -2.05
CISPEP 9 TRP C 363 PRO C 364 0 -3.65
CISPEP 10 SER D 110 PRO D 111 0 -5.02
CISPEP 11 GLY D 136 PRO D 137 0 3.20
CISPEP 12 TRP D 363 PRO D 364 0 -0.70
CISPEP 13 LEU B 365 GLU B 366 0 -27.09
SITE 1 TRI 12 SER A 217 ASP A 300 HIS A 329 SER B 217
SITE 2 TRI 12 ASP B 300 HIS B 329 SER C 217 ASP C 300
SITE 3 TRI 12 HIS C 329 SER D 217 ASP D 300 HIS D 329
SITE 1 AS1 5 ARG A 18 ASP A 22 GLU A 148 SER A 149
SITE 2 AS1 5 ARG A 216
SITE 1 AS2 5 ARG B 18 ASP B 22 GLU B 148 SER B 149
SITE 2 AS2 5 ARG B 216
SITE 1 AS3 5 ARG C 18 ASP C 22 GLU C 148 SER C 149
SITE 2 AS3 5 ARG C 216
SITE 1 AS3 5 ARG D 18 ASP D 22 GLU D 148 SER D 149
SITE 2 AS3 5 ARG D 216
SITE 1 AC1 4 LEU D 200 LEU D 203 ILE D 206 ASN D 208
SITE 1 AC2 6 LEU B 200 THR B 201 LEU B 203 ILE B 206
SITE 2 AC2 6 ASN B 208 HOH Y 95
SITE 1 AC3 5 LEU A 200 THR A 201 LEU A 203 ILE A 206
SITE 2 AC3 5 ASN A 208
SITE 1 AC4 6 LEU C 200 THR C 201 LEU C 203 ILE C 206
SITE 2 AC4 6 ASN C 208 HOH X 169
CRYST1 90.570 57.020 152.697 90.00 103.35 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011041 0.000000 0.002620 0.00000
SCALE2 0.000000 0.017538 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006731 0.00000
MTRIX1 1 0.421495 0.102558 -0.901013 157.08570 1
MTRIX2 1 0.109886 -0.992039 -0.061514 48.19570 1
MTRIX3 1 -0.900149 -0.073081 -0.429409 253.29300 1
MTRIX1 2 0.580614 0.013364 -0.814069 63.86340 1
MTRIX2 2 0.005988 -0.999908 -0.012143 50.72710 1
MTRIX3 2 -0.814157 0.002176 -0.580641 124.82560 1 |