HEADER HYDROLASE/IMMUNE SYSTEM 30-NOV-15 5F1O
TITLE HUMAN CD38 IN COMPLEX WITH NANOBODY MU551
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADP-RIBOSYL CYCLASE/CYCLIC ADP-RIBOSE HYDROLASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ECTODOMAIN, UNP RESIDUES 46-300;
COMPND 5 SYNONYM: CD38;
COMPND 6 EC: 3.2.2.6;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: NANOBODY MU551;
COMPND 11 CHAIN: B;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CD38;
SOURCE 6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: PICHIA PASTORIS;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: X33;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PPICZALPHA;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: LAMA GLAMA;
SOURCE 14 ORGANISM_TAXID: 9844;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PHEN2
KEYWDS CD38, ADP-RIBOSYL CYCLASE, CYCLIC ADP-RIBOSE, X-CRYSTALLOGRAPHY,
KEYWDS 2 CALCIUM SIGNALING, NANOBODY, MU551, HYDROLASE-IMMUNE SYSTEM COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.ZHANG,Q.HAO
REVDAT 2 08-NOV-23 5F1O 1 REMARK
REVDAT 1 15-JUN-16 5F1O 0
JRNL AUTH T.LI,S.QI,M.UNGER,Y.N.HOU,Q.W.DENG,J.LIU,C.M.LAM,X.W.WANG,
JRNL AUTH 2 D.XIN,P.ZHANG,F.KOCH-NOLTE,Q.HAO,H.ZHANG,H.C.LEE,Y.J.ZHAO
JRNL TITL IMMUNO-TARGETING THE MULTIFUNCTIONAL CD38 USING NANOBODY
JRNL REF SCI REP V. 6 27055 2016
JRNL REFN ESSN 2045-2322
JRNL PMID 27251573
JRNL DOI 10.1038/SREP27055
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 22212
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1200
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1257
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.02
REMARK 3 BIN R VALUE (WORKING SET) : 0.1660
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.2470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2958
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 207
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.06000
REMARK 3 B22 (A**2) : 0.94000
REMARK 3 B33 (A**2) : -0.99000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.202
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.131
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.517
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3035 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2769 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4112 ; 1.305 ; 1.934
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6382 ; 0.918 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 365 ; 6.191 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 149 ;38.336 ;23.893
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 513 ;13.670 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;16.052 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 436 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3435 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 730 ; 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): 1472 ; 1.071 ; 1.710
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1471 ; 1.071 ; 1.710
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1833 ; 1.374 ; 2.555
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 5804 ; 0.951 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 71 ;28.620 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5863 ; 4.490 ; 5.000
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 : 16
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 49 A 75
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5710 0.7090 140.2600
REMARK 3 T TENSOR
REMARK 3 T11: 0.1411 T22: 0.0456
REMARK 3 T33: 0.1952 T12: -0.0724
REMARK 3 T13: 0.0283 T23: -0.0428
REMARK 3 L TENSOR
REMARK 3 L11: 4.5470 L22: 4.8249
REMARK 3 L33: 3.7586 L12: -3.4546
REMARK 3 L13: -2.5425 L23: 2.3747
REMARK 3 S TENSOR
REMARK 3 S11: -0.2082 S12: 0.0536 S13: -0.3839
REMARK 3 S21: 0.1035 S22: -0.0807 S23: 0.4398
REMARK 3 S31: 0.3755 S32: -0.2170 S33: 0.2889
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 76 A 86
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3820 -3.6850 143.1280
REMARK 3 T TENSOR
REMARK 3 T11: 0.3655 T22: 0.1166
REMARK 3 T33: 0.0877 T12: 0.1355
REMARK 3 T13: 0.0231 T23: -0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 15.6626 L22: 9.8890
REMARK 3 L33: 20.1111 L12: -7.2312
REMARK 3 L13: -15.0367 L23: 13.0357
REMARK 3 S TENSOR
REMARK 3 S11: -0.7651 S12: -0.1041 S13: -0.4645
REMARK 3 S21: 0.5954 S22: 0.7248 S23: -0.2278
REMARK 3 S31: 1.0020 S32: 0.7440 S33: 0.0403
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 87 A 117
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5900 10.2120 146.7340
REMARK 3 T TENSOR
REMARK 3 T11: 0.0661 T22: 0.0616
REMARK 3 T33: 0.1594 T12: 0.0011
REMARK 3 T13: -0.0118 T23: -0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 4.2895 L22: 4.5966
REMARK 3 L33: 2.2978 L12: -2.6294
REMARK 3 L13: -1.0833 L23: 1.8580
REMARK 3 S TENSOR
REMARK 3 S11: -0.1661 S12: -0.0560 S13: 0.1297
REMARK 3 S21: 0.1547 S22: 0.1851 S23: -0.3294
REMARK 3 S31: 0.1144 S32: 0.1964 S33: -0.0190
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 118 A 138
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0860 7.5980 122.5460
REMARK 3 T TENSOR
REMARK 3 T11: 0.1311 T22: 0.0833
REMARK 3 T33: 0.1049 T12: -0.0337
REMARK 3 T13: 0.0339 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 4.1972 L22: 5.0072
REMARK 3 L33: 3.3279 L12: -1.0800
REMARK 3 L13: -0.0545 L23: 0.8820
REMARK 3 S TENSOR
REMARK 3 S11: 0.0304 S12: 0.0644 S13: -0.0137
REMARK 3 S21: -0.2091 S22: -0.0255 S23: 0.2206
REMARK 3 S31: 0.1714 S32: -0.1319 S33: -0.0048
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 139 A 161
REMARK 3 ORIGIN FOR THE GROUP (A): 22.4860 4.4840 132.5600
REMARK 3 T TENSOR
REMARK 3 T11: 0.1148 T22: 0.0407
REMARK 3 T33: 0.1663 T12: -0.0350
REMARK 3 T13: 0.0179 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 1.3887 L22: 1.9012
REMARK 3 L33: 5.3178 L12: -1.0756
REMARK 3 L13: -1.3204 L23: 1.7068
REMARK 3 S TENSOR
REMARK 3 S11: -0.0207 S12: 0.1339 S13: -0.0532
REMARK 3 S21: -0.1573 S22: -0.0291 S23: -0.0324
REMARK 3 S31: 0.1592 S32: -0.0269 S33: 0.0499
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 162 A 179
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6000 14.4570 147.8580
REMARK 3 T TENSOR
REMARK 3 T11: 0.0193 T22: 0.0984
REMARK 3 T33: 0.1958 T12: -0.0297
REMARK 3 T13: 0.0233 T23: -0.0742
REMARK 3 L TENSOR
REMARK 3 L11: 2.2559 L22: 9.6423
REMARK 3 L33: 3.6771 L12: -1.0899
REMARK 3 L13: -0.6498 L23: -0.1619
REMARK 3 S TENSOR
REMARK 3 S11: -0.1470 S12: 0.0021 S13: -0.1662
REMARK 3 S21: 0.1301 S22: -0.2632 S23: 0.4209
REMARK 3 S31: 0.2130 S32: -0.5461 S33: 0.4102
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 180 A 197
REMARK 3 ORIGIN FOR THE GROUP (A): 23.3070 15.1520 138.8220
REMARK 3 T TENSOR
REMARK 3 T11: 0.0677 T22: 0.0733
REMARK 3 T33: 0.2042 T12: -0.0145
REMARK 3 T13: 0.0011 T23: -0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 5.5843 L22: 1.4141
REMARK 3 L33: 5.6199 L12: -1.1807
REMARK 3 L13: -3.7331 L23: 1.0634
REMARK 3 S TENSOR
REMARK 3 S11: 0.0200 S12: -0.1794 S13: 0.3285
REMARK 3 S21: -0.0532 S22: 0.1005 S23: -0.1711
REMARK 3 S31: -0.0236 S32: 0.1807 S33: -0.1206
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 198 A 225
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3400 18.7750 123.1530
REMARK 3 T TENSOR
REMARK 3 T11: 0.0941 T22: 0.1096
REMARK 3 T33: 0.1161 T12: -0.0396
REMARK 3 T13: 0.0769 T23: -0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 6.3301 L22: 1.7194
REMARK 3 L33: 3.6684 L12: -0.3952
REMARK 3 L13: 2.4746 L23: -0.5138
REMARK 3 S TENSOR
REMARK 3 S11: 0.1417 S12: -0.4272 S13: 0.3473
REMARK 3 S21: -0.0150 S22: -0.0061 S23: 0.0854
REMARK 3 S31: -0.2883 S32: -0.3078 S33: -0.1357
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 226 A 236
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0120 19.4180 127.8280
REMARK 3 T TENSOR
REMARK 3 T11: 0.0646 T22: 0.1207
REMARK 3 T33: 0.1964 T12: -0.0561
REMARK 3 T13: -0.0054 T23: -0.0711
REMARK 3 L TENSOR
REMARK 3 L11: 18.7131 L22: 5.2064
REMARK 3 L33: 9.0795 L12: -8.4470
REMARK 3 L13: -7.8237 L23: 3.9223
REMARK 3 S TENSOR
REMARK 3 S11: -0.3957 S12: -0.3354 S13: 0.0749
REMARK 3 S21: 0.1578 S22: 0.3958 S23: -0.5444
REMARK 3 S31: 0.2462 S32: 0.3315 S33: -0.0001
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 237 A 276
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8300 22.0830 115.4900
REMARK 3 T TENSOR
REMARK 3 T11: 0.1488 T22: 0.0711
REMARK 3 T33: 0.1032 T12: -0.0429
REMARK 3 T13: 0.0749 T23: -0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 3.7382 L22: 1.7965
REMARK 3 L33: 4.3977 L12: 0.3968
REMARK 3 L13: 1.7848 L23: 0.5111
REMARK 3 S TENSOR
REMARK 3 S11: 0.0026 S12: 0.1489 S13: 0.0997
REMARK 3 S21: -0.2782 S22: 0.0426 S23: 0.0296
REMARK 3 S31: -0.4504 S32: 0.0320 S33: -0.0452
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 277 A 296
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8010 4.3420 108.5490
REMARK 3 T TENSOR
REMARK 3 T11: 0.3429 T22: 0.3167
REMARK 3 T33: 0.0436 T12: -0.0549
REMARK 3 T13: 0.0045 T23: -0.0909
REMARK 3 L TENSOR
REMARK 3 L11: 1.4272 L22: 23.1920
REMARK 3 L33: 6.8898 L12: -5.6867
REMARK 3 L13: 1.6467 L23: -6.9865
REMARK 3 S TENSOR
REMARK 3 S11: 0.1285 S12: 0.1583 S13: -0.1013
REMARK 3 S21: -0.6687 S22: -0.2372 S23: 0.3012
REMARK 3 S31: 1.0833 S32: -0.0086 S33: 0.1088
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 1 B 12
REMARK 3 ORIGIN FOR THE GROUP (A): 36.2260 -21.9550 111.7910
REMARK 3 T TENSOR
REMARK 3 T11: 0.2289 T22: 0.1701
REMARK 3 T33: 0.0815 T12: -0.0557
REMARK 3 T13: 0.0772 T23: -0.0815
REMARK 3 L TENSOR
REMARK 3 L11: 19.1939 L22: 22.6558
REMARK 3 L33: 3.7733 L12: -16.9435
REMARK 3 L13: 3.7176 L23: -2.8369
REMARK 3 S TENSOR
REMARK 3 S11: 0.2212 S12: 0.4675 S13: 0.1630
REMARK 3 S21: -0.3870 S22: -0.3139 S23: 0.1805
REMARK 3 S31: -0.1180 S32: 0.1229 S33: 0.0926
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 : B 13 B 86
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6130 -21.7230 122.0540
REMARK 3 T TENSOR
REMARK 3 T11: 0.2242 T22: 0.0356
REMARK 3 T33: 0.0866 T12: -0.0243
REMARK 3 T13: 0.0635 T23: -0.0448
REMARK 3 L TENSOR
REMARK 3 L11: 1.8012 L22: 4.1999
REMARK 3 L33: 2.1665 L12: -1.6231
REMARK 3 L13: -0.6498 L23: 1.0396
REMARK 3 S TENSOR
REMARK 3 S11: -0.1098 S12: -0.0021 S13: -0.1433
REMARK 3 S21: 0.3315 S22: 0.0108 S23: 0.1078
REMARK 3 S31: 0.3933 S32: 0.0919 S33: 0.0990
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 : B 87 B 106
REMARK 3 ORIGIN FOR THE GROUP (A): 29.1070 -20.7530 121.7010
REMARK 3 T TENSOR
REMARK 3 T11: 0.2670 T22: 0.0373
REMARK 3 T33: 0.1839 T12: -0.0344
REMARK 3 T13: 0.0950 T23: -0.0640
REMARK 3 L TENSOR
REMARK 3 L11: 1.5766 L22: 6.6178
REMARK 3 L33: 1.6043 L12: -2.9439
REMARK 3 L13: -1.3204 L23: 2.5935
REMARK 3 S TENSOR
REMARK 3 S11: -0.1781 S12: 0.0985 S13: -0.2593
REMARK 3 S21: 0.6459 S22: -0.1030 S23: 0.4090
REMARK 3 S31: 0.3816 S32: -0.0788 S33: 0.2811
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 : B 107 B 113
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8250 -18.0910 127.8450
REMARK 3 T TENSOR
REMARK 3 T11: 0.3887 T22: 0.1109
REMARK 3 T33: 0.4501 T12: -0.1405
REMARK 3 T13: -0.0243 T23: -0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 48.1826 L22: 14.7575
REMARK 3 L33: 14.0395 L12: 19.3731
REMARK 3 L13: -7.0420 L23: 6.6874
REMARK 3 S TENSOR
REMARK 3 S11: -1.8661 S12: 0.7367 S13: -0.0871
REMARK 3 S21: -0.9272 S22: -0.1348 S23: 1.4085
REMARK 3 S31: -0.0086 S32: -0.6738 S33: 2.0009
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 114 B 128
REMARK 3 ORIGIN FOR THE GROUP (A): 32.2830 -27.2130 114.7870
REMARK 3 T TENSOR
REMARK 3 T11: 0.3043 T22: 0.0918
REMARK 3 T33: 0.1717 T12: -0.0732
REMARK 3 T13: 0.0842 T23: -0.0499
REMARK 3 L TENSOR
REMARK 3 L11: 9.3495 L22: 6.3936
REMARK 3 L33: 3.9291 L12: -4.3596
REMARK 3 L13: -1.3170 L23: 3.3439
REMARK 3 S TENSOR
REMARK 3 S11: 0.0732 S12: 0.0994 S13: -0.4979
REMARK 3 S21: 0.1732 S22: -0.1600 S23: 0.5885
REMARK 3 S31: 0.2609 S32: -0.1294 S33: 0.0867
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5F1O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000215845.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97852
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24162
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 7.600
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 0.46100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1YH3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE, 0.1M TRIS-HCL,
REMARK 280 25% PEG4000, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
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 16.57050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.62700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.09500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.62700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 16.57050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.09500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
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 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 TRP A 46
REMARK 465 ARG A 47
REMARK 465 GLN A 48
REMARK 465 GLY A 246
REMARK 465 ARG A 247
REMARK 465 GLU A 248
REMARK 465 ASP A 249
REMARK 465 ASP A 293
REMARK 465 SER A 294
REMARK 465 SER A 295
REMARK 465 THR A 297
REMARK 465 SER A 298
REMARK 465 GLU A 299
REMARK 465 ILE A 300
REMARK 465 GLU B 129
REMARK 465 PRO B 130
REMARK 465 LYS B 131
REMARK 465 THR B 132
REMARK 465 PRO B 133
REMARK 465 LYS B 134
REMARK 465 PRO B 135
REMARK 465 GLN B 136
REMARK 465 PRO B 137
REMARK 465 ALA B 138
REMARK 465 ALA B 139
REMARK 465 ALA B 140
REMARK 465 HIS B 141
REMARK 465 HIS B 142
REMARK 465 HIS B 143
REMARK 465 HIS B 144
REMARK 465 HIS B 145
REMARK 465 HIS B 146
REMARK 465 GLY B 147
REMARK 465 ALA B 148
REMARK 465 ALA B 149
REMARK 465 GLU B 150
REMARK 465 GLN B 151
REMARK 465 LYS B 152
REMARK 465 LEU B 153
REMARK 465 ILE B 154
REMARK 465 SER B 155
REMARK 465 GLU B 156
REMARK 465 GLU B 157
REMARK 465 ASP B 158
REMARK 465 LEU B 159
REMARK 465 ASN B 160
REMARK 465 GLY B 161
REMARK 465 ALA B 162
REMARK 465 ALA B 163
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 ILE A 128 50.37 -150.20
REMARK 500 ASP A 179 -71.49 -105.03
REMARK 500 ASN A 182 58.44 -92.30
REMARK 500 ASP A 202 -118.32 59.62
REMARK 500 VAL A 225 -62.30 -123.29
REMARK 500 SER B 55 16.77 59.76
REMARK 500 ALA B 92 167.51 179.17
REMARK 500 TYR B 104 74.97 -104.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 560 DISTANCE = 6.51 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5F1K RELATED DB: PDB
REMARK 900 HUMAN CD38 IN COMPLEX WITH NANOBODY MU1053
REMARK 900 RELATED ID: 5F21 RELATED DB: PDB
REMARK 900 HUMAN CD38 IN COMPLEX WITH NANOBODY MU375
DBREF 5F1O A 46 300 UNP P28907 CD38_HUMAN 46 300
DBREF 5F1O B 1 163 PDB 5F1O 5F1O 1 163
SEQADV 5F1O THR A 49 UNP P28907 GLN 49 ENGINEERED MUTATION
SEQADV 5F1O ASP A 100 UNP P28907 ASN 100 ENGINEERED MUTATION
SEQADV 5F1O ASP A 164 UNP P28907 ASN 164 ENGINEERED MUTATION
SEQADV 5F1O ASP A 209 UNP P28907 ASN 209 ENGINEERED MUTATION
SEQADV 5F1O ASP A 219 UNP P28907 ASN 219 ENGINEERED MUTATION
SEQRES 1 A 255 TRP ARG GLN THR TRP SER GLY PRO GLY THR THR LYS ARG
SEQRES 2 A 255 PHE PRO GLU THR VAL LEU ALA ARG CYS VAL LYS TYR THR
SEQRES 3 A 255 GLU ILE HIS PRO GLU MET ARG HIS VAL ASP CYS GLN SER
SEQRES 4 A 255 VAL TRP ASP ALA PHE LYS GLY ALA PHE ILE SER LYS HIS
SEQRES 5 A 255 PRO CYS ASP ILE THR GLU GLU ASP TYR GLN PRO LEU MET
SEQRES 6 A 255 LYS LEU GLY THR GLN THR VAL PRO CYS ASN LYS ILE LEU
SEQRES 7 A 255 LEU TRP SER ARG ILE LYS ASP LEU ALA HIS GLN PHE THR
SEQRES 8 A 255 GLN VAL GLN ARG ASP MET PHE THR LEU GLU ASP THR LEU
SEQRES 9 A 255 LEU GLY TYR LEU ALA ASP ASP LEU THR TRP CYS GLY GLU
SEQRES 10 A 255 PHE ASP THR SER LYS ILE ASN TYR GLN SER CYS PRO ASP
SEQRES 11 A 255 TRP ARG LYS ASP CYS SER ASN ASN PRO VAL SER VAL PHE
SEQRES 12 A 255 TRP LYS THR VAL SER ARG ARG PHE ALA GLU ALA ALA CYS
SEQRES 13 A 255 ASP VAL VAL HIS VAL MET LEU ASP GLY SER ARG SER LYS
SEQRES 14 A 255 ILE PHE ASP LYS ASP SER THR PHE GLY SER VAL GLU VAL
SEQRES 15 A 255 HIS ASN LEU GLN PRO GLU LYS VAL GLN THR LEU GLU ALA
SEQRES 16 A 255 TRP VAL ILE HIS GLY GLY ARG GLU ASP SER ARG ASP LEU
SEQRES 17 A 255 CYS GLN ASP PRO THR ILE LYS GLU LEU GLU SER ILE ILE
SEQRES 18 A 255 SER LYS ARG ASN ILE GLN PHE SER CYS LYS ASN ILE TYR
SEQRES 19 A 255 ARG PRO ASP LYS PHE LEU GLN CYS VAL LYS ASN PRO GLU
SEQRES 20 A 255 ASP SER SER CYS THR SER GLU ILE
SEQRES 1 B 163 ASP VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 B 163 ALA GLY HIS SER LEU ARG LEU SER CYS VAL GLY SER GLY
SEQRES 3 B 163 SER ARG PHE ASP ASN TYR ALA MET GLY TRP PHE ARG GLN
SEQRES 4 B 163 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA ILE SER
SEQRES 5 B 163 TRP SER SER GLY THR THR ARG TYR LEU ASP THR VAL LYS
SEQRES 6 B 163 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SER THR
SEQRES 7 B 163 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR
SEQRES 8 B 163 ALA VAL TYR TYR CYS ALA ALA ARG TYR GLN PRO ARG TYR
SEQRES 9 B 163 TYR ASP SER GLY ASP MET ASP GLY TYR GLU TYR ASP ASN
SEQRES 10 B 163 TRP GLY GLN GLY THR GLN VAL THR VAL SER SER GLU PRO
SEQRES 11 B 163 LYS THR PRO LYS PRO GLN PRO ALA ALA ALA HIS HIS HIS
SEQRES 12 B 163 HIS HIS HIS GLY ALA ALA GLU GLN LYS LEU ILE SER GLU
SEQRES 13 B 163 GLU ASP LEU ASN GLY ALA ALA
FORMUL 3 HOH *207(H2 O)
HELIX 1 AA1 ARG A 58 HIS A 74 1 17
HELIX 2 AA2 PRO A 75 ARG A 78 5 4
HELIX 3 AA3 ASP A 81 ILE A 94 1 14
HELIX 4 AA4 THR A 102 ASP A 105 5 4
HELIX 5 AA5 TYR A 106 THR A 114 1 9
HELIX 6 AA6 ILE A 128 GLN A 139 1 12
HELIX 7 AA7 THR A 144 ASP A 147 5 4
HELIX 8 AA8 THR A 148 ASP A 155 1 8
HELIX 9 AA9 ASN A 183 ALA A 200 1 18
HELIX 10 AB1 SER A 220 VAL A 225 1 6
HELIX 11 AB2 GLU A 226 ASN A 229 5 4
HELIX 12 AB3 ASP A 256 ARG A 269 1 14
HELIX 13 AB4 ARG A 280 ASN A 290 1 11
HELIX 14 AB5 ARG B 28 ASP B 30 5 3
HELIX 15 AB6 ASP B 62 LYS B 65 5 4
HELIX 16 AB7 ASN B 74 LYS B 76 5 3
HELIX 17 AB8 LYS B 87 THR B 91 5 5
HELIX 18 AB9 ASP B 106 GLY B 112 5 7
SHEET 1 AA1 2 GLY A 52 PRO A 53 0
SHEET 2 AA1 2 SER A 172 CYS A 173 -1 O CYS A 173 N GLY A 52
SHEET 1 AA2 4 LEU A 123 SER A 126 0
SHEET 2 AA2 4 ASP A 202 ASP A 209 1 O HIS A 205 N LEU A 124
SHEET 3 AA2 4 VAL A 235 ILE A 243 1 O ILE A 243 N LEU A 208
SHEET 4 AA2 4 GLN A 272 ILE A 278 1 O LYS A 276 N VAL A 242
SHEET 1 AA3 4 VAL B 2 SER B 7 0
SHEET 2 AA3 4 LEU B 18 GLY B 26 -1 O SER B 25 N GLN B 3
SHEET 3 AA3 4 THR B 78 MET B 83 -1 O LEU B 81 N LEU B 20
SHEET 4 AA3 4 PHE B 68 ASP B 73 -1 N ASP B 73 O THR B 78
SHEET 1 AA4 6 GLY B 10 GLN B 13 0
SHEET 2 AA4 6 THR B 122 SER B 127 1 O THR B 125 N GLY B 10
SHEET 3 AA4 6 ALA B 92 TYR B 100 -1 N TYR B 94 O THR B 122
SHEET 4 AA4 6 TYR B 32 GLN B 39 -1 N PHE B 37 O TYR B 95
SHEET 5 AA4 6 GLU B 46 ILE B 51 -1 O ALA B 49 N TRP B 36
SHEET 6 AA4 6 THR B 58 TYR B 60 -1 O ARG B 59 N ALA B 50
SHEET 1 AA5 4 GLY B 10 GLN B 13 0
SHEET 2 AA5 4 THR B 122 SER B 127 1 O THR B 125 N GLY B 10
SHEET 3 AA5 4 ALA B 92 TYR B 100 -1 N TYR B 94 O THR B 122
SHEET 4 AA5 4 ASN B 117 TRP B 118 -1 O ASN B 117 N ALA B 98
SSBOND 1 CYS A 67 CYS A 82 1555 1555 2.16
SSBOND 2 CYS A 99 CYS A 180 1555 1555 2.05
SSBOND 3 CYS A 119 CYS A 201 1555 1555 2.05
SSBOND 4 CYS A 160 CYS A 173 1555 1555 2.13
SSBOND 5 CYS A 254 CYS A 275 1555 1555 2.11
SSBOND 6 CYS A 287 CYS A 296 1555 1555 2.05
SSBOND 7 CYS B 22 CYS B 96 1555 1555 2.07
CRYST1 33.141 96.190 143.254 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.030174 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010396 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006981 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
