HEADER CELL ADHESION 04-APR-07 2PF6
TITLE LUTHERAN GLYCOPROTEIN, N-TERMINAL DOMAINS 1 AND 2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LUTHERAN BLOOD GROUP GLYCOPROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL DOMAINS 1 AND 2;
COMPND 5 SYNONYM: B-CAM CELL SURFACE GLYCOPROTEIN, AUBERGER B ANTIGEN, F8/G253
COMPND 6 ANTIGEN, CD239 ANTIGEN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCAM, LU, MSK19;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PEE
KEYWDS IMMUNOGLOBULIN SUPERFAMILY. CELL ADHESION., CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR N.BURTON,R.L.BRADY
REVDAT 6 30-AUG-23 2PF6 1 REMARK
REVDAT 5 18-OCT-17 2PF6 1 REMARK
REVDAT 4 13-JUL-11 2PF6 1 VERSN
REVDAT 3 24-FEB-09 2PF6 1 VERSN
REVDAT 2 11-MAR-08 2PF6 1 JRNL
REVDAT 1 04-DEC-07 2PF6 0
JRNL AUTH T.J.MANKELOW,N.BURTON,F.O.STEFANSDOTTIR,F.A.SPRING,
JRNL AUTH 2 S.F.PARSONS,J.S.PEDERSEN,C.L.OLIVEIRA,D.LAMMIE,T.WESS,
JRNL AUTH 3 N.MOHANDAS,J.A.CHASIS,R.L.BRADY,D.J.ANSTEE
JRNL TITL THE LAMININ 511/521-BINDING SITE ON THE LUTHERAN BLOOD GROUP
JRNL TITL 2 GLYCOPROTEIN IS LOCATED AT THE FLEXIBLE JUNCTION OF IG
JRNL TITL 3 DOMAINS 2 AND 3.
JRNL REF BLOOD V. 110 3398 2007
JRNL REFN ISSN 0006-4971
JRNL PMID 17638854
JRNL DOI 10.1182/BLOOD-2007-06-094748
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.2.0019
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) : 85.75
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.1
REMARK 3 NUMBER OF REFLECTIONS : 19755
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) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1014
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) : 599
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 39.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.2740
REMARK 3 BIN FREE R VALUE SET COUNT : 26
REMARK 3 BIN FREE R VALUE : 0.2570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3592
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 51
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 45.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.20000
REMARK 3 B22 (A**2) : 1.20000
REMARK 3 B33 (A**2) : -1.80000
REMARK 3 B12 (A**2) : 0.60000
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): 0.442
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.255
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.185
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.231
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3670 ; 0.018 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4986 ; 1.498 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 460 ; 4.801 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 172 ;35.585 ;22.558
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 604 ;14.558 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;18.113 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 552 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2834 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1327 ; 0.219 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2410 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 166 ; 0.144 ; 0.200
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): 102 ; 0.198 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.207 ; 0.200
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): 2364 ; 1.237 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3718 ; 1.561 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1451 ; 2.582 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1268 ; 3.884 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 8 A 36 5
REMARK 3 1 B 8 B 36 5
REMARK 3 2 A 46 A 53 5
REMARK 3 2 B 46 B 53 5
REMARK 3 3 A 57 A 112 5
REMARK 3 3 B 57 B 112 5
REMARK 3 4 A 114 A 154 5
REMARK 3 4 B 114 B 154 5
REMARK 3 5 A 171 A 194 5
REMARK 3 5 B 171 B 194 5
REMARK 3 6 A 203 A 208 5
REMARK 3 6 B 203 B 208 5
REMARK 3 7 A 220 A 231 5
REMARK 3 7 B 220 B 231 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 704 ; 0.360 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 646 ; 0.640 ; 5.000
REMARK 3 MEDIUM THERMAL 1 A (A**2): 704 ; 3.070 ; 2.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 646 ; 3.830 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 40
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 1 A 7
REMARK 3 ORIGIN FOR THE GROUP (A): 41.4620 -4.4553 34.2832
REMARK 3 T TENSOR
REMARK 3 T11: 0.0648 T22: 0.0965
REMARK 3 T33: 0.2779 T12: -0.0353
REMARK 3 T13: -0.0810 T23: 0.0553
REMARK 3 L TENSOR
REMARK 3 L11: 30.2530 L22: 0.8168
REMARK 3 L33: 6.0270 L12: -4.4082
REMARK 3 L13: -9.2572 L23: 2.0953
REMARK 3 S TENSOR
REMARK 3 S11: -0.8809 S12: 0.9975 S13: 0.2198
REMARK 3 S21: -0.1759 S22: -0.0990 S23: -0.1359
REMARK 3 S31: -0.8522 S32: 0.6836 S33: 0.9799
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 8 A 28
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9545 -7.0707 28.6012
REMARK 3 T TENSOR
REMARK 3 T11: 0.1610 T22: 0.1888
REMARK 3 T33: 0.1126 T12: -0.0145
REMARK 3 T13: 0.0193 T23: 0.0408
REMARK 3 L TENSOR
REMARK 3 L11: 10.0539 L22: 2.2759
REMARK 3 L33: 2.2035 L12: 1.4424
REMARK 3 L13: 0.5316 L23: 1.5391
REMARK 3 S TENSOR
REMARK 3 S11: -0.1557 S12: 0.4175 S13: 0.0135
REMARK 3 S21: -0.1950 S22: 0.1220 S23: 0.0185
REMARK 3 S31: -0.1175 S32: 0.0853 S33: 0.0338
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 29 A 35
REMARK 3 ORIGIN FOR THE GROUP (A): 40.9086 -16.1563 34.7871
REMARK 3 T TENSOR
REMARK 3 T11: 0.1549 T22: 0.0937
REMARK 3 T33: 0.1148 T12: -0.0048
REMARK 3 T13: -0.0039 T23: 0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 15.2665 L22: 3.3801
REMARK 3 L33: 10.2832 L12: -1.4660
REMARK 3 L13: -3.5181 L23: 5.8772
REMARK 3 S TENSOR
REMARK 3 S11: -0.3264 S12: -0.6067 S13: -0.8871
REMARK 3 S21: -0.1724 S22: 0.2893 S23: -0.2614
REMARK 3 S31: 0.5053 S32: 0.6763 S33: 0.0372
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 36 A 42
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1889 -9.5243 46.1871
REMARK 3 T TENSOR
REMARK 3 T11: 0.0325 T22: 0.2801
REMARK 3 T33: 0.0972 T12: 0.0914
REMARK 3 T13: -0.0141 T23: 0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 13.6290 L22: 19.3363
REMARK 3 L33: 24.1016 L12: -10.0176
REMARK 3 L13: -13.5445 L23: 16.2291
REMARK 3 S TENSOR
REMARK 3 S11: -0.4912 S12: -0.3986 S13: 0.7559
REMARK 3 S21: 0.7669 S22: 0.3378 S23: 0.9101
REMARK 3 S31: -0.1044 S32: -1.3298 S33: 0.1535
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 43 A 60
REMARK 3 ORIGIN FOR THE GROUP (A): 36.6934 -19.6458 35.0137
REMARK 3 T TENSOR
REMARK 3 T11: 0.0655 T22: 0.1544
REMARK 3 T33: 0.1566 T12: -0.0435
REMARK 3 T13: -0.0285 T23: -0.0458
REMARK 3 L TENSOR
REMARK 3 L11: 1.2572 L22: 5.2699
REMARK 3 L33: 5.0310 L12: -0.4930
REMARK 3 L13: 1.9035 L23: 1.5822
REMARK 3 S TENSOR
REMARK 3 S11: -0.1178 S12: 0.4615 S13: -0.1223
REMARK 3 S21: -0.1970 S22: 0.2941 S23: -0.5734
REMARK 3 S31: 0.1718 S32: 0.8479 S33: -0.1763
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 61 A 67
REMARK 3 ORIGIN FOR THE GROUP (A): 23.9251 -19.7604 39.0999
REMARK 3 T TENSOR
REMARK 3 T11: 0.1782 T22: 0.0993
REMARK 3 T33: 0.1555 T12: -0.0566
REMARK 3 T13: -0.0382 T23: 0.0216
REMARK 3 L TENSOR
REMARK 3 L11: 13.2784 L22: 0.2056
REMARK 3 L33: 11.9878 L12: 0.3944
REMARK 3 L13: 6.4227 L23: 1.5030
REMARK 3 S TENSOR
REMARK 3 S11: 0.0765 S12: -0.8446 S13: -0.1473
REMARK 3 S21: 0.1989 S22: -0.1709 S23: 0.3094
REMARK 3 S31: -0.0927 S32: 0.4069 S33: 0.0944
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 68 A 87
REMARK 3 ORIGIN FOR THE GROUP (A): 24.9986 -15.0550 29.4935
REMARK 3 T TENSOR
REMARK 3 T11: 0.1540 T22: 0.1207
REMARK 3 T33: 0.1599 T12: -0.0356
REMARK 3 T13: -0.0123 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 1.5374 L22: 1.1900
REMARK 3 L33: 2.9668 L12: 0.5882
REMARK 3 L13: -0.9127 L23: -1.8789
REMARK 3 S TENSOR
REMARK 3 S11: -0.1775 S12: 0.0716 S13: -0.1372
REMARK 3 S21: -0.0916 S22: 0.0847 S23: 0.1203
REMARK 3 S31: 0.0481 S32: -0.1486 S33: 0.0928
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 88 A 102
REMARK 3 ORIGIN FOR THE GROUP (A): 33.8263 -9.8224 38.3784
REMARK 3 T TENSOR
REMARK 3 T11: 0.1870 T22: 0.2082
REMARK 3 T33: 0.1260 T12: 0.0133
REMARK 3 T13: -0.0110 T23: -0.0392
REMARK 3 L TENSOR
REMARK 3 L11: 6.7799 L22: 2.4005
REMARK 3 L33: 0.7025 L12: -1.1995
REMARK 3 L13: 0.6946 L23: -0.9275
REMARK 3 S TENSOR
REMARK 3 S11: 0.0055 S12: -0.1394 S13: 0.1178
REMARK 3 S21: -0.0216 S22: 0.0483 S23: 0.0223
REMARK 3 S31: -0.1541 S32: -0.0428 S33: -0.0537
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 103 A 119
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0901 -3.2598 32.6317
REMARK 3 T TENSOR
REMARK 3 T11: 0.1322 T22: 0.1963
REMARK 3 T33: 0.0951 T12: 0.0276
REMARK 3 T13: 0.0369 T23: 0.0612
REMARK 3 L TENSOR
REMARK 3 L11: 27.0574 L22: 2.3061
REMARK 3 L33: 3.4137 L12: -6.6589
REMARK 3 L13: 9.5013 L23: -2.1112
REMARK 3 S TENSOR
REMARK 3 S11: 0.2831 S12: -0.0356 S13: 0.4306
REMARK 3 S21: -0.0141 S22: -0.2093 S23: -0.0148
REMARK 3 S31: 0.0678 S32: -0.0224 S33: -0.0738
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 120 A 132
REMARK 3 ORIGIN FOR THE GROUP (A): -16.7074 9.6752 31.5958
REMARK 3 T TENSOR
REMARK 3 T11: 0.1259 T22: 0.1480
REMARK 3 T33: 0.1362 T12: -0.0249
REMARK 3 T13: -0.0225 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 10.3096 L22: 2.3999
REMARK 3 L33: 8.4768 L12: -1.0366
REMARK 3 L13: -4.9445 L23: 4.2410
REMARK 3 S TENSOR
REMARK 3 S11: -0.0958 S12: 0.2266 S13: 0.1654
REMARK 3 S21: -0.0185 S22: -0.2336 S23: 0.3472
REMARK 3 S31: -0.0924 S32: -0.2678 S33: 0.3294
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 133 A 143
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5052 10.6208 34.5383
REMARK 3 T TENSOR
REMARK 3 T11: 0.1933 T22: 0.1981
REMARK 3 T33: 0.1133 T12: -0.0169
REMARK 3 T13: -0.0253 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 10.3012 L22: 3.0410
REMARK 3 L33: 3.9084 L12: -1.2860
REMARK 3 L13: -2.9660 L23: -0.5492
REMARK 3 S TENSOR
REMARK 3 S11: -0.1709 S12: 0.3090 S13: -0.1379
REMARK 3 S21: 0.3487 S22: -0.1542 S23: 0.2677
REMARK 3 S31: -0.3765 S32: -0.1432 S33: 0.3250
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 144 A 155
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5914 5.5097 30.8013
REMARK 3 T TENSOR
REMARK 3 T11: 0.1091 T22: 0.2020
REMARK 3 T33: 0.2051 T12: 0.0028
REMARK 3 T13: 0.0412 T23: 0.0478
REMARK 3 L TENSOR
REMARK 3 L11: 6.4547 L22: 3.3989
REMARK 3 L33: 1.4151 L12: -4.3269
REMARK 3 L13: 2.7938 L23: -1.5526
REMARK 3 S TENSOR
REMARK 3 S11: -0.0946 S12: -0.0238 S13: -0.0875
REMARK 3 S21: 0.1323 S22: -0.0750 S23: -0.1874
REMARK 3 S31: 0.0180 S32: 0.1177 S33: 0.1696
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 156 A 164
REMARK 3 ORIGIN FOR THE GROUP (A): -3.2214 19.1818 27.5803
REMARK 3 T TENSOR
REMARK 3 T11: 0.2094 T22: 0.0233
REMARK 3 T33: 0.2048 T12: -0.0037
REMARK 3 T13: -0.0394 T23: -0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 5.9446 L22: 0.2265
REMARK 3 L33: 30.1307 L12: 1.0919
REMARK 3 L13: -4.0850 L23: 0.0914
REMARK 3 S TENSOR
REMARK 3 S11: 0.1687 S12: 0.2990 S13: 0.3722
REMARK 3 S21: 0.0453 S22: -0.1256 S23: -0.2018
REMARK 3 S31: -0.8191 S32: 0.6201 S33: -0.0431
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 165 A 171
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4917 20.2241 40.6465
REMARK 3 T TENSOR
REMARK 3 T11: 0.3069 T22: 0.1062
REMARK 3 T33: 0.1457 T12: -0.0691
REMARK 3 T13: -0.0009 T23: -0.0670
REMARK 3 L TENSOR
REMARK 3 L11: 9.3542 L22: 17.2873
REMARK 3 L33: 4.4213 L12: 8.3311
REMARK 3 L13: -0.1882 L23: -1.2717
REMARK 3 S TENSOR
REMARK 3 S11: 0.0009 S12: -0.7522 S13: -0.7652
REMARK 3 S21: 1.3894 S22: 0.0903 S23: 0.5975
REMARK 3 S31: -0.6075 S32: 0.2977 S33: -0.0912
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 172 A 183
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9047 2.6891 39.5748
REMARK 3 T TENSOR
REMARK 3 T11: 0.1423 T22: 0.1964
REMARK 3 T33: 0.1351 T12: -0.0130
REMARK 3 T13: -0.0427 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 5.8643 L22: 12.2103
REMARK 3 L33: 1.9245 L12: -6.6160
REMARK 3 L13: -1.8106 L23: -0.4080
REMARK 3 S TENSOR
REMARK 3 S11: 0.2014 S12: -0.3853 S13: -0.2275
REMARK 3 S21: -0.5189 S22: -0.2013 S23: -0.2427
REMARK 3 S31: 0.3348 S32: 0.3810 S33: -0.0002
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 : A 184 A 190
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8399 2.2492 35.7579
REMARK 3 T TENSOR
REMARK 3 T11: 0.1274 T22: 0.1722
REMARK 3 T33: 0.1837 T12: 0.0215
REMARK 3 T13: 0.0278 T23: 0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 1.3588 L22: 2.4707
REMARK 3 L33: 4.6688 L12: -1.7330
REMARK 3 L13: 2.4693 L23: -3.3667
REMARK 3 S TENSOR
REMARK 3 S11: 0.3334 S12: 0.1171 S13: -0.1074
REMARK 3 S21: -0.1406 S22: -0.2780 S23: 0.1510
REMARK 3 S31: -0.1999 S32: 0.5152 S33: -0.0554
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 : A 191 A 198
REMARK 3 ORIGIN FOR THE GROUP (A): -13.7773 19.3533 31.5326
REMARK 3 T TENSOR
REMARK 3 T11: 0.1180 T22: 0.1337
REMARK 3 T33: 0.1554 T12: -0.0178
REMARK 3 T13: 0.0190 T23: -0.0329
REMARK 3 L TENSOR
REMARK 3 L11: 7.5802 L22: 13.0841
REMARK 3 L33: 13.6088 L12: -1.1526
REMARK 3 L13: 0.8518 L23: -3.2071
REMARK 3 S TENSOR
REMARK 3 S11: -0.1852 S12: 0.0058 S13: 1.2509
REMARK 3 S21: -0.4496 S22: 0.0789 S23: 0.1652
REMARK 3 S31: -0.9844 S32: -0.7068 S33: 0.1063
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 : A 199 A 208
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2304 13.9898 23.9318
REMARK 3 T TENSOR
REMARK 3 T11: 0.0867 T22: 0.2014
REMARK 3 T33: 0.1944 T12: -0.0224
REMARK 3 T13: 0.0112 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 18.6388 L22: 12.6353
REMARK 3 L33: 4.5896 L12: -11.7943
REMARK 3 L13: 2.8083 L23: -1.4231
REMARK 3 S TENSOR
REMARK 3 S11: -0.0644 S12: 0.5242 S13: -0.0806
REMARK 3 S21: -0.1255 S22: -0.0503 S23: 0.7042
REMARK 3 S31: -0.1736 S32: -0.4879 S33: 0.1147
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 : A 209 A 225
REMARK 3 ORIGIN FOR THE GROUP (A): 7.3159 6.0834 23.8593
REMARK 3 T TENSOR
REMARK 3 T11: 0.0815 T22: 0.2153
REMARK 3 T33: 0.1269 T12: 0.0033
REMARK 3 T13: 0.0336 T23: 0.1150
REMARK 3 L TENSOR
REMARK 3 L11: 34.0716 L22: 3.0955
REMARK 3 L33: 0.5673 L12: -9.1369
REMARK 3 L13: 3.2912 L23: -0.4814
REMARK 3 S TENSOR
REMARK 3 S11: -0.1142 S12: 1.2307 S13: 0.7700
REMARK 3 S21: 0.0747 S22: -0.1994 S23: -0.3921
REMARK 3 S31: -0.1915 S32: 0.2762 S33: 0.3136
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 : A 226 A 231
REMARK 3 ORIGIN FOR THE GROUP (A): -21.2497 11.9817 27.0827
REMARK 3 T TENSOR
REMARK 3 T11: 0.0814 T22: 0.2461
REMARK 3 T33: 0.1229 T12: -0.0092
REMARK 3 T13: -0.0498 T23: 0.0656
REMARK 3 L TENSOR
REMARK 3 L11: 28.1092 L22: 4.3727
REMARK 3 L33: 43.2715 L12: -1.9095
REMARK 3 L13: -23.1219 L23: -0.5853
REMARK 3 S TENSOR
REMARK 3 S11: -0.0132 S12: 1.8409 S13: 0.4469
REMARK 3 S21: -0.2165 S22: 0.4703 S23: 0.6662
REMARK 3 S31: -0.4549 S32: -2.0975 S33: -0.4571
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 1 B 8
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1884 -10.3814 8.3602
REMARK 3 T TENSOR
REMARK 3 T11: 0.1537 T22: 0.2748
REMARK 3 T33: 0.3347 T12: -0.3068
REMARK 3 T13: 0.2940 T23: -0.3189
REMARK 3 L TENSOR
REMARK 3 L11: 5.5513 L22: 83.8402
REMARK 3 L33: 1.3691 L12: 10.3763
REMARK 3 L13: -2.7549 L23: -5.5048
REMARK 3 S TENSOR
REMARK 3 S11: 1.0782 S12: -0.9379 S13: 0.4503
REMARK 3 S21: 4.3203 S22: -2.8626 S23: 4.8403
REMARK 3 S31: 0.8462 S32: -1.3434 S33: 1.7844
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 9 B 17
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7858 7.8264 15.0113
REMARK 3 T TENSOR
REMARK 3 T11: 0.2502 T22: 0.0985
REMARK 3 T33: 0.0448 T12: -0.0214
REMARK 3 T13: 0.0080 T23: 0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 21.5313 L22: 16.2874
REMARK 3 L33: 14.3761 L12: 6.2426
REMARK 3 L13: 5.0258 L23: 8.4869
REMARK 3 S TENSOR
REMARK 3 S11: -0.1120 S12: -0.8509 S13: 0.1781
REMARK 3 S21: -0.0625 S22: -0.4745 S23: 0.6095
REMARK 3 S31: -0.1388 S32: 0.0973 S33: 0.5865
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 18 B 31
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9044 -14.7827 12.3378
REMARK 3 T TENSOR
REMARK 3 T11: 0.4202 T22: 0.1691
REMARK 3 T33: 0.1628 T12: -0.2280
REMARK 3 T13: 0.0385 T23: 0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 6.2717 L22: 13.1190
REMARK 3 L33: 6.4722 L12: 2.1663
REMARK 3 L13: 5.5782 L23: 6.2500
REMARK 3 S TENSOR
REMARK 3 S11: 0.7485 S12: -0.2677 S13: -0.3869
REMARK 3 S21: 0.3703 S22: -1.2168 S23: 1.8348
REMARK 3 S31: 1.3293 S32: -0.3367 S33: 0.4683
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 32 B 39
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7058 -7.4736 3.2008
REMARK 3 T TENSOR
REMARK 3 T11: 0.1438 T22: 0.1618
REMARK 3 T33: 0.1567 T12: 0.0862
REMARK 3 T13: -0.0887 T23: -0.0921
REMARK 3 L TENSOR
REMARK 3 L11: 17.0009 L22: 14.5307
REMARK 3 L33: 11.2713 L12: 15.6454
REMARK 3 L13: -5.9126 L23: -4.3357
REMARK 3 S TENSOR
REMARK 3 S11: -0.0589 S12: -0.6236 S13: 0.0866
REMARK 3 S21: 0.1585 S22: -0.0778 S23: -0.2895
REMARK 3 S31: -0.2023 S32: 0.4367 S33: 0.1367
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 40 B 52
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6277 -7.5380 1.1308
REMARK 3 T TENSOR
REMARK 3 T11: 0.1712 T22: 0.1526
REMARK 3 T33: 0.1460 T12: -0.0301
REMARK 3 T13: -0.0800 T23: -0.0603
REMARK 3 L TENSOR
REMARK 3 L11: 6.4074 L22: 2.0323
REMARK 3 L33: 1.8068 L12: 3.4867
REMARK 3 L13: -1.9283 L23: -0.6425
REMARK 3 S TENSOR
REMARK 3 S11: 0.1422 S12: -0.0681 S13: -0.0195
REMARK 3 S21: -0.1197 S22: -0.0289 S23: 0.2297
REMARK 3 S31: 0.3973 S32: 0.2996 S33: -0.1133
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 53 B 62
REMARK 3 ORIGIN FOR THE GROUP (A): 16.2973 -17.2482 11.5241
REMARK 3 T TENSOR
REMARK 3 T11: 0.2170 T22: 0.1691
REMARK 3 T33: 0.1272 T12: 0.0636
REMARK 3 T13: -0.0763 T23: 0.0558
REMARK 3 L TENSOR
REMARK 3 L11: 22.4963 L22: 16.8664
REMARK 3 L33: 39.4107 L12: 11.2310
REMARK 3 L13: -12.0214 L23: -17.6947
REMARK 3 S TENSOR
REMARK 3 S11: -0.8123 S12: -0.7124 S13: -1.8241
REMARK 3 S21: 0.5208 S22: 0.2177 S23: -1.4006
REMARK 3 S31: 1.8799 S32: -0.6497 S33: 0.5947
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 63 B 70
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8572 0.0271 6.1397
REMARK 3 T TENSOR
REMARK 3 T11: 0.1128 T22: 0.2580
REMARK 3 T33: 0.2040 T12: -0.0885
REMARK 3 T13: -0.0714 T23: -0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 10.1264 L22: 9.0463
REMARK 3 L33: 11.9467 L12: -1.1054
REMARK 3 L13: -10.5933 L23: -1.6223
REMARK 3 S TENSOR
REMARK 3 S11: 0.2810 S12: 0.2187 S13: -0.3191
REMARK 3 S21: -0.3851 S22: -0.4668 S23: 0.2266
REMARK 3 S31: -0.6440 S32: -0.3506 S33: 0.1858
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 71 B 90
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6713 -1.0163 11.9741
REMARK 3 T TENSOR
REMARK 3 T11: 0.1947 T22: 0.2042
REMARK 3 T33: 0.0927 T12: -0.0431
REMARK 3 T13: -0.0576 T23: -0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 2.9720 L22: 17.2551
REMARK 3 L33: 2.7580 L12: -1.0938
REMARK 3 L13: -1.1930 L23: -1.7775
REMARK 3 S TENSOR
REMARK 3 S11: 0.3301 S12: -0.2694 S13: -0.0512
REMARK 3 S21: 0.9638 S22: -0.2013 S23: -0.2055
REMARK 3 S31: -0.2957 S32: 0.4188 S33: -0.1287
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 91 B 104
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9482 -12.7291 3.6781
REMARK 3 T TENSOR
REMARK 3 T11: 0.1362 T22: 0.1733
REMARK 3 T33: 0.0916 T12: -0.0935
REMARK 3 T13: -0.0693 T23: -0.0572
REMARK 3 L TENSOR
REMARK 3 L11: 5.0841 L22: 20.6581
REMARK 3 L33: 8.1012 L12: 7.2772
REMARK 3 L13: -0.9554 L23: 1.9384
REMARK 3 S TENSOR
REMARK 3 S11: 0.2128 S12: -0.1582 S13: -0.1629
REMARK 3 S21: 0.6856 S22: -0.4585 S23: 0.4908
REMARK 3 S31: 0.6602 S32: -0.6276 S33: 0.2458
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 105 B 123
REMARK 3 ORIGIN FOR THE GROUP (A): 9.5723 15.2054 11.3044
REMARK 3 T TENSOR
REMARK 3 T11: 0.2940 T22: 0.1713
REMARK 3 T33: 0.0571 T12: -0.0515
REMARK 3 T13: 0.0459 T23: -0.0464
REMARK 3 L TENSOR
REMARK 3 L11: 2.0407 L22: 18.8979
REMARK 3 L33: 0.2107 L12: 4.9139
REMARK 3 L13: 0.5860 L23: 1.9586
REMARK 3 S TENSOR
REMARK 3 S11: -0.3007 S12: 0.2582 S13: -0.1062
REMARK 3 S21: -0.8078 S22: 0.4024 S23: 0.0283
REMARK 3 S31: -0.1640 S32: 0.2134 S33: -0.1017
REMARK 3
REMARK 3 TLS GROUP : 31
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 124 B 132
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3748 50.8541 9.6612
REMARK 3 T TENSOR
REMARK 3 T11: 0.1392 T22: 0.2117
REMARK 3 T33: 0.1393 T12: -0.0071
REMARK 3 T13: 0.0028 T23: -0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 8.6216 L22: 3.6591
REMARK 3 L33: 18.0211 L12: 5.4126
REMARK 3 L13: -1.6467 L23: -3.1840
REMARK 3 S TENSOR
REMARK 3 S11: 0.4193 S12: 0.5536 S13: 0.9884
REMARK 3 S21: 0.1028 S22: -0.9022 S23: -0.4677
REMARK 3 S31: -0.8736 S32: -0.4050 S33: 0.4828
REMARK 3
REMARK 3 TLS GROUP : 32
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 133 B 143
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0829 41.3475 8.3239
REMARK 3 T TENSOR
REMARK 3 T11: 0.1690 T22: 0.2825
REMARK 3 T33: 0.1230 T12: 0.0447
REMARK 3 T13: 0.0445 T23: 0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 2.7823 L22: 5.2318
REMARK 3 L33: 3.4915 L12: 2.8580
REMARK 3 L13: 0.4517 L23: -1.8838
REMARK 3 S TENSOR
REMARK 3 S11: 0.2487 S12: 0.5681 S13: 0.3380
REMARK 3 S21: -0.2359 S22: -1.1832 S23: -0.5324
REMARK 3 S31: 0.1064 S32: -0.0038 S33: 0.9345
REMARK 3
REMARK 3 TLS GROUP : 33
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 144 B 153
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1154 23.3751 10.2665
REMARK 3 T TENSOR
REMARK 3 T11: 0.3040 T22: 0.1488
REMARK 3 T33: 0.0735 T12: -0.0630
REMARK 3 T13: 0.0761 T23: -0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 3.7514 L22: 20.5971
REMARK 3 L33: 1.7293 L12: -2.6014
REMARK 3 L13: 2.1430 L23: 1.5950
REMARK 3 S TENSOR
REMARK 3 S11: -0.0297 S12: 0.0648 S13: -0.2379
REMARK 3 S21: 0.1334 S22: 0.1135 S23: -0.0749
REMARK 3 S31: 0.0865 S32: 0.0534 S33: -0.0838
REMARK 3
REMARK 3 TLS GROUP : 34
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 154 B 168
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0342 38.4487 12.2774
REMARK 3 T TENSOR
REMARK 3 T11: 0.0049 T22: 0.1643
REMARK 3 T33: 0.1434 T12: -0.0023
REMARK 3 T13: -0.0301 T23: 0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 5.6632 L22: 7.2540
REMARK 3 L33: 17.7768 L12: 0.7176
REMARK 3 L13: 2.0836 L23: -3.0946
REMARK 3 S TENSOR
REMARK 3 S11: 0.0560 S12: 0.2395 S13: -0.1127
REMARK 3 S21: -0.2516 S22: 0.1981 S23: 0.0797
REMARK 3 S31: 0.6467 S32: -1.1150 S33: -0.2541
REMARK 3
REMARK 3 TLS GROUP : 35
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 169 B 173
REMARK 3 ORIGIN FOR THE GROUP (A): 2.4548 42.7494 4.7716
REMARK 3 T TENSOR
REMARK 3 T11: 0.1467 T22: 0.2786
REMARK 3 T33: 0.1411 T12: -0.0342
REMARK 3 T13: 0.0004 T23: 0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 14.1588 L22: 2.6171
REMARK 3 L33: 6.0231 L12: -2.0609
REMARK 3 L13: 1.9835 L23: 3.3599
REMARK 3 S TENSOR
REMARK 3 S11: -0.5843 S12: -0.0253 S13: 0.8451
REMARK 3 S21: -0.3772 S22: 0.4400 S23: -0.3003
REMARK 3 S31: -0.1929 S32: -0.2768 S33: 0.1442
REMARK 3
REMARK 3 TLS GROUP : 36
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 174 B 192
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5796 27.0780 4.8164
REMARK 3 T TENSOR
REMARK 3 T11: 0.2326 T22: 0.1676
REMARK 3 T33: 0.0651 T12: 0.0452
REMARK 3 T13: 0.0675 T23: 0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 1.4817 L22: 15.2699
REMARK 3 L33: 0.2896 L12: -2.4898
REMARK 3 L13: -0.6544 L23: 1.0247
REMARK 3 S TENSOR
REMARK 3 S11: -0.2357 S12: -0.0040 S13: -0.1456
REMARK 3 S21: -0.4284 S22: 0.0214 S23: 0.0019
REMARK 3 S31: 0.3423 S32: 0.1878 S33: 0.2143
REMARK 3
REMARK 3 TLS GROUP : 37
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 193 B 200
REMARK 3 ORIGIN FOR THE GROUP (A): 4.6122 51.4582 13.9136
REMARK 3 T TENSOR
REMARK 3 T11: 0.1864 T22: 0.2048
REMARK 3 T33: 0.2223 T12: 0.0549
REMARK 3 T13: -0.0777 T23: -0.1009
REMARK 3 L TENSOR
REMARK 3 L11: 11.6791 L22: 20.0691
REMARK 3 L33: 24.1960 L12: -3.1614
REMARK 3 L13: 10.9614 L23: 13.3799
REMARK 3 S TENSOR
REMARK 3 S11: -1.8066 S12: -1.0524 S13: 1.4621
REMARK 3 S21: 0.0686 S22: 0.1486 S23: 0.8751
REMARK 3 S31: -0.9922 S32: -0.7120 S33: 1.6580
REMARK 3
REMARK 3 TLS GROUP : 38
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 201 B 209
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8090 37.2056 18.3983
REMARK 3 T TENSOR
REMARK 3 T11: 0.1708 T22: 0.1717
REMARK 3 T33: 0.1468 T12: -0.0484
REMARK 3 T13: 0.0149 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 4.3385 L22: 9.0377
REMARK 3 L33: 2.7769 L12: 2.6842
REMARK 3 L13: 2.0044 L23: -0.2348
REMARK 3 S TENSOR
REMARK 3 S11: -0.0885 S12: -0.3614 S13: 0.2650
REMARK 3 S21: 0.2835 S22: -0.0936 S23: 0.3134
REMARK 3 S31: 0.1939 S32: -0.1870 S33: 0.1822
REMARK 3
REMARK 3 TLS GROUP : 39
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 210 B 223
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2532 20.9236 18.0297
REMARK 3 T TENSOR
REMARK 3 T11: 0.1102 T22: 0.1326
REMARK 3 T33: 0.0996 T12: -0.0738
REMARK 3 T13: 0.0973 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 8.3476 L22: 26.9892
REMARK 3 L33: 4.0585 L12: 12.3980
REMARK 3 L13: 5.0712 L23: 7.4979
REMARK 3 S TENSOR
REMARK 3 S11: 0.4689 S12: -0.4072 S13: -0.0158
REMARK 3 S21: 0.5135 S22: -0.6132 S23: 0.6684
REMARK 3 S31: 0.5775 S32: -0.6414 S33: 0.1442
REMARK 3
REMARK 3 TLS GROUP : 40
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 224 B 231
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6359 48.3662 16.7862
REMARK 3 T TENSOR
REMARK 3 T11: 0.1925 T22: 0.1804
REMARK 3 T33: 0.2000 T12: -0.0273
REMARK 3 T13: 0.0120 T23: -0.0374
REMARK 3 L TENSOR
REMARK 3 L11: 6.8280 L22: 8.9125
REMARK 3 L33: 11.0561 L12: 1.5374
REMARK 3 L13: -4.5498 L23: -4.6852
REMARK 3 S TENSOR
REMARK 3 S11: -0.1786 S12: 0.3732 S13: 0.6436
REMARK 3 S21: 0.2862 S22: 0.3971 S23: -1.0676
REMARK 3 S31: -1.0758 S32: -0.2831 S33: -0.2185
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 : 1.40
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
REMARK 4
REMARK 4 2PF6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042308.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-SEP-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.488
REMARK 200 MONOCHROMATOR : ASYMMETRIC CUT SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19830
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.1
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
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 (%) : 41.3
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.48200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
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: PDB ENTRY 2PET
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG4000, 0.2M AMMONIUM ACETATE,
REMARK 280 0.1M SODIUM CITRATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 171.22800
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 85.61400
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 85.61400
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 171.22800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: ASYMMETIC UNIT CONATINS TWO COPIES OF BIOLOGICAL UNIT
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 (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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 214 CD GLU A 214 OE1 0.096
REMARK 500 GLU A 214 CD GLU A 214 OE2 0.076
REMARK 500 GLN B 53 CD GLN B 53 OE1 0.194
REMARK 500 GLU B 105 CD GLU B 105 OE1 0.128
REMARK 500 GLU B 105 CD GLU B 105 OE2 0.101
REMARK 500 GLU B 132 CD GLU B 132 OE1 0.075
REMARK 500 GLU B 166 CD GLU B 166 OE2 0.081
REMARK 500
REMARK 500 REMARK: NULL
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 90 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG B 3 NE - CZ - NH2 ANGL. DEV. = -3.0 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 CYS A 22 83.20 -153.78
REMARK 500 HIS A 28 -156.58 -96.00
REMARK 500 ARG A 90 -173.98 -173.59
REMARK 500 PRO A 148 -168.37 -61.26
REMARK 500 SER B 5 49.82 -148.51
REMARK 500 CYS B 22 86.01 -158.25
REMARK 500 HIS B 28 -148.09 -90.36
REMARK 500 GLU B 83 60.28 62.63
REMARK 500 ALA B 118 134.54 -39.40
REMARK 500 ASN B 147 120.26 -171.48
REMARK 500 PRO B 148 -178.29 -67.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PET RELATED DB: PDB
REMARK 900 DIFFERENT CRYSTAL FORM
DBREF 2PF6 A 1 231 UNP P50895 LU_HUMAN 32 262
DBREF 2PF6 B 1 231 UNP P50895 LU_HUMAN 32 262
SEQRES 1 A 231 GLU VAL ARG LEU SER VAL PRO PRO LEU VAL GLU VAL MET
SEQRES 2 A 231 ARG GLY LYS SER VAL ILE LEU ASP CYS THR PRO THR GLY
SEQRES 3 A 231 THR HIS ASP HIS TYR MET LEU GLU TRP PHE LEU THR ASP
SEQRES 4 A 231 ARG SER GLY ALA ARG PRO ARG LEU ALA SER ALA GLU MET
SEQRES 5 A 231 GLN GLY SER GLU LEU GLN VAL THR MET HIS ASP THR ARG
SEQRES 6 A 231 GLY ARG SER PRO PRO TYR GLN LEU ASP SER GLN GLY ARG
SEQRES 7 A 231 LEU VAL LEU ALA GLU ALA GLN VAL GLY ASP GLU ARG ASP
SEQRES 8 A 231 TYR VAL CYS VAL VAL ARG ALA GLY ALA ALA GLY THR ALA
SEQRES 9 A 231 GLU ALA THR ALA ARG LEU ASN VAL PHE ALA LYS PRO GLU
SEQRES 10 A 231 ALA THR GLU VAL SER PRO ASN LYS GLY THR LEU SER VAL
SEQRES 11 A 231 MET GLU ASP SER ALA GLN GLU ILE ALA THR CYS ASN SER
SEQRES 12 A 231 ARG ASN GLY ASN PRO ALA PRO LYS ILE THR TRP TYR ARG
SEQRES 13 A 231 ASN GLY GLN ARG LEU GLU VAL PRO VAL GLU MET ASN PRO
SEQRES 14 A 231 GLU GLY TYR MET THR SER ARG THR VAL ARG GLU ALA SER
SEQRES 15 A 231 GLY LEU LEU SER LEU THR SER THR LEU TYR LEU ARG LEU
SEQRES 16 A 231 ARG LYS ASP ASP ARG ASP ALA SER PHE HIS CYS ALA ALA
SEQRES 17 A 231 HIS TYR SER LEU PRO GLU GLY ARG HIS GLY ARG LEU ASP
SEQRES 18 A 231 SER PRO THR PHE HIS LEU THR LEU HIS TYR
SEQRES 1 B 231 GLU VAL ARG LEU SER VAL PRO PRO LEU VAL GLU VAL MET
SEQRES 2 B 231 ARG GLY LYS SER VAL ILE LEU ASP CYS THR PRO THR GLY
SEQRES 3 B 231 THR HIS ASP HIS TYR MET LEU GLU TRP PHE LEU THR ASP
SEQRES 4 B 231 ARG SER GLY ALA ARG PRO ARG LEU ALA SER ALA GLU MET
SEQRES 5 B 231 GLN GLY SER GLU LEU GLN VAL THR MET HIS ASP THR ARG
SEQRES 6 B 231 GLY ARG SER PRO PRO TYR GLN LEU ASP SER GLN GLY ARG
SEQRES 7 B 231 LEU VAL LEU ALA GLU ALA GLN VAL GLY ASP GLU ARG ASP
SEQRES 8 B 231 TYR VAL CYS VAL VAL ARG ALA GLY ALA ALA GLY THR ALA
SEQRES 9 B 231 GLU ALA THR ALA ARG LEU ASN VAL PHE ALA LYS PRO GLU
SEQRES 10 B 231 ALA THR GLU VAL SER PRO ASN LYS GLY THR LEU SER VAL
SEQRES 11 B 231 MET GLU ASP SER ALA GLN GLU ILE ALA THR CYS ASN SER
SEQRES 12 B 231 ARG ASN GLY ASN PRO ALA PRO LYS ILE THR TRP TYR ARG
SEQRES 13 B 231 ASN GLY GLN ARG LEU GLU VAL PRO VAL GLU MET ASN PRO
SEQRES 14 B 231 GLU GLY TYR MET THR SER ARG THR VAL ARG GLU ALA SER
SEQRES 15 B 231 GLY LEU LEU SER LEU THR SER THR LEU TYR LEU ARG LEU
SEQRES 16 B 231 ARG LYS ASP ASP ARG ASP ALA SER PHE HIS CYS ALA ALA
SEQRES 17 B 231 HIS TYR SER LEU PRO GLU GLY ARG HIS GLY ARG LEU ASP
SEQRES 18 B 231 SER PRO THR PHE HIS LEU THR LEU HIS TYR
FORMUL 3 HOH *51(H2 O)
HELIX 1 1 GLN A 85 GLU A 89 5 5
HELIX 2 2 GLY A 99 ALA A 101 5 3
HELIX 3 3 ARG A 196 ASP A 201 5 6
HELIX 4 4 PRO A 213 GLY A 215 5 3
HELIX 5 5 GLN B 85 GLU B 89 5 5
HELIX 6 6 GLY B 99 ALA B 101 5 3
HELIX 7 7 ARG B 196 ARG B 200 5 5
HELIX 8 8 PRO B 213 GLY B 215 5 3
SHEET 1 A 2 ARG A 3 SER A 5 0
SHEET 2 A 2 THR A 23 THR A 25 -1 O THR A 23 N SER A 5
SHEET 1 B 6 LEU A 9 MET A 13 0
SHEET 2 B 6 THR A 103 PHE A 113 1 O PHE A 113 N VAL A 12
SHEET 3 B 6 ARG A 90 ARG A 97 -1 N TYR A 92 O ALA A 108
SHEET 4 B 6 HIS A 30 LEU A 37 -1 N GLU A 34 O VAL A 95
SHEET 5 B 6 ARG A 46 GLN A 53 -1 O LEU A 47 N TRP A 35
SHEET 6 B 6 GLU A 56 MET A 61 -1 O THR A 60 N SER A 49
SHEET 1 C 3 VAL A 18 LEU A 20 0
SHEET 2 C 3 LEU A 79 LEU A 81 -1 O LEU A 81 N VAL A 18
SHEET 3 C 3 GLN A 72 LEU A 73 -1 N GLN A 72 O VAL A 80
SHEET 1 D 4 GLU A 120 PRO A 123 0
SHEET 2 D 4 ALA A 135 GLY A 146 -1 O THR A 140 N SER A 122
SHEET 3 D 4 LEU A 185 ARG A 194 -1 O SER A 189 N CYS A 141
SHEET 4 D 4 GLY A 171 MET A 173 -1 N TYR A 172 O TYR A 192
SHEET 1 E 4 GLU A 120 PRO A 123 0
SHEET 2 E 4 ALA A 135 GLY A 146 -1 O THR A 140 N SER A 122
SHEET 3 E 4 LEU A 185 ARG A 194 -1 O SER A 189 N CYS A 141
SHEET 4 E 4 ARG A 176 ARG A 179 -1 N VAL A 178 O SER A 186
SHEET 1 F 4 GLN A 159 LEU A 161 0
SHEET 2 F 4 LYS A 151 ARG A 156 -1 N TRP A 154 O LEU A 161
SHEET 3 F 4 SER A 203 SER A 211 -1 O HIS A 209 N LYS A 151
SHEET 4 F 4 HIS A 217 ASP A 221 -1 O GLY A 218 N TYR A 210
SHEET 1 G 4 GLN A 159 LEU A 161 0
SHEET 2 G 4 LYS A 151 ARG A 156 -1 N TRP A 154 O LEU A 161
SHEET 3 G 4 SER A 203 SER A 211 -1 O HIS A 209 N LYS A 151
SHEET 4 G 4 PHE A 225 HIS A 226 -1 O PHE A 225 N PHE A 204
SHEET 1 H 6 LEU B 9 MET B 13 0
SHEET 2 H 6 THR B 103 PHE B 113 1 O ARG B 109 N VAL B 10
SHEET 3 H 6 ASP B 91 ARG B 97 -1 N TYR B 92 O ALA B 108
SHEET 4 H 6 HIS B 30 LEU B 37 -1 N GLU B 34 O VAL B 95
SHEET 5 H 6 ARG B 46 GLN B 53 -1 O LEU B 47 N TRP B 35
SHEET 6 H 6 LEU B 57 MET B 61 -1 O THR B 60 N SER B 49
SHEET 1 I 3 VAL B 18 LEU B 20 0
SHEET 2 I 3 LEU B 79 LEU B 81 -1 O LEU B 79 N LEU B 20
SHEET 3 I 3 GLN B 72 LEU B 73 -1 N GLN B 72 O VAL B 80
SHEET 1 J 4 GLU B 120 PRO B 123 0
SHEET 2 J 4 GLN B 136 GLY B 146 -1 O THR B 140 N SER B 122
SHEET 3 J 4 LEU B 185 LEU B 193 -1 O LEU B 185 N GLY B 146
SHEET 4 J 4 GLY B 171 MET B 173 -1 N TYR B 172 O TYR B 192
SHEET 1 K 4 GLU B 120 PRO B 123 0
SHEET 2 K 4 GLN B 136 GLY B 146 -1 O THR B 140 N SER B 122
SHEET 3 K 4 LEU B 185 LEU B 193 -1 O LEU B 185 N GLY B 146
SHEET 4 K 4 ARG B 176 ARG B 179 -1 N VAL B 178 O SER B 186
SHEET 1 L 4 GLN B 159 LEU B 161 0
SHEET 2 L 4 LYS B 151 ARG B 156 -1 N TRP B 154 O LEU B 161
SHEET 3 L 4 PHE B 204 SER B 211 -1 O HIS B 205 N TYR B 155
SHEET 4 L 4 HIS B 217 ASP B 221 -1 O GLY B 218 N TYR B 210
SSBOND 1 CYS A 22 CYS A 94 1555 1555 2.02
SSBOND 2 CYS A 141 CYS A 206 1555 1555 2.07
SSBOND 3 CYS B 22 CYS B 94 1555 1555 2.04
SSBOND 4 CYS B 141 CYS B 206 1555 1555 2.08
CISPEP 1 SER A 68 PRO A 69 0 -5.58
CISPEP 2 ASN A 147 PRO A 148 0 -5.71
CISPEP 3 SER B 68 PRO B 69 0 -6.44
CISPEP 4 ASN B 147 PRO B 148 0 -3.30
CRYST1 52.248 52.248 256.842 90.00 90.00 120.00 P 32 2 1 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 0.019139 0.011050 0.000000 0.00000
SCALE2 0.000000 0.022100 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003893 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
