HEADER TRANSCRIPTION, TRANSCRIPTION REGULATION 30-AUG-08 3ECH
TITLE THE MARR-FAMILY REPRESSOR MEXR IN COMPLEX WITH ITS ANTIREPRESSOR ARMR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MULTIDRUG RESISTANCE OPERON REPRESSOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-142;
COMPND 5 SYNONYM: MEXR;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 25-MER FRAGMENT OF PROTEIN ARMR;
COMPND 10 CHAIN: C;
COMPND 11 FRAGMENT: RESIDUES 29-53;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: MEXR, PA0424;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET41A;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 12 ORGANISM_TAXID: 287;
SOURCE 13 GENE: PA3719;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PTYB12
KEYWDS WINGED HELIX, HELIX-TURN-HELIX, PROTEIN-PEPTIDE COMPLEX, DNA-BINDING,
KEYWDS 2 REPRESSOR, TRANSCRIPTION, TRANSCRIPTION REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.S.WILKE,N.C.J.STRYNADKA
REVDAT 6 30-AUG-23 3ECH 1 REMARK
REVDAT 5 20-OCT-21 3ECH 1 SEQADV
REVDAT 4 25-OCT-17 3ECH 1 REMARK
REVDAT 3 13-JUL-11 3ECH 1 VERSN
REVDAT 2 24-FEB-09 3ECH 1 VERSN
REVDAT 1 21-OCT-08 3ECH 0
JRNL AUTH M.S.WILKE,M.HELLER,A.L.CREAGH,C.A.HAYNES,L.P.MCINTOSH,
JRNL AUTH 2 K.POOLE,N.C.J.STRYNADKA
JRNL TITL THE CRYSTAL STRUCTURE OF MEXR FROM PSEUDOMONAS AERUGINOSA IN
JRNL TITL 2 COMPLEX WITH ITS ANTIREPRESSOR ARMR
JRNL REF PROC.NATL.ACAD.SCI.USA V. 105 14832 2008
JRNL REFN ISSN 0027-8424
JRNL PMID 18812515
JRNL DOI 10.1073/PNAS.0805489105
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 24697
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1325
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1759
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.1810
REMARK 3 BIN FREE R VALUE SET COUNT : 96
REMARK 3 BIN FREE R VALUE : 0.2360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2346
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 212
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.81000
REMARK 3 B22 (A**2) : -0.04000
REMARK 3 B33 (A**2) : -0.77000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.140
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.138
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.081
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.023
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2502 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1737 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3411 ; 1.401 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4238 ; 0.966 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 315 ; 4.515 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 134 ;36.269 ;23.358
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 471 ;12.710 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;17.283 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 396 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2762 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 499 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 592 ; 0.237 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1780 ; 0.189 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1216 ; 0.173 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1313 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 167 ; 0.174 ; 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): 36 ; 0.234 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 85 ; 0.246 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 28 ; 0.185 ; 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): 1993 ; 1.032 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 584 ; 0.244 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2444 ; 1.162 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1084 ; 2.259 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 950 ; 3.357 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 19
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 10
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1694 -4.8075 1.2898
REMARK 3 T TENSOR
REMARK 3 T11: 0.0998 T22: 0.0794
REMARK 3 T33: 0.0399 T12: 0.0250
REMARK 3 T13: -0.0512 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 12.7218 L22: 6.6687
REMARK 3 L33: 6.8811 L12: 2.8610
REMARK 3 L13: 4.6245 L23: 1.2087
REMARK 3 S TENSOR
REMARK 3 S11: 0.0535 S12: 0.2746 S13: -0.1805
REMARK 3 S21: 0.2124 S22: 0.0978 S23: -0.5016
REMARK 3 S31: 0.1938 S32: 0.7975 S33: -0.1513
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 11 A 31
REMARK 3 ORIGIN FOR THE GROUP (A): -14.4651 -1.0087 -4.4370
REMARK 3 T TENSOR
REMARK 3 T11: 0.0919 T22: 0.0548
REMARK 3 T33: 0.0401 T12: -0.0292
REMARK 3 T13: 0.0109 T23: 0.0160
REMARK 3 L TENSOR
REMARK 3 L11: 14.7690 L22: 1.8761
REMARK 3 L33: 3.4992 L12: -2.7148
REMARK 3 L13: 5.1920 L23: -1.3326
REMARK 3 S TENSOR
REMARK 3 S11: 0.1750 S12: -0.3524 S13: -0.0356
REMARK 3 S21: 0.0444 S22: 0.0526 S23: 0.2453
REMARK 3 S31: 0.1785 S32: -0.3561 S33: -0.2275
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 32 A 62
REMARK 3 ORIGIN FOR THE GROUP (A): -15.8435 7.1256 -23.2954
REMARK 3 T TENSOR
REMARK 3 T11: 0.1157 T22: 0.1143
REMARK 3 T33: 0.1334 T12: -0.0291
REMARK 3 T13: -0.0018 T23: -0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 3.2427 L22: 3.2564
REMARK 3 L33: 6.4678 L12: 1.0308
REMARK 3 L13: -2.3210 L23: -2.7816
REMARK 3 S TENSOR
REMARK 3 S11: -0.0898 S12: 0.1994 S13: -0.1004
REMARK 3 S21: -0.1572 S22: 0.0415 S23: 0.0015
REMARK 3 S31: 0.1824 S32: -0.2078 S33: 0.0483
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 66 A 76
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8713 -0.0206 -28.0431
REMARK 3 T TENSOR
REMARK 3 T11: 0.1114 T22: 0.0670
REMARK 3 T33: 0.2123 T12: -0.1291
REMARK 3 T13: 0.0442 T23: -0.2053
REMARK 3 L TENSOR
REMARK 3 L11: 44.8332 L22: 27.7015
REMARK 3 L33: 13.9902 L12: -18.2467
REMARK 3 L13: -9.9000 L23: 10.9031
REMARK 3 S TENSOR
REMARK 3 S11: 0.1882 S12: 1.4930 S13: -3.0029
REMARK 3 S21: -0.4741 S22: -0.3444 S23: -0.4582
REMARK 3 S31: 1.1230 S32: 0.2226 S33: 0.1562
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 77 A 100
REMARK 3 ORIGIN FOR THE GROUP (A): -24.7893 11.1903 -26.6476
REMARK 3 T TENSOR
REMARK 3 T11: 0.0831 T22: 0.1976
REMARK 3 T33: 0.0131 T12: -0.0534
REMARK 3 T13: -0.0241 T23: -0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 12.6880 L22: 4.5390
REMARK 3 L33: 5.5552 L12: 3.6499
REMARK 3 L13: -2.7931 L23: -2.6654
REMARK 3 S TENSOR
REMARK 3 S11: -0.2945 S12: 0.9796 S13: 0.1667
REMARK 3 S21: -0.4452 S22: 0.3262 S23: 0.0766
REMARK 3 S31: 0.0707 S32: -0.5390 S33: -0.0317
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 113
REMARK 3 ORIGIN FOR THE GROUP (A): -20.2705 11.6515 -11.6093
REMARK 3 T TENSOR
REMARK 3 T11: 0.0424 T22: 0.0477
REMARK 3 T33: 0.0447 T12: 0.0222
REMARK 3 T13: -0.0028 T23: -0.0240
REMARK 3 L TENSOR
REMARK 3 L11: 5.2072 L22: 2.1355
REMARK 3 L33: 8.0067 L12: -0.6155
REMARK 3 L13: 4.6285 L23: -1.0393
REMARK 3 S TENSOR
REMARK 3 S11: -0.1335 S12: -0.0505 S13: 0.1341
REMARK 3 S21: 0.1045 S22: 0.0574 S23: -0.0877
REMARK 3 S31: -0.2153 S32: -0.1347 S33: 0.0761
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 114 A 136
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1484 9.2296 3.1129
REMARK 3 T TENSOR
REMARK 3 T11: 0.0967 T22: 0.0433
REMARK 3 T33: 0.0274 T12: -0.0109
REMARK 3 T13: -0.0081 T23: -0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 3.0008 L22: 1.9702
REMARK 3 L33: 2.8550 L12: 0.4372
REMARK 3 L13: 0.7026 L23: 0.5547
REMARK 3 S TENSOR
REMARK 3 S11: 0.0987 S12: -0.2209 S13: 0.0240
REMARK 3 S21: 0.0568 S22: -0.0331 S23: 0.0341
REMARK 3 S31: -0.0878 S32: -0.1416 S33: -0.0656
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 137 A 142
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6398 6.0726 -6.3656
REMARK 3 T TENSOR
REMARK 3 T11: 0.1044 T22: 0.0888
REMARK 3 T33: 0.0996 T12: 0.0086
REMARK 3 T13: -0.0415 T23: -0.0451
REMARK 3 L TENSOR
REMARK 3 L11: 24.7635 L22: 33.6587
REMARK 3 L33: 25.6937 L12: 3.8782
REMARK 3 L13: -21.9346 L23: 3.7447
REMARK 3 S TENSOR
REMARK 3 S11: 0.1439 S12: -0.3095 S13: 0.0059
REMARK 3 S21: -0.0957 S22: -0.1222 S23: -0.7378
REMARK 3 S31: -0.0894 S32: 0.6127 S33: -0.0217
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 5
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1881 15.9085 7.2094
REMARK 3 T TENSOR
REMARK 3 T11: 0.1645 T22: 0.0398
REMARK 3 T33: 0.0378 T12: 0.0193
REMARK 3 T13: 0.0146 T23: -0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 54.1331 L22: 1.1476
REMARK 3 L33: 23.5659 L12: -0.3170
REMARK 3 L13: -35.6182 L23: -0.1775
REMARK 3 S TENSOR
REMARK 3 S11: 0.1765 S12: -0.9398 S13: 0.7341
REMARK 3 S21: 0.0727 S22: 0.3971 S23: 0.0137
REMARK 3 S31: -0.0548 S32: 0.3901 S33: -0.5736
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 6 B 31
REMARK 3 ORIGIN FOR THE GROUP (A): 0.3104 2.2243 -11.7265
REMARK 3 T TENSOR
REMARK 3 T11: 0.0601 T22: 0.0428
REMARK 3 T33: 0.0509 T12: 0.0072
REMARK 3 T13: -0.0044 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 0.9093 L22: 4.6327
REMARK 3 L33: 4.1665 L12: -1.5932
REMARK 3 L13: -1.8165 L23: 3.4578
REMARK 3 S TENSOR
REMARK 3 S11: 0.0551 S12: 0.0232 S13: -0.0192
REMARK 3 S21: -0.0780 S22: -0.0551 S23: -0.0469
REMARK 3 S31: -0.1182 S32: 0.0220 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 32 B 60
REMARK 3 ORIGIN FOR THE GROUP (A): -8.7756 -17.3174 -15.9813
REMARK 3 T TENSOR
REMARK 3 T11: 0.1089 T22: 0.0809
REMARK 3 T33: 0.0645 T12: 0.0075
REMARK 3 T13: 0.0211 T23: -0.0283
REMARK 3 L TENSOR
REMARK 3 L11: 6.7705 L22: 5.9090
REMARK 3 L33: 2.6158 L12: 3.7514
REMARK 3 L13: -2.6132 L23: -2.0719
REMARK 3 S TENSOR
REMARK 3 S11: -0.0769 S12: -0.1618 S13: 0.0103
REMARK 3 S21: 0.1189 S22: 0.0732 S23: 0.1019
REMARK 3 S31: 0.0341 S32: -0.1493 S33: 0.0037
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 61 B 78
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2821 -17.7968 -25.5135
REMARK 3 T TENSOR
REMARK 3 T11: 0.1104 T22: 0.0515
REMARK 3 T33: 0.0630 T12: 0.0100
REMARK 3 T13: 0.0022 T23: 0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 11.9918 L22: 6.4433
REMARK 3 L33: 8.0281 L12: -3.8753
REMARK 3 L13: -2.9100 L23: 0.7026
REMARK 3 S TENSOR
REMARK 3 S11: 0.0101 S12: 0.0684 S13: 0.4515
REMARK 3 S21: -0.0676 S22: 0.1673 S23: 0.1604
REMARK 3 S31: -0.5114 S32: -0.5083 S33: -0.1774
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 79 B 89
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7444 -29.8253 -21.0200
REMARK 3 T TENSOR
REMARK 3 T11: 0.0919 T22: 0.0363
REMARK 3 T33: 0.1208 T12: -0.0271
REMARK 3 T13: 0.0406 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 12.4876 L22: 7.5083
REMARK 3 L33: 4.3560 L12: 6.7527
REMARK 3 L13: -4.2107 L23: -0.8152
REMARK 3 S TENSOR
REMARK 3 S11: -0.2030 S12: 0.3104 S13: -0.1776
REMARK 3 S21: 0.1622 S22: 0.0952 S23: 0.5956
REMARK 3 S31: 0.4018 S32: -0.4723 S33: 0.1078
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 90 B 106
REMARK 3 ORIGIN FOR THE GROUP (A): -7.8261 -26.0664 -18.6342
REMARK 3 T TENSOR
REMARK 3 T11: 0.1030 T22: 0.0272
REMARK 3 T33: 0.0922 T12: -0.0066
REMARK 3 T13: 0.0346 T23: 0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 9.5649 L22: 4.6055
REMARK 3 L33: 3.5666 L12: 3.2833
REMARK 3 L13: 1.7533 L23: 2.1395
REMARK 3 S TENSOR
REMARK 3 S11: -0.0044 S12: 0.1675 S13: -0.4961
REMARK 3 S21: 0.0679 S22: -0.0075 S23: 0.1038
REMARK 3 S31: 0.1512 S32: -0.2157 S33: 0.0119
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 123
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0718 -6.9526 -7.9673
REMARK 3 T TENSOR
REMARK 3 T11: 0.0743 T22: 0.0538
REMARK 3 T33: 0.0657 T12: 0.0144
REMARK 3 T13: -0.0294 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.2398 L22: 8.4266
REMARK 3 L33: 6.1554 L12: 1.1574
REMARK 3 L13: 0.3926 L23: 5.8514
REMARK 3 S TENSOR
REMARK 3 S11: -0.0569 S12: -0.0399 S13: -0.0943
REMARK 3 S21: 0.0260 S22: 0.0738 S23: -0.1453
REMARK 3 S31: 0.0411 S32: 0.1210 S33: -0.0169
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 124 B 141
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2492 1.0957 7.0240
REMARK 3 T TENSOR
REMARK 3 T11: 0.1069 T22: 0.0548
REMARK 3 T33: 0.0157 T12: -0.0108
REMARK 3 T13: -0.0452 T23: 0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 16.5875 L22: 4.2595
REMARK 3 L33: 2.5537 L12: 0.6157
REMARK 3 L13: 0.9486 L23: 0.5607
REMARK 3 S TENSOR
REMARK 3 S11: 0.0009 S12: -0.7945 S13: -0.1298
REMARK 3 S21: 0.1608 S22: 0.0435 S23: 0.2013
REMARK 3 S31: 0.0350 S32: -0.1744 S33: -0.0444
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 30 C 38
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5219 14.5710 -12.5011
REMARK 3 T TENSOR
REMARK 3 T11: 0.1375 T22: 0.0183
REMARK 3 T33: 0.0700 T12: -0.0299
REMARK 3 T13: 0.0241 T23: 0.0227
REMARK 3 L TENSOR
REMARK 3 L11: 19.3339 L22: 1.8977
REMARK 3 L33: 7.7656 L12: -0.4376
REMARK 3 L13: 2.6604 L23: -1.4601
REMARK 3 S TENSOR
REMARK 3 S11: -0.0879 S12: 0.7787 S13: 1.2430
REMARK 3 S21: 0.3140 S22: 0.1438 S23: 0.1009
REMARK 3 S31: -0.9277 S32: 0.4253 S33: -0.0559
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 39 C 43
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1302 9.9728 -14.7601
REMARK 3 T TENSOR
REMARK 3 T11: 0.0426 T22: 0.0157
REMARK 3 T33: 0.1327 T12: 0.0226
REMARK 3 T13: 0.0347 T23: 0.0843
REMARK 3 L TENSOR
REMARK 3 L11: 28.7448 L22: 14.9008
REMARK 3 L33: 8.7129 L12: 4.4523
REMARK 3 L13: 5.6811 L23: 11.2657
REMARK 3 S TENSOR
REMARK 3 S11: 0.0995 S12: 0.8007 S13: 1.0523
REMARK 3 S21: 0.2436 S22: -0.1102 S23: 0.8904
REMARK 3 S31: 0.0247 S32: 0.1146 S33: 0.0107
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 : C 44 C 53
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9737 -0.6581 -12.9890
REMARK 3 T TENSOR
REMARK 3 T11: 0.0314 T22: 0.0284
REMARK 3 T33: 0.0333 T12: -0.0041
REMARK 3 T13: 0.0043 T23: -0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 7.6879 L22: 8.0966
REMARK 3 L33: 0.6048 L12: -6.3688
REMARK 3 L13: 0.6081 L23: -0.1568
REMARK 3 S TENSOR
REMARK 3 S11: 0.1405 S12: 0.2507 S13: -0.1093
REMARK 3 S21: -0.0423 S22: -0.1810 S23: -0.0402
REMARK 3 S31: 0.0348 S32: -0.1429 S33: 0.0406
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 3ECH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-SEP-08.
REMARK 100 THE DEPOSITION ID IS D_1000049149.
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 : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : KOHZU: DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : KOHZU: DOUBLE CRYSTAL SI(111)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26074
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.802
REMARK 200 RESOLUTION RANGE LOW (A) : 48.560
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 7.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 8.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.05600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER, MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1LNW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3000, 0.1M SODIUM CITRATE, PH
REMARK 280 5.5, MICROBATCH, TEMPERATURE 291K
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 26.10050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.96550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.57550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.96550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.10050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.57550
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14970 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ARG A 63
REMARK 465 ASP A 64
REMARK 465 LYS A 65
REMARK 465 GLU A 84
REMARK 465 ARG A 85
REMARK 465 ASN A 86
REMARK 465 PRO A 87
REMARK 465 SER A 88
REMARK 465 ASP A 89
REMARK 465 GLN A 90
REMARK 465 ARG A 91
REMARK 465 SER A 92
REMARK 465 PHE A 93
REMARK 465 CYS B 62
REMARK 465 ARG B 63
REMARK 465 ASP B 64
REMARK 465 LYS B 65
REMARK 465 ALA B 66
REMARK 465 LEU B 67
REMARK 465 GLN B 142
REMARK 465 ARG C 29
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 ASN A 2 CG OD1 ND2
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 O HOH A 661 O HOH A 662 2.07
REMARK 500 O HOH B 620 O HOH B 698 2.11
REMARK 500 OE2 GLU B 76 O HOH B 544 2.16
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 ARG A 50 122.45 -36.45
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3ECH A 1 142 UNP P52003 MEXR_PSEAE 1 142
DBREF 3ECH B 1 142 UNP P52003 MEXR_PSEAE 1 142
DBREF 3ECH C 29 53 UNP Q9HXS2 Q9HXS2_PSEAE 29 53
SEQADV 3ECH LEU A 106 UNP P52003 GLN 106 ENGINEERED MUTATION
SEQADV 3ECH LEU A 110 UNP P52003 ALA 110 ENGINEERED MUTATION
SEQADV 3ECH LEU B 106 UNP P52003 GLN 106 ENGINEERED MUTATION
SEQADV 3ECH LEU B 110 UNP P52003 ALA 110 ENGINEERED MUTATION
SEQRES 1 A 142 MET ASN TYR PRO VAL ASN PRO ASP LEU MET PRO ALA LEU
SEQRES 2 A 142 MET ALA VAL PHE GLN HIS VAL ARG THR ARG ILE GLN SER
SEQRES 3 A 142 GLU LEU ASP CYS GLN ARG LEU ASP LEU THR PRO PRO ASP
SEQRES 4 A 142 VAL HIS VAL LEU LYS LEU ILE ASP GLU GLN ARG GLY LEU
SEQRES 5 A 142 ASN LEU GLN ASP LEU GLY ARG GLN MET CYS ARG ASP LYS
SEQRES 6 A 142 ALA LEU ILE THR ARG LYS ILE ARG GLU LEU GLU GLY ARG
SEQRES 7 A 142 ASN LEU VAL ARG ARG GLU ARG ASN PRO SER ASP GLN ARG
SEQRES 8 A 142 SER PHE GLN LEU PHE LEU THR ASP GLU GLY LEU ALA ILE
SEQRES 9 A 142 HIS LEU HIS ALA GLU LEU ILE MET SER ARG VAL HIS ASP
SEQRES 10 A 142 GLU LEU PHE ALA PRO LEU THR PRO VAL GLU GLN ALA THR
SEQRES 11 A 142 LEU VAL HIS LEU LEU ASP GLN CYS LEU ALA ALA GLN
SEQRES 1 B 142 MET ASN TYR PRO VAL ASN PRO ASP LEU MET PRO ALA LEU
SEQRES 2 B 142 MET ALA VAL PHE GLN HIS VAL ARG THR ARG ILE GLN SER
SEQRES 3 B 142 GLU LEU ASP CYS GLN ARG LEU ASP LEU THR PRO PRO ASP
SEQRES 4 B 142 VAL HIS VAL LEU LYS LEU ILE ASP GLU GLN ARG GLY LEU
SEQRES 5 B 142 ASN LEU GLN ASP LEU GLY ARG GLN MET CYS ARG ASP LYS
SEQRES 6 B 142 ALA LEU ILE THR ARG LYS ILE ARG GLU LEU GLU GLY ARG
SEQRES 7 B 142 ASN LEU VAL ARG ARG GLU ARG ASN PRO SER ASP GLN ARG
SEQRES 8 B 142 SER PHE GLN LEU PHE LEU THR ASP GLU GLY LEU ALA ILE
SEQRES 9 B 142 HIS LEU HIS ALA GLU LEU ILE MET SER ARG VAL HIS ASP
SEQRES 10 B 142 GLU LEU PHE ALA PRO LEU THR PRO VAL GLU GLN ALA THR
SEQRES 11 B 142 LEU VAL HIS LEU LEU ASP GLN CYS LEU ALA ALA GLN
SEQRES 1 C 25 ARG ARG ASP TYR THR GLU GLN LEU ARG ARG ALA ALA ARG
SEQRES 2 C 25 ARG ASN ALA TRP ASP LEU TYR GLY GLU HIS PHE TYR
FORMUL 4 HOH *212(H2 O)
HELIX 1 1 ASP A 8 GLN A 31 1 24
HELIX 2 2 THR A 36 GLN A 49 1 14
HELIX 3 3 ASN A 53 CYS A 62 1 10
HELIX 4 4 ALA A 66 ARG A 78 1 13
HELIX 5 5 THR A 98 ALA A 121 1 24
HELIX 6 6 THR A 124 ALA A 141 1 18
HELIX 7 7 ASP B 8 GLN B 31 1 24
HELIX 8 8 THR B 36 GLN B 49 1 14
HELIX 9 9 LEU B 54 MET B 61 1 8
HELIX 10 10 ILE B 68 ARG B 78 1 11
HELIX 11 11 THR B 98 ALA B 121 1 24
HELIX 12 12 THR B 124 ALA B 141 1 18
HELIX 13 13 ASP C 31 ASN C 43 1 13
HELIX 14 14 ASN C 43 GLU C 50 1 8
SHEET 1 A 2 VAL A 81 ARG A 82 0
SHEET 2 A 2 PHE A 96 LEU A 97 -1 O PHE A 96 N ARG A 82
SHEET 1 B 3 LEU B 52 ASN B 53 0
SHEET 2 B 3 PHE B 93 LEU B 97 -1 O LEU B 95 N LEU B 52
SHEET 3 B 3 VAL B 81 ARG B 85 -1 N ARG B 82 O PHE B 96
CRYST1 52.201 57.151 91.931 90.00 90.00 90.00 P 21 21 21 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 0.019157 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017498 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010878 0.00000
(ATOM LINES ARE NOT SHOWN.)
END