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HEADER HYDROLASE 02-AUG-16 5L2P
TITLE STRUCTURE OF ARYLESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARYLESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: A-ESTERASE,PARAOXONASE;
COMPND 5 EC: 3.1.1.2,3.1.8.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE 3 ORGANISM_TAXID: 2287;
SOURCE 4 GENE: ARE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI-PICHIA PASTORIS SHUTTLE VECTOR
SOURCE 6 PPPARG4;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 1182032
KEYWDS ARYLESTERASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.B.LEE,Y.J.PARK
REVDAT 1 09-AUG-17 5L2P 0
JRNL AUTH H.B.LEE,Y.J.PARK
JRNL TITL STRUCTURE OF ARYLESTERASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.56 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.56
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 38349
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2029
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) : 2.56
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.63
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1875
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 61.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE SET COUNT : 89
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9684
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.99
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.28000
REMARK 3 B22 (A**2) : -3.92000
REMARK 3 B33 (A**2) : 7.47000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.34000
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): 0.310
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.241
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.393
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9894 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 9781 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13427 ; 1.347 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): 22230 ; 0.754 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1213 ; 5.275 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 450 ;35.009 ;23.889
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1703 ;13.622 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 68 ;13.919 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1508 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11116 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2232 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 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 : 28
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 20
REMARK 3 ORIGIN FOR THE GROUP (A): 45.2599 6.0515 78.3229
REMARK 3 T TENSOR
REMARK 3 T11: 0.3666 T22: 0.3892
REMARK 3 T33: 0.2032 T12: 0.0268
REMARK 3 T13: 0.0704 T23: -0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 4.9298 L22: 7.4705
REMARK 3 L33: 8.4414 L12: 1.0304
REMARK 3 L13: -1.0543 L23: -2.8113
REMARK 3 S TENSOR
REMARK 3 S11: 0.1274 S12: -0.0492 S13: -0.0434
REMARK 3 S21: -0.2352 S22: -0.1557 S23: 0.1136
REMARK 3 S31: 0.3067 S32: 0.5991 S33: 0.0283
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 21 A 72
REMARK 3 ORIGIN FOR THE GROUP (A): 26.2620 15.9618 67.3933
REMARK 3 T TENSOR
REMARK 3 T11: 0.5080 T22: 0.3912
REMARK 3 T33: 0.0974 T12: 0.0175
REMARK 3 T13: 0.0322 T23: -0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 3.4837 L22: 1.7166
REMARK 3 L33: 1.4715 L12: 0.5742
REMARK 3 L13: -0.1059 L23: -0.2306
REMARK 3 S TENSOR
REMARK 3 S11: -0.0738 S12: 0.1656 S13: -0.0153
REMARK 3 S21: -0.3085 S22: 0.0108 S23: -0.1338
REMARK 3 S31: -0.0464 S32: 0.0729 S33: 0.0630
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 73 A 141
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4575 18.8486 74.8171
REMARK 3 T TENSOR
REMARK 3 T11: 0.4187 T22: 0.3406
REMARK 3 T33: 0.0557 T12: 0.0271
REMARK 3 T13: 0.0418 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 2.1685 L22: 2.6971
REMARK 3 L33: 0.7772 L12: 0.3759
REMARK 3 L13: 0.8620 L23: 0.3874
REMARK 3 S TENSOR
REMARK 3 S11: 0.0245 S12: 0.2236 S13: 0.0221
REMARK 3 S21: -0.0956 S22: -0.0452 S23: 0.1049
REMARK 3 S31: -0.1965 S32: -0.0687 S33: 0.0207
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 142 A 212
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8955 19.7631 85.4961
REMARK 3 T TENSOR
REMARK 3 T11: 0.3899 T22: 0.2873
REMARK 3 T33: 0.0758 T12: 0.0224
REMARK 3 T13: 0.0414 T23: -0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 2.7914 L22: 1.2622
REMARK 3 L33: 1.3318 L12: 0.2482
REMARK 3 L13: 0.9180 L23: 0.0100
REMARK 3 S TENSOR
REMARK 3 S11: 0.0311 S12: 0.2067 S13: 0.1239
REMARK 3 S21: -0.1309 S22: -0.0807 S23: 0.0716
REMARK 3 S31: -0.1612 S32: -0.0703 S33: 0.0497
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 213 A 234
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7822 31.8780 85.8094
REMARK 3 T TENSOR
REMARK 3 T11: 0.4286 T22: 0.3243
REMARK 3 T33: 0.2355 T12: 0.0037
REMARK 3 T13: -0.0088 T23: 0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 0.3662 L22: 6.0966
REMARK 3 L33: 5.9155 L12: -1.4593
REMARK 3 L13: 0.5127 L23: -1.3682
REMARK 3 S TENSOR
REMARK 3 S11: -0.0896 S12: 0.0127 S13: 0.0502
REMARK 3 S21: 0.2158 S22: 0.1726 S23: -0.1136
REMARK 3 S31: -0.6657 S32: 0.1568 S33: -0.0830
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 235 A 270
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7476 16.8640 94.1200
REMARK 3 T TENSOR
REMARK 3 T11: 0.3599 T22: 0.3368
REMARK 3 T33: 0.0305 T12: -0.0096
REMARK 3 T13: 0.0412 T23: -0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 8.9786 L22: 3.3775
REMARK 3 L33: 0.8189 L12: -2.1984
REMARK 3 L13: -2.2553 L23: 0.2439
REMARK 3 S TENSOR
REMARK 3 S11: 0.0237 S12: -0.1157 S13: 0.1189
REMARK 3 S21: 0.1582 S22: -0.0037 S23: 0.1713
REMARK 3 S31: -0.1803 S32: -0.1395 S33: -0.0200
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 271 A 306
REMARK 3 ORIGIN FOR THE GROUP (A): 25.6280 5.0214 84.9193
REMARK 3 T TENSOR
REMARK 3 T11: 0.3947 T22: 0.3153
REMARK 3 T33: 0.0850 T12: 0.0437
REMARK 3 T13: 0.0408 T23: -0.0636
REMARK 3 L TENSOR
REMARK 3 L11: 4.1876 L22: 1.4297
REMARK 3 L33: 0.5070 L12: 0.2724
REMARK 3 L13: 0.8433 L23: -0.5661
REMARK 3 S TENSOR
REMARK 3 S11: 0.0299 S12: 0.2773 S13: -0.2912
REMARK 3 S21: 0.0066 S22: 0.0657 S23: 0.1352
REMARK 3 S31: -0.0922 S32: -0.0713 S33: -0.0956
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 7
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2924 11.4093 106.4357
REMARK 3 T TENSOR
REMARK 3 T11: 0.4199 T22: 0.3313
REMARK 3 T33: 0.2827 T12: 0.0572
REMARK 3 T13: 0.0598 T23: -0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 1.1874 L22: 10.2734
REMARK 3 L33: 16.1963 L12: 2.8760
REMARK 3 L13: -3.0302 L23: -2.0524
REMARK 3 S TENSOR
REMARK 3 S11: -0.0721 S12: 0.0687 S13: 0.0039
REMARK 3 S21: -0.2537 S22: 0.2011 S23: -0.0681
REMARK 3 S31: 0.0597 S32: -0.0600 S33: -0.1290
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 8 B 20
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8349 4.8113 116.3213
REMARK 3 T TENSOR
REMARK 3 T11: 0.4464 T22: 0.4174
REMARK 3 T33: 0.2632 T12: -0.0061
REMARK 3 T13: 0.1375 T23: 0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 9.8213 L22: 0.6206
REMARK 3 L33: 12.0389 L12: -1.9316
REMARK 3 L13: 0.5632 L23: -1.5404
REMARK 3 S TENSOR
REMARK 3 S11: -0.1837 S12: -0.4235 S13: 0.2058
REMARK 3 S21: 0.2034 S22: 0.1522 S23: 0.0795
REMARK 3 S31: -0.3481 S32: -0.2234 S33: 0.0315
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 21 B 72
REMARK 3 ORIGIN FOR THE GROUP (A): 14.3572 -14.8787 106.1232
REMARK 3 T TENSOR
REMARK 3 T11: 0.3193 T22: 0.4404
REMARK 3 T33: 0.1832 T12: -0.0334
REMARK 3 T13: 0.1198 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 1.1579 L22: 2.0157
REMARK 3 L33: 3.3793 L12: 0.1729
REMARK 3 L13: 0.7341 L23: 0.5117
REMARK 3 S TENSOR
REMARK 3 S11: 0.0080 S12: -0.2190 S13: -0.2077
REMARK 3 S21: 0.2877 S22: 0.0568 S23: 0.0144
REMARK 3 S31: 0.1242 S32: -0.2202 S33: -0.0648
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 73 B 141
REMARK 3 ORIGIN FOR THE GROUP (A): 20.7113 -17.5783 99.2883
REMARK 3 T TENSOR
REMARK 3 T11: 0.3254 T22: 0.3388
REMARK 3 T33: 0.1511 T12: -0.0490
REMARK 3 T13: 0.1236 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 1.6226 L22: 0.9730
REMARK 3 L33: 2.0659 L12: -0.5185
REMARK 3 L13: 1.5883 L23: 0.0156
REMARK 3 S TENSOR
REMARK 3 S11: 0.0218 S12: -0.0406 S13: -0.1193
REMARK 3 S21: 0.0200 S22: 0.0742 S23: 0.0543
REMARK 3 S31: 0.0512 S32: -0.0768 S33: -0.0960
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 142 B 210
REMARK 3 ORIGIN FOR THE GROUP (A): 31.0064 -10.6778 99.8126
REMARK 3 T TENSOR
REMARK 3 T11: 0.3247 T22: 0.2985
REMARK 3 T33: 0.0838 T12: -0.0230
REMARK 3 T13: 0.1068 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 1.4246 L22: 0.9524
REMARK 3 L33: 0.3395 L12: 0.0639
REMARK 3 L13: 0.2404 L23: -0.2503
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: -0.0346 S13: -0.1403
REMARK 3 S21: 0.0127 S22: -0.0596 S23: 0.1336
REMARK 3 S31: 0.1312 S32: -0.0686 S33: 0.0250
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 211 B 235
REMARK 3 ORIGIN FOR THE GROUP (A): 38.5431 -16.4208 109.0311
REMARK 3 T TENSOR
REMARK 3 T11: 0.3198 T22: 0.2890
REMARK 3 T33: 0.1381 T12: 0.0294
REMARK 3 T13: 0.0418 T23: 0.0757
REMARK 3 L TENSOR
REMARK 3 L11: 3.0952 L22: 2.6095
REMARK 3 L33: 10.8901 L12: 2.1977
REMARK 3 L13: -1.3313 L23: 0.2317
REMARK 3 S TENSOR
REMARK 3 S11: 0.0705 S12: -0.3130 S13: -0.3821
REMARK 3 S21: 0.2141 S22: -0.2250 S23: 0.0046
REMARK 3 S31: 0.0357 S32: 0.2664 S33: 0.1545
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 236 B 305
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9165 -2.9088 94.3328
REMARK 3 T TENSOR
REMARK 3 T11: 0.3120 T22: 0.2986
REMARK 3 T33: 0.1104 T12: -0.0094
REMARK 3 T13: 0.0966 T23: 0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 0.7607 L22: 1.5427
REMARK 3 L33: 1.6484 L12: 0.5306
REMARK 3 L13: 0.2330 L23: 0.9357
REMARK 3 S TENSOR
REMARK 3 S11: -0.0495 S12: 0.0312 S13: -0.1447
REMARK 3 S21: -0.1687 S22: -0.0444 S23: 0.1098
REMARK 3 S31: -0.1464 S32: 0.0193 S33: 0.0938
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 25
REMARK 3 ORIGIN FOR THE GROUP (A): 61.8137 7.8181 90.2284
REMARK 3 T TENSOR
REMARK 3 T11: 0.4735 T22: 0.4274
REMARK 3 T33: 0.1881 T12: -0.0178
REMARK 3 T13: 0.0559 T23: -0.0379
REMARK 3 L TENSOR
REMARK 3 L11: 2.8623 L22: 10.1144
REMARK 3 L33: 2.8537 L12: -1.3099
REMARK 3 L13: -1.9754 L23: 1.6166
REMARK 3 S TENSOR
REMARK 3 S11: 0.1117 S12: 0.4610 S13: 0.1162
REMARK 3 S21: -0.1608 S22: -0.0400 S23: -0.3422
REMARK 3 S31: 0.0891 S32: -0.2513 S33: -0.0717
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 26 C 41
REMARK 3 ORIGIN FOR THE GROUP (A): 72.6783 -4.3972 98.0083
REMARK 3 T TENSOR
REMARK 3 T11: 0.3702 T22: 0.4254
REMARK 3 T33: 0.0272 T12: -0.0028
REMARK 3 T13: 0.0549 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 4.5883 L22: 9.0305
REMARK 3 L33: 8.7591 L12: 2.9315
REMARK 3 L13: 0.1392 L23: 2.6035
REMARK 3 S TENSOR
REMARK 3 S11: 0.1547 S12: 0.4157 S13: -0.0196
REMARK 3 S21: -0.2690 S22: -0.2906 S23: -0.3296
REMARK 3 S31: 0.0521 S32: -0.1242 S33: 0.1359
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 42 C 72
REMARK 3 ORIGIN FOR THE GROUP (A): 77.4506 2.5782 117.9010
REMARK 3 T TENSOR
REMARK 3 T11: 0.2822 T22: 0.3815
REMARK 3 T33: 0.1022 T12: 0.0113
REMARK 3 T13: 0.0777 T23: -0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 2.2659 L22: 8.9322
REMARK 3 L33: 2.0093 L12: 1.2666
REMARK 3 L13: -0.0512 L23: -1.8374
REMARK 3 S TENSOR
REMARK 3 S11: 0.0034 S12: -0.1312 S13: 0.0917
REMARK 3 S21: 0.1486 S22: -0.1583 S23: -0.4723
REMARK 3 S31: 0.0089 S32: 0.1100 S33: 0.1549
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 73 C 140
REMARK 3 ORIGIN FOR THE GROUP (A): 69.0307 -0.7900 116.2354
REMARK 3 T TENSOR
REMARK 3 T11: 0.2845 T22: 0.2788
REMARK 3 T33: 0.0610 T12: 0.0262
REMARK 3 T13: 0.0907 T23: 0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 1.2507 L22: 2.7344
REMARK 3 L33: 1.9516 L12: 0.1911
REMARK 3 L13: 0.7306 L23: 1.0803
REMARK 3 S TENSOR
REMARK 3 S11: -0.0007 S12: -0.0212 S13: 0.0135
REMARK 3 S21: 0.0386 S22: 0.0414 S23: -0.2032
REMARK 3 S31: -0.0123 S32: 0.0666 S33: -0.0407
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 141 C 209
REMARK 3 ORIGIN FOR THE GROUP (A): 57.1949 0.0850 113.3480
REMARK 3 T TENSOR
REMARK 3 T11: 0.3037 T22: 0.2300
REMARK 3 T33: 0.0691 T12: 0.0353
REMARK 3 T13: 0.0962 T23: -0.0196
REMARK 3 L TENSOR
REMARK 3 L11: 2.2448 L22: 0.9075
REMARK 3 L33: 2.0973 L12: 0.1717
REMARK 3 L13: 1.3313 L23: -0.0695
REMARK 3 S TENSOR
REMARK 3 S11: 0.0681 S12: -0.0474 S13: -0.0979
REMARK 3 S21: 0.1075 S22: -0.0246 S23: -0.0993
REMARK 3 S31: 0.2359 S32: -0.0307 S33: -0.0435
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 : C 210 C 236
REMARK 3 ORIGIN FOR THE GROUP (A): 53.4361 -12.3201 110.2092
REMARK 3 T TENSOR
REMARK 3 T11: 0.3797 T22: 0.2878
REMARK 3 T33: 0.1890 T12: -0.0198
REMARK 3 T13: 0.1057 T23: -0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 4.6007 L22: 5.3159
REMARK 3 L33: 1.9750 L12: -1.8233
REMARK 3 L13: 0.2901 L23: 1.7343
REMARK 3 S TENSOR
REMARK 3 S11: 0.0618 S12: 0.4212 S13: -0.2468
REMARK 3 S21: 0.0601 S22: -0.0772 S23: -0.0865
REMARK 3 S31: 0.3291 S32: -0.1632 S33: 0.0153
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 : C 237 C 306
REMARK 3 ORIGIN FOR THE GROUP (A): 55.5113 9.6879 112.4649
REMARK 3 T TENSOR
REMARK 3 T11: 0.3437 T22: 0.2442
REMARK 3 T33: 0.0548 T12: 0.0110
REMARK 3 T13: 0.0853 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 1.7177 L22: 0.5895
REMARK 3 L33: 2.3765 L12: -0.1031
REMARK 3 L13: 0.4570 L23: 0.1256
REMARK 3 S TENSOR
REMARK 3 S11: -0.0547 S12: -0.0284 S13: 0.0424
REMARK 3 S21: 0.1449 S22: 0.0776 S23: -0.0886
REMARK 3 S31: -0.1496 S32: 0.0562 S33: -0.0229
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 : D 1 D 17
REMARK 3 ORIGIN FOR THE GROUP (A): 35.6406 17.1495 122.1648
REMARK 3 T TENSOR
REMARK 3 T11: 0.4434 T22: 0.4521
REMARK 3 T33: 0.1961 T12: 0.0199
REMARK 3 T13: 0.0734 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 11.7794 L22: 11.5589
REMARK 3 L33: 4.6738 L12: -10.0519
REMARK 3 L13: -1.0596 L23: 3.8730
REMARK 3 S TENSOR
REMARK 3 S11: -0.1151 S12: 0.0171 S13: -0.3428
REMARK 3 S21: 0.2659 S22: -0.1695 S23: 0.3251
REMARK 3 S31: 0.1339 S32: -0.3220 S33: 0.2846
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 : D 18 D 41
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5789 35.0934 122.9568
REMARK 3 T TENSOR
REMARK 3 T11: 0.6028 T22: 0.6580
REMARK 3 T33: 0.4461 T12: 0.0160
REMARK 3 T13: 0.0636 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 9.9019 L22: 0.9751
REMARK 3 L33: 0.5205 L12: 0.2036
REMARK 3 L13: -2.0843 L23: -0.2833
REMARK 3 S TENSOR
REMARK 3 S11: 0.0405 S12: -0.4970 S13: -0.4667
REMARK 3 S21: 0.1492 S22: 0.0261 S23: 0.6292
REMARK 3 S31: -0.0458 S32: -0.0257 S33: -0.0666
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 : D 42 D 72
REMARK 3 ORIGIN FOR THE GROUP (A): 56.7292 41.8483 120.8840
REMARK 3 T TENSOR
REMARK 3 T11: 0.3939 T22: 0.3285
REMARK 3 T33: 0.1334 T12: -0.0204
REMARK 3 T13: 0.0130 T23: -0.0735
REMARK 3 L TENSOR
REMARK 3 L11: 3.2132 L22: 3.1896
REMARK 3 L33: 2.4435 L12: -0.9857
REMARK 3 L13: 0.5187 L23: -0.8875
REMARK 3 S TENSOR
REMARK 3 S11: -0.1527 S12: 0.0498 S13: 0.1461
REMARK 3 S21: 0.1982 S22: 0.0486 S23: -0.0499
REMARK 3 S31: -0.1679 S32: 0.0986 S33: 0.1040
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 : D 73 D 170
REMARK 3 ORIGIN FOR THE GROUP (A): 53.5102 38.7088 111.6042
REMARK 3 T TENSOR
REMARK 3 T11: 0.3919 T22: 0.2606
REMARK 3 T33: 0.0929 T12: -0.0084
REMARK 3 T13: 0.0605 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 1.7120 L22: 1.6254
REMARK 3 L33: 1.7761 L12: 0.4954
REMARK 3 L13: 0.8953 L23: -0.3063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0622 S12: 0.0262 S13: 0.2717
REMARK 3 S21: -0.0005 S22: -0.0190 S23: -0.1053
REMARK 3 S31: -0.1182 S32: 0.0592 S33: 0.0813
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 : D 171 D 212
REMARK 3 ORIGIN FOR THE GROUP (A): 41.2298 27.6517 104.5553
REMARK 3 T TENSOR
REMARK 3 T11: 0.3745 T22: 0.2699
REMARK 3 T33: 0.0542 T12: 0.0500
REMARK 3 T13: 0.0625 T23: -0.0602
REMARK 3 L TENSOR
REMARK 3 L11: 2.8488 L22: 2.5435
REMARK 3 L33: 0.9817 L12: 1.5500
REMARK 3 L13: 0.7529 L23: -0.2313
REMARK 3 S TENSOR
REMARK 3 S11: 0.0187 S12: 0.0270 S13: 0.2031
REMARK 3 S21: 0.2051 S22: 0.0141 S23: 0.2455
REMARK 3 S31: -0.2271 S32: -0.1364 S33: -0.0328
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 : D 213 D 285
REMARK 3 ORIGIN FOR THE GROUP (A): 45.8521 27.7275 102.0391
REMARK 3 T TENSOR
REMARK 3 T11: 0.3639 T22: 0.2547
REMARK 3 T33: 0.0471 T12: -0.0167
REMARK 3 T13: 0.0331 T23: -0.0315
REMARK 3 L TENSOR
REMARK 3 L11: 2.4916 L22: 2.4263
REMARK 3 L33: 1.5867 L12: -0.4489
REMARK 3 L13: -0.0535 L23: -0.4053
REMARK 3 S TENSOR
REMARK 3 S11: 0.0095 S12: 0.1579 S13: 0.1426
REMARK 3 S21: -0.2786 S22: -0.0387 S23: 0.1880
REMARK 3 S31: -0.0065 S32: -0.0156 S33: 0.0291
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 : D 286 D 306
REMARK 3 ORIGIN FOR THE GROUP (A): 58.8882 23.1543 116.1397
REMARK 3 T TENSOR
REMARK 3 T11: 0.3100 T22: 0.2602
REMARK 3 T33: 0.0221 T12: 0.0184
REMARK 3 T13: 0.0167 T23: -0.0459
REMARK 3 L TENSOR
REMARK 3 L11: 9.1369 L22: 4.7656
REMARK 3 L33: 4.2343 L12: 1.5332
REMARK 3 L13: -3.1043 L23: -1.1482
REMARK 3 S TENSOR
REMARK 3 S11: 0.0145 S12: -0.2375 S13: -0.0431
REMARK 3 S21: -0.0261 S22: -0.1125 S23: -0.1371
REMARK 3 S31: 0.1617 S32: 0.3468 S33: 0.0980
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 5L2P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1000223117.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : LIQUID NITROGEN-COOLED DOUBLE
REMARK 200 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SCALEPACK
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40400
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.560
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.14100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.80
REMARK 200 R MERGE FOR SHELL (I) : 0.41100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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 2.5.1
REMARK 200 STARTING MODEL: 3AIM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH7.5, 70%(V/V) MPD, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 54.65450
REMARK 290 SMTRY3 2 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 LYS B 306
REMARK 465 ILE C 20
REMARK 465 ASP C 21
REMARK 465 PHE C 22
REMARK 465 THR C 23
REMARK 465 LYS C 24
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 LYS A 306 CG CD CE NZ
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 C 254 NE - CZ - NH2 ANGL. DEV. = -3.2 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 TRP A 86 -0.90 62.75
REMARK 500 SER A 156 -109.11 68.62
REMARK 500 VAL A 183 49.99 34.96
REMARK 500 LYS A 200 114.82 -167.87
REMARK 500 TYR A 202 50.69 -147.99
REMARK 500 PHE A 203 -65.65 66.59
REMARK 500 TYR A 250 47.87 -106.77
REMARK 500 SER B 156 -110.58 69.67
REMARK 500 VAL B 183 48.90 39.21
REMARK 500 PHE B 203 -65.07 69.68
REMARK 500 TYR B 250 51.31 -109.25
REMARK 500 SER C 156 -106.78 69.97
REMARK 500 PHE C 203 -69.08 66.40
REMARK 500 TRP D 86 -3.49 65.48
REMARK 500 SER D 156 -108.65 64.64
REMARK 500 VAL D 183 48.10 39.53
REMARK 500 PHE D 203 -67.33 67.14
REMARK 500 TYR D 250 49.41 -108.19
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5L2P A 1 306 UNP B5BLW5 ARE_SULSF 1 306
DBREF 5L2P B 1 306 UNP B5BLW5 ARE_SULSF 1 306
DBREF 5L2P C 1 306 UNP B5BLW5 ARE_SULSF 1 306
DBREF 5L2P D 1 306 UNP B5BLW5 ARE_SULSF 1 306
SEQRES 1 A 306 MET PRO LEU ASP PRO GLU VAL ARG ASN PHE LEU GLN VAL
SEQRES 2 A 306 TYR TYR LYS ALA ASN ILE ILE ASP PHE THR LYS TYR GLN
SEQRES 3 A 306 PHE GLN GLU ILE ARG GLN LYS VAL ASN GLU LEU LEU ALA
SEQRES 4 A 306 LYS ALA VAL PRO LYS ASP PRO VAL GLY GLU THR ARG ASP
SEQRES 5 A 306 MET LYS ILE LYS LEU GLU ASP TYR GLU LEU PRO ILE ARG
SEQRES 6 A 306 ILE TYR SER PRO ILE LYS ARG THR ASN ASN GLY LEU VAL
SEQRES 7 A 306 MET HIS PHE HIS GLY GLY ALA TRP ILE LEU GLY SER ILE
SEQRES 8 A 306 GLU THR GLU ASP ALA ILE SER ARG ILE LEU SER ASN SER
SEQRES 9 A 306 CYS GLU CYS THR VAL ILE SER VAL ASP TYR ARG LEU ALA
SEQRES 10 A 306 PRO GLU TYR LYS PHE PRO THR ALA VAL TYR ASP CYS PHE
SEQRES 11 A 306 ASN ALA ILE VAL TRP ALA ARG ASP ASN ALA GLY GLU LEU
SEQRES 12 A 306 GLY ILE ASP LYS ASP LYS ILE ALA THR PHE GLY ILE SER
SEQRES 13 A 306 ALA GLY GLY ASN LEU VAL ALA ALA THR SER LEU LEU ALA
SEQRES 14 A 306 ARG ASP ASN LYS LEU LYS LEU THR ALA GLN VAL PRO VAL
SEQRES 15 A 306 VAL PRO PHE VAL TYR LEU ASP LEU ALA SER LYS SER MET
SEQRES 16 A 306 ASN ARG TYR ARG LYS GLY TYR PHE LEU ASP ILE ASN LEU
SEQRES 17 A 306 PRO VAL ASP TYR GLY VAL LYS MET TYR ILE ARG ASP GLU
SEQRES 18 A 306 LYS ASP LEU TYR ASN PRO LEU PHE SER PRO LEU ILE ALA
SEQRES 19 A 306 GLU ASP LEU SER ASN LEU PRO GLN ALA ILE VAL VAL THR
SEQRES 20 A 306 ALA GLU TYR ASP PRO LEU ARG ASP GLN GLY GLU ALA TYR
SEQRES 21 A 306 ALA TYR ARG LEU MET GLU SER GLY VAL PRO THR LEU SER
SEQRES 22 A 306 PHE ARG VAL ASN GLY ASN VAL HIS ALA PHE LEU GLY SER
SEQRES 23 A 306 PRO ARG THR SER ARG GLN VAL THR VAL MET ILE GLY ALA
SEQRES 24 A 306 LEU LEU LYS ASP ILE PHE LYS
SEQRES 1 B 306 MET PRO LEU ASP PRO GLU VAL ARG ASN PHE LEU GLN VAL
SEQRES 2 B 306 TYR TYR LYS ALA ASN ILE ILE ASP PHE THR LYS TYR GLN
SEQRES 3 B 306 PHE GLN GLU ILE ARG GLN LYS VAL ASN GLU LEU LEU ALA
SEQRES 4 B 306 LYS ALA VAL PRO LYS ASP PRO VAL GLY GLU THR ARG ASP
SEQRES 5 B 306 MET LYS ILE LYS LEU GLU ASP TYR GLU LEU PRO ILE ARG
SEQRES 6 B 306 ILE TYR SER PRO ILE LYS ARG THR ASN ASN GLY LEU VAL
SEQRES 7 B 306 MET HIS PHE HIS GLY GLY ALA TRP ILE LEU GLY SER ILE
SEQRES 8 B 306 GLU THR GLU ASP ALA ILE SER ARG ILE LEU SER ASN SER
SEQRES 9 B 306 CYS GLU CYS THR VAL ILE SER VAL ASP TYR ARG LEU ALA
SEQRES 10 B 306 PRO GLU TYR LYS PHE PRO THR ALA VAL TYR ASP CYS PHE
SEQRES 11 B 306 ASN ALA ILE VAL TRP ALA ARG ASP ASN ALA GLY GLU LEU
SEQRES 12 B 306 GLY ILE ASP LYS ASP LYS ILE ALA THR PHE GLY ILE SER
SEQRES 13 B 306 ALA GLY GLY ASN LEU VAL ALA ALA THR SER LEU LEU ALA
SEQRES 14 B 306 ARG ASP ASN LYS LEU LYS LEU THR ALA GLN VAL PRO VAL
SEQRES 15 B 306 VAL PRO PHE VAL TYR LEU ASP LEU ALA SER LYS SER MET
SEQRES 16 B 306 ASN ARG TYR ARG LYS GLY TYR PHE LEU ASP ILE ASN LEU
SEQRES 17 B 306 PRO VAL ASP TYR GLY VAL LYS MET TYR ILE ARG ASP GLU
SEQRES 18 B 306 LYS ASP LEU TYR ASN PRO LEU PHE SER PRO LEU ILE ALA
SEQRES 19 B 306 GLU ASP LEU SER ASN LEU PRO GLN ALA ILE VAL VAL THR
SEQRES 20 B 306 ALA GLU TYR ASP PRO LEU ARG ASP GLN GLY GLU ALA TYR
SEQRES 21 B 306 ALA TYR ARG LEU MET GLU SER GLY VAL PRO THR LEU SER
SEQRES 22 B 306 PHE ARG VAL ASN GLY ASN VAL HIS ALA PHE LEU GLY SER
SEQRES 23 B 306 PRO ARG THR SER ARG GLN VAL THR VAL MET ILE GLY ALA
SEQRES 24 B 306 LEU LEU LYS ASP ILE PHE LYS
SEQRES 1 C 306 MET PRO LEU ASP PRO GLU VAL ARG ASN PHE LEU GLN VAL
SEQRES 2 C 306 TYR TYR LYS ALA ASN ILE ILE ASP PHE THR LYS TYR GLN
SEQRES 3 C 306 PHE GLN GLU ILE ARG GLN LYS VAL ASN GLU LEU LEU ALA
SEQRES 4 C 306 LYS ALA VAL PRO LYS ASP PRO VAL GLY GLU THR ARG ASP
SEQRES 5 C 306 MET LYS ILE LYS LEU GLU ASP TYR GLU LEU PRO ILE ARG
SEQRES 6 C 306 ILE TYR SER PRO ILE LYS ARG THR ASN ASN GLY LEU VAL
SEQRES 7 C 306 MET HIS PHE HIS GLY GLY ALA TRP ILE LEU GLY SER ILE
SEQRES 8 C 306 GLU THR GLU ASP ALA ILE SER ARG ILE LEU SER ASN SER
SEQRES 9 C 306 CYS GLU CYS THR VAL ILE SER VAL ASP TYR ARG LEU ALA
SEQRES 10 C 306 PRO GLU TYR LYS PHE PRO THR ALA VAL TYR ASP CYS PHE
SEQRES 11 C 306 ASN ALA ILE VAL TRP ALA ARG ASP ASN ALA GLY GLU LEU
SEQRES 12 C 306 GLY ILE ASP LYS ASP LYS ILE ALA THR PHE GLY ILE SER
SEQRES 13 C 306 ALA GLY GLY ASN LEU VAL ALA ALA THR SER LEU LEU ALA
SEQRES 14 C 306 ARG ASP ASN LYS LEU LYS LEU THR ALA GLN VAL PRO VAL
SEQRES 15 C 306 VAL PRO PHE VAL TYR LEU ASP LEU ALA SER LYS SER MET
SEQRES 16 C 306 ASN ARG TYR ARG LYS GLY TYR PHE LEU ASP ILE ASN LEU
SEQRES 17 C 306 PRO VAL ASP TYR GLY VAL LYS MET TYR ILE ARG ASP GLU
SEQRES 18 C 306 LYS ASP LEU TYR ASN PRO LEU PHE SER PRO LEU ILE ALA
SEQRES 19 C 306 GLU ASP LEU SER ASN LEU PRO GLN ALA ILE VAL VAL THR
SEQRES 20 C 306 ALA GLU TYR ASP PRO LEU ARG ASP GLN GLY GLU ALA TYR
SEQRES 21 C 306 ALA TYR ARG LEU MET GLU SER GLY VAL PRO THR LEU SER
SEQRES 22 C 306 PHE ARG VAL ASN GLY ASN VAL HIS ALA PHE LEU GLY SER
SEQRES 23 C 306 PRO ARG THR SER ARG GLN VAL THR VAL MET ILE GLY ALA
SEQRES 24 C 306 LEU LEU LYS ASP ILE PHE LYS
SEQRES 1 D 306 MET PRO LEU ASP PRO GLU VAL ARG ASN PHE LEU GLN VAL
SEQRES 2 D 306 TYR TYR LYS ALA ASN ILE ILE ASP PHE THR LYS TYR GLN
SEQRES 3 D 306 PHE GLN GLU ILE ARG GLN LYS VAL ASN GLU LEU LEU ALA
SEQRES 4 D 306 LYS ALA VAL PRO LYS ASP PRO VAL GLY GLU THR ARG ASP
SEQRES 5 D 306 MET LYS ILE LYS LEU GLU ASP TYR GLU LEU PRO ILE ARG
SEQRES 6 D 306 ILE TYR SER PRO ILE LYS ARG THR ASN ASN GLY LEU VAL
SEQRES 7 D 306 MET HIS PHE HIS GLY GLY ALA TRP ILE LEU GLY SER ILE
SEQRES 8 D 306 GLU THR GLU ASP ALA ILE SER ARG ILE LEU SER ASN SER
SEQRES 9 D 306 CYS GLU CYS THR VAL ILE SER VAL ASP TYR ARG LEU ALA
SEQRES 10 D 306 PRO GLU TYR LYS PHE PRO THR ALA VAL TYR ASP CYS PHE
SEQRES 11 D 306 ASN ALA ILE VAL TRP ALA ARG ASP ASN ALA GLY GLU LEU
SEQRES 12 D 306 GLY ILE ASP LYS ASP LYS ILE ALA THR PHE GLY ILE SER
SEQRES 13 D 306 ALA GLY GLY ASN LEU VAL ALA ALA THR SER LEU LEU ALA
SEQRES 14 D 306 ARG ASP ASN LYS LEU LYS LEU THR ALA GLN VAL PRO VAL
SEQRES 15 D 306 VAL PRO PHE VAL TYR LEU ASP LEU ALA SER LYS SER MET
SEQRES 16 D 306 ASN ARG TYR ARG LYS GLY TYR PHE LEU ASP ILE ASN LEU
SEQRES 17 D 306 PRO VAL ASP TYR GLY VAL LYS MET TYR ILE ARG ASP GLU
SEQRES 18 D 306 LYS ASP LEU TYR ASN PRO LEU PHE SER PRO LEU ILE ALA
SEQRES 19 D 306 GLU ASP LEU SER ASN LEU PRO GLN ALA ILE VAL VAL THR
SEQRES 20 D 306 ALA GLU TYR ASP PRO LEU ARG ASP GLN GLY GLU ALA TYR
SEQRES 21 D 306 ALA TYR ARG LEU MET GLU SER GLY VAL PRO THR LEU SER
SEQRES 22 D 306 PHE ARG VAL ASN GLY ASN VAL HIS ALA PHE LEU GLY SER
SEQRES 23 D 306 PRO ARG THR SER ARG GLN VAL THR VAL MET ILE GLY ALA
SEQRES 24 D 306 LEU LEU LYS ASP ILE PHE LYS
HELIX 1 AA1 ASP A 4 ASN A 18 1 15
HELIX 2 AA2 GLN A 26 LYS A 40 1 15
HELIX 3 AA3 GLU A 94 GLU A 106 1 13
HELIX 4 AA4 PRO A 123 ASN A 139 1 17
HELIX 5 AA5 ASN A 139 GLY A 144 1 6
HELIX 6 AA6 SER A 156 ASN A 172 1 17
HELIX 7 AA7 SER A 192 TYR A 198 1 7
HELIX 8 AA8 ASP A 211 ILE A 218 1 8
HELIX 9 AA9 ASP A 220 ASN A 226 5 7
HELIX 10 AB1 SER A 230 ALA A 234 5 5
HELIX 11 AB2 LEU A 253 SER A 267 1 15
HELIX 12 AB3 ALA A 282 LEU A 284 5 3
HELIX 13 AB4 SER A 286 LYS A 306 1 21
HELIX 14 AB5 ASP B 4 ASN B 18 1 15
HELIX 15 AB6 GLN B 26 LYS B 40 1 15
HELIX 16 AB7 GLU B 94 GLU B 106 1 13
HELIX 17 AB8 PRO B 123 ASN B 139 1 17
HELIX 18 AB9 ASN B 139 GLY B 144 1 6
HELIX 19 AC1 ASP B 146 ASP B 148 5 3
HELIX 20 AC2 SER B 156 ASN B 172 1 17
HELIX 21 AC3 SER B 192 ARG B 199 1 8
HELIX 22 AC4 ASP B 211 ILE B 218 1 8
HELIX 23 AC5 ASP B 220 ASN B 226 5 7
HELIX 24 AC6 SER B 230 ALA B 234 5 5
HELIX 25 AC7 LEU B 253 SER B 267 1 15
HELIX 26 AC8 ALA B 282 LEU B 284 5 3
HELIX 27 AC9 SER B 286 PHE B 305 1 20
HELIX 28 AD1 ASP C 4 ASN C 18 1 15
HELIX 29 AD2 GLN C 26 LYS C 40 1 15
HELIX 30 AD3 GLU C 94 GLU C 106 1 13
HELIX 31 AD4 PRO C 123 ASN C 139 1 17
HELIX 32 AD5 ASN C 139 GLY C 144 1 6
HELIX 33 AD6 SER C 156 ASN C 172 1 17
HELIX 34 AD7 SER C 192 ARG C 199 1 8
HELIX 35 AD8 ASP C 211 ILE C 218 1 8
HELIX 36 AD9 ASP C 220 ASN C 226 5 7
HELIX 37 AE1 SER C 230 ALA C 234 5 5
HELIX 38 AE2 LEU C 253 SER C 267 1 15
HELIX 39 AE3 VAL C 280 LEU C 284 5 5
HELIX 40 AE4 SER C 286 PHE C 305 1 20
HELIX 41 AE5 ASP D 4 ASN D 18 1 15
HELIX 42 AE6 GLN D 26 LYS D 40 1 15
HELIX 43 AE7 GLU D 94 GLU D 106 1 13
HELIX 44 AE8 PRO D 123 ASN D 139 1 17
HELIX 45 AE9 ASN D 139 GLY D 144 1 6
HELIX 46 AF1 ASP D 146 ASP D 148 5 3
HELIX 47 AF2 SER D 156 ASN D 172 1 17
HELIX 48 AF3 SER D 192 ARG D 199 1 8
HELIX 49 AF4 ASP D 211 ILE D 218 1 8
HELIX 50 AF5 ASP D 220 ASN D 226 5 7
HELIX 51 AF6 SER D 230 ALA D 234 5 5
HELIX 52 AF7 LEU D 253 SER D 267 1 15
HELIX 53 AF8 ALA D 282 LEU D 284 5 3
HELIX 54 AF9 SER D 286 PHE D 305 1 20
SHEET 1 AA116 GLU A 49 LYS A 56 0
SHEET 2 AA116 GLU A 61 SER A 68 -1 O LEU A 62 N ILE A 55
SHEET 3 AA116 THR A 108 VAL A 112 -1 O VAL A 109 N TYR A 67
SHEET 4 AA116 LEU A 77 PHE A 81 1 N HIS A 80 O ILE A 110
SHEET 5 AA116 ILE A 150 ILE A 155 1 O ALA A 151 N MET A 79
SHEET 6 AA116 ALA A 178 VAL A 182 1 O VAL A 182 N GLY A 154
SHEET 7 AA116 GLN A 242 TYR A 250 1 O ILE A 244 N GLN A 179
SHEET 8 AA116 THR A 271 VAL A 280 1 O VAL A 276 N THR A 247
SHEET 9 AA116 THR B 271 VAL B 280 -1 O SER B 273 N ASN A 277
SHEET 10 AA116 GLN B 242 TYR B 250 1 N THR B 247 O VAL B 276
SHEET 11 AA116 ALA B 178 VAL B 182 1 N GLN B 179 O ILE B 244
SHEET 12 AA116 ILE B 150 ILE B 155 1 N GLY B 154 O VAL B 182
SHEET 13 AA116 LEU B 77 PHE B 81 1 N LEU B 77 O ALA B 151
SHEET 14 AA116 THR B 108 VAL B 112 1 O ILE B 110 N HIS B 80
SHEET 15 AA116 GLU B 61 SER B 68 -1 N TYR B 67 O VAL B 109
SHEET 16 AA116 GLU B 49 LYS B 56 -1 N ARG B 51 O ILE B 66
SHEET 1 AA216 GLU C 49 LYS C 56 0
SHEET 2 AA216 GLU C 61 SER C 68 -1 O ILE C 66 N ARG C 51
SHEET 3 AA216 THR C 108 VAL C 112 -1 O VAL C 109 N TYR C 67
SHEET 4 AA216 LEU C 77 PHE C 81 1 N HIS C 80 O ILE C 110
SHEET 5 AA216 ILE C 150 ILE C 155 1 O ALA C 151 N LEU C 77
SHEET 6 AA216 ALA C 178 VAL C 182 1 O VAL C 182 N GLY C 154
SHEET 7 AA216 GLN C 242 ALA C 248 1 O GLN C 242 N GLN C 179
SHEET 8 AA216 THR C 271 VAL C 276 1 O VAL C 276 N THR C 247
SHEET 9 AA216 THR D 271 VAL D 280 -1 O ASN D 277 N SER C 273
SHEET 10 AA216 GLN D 242 TYR D 250 1 N THR D 247 O VAL D 276
SHEET 11 AA216 ALA D 178 VAL D 182 1 N GLN D 179 O GLN D 242
SHEET 12 AA216 ILE D 150 ILE D 155 1 N GLY D 154 O VAL D 182
SHEET 13 AA216 LEU D 77 PHE D 81 1 N LEU D 77 O ALA D 151
SHEET 14 AA216 THR D 108 VAL D 112 1 O ILE D 110 N HIS D 80
SHEET 15 AA216 GLU D 61 SER D 68 -1 N TYR D 67 O VAL D 109
SHEET 16 AA216 GLU D 49 LYS D 56 -1 N ARG D 51 O ILE D 66
CISPEP 1 ALA A 117 PRO A 118 0 -2.11
CISPEP 2 PHE A 122 PRO A 123 0 5.10
CISPEP 3 LEU A 208 PRO A 209 0 5.75
CISPEP 4 ALA B 117 PRO B 118 0 3.27
CISPEP 5 PHE B 122 PRO B 123 0 3.49
CISPEP 6 LEU B 208 PRO B 209 0 2.97
CISPEP 7 ALA C 117 PRO C 118 0 2.16
CISPEP 8 PHE C 122 PRO C 123 0 6.45
CISPEP 9 LEU C 208 PRO C 209 0 4.23
CISPEP 10 ALA D 117 PRO D 118 0 1.00
CISPEP 11 PHE D 122 PRO D 123 0 2.70
CISPEP 12 LEU D 208 PRO D 209 0 3.76
CRYST1 73.913 109.309 90.044 90.00 109.37 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013529 0.000000 0.004757 0.00000
SCALE2 0.000000 0.009148 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011772 0.00000
TER 2432 LYS A 306
TER 4859 PHE B 305
TER 7252 LYS C 306
TER 9688 LYS D 306
MASTER 809 0 0 54 32 0 0 6 9684 4 0 96
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