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HEADER HYDROLASE 25-MAY-17 5O3V
TITLE STRUCTURAL CHARACTERIZATION OF THE FAST AND PROMISCUOUS MACROCYCLASE
TITLE 2 FROM PLANT - PCY1-S562A BOUND TO PRESEGETALIN B1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDE CYCLASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PUTATIVE PRESEGETALIN B1;
COMPND 8 CHAIN: D, C;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VACCARIA HISPANICA;
SOURCE 3 ORGANISM_TAXID: 39387;
SOURCE 4 GENE: PCY1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: VACCARIA HISPANICA;
SOURCE 9 ORGANISM_TAXID: 39387;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS SEGETALIN BIOSYNTHESIS, PROLYL OLIGOPEPTIDASE, MACROCYCLASE,
KEYWDS 2 PEPTIDASE, BETA-PROPELLER, CLOSED FORM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LUDEWIG,C.M.CZEKSTER,A.F.BENT,J.H.NAISMITH
REVDAT 3 16-OCT-19 5O3V 1 REMARK
REVDAT 2 28-MAR-18 5O3V 1 JRNL
REVDAT 1 07-FEB-18 5O3V 0
JRNL AUTH H.LUDEWIG,C.M.CZEKSTER,E.OUEIS,E.S.MUNDAY,M.ARSHAD,
JRNL AUTH 2 S.A.SYNOWSKY,A.F.BENT,J.H.NAISMITH
JRNL TITL CHARACTERIZATION OF THE FAST AND PROMISCUOUS MACROCYCLASE
JRNL TITL 2 FROM PLANT PCY1 ENABLES THE USE OF SIMPLE SUBSTRATES.
JRNL REF ACS CHEM. BIOL. V. 13 801 2018
JRNL REFN ESSN 1554-8937
JRNL PMID 29377663
JRNL DOI 10.1021/ACSCHEMBIO.8B00050
REMARK 2
REMARK 2 RESOLUTION. 2.17 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 80090
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 : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4273
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) : 2.17
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5874
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.3300
REMARK 3 BIN FREE R VALUE SET COUNT : 328
REMARK 3 BIN FREE R VALUE : 0.3510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11692
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 257
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.19000
REMARK 3 B22 (A**2) : -0.20000
REMARK 3 B33 (A**2) : -3.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.38000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.292
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.213
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.194
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.156
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
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): 12068 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 10943 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16364 ; 1.257 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 25428 ; 0.919 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1471 ; 6.182 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 598 ;33.337 ;23.946
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2017 ;12.778 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 76 ;15.929 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1737 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13503 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2581 ; 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): 5848 ; 1.300 ; 1.145
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5847 ; 1.296 ; 1.144
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7301 ; 2.115 ; 1.707
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 7302 ; 2.116 ; 1.708
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6218 ; 1.813 ; 1.311
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 6202 ; 1.779 ; 1.299
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 9029 ; 2.858 ; 1.890
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 12390 ; 5.252 ;13.022
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 12391 ; 5.252 ;13.024
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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 2
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 4 724 B 4 724 45560 0.05 0.05
REMARK 3 2 D 2 17 C 2 17 406 0.10 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 60
REMARK 3 ORIGIN FOR THE GROUP (A): -7.2670 -12.2440 287.4940
REMARK 3 T TENSOR
REMARK 3 T11: 0.1837 T22: 0.3303
REMARK 3 T33: 0.4363 T12: 0.1012
REMARK 3 T13: -0.1215 T23: -0.1410
REMARK 3 L TENSOR
REMARK 3 L11: 2.8736 L22: 3.3663
REMARK 3 L33: 2.7422 L12: 0.8459
REMARK 3 L13: 0.6753 L23: 0.4668
REMARK 3 S TENSOR
REMARK 3 S11: 0.1413 S12: 0.4848 S13: -0.4433
REMARK 3 S21: -0.5136 S22: 0.0334 S23: 0.0899
REMARK 3 S31: 0.4093 S32: 0.2947 S33: -0.1747
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 61 A 148
REMARK 3 ORIGIN FOR THE GROUP (A): -2.1500 3.1230 322.6150
REMARK 3 T TENSOR
REMARK 3 T11: 0.1232 T22: 0.1601
REMARK 3 T33: 0.3241 T12: 0.0870
REMARK 3 T13: -0.0114 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 1.9665 L22: 1.7477
REMARK 3 L33: 5.0829 L12: -0.1785
REMARK 3 L13: 0.2594 L23: -2.5802
REMARK 3 S TENSOR
REMARK 3 S11: -0.1939 S12: -0.2463 S13: -0.1086
REMARK 3 S21: 0.3264 S22: 0.3101 S23: 0.0500
REMARK 3 S31: -0.5741 S32: -0.1860 S33: -0.1162
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 149 A 266
REMARK 3 ORIGIN FOR THE GROUP (A): -12.8960 -18.1130 324.7700
REMARK 3 T TENSOR
REMARK 3 T11: 0.0372 T22: 0.2671
REMARK 3 T33: 0.6863 T12: 0.0157
REMARK 3 T13: -0.0118 T23: 0.2178
REMARK 3 L TENSOR
REMARK 3 L11: 2.0953 L22: 0.9668
REMARK 3 L33: 1.7547 L12: -1.0419
REMARK 3 L13: 0.4088 L23: -0.3070
REMARK 3 S TENSOR
REMARK 3 S11: -0.1036 S12: -0.4284 S13: -0.7588
REMARK 3 S21: -0.0252 S22: 0.2837 S23: 0.3803
REMARK 3 S31: 0.1117 S32: -0.3129 S33: -0.1801
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 267 A 381
REMARK 3 ORIGIN FOR THE GROUP (A): -31.9020 -4.9580 329.9710
REMARK 3 T TENSOR
REMARK 3 T11: 0.0424 T22: 0.5818
REMARK 3 T33: 0.5834 T12: 0.1475
REMARK 3 T13: 0.0888 T23: 0.2664
REMARK 3 L TENSOR
REMARK 3 L11: 2.4672 L22: 1.9231
REMARK 3 L33: 2.0742 L12: -0.6063
REMARK 3 L13: 0.7907 L23: -0.6811
REMARK 3 S TENSOR
REMARK 3 S11: -0.1225 S12: -0.7423 S13: -0.5540
REMARK 3 S21: 0.1025 S22: 0.3617 S23: 0.2546
REMARK 3 S31: -0.1342 S32: -0.5262 S33: -0.2392
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 382 A 430
REMARK 3 ORIGIN FOR THE GROUP (A): -19.2720 11.9170 328.7170
REMARK 3 T TENSOR
REMARK 3 T11: 0.5178 T22: 0.7149
REMARK 3 T33: 0.4738 T12: 0.3818
REMARK 3 T13: 0.0203 T23: 0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 3.1902 L22: 2.7932
REMARK 3 L33: 4.3441 L12: 2.6325
REMARK 3 L13: -2.4794 L23: -3.2555
REMARK 3 S TENSOR
REMARK 3 S11: 0.0659 S12: -0.7005 S13: 0.0677
REMARK 3 S21: 0.3348 S22: -0.1956 S23: 0.0249
REMARK 3 S31: -0.5857 S32: -0.0575 S33: 0.1297
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 431 A 627
REMARK 3 ORIGIN FOR THE GROUP (A): -22.4010 4.4480 300.7460
REMARK 3 T TENSOR
REMARK 3 T11: 0.0104 T22: 0.2341
REMARK 3 T33: 0.3822 T12: 0.0190
REMARK 3 T13: -0.0149 T23: 0.0301
REMARK 3 L TENSOR
REMARK 3 L11: 1.8295 L22: 0.9781
REMARK 3 L33: 1.5521 L12: -0.7403
REMARK 3 L13: 0.6555 L23: -0.1585
REMARK 3 S TENSOR
REMARK 3 S11: -0.0563 S12: 0.0298 S13: -0.1750
REMARK 3 S21: 0.0307 S22: 0.1483 S23: 0.2253
REMARK 3 S31: -0.1108 S32: -0.2456 S33: -0.0919
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 628 A 724
REMARK 3 ORIGIN FOR THE GROUP (A): -9.3540 -0.4070 291.8650
REMARK 3 T TENSOR
REMARK 3 T11: 0.0157 T22: 0.2937
REMARK 3 T33: 0.4071 T12: 0.0247
REMARK 3 T13: -0.0322 T23: -0.0544
REMARK 3 L TENSOR
REMARK 3 L11: 1.6789 L22: 1.1227
REMARK 3 L33: 2.3085 L12: -0.3186
REMARK 3 L13: 1.0749 L23: -0.8810
REMARK 3 S TENSOR
REMARK 3 S11: 0.1248 S12: 0.4505 S13: -0.2444
REMARK 3 S21: -0.1022 S22: 0.0098 S23: 0.1024
REMARK 3 S31: 0.1063 S32: 0.2396 S33: -0.1345
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 4 B 60
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8250 34.9830 290.3400
REMARK 3 T TENSOR
REMARK 3 T11: 0.1999 T22: 0.4295
REMARK 3 T33: 0.4375 T12: 0.0367
REMARK 3 T13: 0.0156 T23: 0.1833
REMARK 3 L TENSOR
REMARK 3 L11: 2.9283 L22: 3.3588
REMARK 3 L33: 3.7859 L12: 0.3565
REMARK 3 L13: -0.8278 L23: -0.1787
REMARK 3 S TENSOR
REMARK 3 S11: 0.1413 S12: 0.6231 S13: 0.5247
REMARK 3 S21: -0.5746 S22: 0.0424 S23: -0.0755
REMARK 3 S31: -0.5668 S32: -0.1789 S33: -0.1837
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 61 B 230
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4100 30.2310 325.4110
REMARK 3 T TENSOR
REMARK 3 T11: 0.0505 T22: 0.2211
REMARK 3 T33: 0.4581 T12: 0.0339
REMARK 3 T13: -0.0992 T23: -0.0383
REMARK 3 L TENSOR
REMARK 3 L11: 1.4934 L22: 1.7237
REMARK 3 L33: 2.5946 L12: -0.5266
REMARK 3 L13: -1.1034 L23: 1.5613
REMARK 3 S TENSOR
REMARK 3 S11: -0.0763 S12: -0.0440 S13: 0.2985
REMARK 3 S21: 0.1502 S22: 0.1195 S23: -0.0618
REMARK 3 S31: 0.1869 S32: -0.1731 S33: -0.0432
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 231 B 266
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9660 41.5110 330.0030
REMARK 3 T TENSOR
REMARK 3 T11: 0.0283 T22: 0.3731
REMARK 3 T33: 0.6317 T12: -0.0150
REMARK 3 T13: -0.0893 T23: -0.2165
REMARK 3 L TENSOR
REMARK 3 L11: 2.9873 L22: 4.1585
REMARK 3 L33: 7.5345 L12: -0.5602
REMARK 3 L13: -1.0194 L23: -3.4667
REMARK 3 S TENSOR
REMARK 3 S11: -0.0273 S12: -0.1120 S13: 0.5432
REMARK 3 S21: -0.1717 S22: 0.3602 S23: -0.2134
REMARK 3 S31: 0.0788 S32: 0.4240 S33: -0.3328
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 267 B 401
REMARK 3 ORIGIN FOR THE GROUP (A): 36.5440 27.8070 336.6860
REMARK 3 T TENSOR
REMARK 3 T11: 0.1410 T22: 0.6538
REMARK 3 T33: 0.4888 T12: 0.2395
REMARK 3 T13: -0.1804 T23: -0.2432
REMARK 3 L TENSOR
REMARK 3 L11: 2.1356 L22: 2.0192
REMARK 3 L33: 3.2049 L12: -0.3048
REMARK 3 L13: -0.5076 L23: 1.7613
REMARK 3 S TENSOR
REMARK 3 S11: -0.1466 S12: -0.6897 S13: 0.3643
REMARK 3 S21: 0.2136 S22: 0.3698 S23: -0.1724
REMARK 3 S31: 0.4954 S32: 0.7886 S33: -0.2232
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 402 B 522
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8940 9.9270 317.1130
REMARK 3 T TENSOR
REMARK 3 T11: 0.3627 T22: 0.2964
REMARK 3 T33: 0.3954 T12: 0.2409
REMARK 3 T13: -0.0809 T23: -0.0226
REMARK 3 L TENSOR
REMARK 3 L11: 2.3718 L22: 1.7222
REMARK 3 L33: 2.8976 L12: -0.3109
REMARK 3 L13: -1.0465 L23: 0.8438
REMARK 3 S TENSOR
REMARK 3 S11: -0.3568 S12: -0.2255 S13: -0.2156
REMARK 3 S21: 0.3522 S22: 0.3349 S23: -0.1029
REMARK 3 S31: 0.9777 S32: 0.5540 S33: 0.0219
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 523 B 627
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8540 27.9030 302.8650
REMARK 3 T TENSOR
REMARK 3 T11: 0.0149 T22: 0.3444
REMARK 3 T33: 0.4527 T12: -0.0227
REMARK 3 T13: -0.0227 T23: -0.0398
REMARK 3 L TENSOR
REMARK 3 L11: 2.1048 L22: 1.8551
REMARK 3 L33: 2.9859 L12: -0.6313
REMARK 3 L13: -0.7744 L23: 0.1808
REMARK 3 S TENSOR
REMARK 3 S11: 0.0373 S12: 0.1031 S13: 0.4956
REMARK 3 S21: -0.1110 S22: 0.1982 S23: -0.2835
REMARK 3 S31: -0.0959 S32: 0.6246 S33: -0.2355
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 628 B 724
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8580 23.3600 295.3460
REMARK 3 T TENSOR
REMARK 3 T11: 0.0548 T22: 0.3316
REMARK 3 T33: 0.3564 T12: 0.0001
REMARK 3 T13: -0.0566 T23: 0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 1.6818 L22: 1.4765
REMARK 3 L33: 3.2134 L12: 0.0077
REMARK 3 L13: -0.6711 L23: 0.3582
REMARK 3 S TENSOR
REMARK 3 S11: 0.0066 S12: 0.5001 S13: 0.1855
REMARK 3 S21: -0.2301 S22: 0.0458 S23: -0.0548
REMARK 3 S31: 0.0609 S32: -0.0310 S33: -0.0524
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 2 C 14
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5190 4.0030 315.2890
REMARK 3 T TENSOR
REMARK 3 T11: 0.3134 T22: 0.5236
REMARK 3 T33: 0.5059 T12: 0.0015
REMARK 3 T13: 0.0342 T23: -0.0954
REMARK 3 L TENSOR
REMARK 3 L11: 10.8484 L22: 10.6129
REMARK 3 L33: 1.5605 L12: 4.9188
REMARK 3 L13: 4.0362 L23: 1.9235
REMARK 3 S TENSOR
REMARK 3 S11: -0.2213 S12: -0.5463 S13: 0.4921
REMARK 3 S21: -0.1624 S22: -0.1910 S23: 0.9907
REMARK 3 S31: -0.0734 S32: -0.3405 S33: 0.4123
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 : D 1 D 14
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4850 18.9920 318.0040
REMARK 3 T TENSOR
REMARK 3 T11: 0.3656 T22: 0.8277
REMARK 3 T33: 0.6596 T12: -0.0830
REMARK 3 T13: 0.0232 T23: 0.0348
REMARK 3 L TENSOR
REMARK 3 L11: 1.3869 L22: 16.7101
REMARK 3 L33: 3.3256 L12: 2.9430
REMARK 3 L13: 1.2271 L23: 7.3890
REMARK 3 S TENSOR
REMARK 3 S11: 0.3526 S12: -0.3064 S13: 0.5448
REMARK 3 S21: 0.8280 S22: -0.0833 S23: -0.5940
REMARK 3 S31: 0.3119 S32: 0.1887 S33: -0.2693
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.10
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 5O3V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1200005111.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-AUG-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.920
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80090
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.170
REMARK 200 RESOLUTION RANGE LOW (A) : 47.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PCY1-S562A COMPLEX WITH PRESEGB1 WAS
REMARK 280 CRYSTALLIZED AT 13.3 MG/ML WITH 0.163 MM PRESEGB1 IN 34.5% (W/V)
REMARK 280 PEG 3350 AND 70 MM MG SULFATE. FOR CRYO PROTECTION 5 % (V/V)
REMARK 280 GLYCEROL WERE ADDED TO RESERVOIR SOLUTION., VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-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 0.00000
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 APPLY THE FOLLOWING TO CHAINS: A, B, D, 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 MET A 1
REMARK 465 ALA A 2
REMARK 465 THR A 3
REMARK 465 ARG A 281
REMARK 465 GLY A 282
REMARK 465 ARG A 283
REMARK 465 GLU A 284
REMARK 465 ASP A 285
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 ARG B 281
REMARK 465 GLY B 282
REMARK 465 ARG B 283
REMARK 465 GLU B 284
REMARK 465 ASP B 285
REMARK 465 MET D -12
REMARK 465 SER D -11
REMARK 465 PRO D -10
REMARK 465 ILE D -9
REMARK 465 LEU D -8
REMARK 465 ALA D -7
REMARK 465 HIS D -6
REMARK 465 ASP D -5
REMARK 465 VAL D -4
REMARK 465 VAL D -3
REMARK 465 LYS D -2
REMARK 465 PRO D -1
REMARK 465 GLN D 0
REMARK 465 LYS D 9
REMARK 465 ASP D 10
REMARK 465 VAL D 11
REMARK 465 GLU D 12
REMARK 465 MET C -12
REMARK 465 SER C -11
REMARK 465 PRO C -10
REMARK 465 ILE C -9
REMARK 465 LEU C -8
REMARK 465 ALA C -7
REMARK 465 HIS C -6
REMARK 465 ASP C -5
REMARK 465 VAL C -4
REMARK 465 VAL C -3
REMARK 465 LYS C -2
REMARK 465 PRO C -1
REMARK 465 GLN C 0
REMARK 465 GLY C 1
REMARK 465 LYS C 9
REMARK 465 ASP C 10
REMARK 465 VAL C 11
REMARK 465 GLU C 12
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 710 NE - CZ - NH2 ANGL. DEV. = -3.3 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 ALA A 89 -123.36 50.97
REMARK 500 TRP A 175 31.93 75.26
REMARK 500 LYS A 177 -84.69 -110.35
REMARK 500 LEU A 277 -26.46 91.96
REMARK 500 PHE A 296 42.05 -101.97
REMARK 500 ALA A 318 79.88 -156.09
REMARK 500 LYS A 321 165.36 73.22
REMARK 500 GLU A 354 -44.59 65.39
REMARK 500 ASP A 423 87.69 -163.13
REMARK 500 TYR A 481 -74.74 -138.52
REMARK 500 ARG A 528 -121.44 52.61
REMARK 500 ALA A 562 -112.09 60.31
REMARK 500 THR A 598 -120.96 38.06
REMARK 500 CYS A 673 -59.42 -122.19
REMARK 500 ASP A 678 69.84 -154.23
REMARK 500 GLN A 681 98.78 -67.42
REMARK 500 ALA B 89 -122.13 49.51
REMARK 500 TRP B 175 32.75 74.96
REMARK 500 LYS B 177 -85.33 -109.89
REMARK 500 PHE B 296 43.20 -102.15
REMARK 500 ALA B 318 78.93 -156.56
REMARK 500 LYS B 321 165.31 74.70
REMARK 500 GLU B 354 -44.81 65.24
REMARK 500 ASP B 423 87.51 -162.66
REMARK 500 TYR B 481 -74.99 -139.19
REMARK 500 ARG B 528 -121.25 52.55
REMARK 500 ALA B 562 -111.88 61.27
REMARK 500 THR B 598 -122.02 38.43
REMARK 500 ASN B 637 50.18 -118.88
REMARK 500 CYS B 673 -59.74 -122.07
REMARK 500 ASP B 678 70.15 -154.34
REMARK 500 GLN B 681 98.35 -67.30
REMARK 500 ALA D 5 81.54 -66.42
REMARK 500 ALA C 5 80.77 -67.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 904 O
REMARK 620 2 HOH A 911 O 86.3
REMARK 620 3 HOH A 974 O 98.7 103.0
REMARK 620 4 HOH A 975 O 90.8 85.3 167.6
REMARK 620 5 HOH A1006 O 90.5 166.7 90.2 81.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 992 O
REMARK 620 2 HOH B 929 O 95.4
REMARK 620 3 HOH B 961 O 86.9 169.8
REMARK 620 4 HOH B 916 O 86.0 91.7 98.4
REMARK 620 5 HOH B 914 O 167.8 96.8 80.9 94.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 803
DBREF 5O3V A 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5O3V B 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5O3V D -12 18 UNP F6LNL6 F6LNL6_9CARY 1 31
DBREF 5O3V C -12 18 UNP F6LNL6 F6LNL6_9CARY 1 31
SEQADV 5O3V ALA A 562 UNP R4P353 SER 562 ENGINEERED MUTATION
SEQADV 5O3V ALA B 562 UNP R4P353 SER 562 ENGINEERED MUTATION
SEQRES 1 A 724 MET ALA THR SER GLY PHE SER LYS PRO LEU HIS TYR PRO
SEQRES 2 A 724 PRO VAL ARG ARG ASP GLU THR VAL VAL ASP ASP TYR PHE
SEQRES 3 A 724 GLY VAL LYS VAL ALA ASP PRO TYR ARG TRP LEU GLU ASP
SEQRES 4 A 724 PRO ASN SER GLU GLU THR LYS GLU PHE VAL ASP ASN GLN
SEQRES 5 A 724 GLU LYS LEU ALA ASN SER VAL LEU GLU GLU CYS GLU LEU
SEQRES 6 A 724 ILE ASP LYS PHE LYS GLN LYS ILE ILE ASP PHE VAL ASN
SEQRES 7 A 724 PHE PRO ARG CYS GLY VAL PRO PHE ARG ARG ALA ASN LYS
SEQRES 8 A 724 TYR PHE HIS PHE TYR ASN SER GLY LEU GLN ALA GLN ASN
SEQRES 9 A 724 VAL PHE GLN MET GLN ASP ASP LEU ASP GLY LYS PRO GLU
SEQRES 10 A 724 VAL LEU TYR ASP PRO ASN LEU ARG GLU GLY GLY ARG SER
SEQRES 11 A 724 GLY LEU SER LEU TYR SER VAL SER GLU ASP ALA LYS TYR
SEQRES 12 A 724 PHE ALA PHE GLY ILE HIS SER GLY LEU THR GLU TRP VAL
SEQRES 13 A 724 THR ILE LYS ILE LEU LYS THR GLU ASP ARG SER TYR LEU
SEQRES 14 A 724 PRO ASP THR LEU GLU TRP VAL LYS PHE SER PRO ALA ILE
SEQRES 15 A 724 TRP THR HIS ASP ASN LYS GLY PHE PHE TYR CYS PRO TYR
SEQRES 16 A 724 PRO PRO LEU LYS GLU GLY GLU ASP HIS MET THR ARG SER
SEQRES 17 A 724 ALA VAL ASN GLN GLU ALA ARG TYR HIS PHE LEU GLY THR
SEQRES 18 A 724 ASP GLN SER GLU ASP ILE LEU LEU TRP ARG ASP LEU GLU
SEQRES 19 A 724 ASN PRO ALA HIS HIS LEU LYS CYS GLN ILE THR ASP ASP
SEQRES 20 A 724 GLY LYS TYR PHE LEU LEU TYR ILE LEU ASP GLY CYS ASP
SEQRES 21 A 724 ASP ALA ASN LYS VAL TYR CYS LEU ASP LEU THR LYS LEU
SEQRES 22 A 724 PRO ASN GLY LEU GLU SER PHE ARG GLY ARG GLU ASP SER
SEQRES 23 A 724 ALA PRO PHE MET LYS LEU ILE ASP SER PHE ASP ALA SER
SEQRES 24 A 724 TYR THR ALA ILE ALA ASN ASP GLY SER VAL PHE THR PHE
SEQRES 25 A 724 GLN THR ASN LYS ASP ALA PRO ARG LYS LYS LEU VAL ARG
SEQRES 26 A 724 VAL ASP LEU ASN ASN PRO SER VAL TRP THR ASP LEU VAL
SEQRES 27 A 724 PRO GLU SER LYS LYS ASP LEU LEU GLU SER ALA HIS ALA
SEQRES 28 A 724 VAL ASN GLU ASN GLN LEU ILE LEU ARG TYR LEU SER ASP
SEQRES 29 A 724 VAL LYS HIS VAL LEU GLU ILE ARG ASP LEU GLU SER GLY
SEQRES 30 A 724 ALA LEU GLN HIS ARG LEU PRO ILE ASP ILE GLY SER VAL
SEQRES 31 A 724 ASP GLY ILE THR ALA ARG ARG ARG ASP SER VAL VAL PHE
SEQRES 32 A 724 PHE LYS PHE THR SER ILE LEU THR PRO GLY ILE VAL TYR
SEQRES 33 A 724 GLN CYS ASP LEU LYS ASN ASP PRO THR GLN LEU LYS ILE
SEQRES 34 A 724 PHE ARG GLU SER VAL VAL PRO ASP PHE ASP ARG SER GLU
SEQRES 35 A 724 PHE GLU VAL LYS GLN VAL PHE VAL PRO SER LYS ASP GLY
SEQRES 36 A 724 THR LYS ILE PRO ILE PHE ILE ALA ALA ARG LYS GLY ILE
SEQRES 37 A 724 SER LEU ASP GLY SER HIS PRO CYS GLU MET HIS GLY TYR
SEQRES 38 A 724 GLY GLY PHE GLY ILE ASN MET MET PRO THR PHE SER ALA
SEQRES 39 A 724 SER ARG ILE VAL PHE LEU LYS HIS LEU GLY GLY VAL PHE
SEQRES 40 A 724 CYS LEU ALA ASN ILE ARG GLY GLY GLY GLU TYR GLY GLU
SEQRES 41 A 724 GLU TRP HIS LYS ALA GLY PHE ARG ASP LYS LYS GLN ASN
SEQRES 42 A 724 VAL PHE ASP ASP PHE ILE SER ALA ALA GLU TYR LEU ILE
SEQRES 43 A 724 SER SER GLY TYR THR LYS ALA ARG ARG VAL ALA ILE GLU
SEQRES 44 A 724 GLY GLY ALA ASN GLY GLY LEU LEU VAL ALA ALA CYS ILE
SEQRES 45 A 724 ASN GLN ARG PRO ASP LEU PHE GLY CYS ALA GLU ALA ASN
SEQRES 46 A 724 CYS GLY VAL MET ASP MET LEU ARG PHE HIS LYS PHE THR
SEQRES 47 A 724 LEU GLY TYR LEU TRP THR GLY ASP TYR GLY CYS SER ASP
SEQRES 48 A 724 LYS GLU GLU GLU PHE LYS TRP LEU ILE LYS TYR SER PRO
SEQRES 49 A 724 ILE HIS ASN VAL ARG ARG PRO TRP GLU GLN PRO GLY ASN
SEQRES 50 A 724 GLU GLU THR GLN TYR PRO ALA THR MET ILE LEU THR ALA
SEQRES 51 A 724 ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER PHE LYS
SEQRES 52 A 724 LEU LEU ALA THR MET GLN HIS VAL LEU CYS THR SER LEU
SEQRES 53 A 724 GLU ASP SER PRO GLN LYS ASN PRO ILE ILE ALA ARG ILE
SEQRES 54 A 724 GLN ARG LYS ALA ALA HIS TYR GLY ARG ALA THR MET THR
SEQRES 55 A 724 GLN ILE ALA GLU VAL ALA ASP ARG TYR GLY PHE MET ALA
SEQRES 56 A 724 LYS ALA LEU GLU ALA PRO TRP ILE ASP
SEQRES 1 B 724 MET ALA THR SER GLY PHE SER LYS PRO LEU HIS TYR PRO
SEQRES 2 B 724 PRO VAL ARG ARG ASP GLU THR VAL VAL ASP ASP TYR PHE
SEQRES 3 B 724 GLY VAL LYS VAL ALA ASP PRO TYR ARG TRP LEU GLU ASP
SEQRES 4 B 724 PRO ASN SER GLU GLU THR LYS GLU PHE VAL ASP ASN GLN
SEQRES 5 B 724 GLU LYS LEU ALA ASN SER VAL LEU GLU GLU CYS GLU LEU
SEQRES 6 B 724 ILE ASP LYS PHE LYS GLN LYS ILE ILE ASP PHE VAL ASN
SEQRES 7 B 724 PHE PRO ARG CYS GLY VAL PRO PHE ARG ARG ALA ASN LYS
SEQRES 8 B 724 TYR PHE HIS PHE TYR ASN SER GLY LEU GLN ALA GLN ASN
SEQRES 9 B 724 VAL PHE GLN MET GLN ASP ASP LEU ASP GLY LYS PRO GLU
SEQRES 10 B 724 VAL LEU TYR ASP PRO ASN LEU ARG GLU GLY GLY ARG SER
SEQRES 11 B 724 GLY LEU SER LEU TYR SER VAL SER GLU ASP ALA LYS TYR
SEQRES 12 B 724 PHE ALA PHE GLY ILE HIS SER GLY LEU THR GLU TRP VAL
SEQRES 13 B 724 THR ILE LYS ILE LEU LYS THR GLU ASP ARG SER TYR LEU
SEQRES 14 B 724 PRO ASP THR LEU GLU TRP VAL LYS PHE SER PRO ALA ILE
SEQRES 15 B 724 TRP THR HIS ASP ASN LYS GLY PHE PHE TYR CYS PRO TYR
SEQRES 16 B 724 PRO PRO LEU LYS GLU GLY GLU ASP HIS MET THR ARG SER
SEQRES 17 B 724 ALA VAL ASN GLN GLU ALA ARG TYR HIS PHE LEU GLY THR
SEQRES 18 B 724 ASP GLN SER GLU ASP ILE LEU LEU TRP ARG ASP LEU GLU
SEQRES 19 B 724 ASN PRO ALA HIS HIS LEU LYS CYS GLN ILE THR ASP ASP
SEQRES 20 B 724 GLY LYS TYR PHE LEU LEU TYR ILE LEU ASP GLY CYS ASP
SEQRES 21 B 724 ASP ALA ASN LYS VAL TYR CYS LEU ASP LEU THR LYS LEU
SEQRES 22 B 724 PRO ASN GLY LEU GLU SER PHE ARG GLY ARG GLU ASP SER
SEQRES 23 B 724 ALA PRO PHE MET LYS LEU ILE ASP SER PHE ASP ALA SER
SEQRES 24 B 724 TYR THR ALA ILE ALA ASN ASP GLY SER VAL PHE THR PHE
SEQRES 25 B 724 GLN THR ASN LYS ASP ALA PRO ARG LYS LYS LEU VAL ARG
SEQRES 26 B 724 VAL ASP LEU ASN ASN PRO SER VAL TRP THR ASP LEU VAL
SEQRES 27 B 724 PRO GLU SER LYS LYS ASP LEU LEU GLU SER ALA HIS ALA
SEQRES 28 B 724 VAL ASN GLU ASN GLN LEU ILE LEU ARG TYR LEU SER ASP
SEQRES 29 B 724 VAL LYS HIS VAL LEU GLU ILE ARG ASP LEU GLU SER GLY
SEQRES 30 B 724 ALA LEU GLN HIS ARG LEU PRO ILE ASP ILE GLY SER VAL
SEQRES 31 B 724 ASP GLY ILE THR ALA ARG ARG ARG ASP SER VAL VAL PHE
SEQRES 32 B 724 PHE LYS PHE THR SER ILE LEU THR PRO GLY ILE VAL TYR
SEQRES 33 B 724 GLN CYS ASP LEU LYS ASN ASP PRO THR GLN LEU LYS ILE
SEQRES 34 B 724 PHE ARG GLU SER VAL VAL PRO ASP PHE ASP ARG SER GLU
SEQRES 35 B 724 PHE GLU VAL LYS GLN VAL PHE VAL PRO SER LYS ASP GLY
SEQRES 36 B 724 THR LYS ILE PRO ILE PHE ILE ALA ALA ARG LYS GLY ILE
SEQRES 37 B 724 SER LEU ASP GLY SER HIS PRO CYS GLU MET HIS GLY TYR
SEQRES 38 B 724 GLY GLY PHE GLY ILE ASN MET MET PRO THR PHE SER ALA
SEQRES 39 B 724 SER ARG ILE VAL PHE LEU LYS HIS LEU GLY GLY VAL PHE
SEQRES 40 B 724 CYS LEU ALA ASN ILE ARG GLY GLY GLY GLU TYR GLY GLU
SEQRES 41 B 724 GLU TRP HIS LYS ALA GLY PHE ARG ASP LYS LYS GLN ASN
SEQRES 42 B 724 VAL PHE ASP ASP PHE ILE SER ALA ALA GLU TYR LEU ILE
SEQRES 43 B 724 SER SER GLY TYR THR LYS ALA ARG ARG VAL ALA ILE GLU
SEQRES 44 B 724 GLY GLY ALA ASN GLY GLY LEU LEU VAL ALA ALA CYS ILE
SEQRES 45 B 724 ASN GLN ARG PRO ASP LEU PHE GLY CYS ALA GLU ALA ASN
SEQRES 46 B 724 CYS GLY VAL MET ASP MET LEU ARG PHE HIS LYS PHE THR
SEQRES 47 B 724 LEU GLY TYR LEU TRP THR GLY ASP TYR GLY CYS SER ASP
SEQRES 48 B 724 LYS GLU GLU GLU PHE LYS TRP LEU ILE LYS TYR SER PRO
SEQRES 49 B 724 ILE HIS ASN VAL ARG ARG PRO TRP GLU GLN PRO GLY ASN
SEQRES 50 B 724 GLU GLU THR GLN TYR PRO ALA THR MET ILE LEU THR ALA
SEQRES 51 B 724 ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER PHE LYS
SEQRES 52 B 724 LEU LEU ALA THR MET GLN HIS VAL LEU CYS THR SER LEU
SEQRES 53 B 724 GLU ASP SER PRO GLN LYS ASN PRO ILE ILE ALA ARG ILE
SEQRES 54 B 724 GLN ARG LYS ALA ALA HIS TYR GLY ARG ALA THR MET THR
SEQRES 55 B 724 GLN ILE ALA GLU VAL ALA ASP ARG TYR GLY PHE MET ALA
SEQRES 56 B 724 LYS ALA LEU GLU ALA PRO TRP ILE ASP
SEQRES 1 D 31 MET SER PRO ILE LEU ALA HIS ASP VAL VAL LYS PRO GLN
SEQRES 2 D 31 GLY VAL ALA TRP ALA PHE GLN ALA LYS ASP VAL GLU ASN
SEQRES 3 D 31 ALA SER ALA PRO VAL
SEQRES 1 C 31 MET SER PRO ILE LEU ALA HIS ASP VAL VAL LYS PRO GLN
SEQRES 2 C 31 GLY VAL ALA TRP ALA PHE GLN ALA LYS ASP VAL GLU ASN
SEQRES 3 C 31 ALA SER ALA PRO VAL
HET MG A 801 1
HET SO4 A 802 5
HET SO4 A 803 5
HET MG B 801 1
HET SO4 B 802 5
HET SO4 B 803 5
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
FORMUL 5 MG 2(MG 2+)
FORMUL 6 SO4 4(O4 S 2-)
FORMUL 11 HOH *257(H2 O)
HELIX 1 AA1 TYR A 34 ASP A 39 5 6
HELIX 2 AA2 SER A 42 GLU A 62 1 21
HELIX 3 AA3 LEU A 65 ASN A 78 1 14
HELIX 4 AA4 ASP A 121 ARG A 129 5 9
HELIX 5 AA5 ASP A 222 ASP A 226 5 5
HELIX 6 AA6 THR A 271 LEU A 273 5 3
HELIX 7 AA7 ASP A 439 SER A 441 5 3
HELIX 8 AA8 SER A 493 GLY A 504 1 12
HELIX 9 AA9 GLY A 519 ALA A 525 1 7
HELIX 10 AB1 GLY A 526 ASP A 529 5 4
HELIX 11 AB2 LYS A 530 SER A 548 1 19
HELIX 12 AB3 LYS A 552 ARG A 554 5 3
HELIX 13 AB4 ALA A 562 ARG A 575 1 14
HELIX 14 AB5 PRO A 576 PHE A 579 5 4
HELIX 15 AB6 ARG A 593 PHE A 597 5 5
HELIX 16 AB7 LEU A 599 LEU A 602 5 4
HELIX 17 AB8 TRP A 603 GLY A 608 1 6
HELIX 18 AB9 LYS A 612 SER A 623 1 12
HELIX 19 AC1 PRO A 624 ASN A 627 5 4
HELIX 20 AC2 ARG A 630 GLN A 634 5 5
HELIX 21 AC3 PRO A 658 CYS A 673 1 16
HELIX 22 AC4 ALA A 699 GLU A 719 1 21
HELIX 23 AC5 TYR B 34 ASP B 39 5 6
HELIX 24 AC6 SER B 42 GLU B 62 1 21
HELIX 25 AC7 LEU B 65 ASN B 78 1 14
HELIX 26 AC8 ASP B 121 ARG B 129 5 9
HELIX 27 AC9 ASP B 222 ASP B 226 5 5
HELIX 28 AD1 THR B 271 LEU B 273 5 3
HELIX 29 AD2 ASP B 439 SER B 441 5 3
HELIX 30 AD3 SER B 493 LEU B 503 1 11
HELIX 31 AD4 GLY B 519 ALA B 525 1 7
HELIX 32 AD5 GLY B 526 ASP B 529 5 4
HELIX 33 AD6 LYS B 530 SER B 548 1 19
HELIX 34 AD7 LYS B 552 ARG B 554 5 3
HELIX 35 AD8 ALA B 562 ARG B 575 1 14
HELIX 36 AD9 PRO B 576 PHE B 579 5 4
HELIX 37 AE1 ARG B 593 PHE B 597 5 5
HELIX 38 AE2 LEU B 599 LEU B 602 5 4
HELIX 39 AE3 TRP B 603 GLY B 608 1 6
HELIX 40 AE4 LYS B 612 SER B 623 1 12
HELIX 41 AE5 PRO B 624 ASN B 627 5 4
HELIX 42 AE6 ARG B 630 GLN B 634 5 5
HELIX 43 AE7 PRO B 658 CYS B 673 1 16
HELIX 44 AE8 ALA B 699 GLU B 719 1 21
SHEET 1 AA1 2 VAL A 22 TYR A 25 0
SHEET 2 AA1 2 VAL A 28 ALA A 31 -1 O VAL A 28 N TYR A 25
SHEET 1 AA2 3 ARG A 81 CYS A 82 0
SHEET 2 AA2 3 LYS A 91 ASN A 97 -1 O ASN A 97 N ARG A 81
SHEET 3 AA2 3 PHE A 86 ARG A 88 -1 N PHE A 86 O PHE A 93
SHEET 1 AA3 4 ARG A 81 CYS A 82 0
SHEET 2 AA3 4 LYS A 91 ASN A 97 -1 O ASN A 97 N ARG A 81
SHEET 3 AA3 4 VAL A 105 GLN A 109 -1 O VAL A 105 N TYR A 96
SHEET 4 AA3 4 GLU A 117 TYR A 120 -1 O LEU A 119 N PHE A 106
SHEET 1 AA4 4 LEU A 134 VAL A 137 0
SHEET 2 AA4 4 TYR A 143 ILE A 148 -1 O ALA A 145 N SER A 136
SHEET 3 AA4 4 VAL A 156 LYS A 162 -1 O LYS A 159 N PHE A 146
SHEET 4 AA4 4 LEU A 173 VAL A 176 -1 O VAL A 176 N VAL A 156
SHEET 1 AA5 4 ILE A 182 TRP A 183 0
SHEET 2 AA5 4 GLY A 189 TYR A 192 -1 O PHE A 191 N ILE A 182
SHEET 3 AA5 4 ALA A 214 PHE A 218 -1 O ARG A 215 N TYR A 192
SHEET 4 AA5 4 ILE A 227 TRP A 230 -1 O LEU A 229 N ALA A 214
SHEET 1 AA6 4 HIS A 239 ILE A 244 0
SHEET 2 AA6 4 TYR A 250 LEU A 256 -1 O LEU A 252 N GLN A 243
SHEET 3 AA6 4 ASN A 263 ASP A 269 -1 O TYR A 266 N LEU A 253
SHEET 4 AA6 4 MET A 290 ILE A 293 -1 O MET A 290 N CYS A 267
SHEET 1 AA7 4 TYR A 300 ASP A 306 0
SHEET 2 AA7 4 VAL A 309 THR A 314 -1 O THR A 311 N ILE A 303
SHEET 3 AA7 4 LYS A 322 ASP A 327 -1 O VAL A 324 N PHE A 312
SHEET 4 AA7 4 ASN A 330 VAL A 338 -1 O THR A 335 N ARG A 325
SHEET 1 AA8 4 LEU A 345 VAL A 352 0
SHEET 2 AA8 4 GLN A 356 LEU A 362 -1 O ARG A 360 N SER A 348
SHEET 3 AA8 4 HIS A 367 ASP A 373 -1 O VAL A 368 N TYR A 361
SHEET 4 AA8 4 LEU A 379 PRO A 384 -1 O GLN A 380 N ILE A 371
SHEET 1 AA9 4 SER A 389 ASP A 391 0
SHEET 2 AA9 4 VAL A 401 SER A 408 -1 O LYS A 405 N ASP A 391
SHEET 3 AA9 4 THR A 411 ASP A 419 -1 O ILE A 414 N PHE A 406
SHEET 4 AA9 4 LYS A 428 GLU A 432 -1 O ARG A 431 N VAL A 415
SHEET 1 AB1 8 PHE A 443 PRO A 451 0
SHEET 2 AB1 8 LYS A 457 ARG A 465 -1 O ILE A 458 N VAL A 450
SHEET 3 AB1 8 VAL A 506 ALA A 510 -1 O PHE A 507 N ALA A 463
SHEET 4 AB1 8 CYS A 476 HIS A 479 1 N HIS A 479 O CYS A 508
SHEET 5 AB1 8 VAL A 556 GLY A 561 1 O ALA A 557 N CYS A 476
SHEET 6 AB1 8 CYS A 581 ASN A 585 1 O ASN A 585 N GLY A 560
SHEET 7 AB1 8 ALA A 644 ALA A 650 1 O MET A 646 N ALA A 582
SHEET 8 AB1 8 ILE A 685 GLN A 690 1 O GLN A 690 N THR A 649
SHEET 1 AB2 2 VAL B 22 TYR B 25 0
SHEET 2 AB2 2 VAL B 28 ALA B 31 -1 O VAL B 28 N TYR B 25
SHEET 1 AB3 3 ARG B 81 CYS B 82 0
SHEET 2 AB3 3 LYS B 91 ASN B 97 -1 O ASN B 97 N ARG B 81
SHEET 3 AB3 3 PHE B 86 ARG B 88 -1 N PHE B 86 O PHE B 93
SHEET 1 AB4 4 ARG B 81 CYS B 82 0
SHEET 2 AB4 4 LYS B 91 ASN B 97 -1 O ASN B 97 N ARG B 81
SHEET 3 AB4 4 VAL B 105 GLN B 109 -1 O VAL B 105 N TYR B 96
SHEET 4 AB4 4 GLU B 117 TYR B 120 -1 O LEU B 119 N PHE B 106
SHEET 1 AB5 4 LEU B 134 VAL B 137 0
SHEET 2 AB5 4 TYR B 143 ILE B 148 -1 O ALA B 145 N SER B 136
SHEET 3 AB5 4 VAL B 156 LYS B 162 -1 O LYS B 159 N PHE B 146
SHEET 4 AB5 4 TYR B 168 VAL B 176 -1 O VAL B 176 N VAL B 156
SHEET 1 AB6 4 ILE B 182 TRP B 183 0
SHEET 2 AB6 4 GLY B 189 TYR B 192 -1 O PHE B 191 N ILE B 182
SHEET 3 AB6 4 ALA B 214 PHE B 218 -1 O ARG B 215 N TYR B 192
SHEET 4 AB6 4 ILE B 227 TRP B 230 -1 O LEU B 229 N ALA B 214
SHEET 1 AB7 4 HIS B 239 ILE B 244 0
SHEET 2 AB7 4 TYR B 250 LEU B 256 -1 O LEU B 252 N GLN B 243
SHEET 3 AB7 4 ASN B 263 ASP B 269 -1 O TYR B 266 N LEU B 253
SHEET 4 AB7 4 MET B 290 ILE B 293 -1 O MET B 290 N CYS B 267
SHEET 1 AB8 4 TYR B 300 ASP B 306 0
SHEET 2 AB8 4 VAL B 309 THR B 314 -1 O THR B 311 N ILE B 303
SHEET 3 AB8 4 LYS B 322 ASP B 327 -1 O VAL B 324 N PHE B 312
SHEET 4 AB8 4 ASN B 330 VAL B 338 -1 O THR B 335 N ARG B 325
SHEET 1 AB9 4 LEU B 345 VAL B 352 0
SHEET 2 AB9 4 GLN B 356 LEU B 362 -1 O ARG B 360 N SER B 348
SHEET 3 AB9 4 HIS B 367 ASP B 373 -1 O VAL B 368 N TYR B 361
SHEET 4 AB9 4 LEU B 379 PRO B 384 -1 O GLN B 380 N ILE B 371
SHEET 1 AC1 4 SER B 389 ASP B 391 0
SHEET 2 AC1 4 VAL B 401 SER B 408 -1 O LYS B 405 N ASP B 391
SHEET 3 AC1 4 THR B 411 ASP B 419 -1 O ILE B 414 N PHE B 406
SHEET 4 AC1 4 LYS B 428 GLU B 432 -1 O ARG B 431 N VAL B 415
SHEET 1 AC2 8 PHE B 443 PRO B 451 0
SHEET 2 AC2 8 LYS B 457 ARG B 465 -1 O ILE B 458 N VAL B 450
SHEET 3 AC2 8 VAL B 506 ALA B 510 -1 O PHE B 507 N ALA B 463
SHEET 4 AC2 8 CYS B 476 HIS B 479 1 N HIS B 479 O CYS B 508
SHEET 5 AC2 8 VAL B 556 GLY B 561 1 O ALA B 557 N CYS B 476
SHEET 6 AC2 8 CYS B 581 ASN B 585 1 O ASN B 585 N GLY B 560
SHEET 7 AC2 8 ALA B 644 ALA B 650 1 O MET B 646 N ALA B 582
SHEET 8 AC2 8 ILE B 685 GLN B 690 1 O GLN B 690 N THR B 649
LINK MG MG A 801 O HOH A 904 1555 1555 2.01
LINK MG MG A 801 O HOH A 911 1555 1555 2.02
LINK MG MG A 801 O HOH A 974 1555 1555 2.17
LINK MG MG A 801 O HOH A 975 1555 1555 2.17
LINK MG MG A 801 O HOH A1006 1555 1555 2.06
LINK MG MG B 801 O HOH B 992 1555 1555 1.86
LINK MG MG B 801 O HOH B 929 1555 1555 2.27
LINK MG MG B 801 O HOH B 961 1555 1555 2.05
LINK MG MG B 801 O HOH B 916 1555 1555 2.10
LINK MG MG B 801 O HOH B 914 1555 1555 2.29
SITE 1 AC1 6 HIS A 652 HOH A 904 HOH A 911 HOH A 974
SITE 2 AC1 6 HOH A 975 HOH A1006
SITE 1 AC2 5 GLY A 151 LEU A 152 THR A 153 HOH A 911
SITE 2 AC2 5 HOH A 975
SITE 1 AC3 1 ARG A 593
SITE 1 AC4 6 HIS B 652 HOH B 914 HOH B 916 HOH B 929
SITE 2 AC4 6 HOH B 961 HOH B 992
SITE 1 AC5 5 GLY B 151 LEU B 152 THR B 153 HOH B 914
SITE 2 AC5 5 HOH B 961
SITE 1 AC6 1 ARG B 593
CRYST1 88.860 65.200 140.170 90.00 95.91 90.00 P 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011254 0.000000 0.001165 0.00000
SCALE2 0.000000 0.015337 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007172 0.00000
TER 5776 ASP A 724
TER 11548 ASP B 724
TER 11648 VAL D 18
TER 11744 VAL C 18
MASTER 698 0 6 44 82 0 10 611971 4 34 118
END |