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HEADER HYDROLASE 25-MAY-17 5O3X
TITLE STRUCTURAL CHARACTERIZATION OF THE FAST AND PROMISCUOUS MACROCYCLASE
TITLE 2 FROM PLANT - APO PCY1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDE CYCLASE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 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 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PJ414
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 5O3X 1 REMARK
REVDAT 2 28-MAR-18 5O3X 1 JRNL
REVDAT 1 07-FEB-18 5O3X 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. 2.55 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) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 87.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 44824
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2362
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) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3310
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.06
REMARK 3 BIN R VALUE (WORKING SET) : 0.3250
REMARK 3 BIN FREE R VALUE SET COUNT : 162
REMARK 3 BIN FREE R VALUE : 0.3710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11414
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 139
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.98000
REMARK 3 B22 (A**2) : 2.07000
REMARK 3 B33 (A**2) : 1.98000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.88000
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): 0.349
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.334
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.652
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.909
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 11721 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 10645 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 15876 ; 1.242 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 24728 ; 0.912 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1417 ; 6.444 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 587 ;32.877 ;23.969
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1972 ;14.835 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 76 ;14.818 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1679 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 13105 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2503 ; 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): 5677 ; 0.806 ; 2.909
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 5676 ; 0.806 ; 2.909
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7088 ; 1.395 ; 4.362
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 7089 ; 1.395 ; 4.362
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6044 ; 0.681 ; 2.976
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 6045 ; 0.681 ; 2.977
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 8788 ; 1.166 ; 4.443
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 12502 ; 4.152 ;33.061
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 12500 ; 4.148 ;33.051
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 : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 8 724 B 8 724 45458 0.08 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
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 8 A 73
REMARK 3 ORIGIN FOR THE GROUP (A): 289.8900 5.6350 4.5460
REMARK 3 T TENSOR
REMARK 3 T11: 0.1703 T22: 0.7969
REMARK 3 T33: 0.3567 T12: -0.1559
REMARK 3 T13: 0.0459 T23: -0.0434
REMARK 3 L TENSOR
REMARK 3 L11: 2.3826 L22: 3.4742
REMARK 3 L33: 2.6338 L12: 1.1010
REMARK 3 L13: -0.6858 L23: -1.1095
REMARK 3 S TENSOR
REMARK 3 S11: -0.1140 S12: 0.1127 S13: -0.1121
REMARK 3 S21: -0.3045 S22: 0.2027 S23: 0.5390
REMARK 3 S31: 0.4134 S32: -0.9530 S33: -0.0887
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 74 A 134
REMARK 3 ORIGIN FOR THE GROUP (A): 324.3230 19.6640 -3.0330
REMARK 3 T TENSOR
REMARK 3 T11: 0.1284 T22: 0.1315
REMARK 3 T33: 0.1918 T12: -0.0192
REMARK 3 T13: 0.1052 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 7.9269 L22: 2.9731
REMARK 3 L33: 3.6709 L12: -1.9760
REMARK 3 L13: 1.4513 L23: -1.8571
REMARK 3 S TENSOR
REMARK 3 S11: -0.2235 S12: 0.3854 S13: 0.4242
REMARK 3 S21: 0.0518 S22: 0.1147 S23: -0.0413
REMARK 3 S31: -0.0279 S32: -0.0520 S33: 0.1088
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 135 A 272
REMARK 3 ORIGIN FOR THE GROUP (A): 326.9330 -1.4850 5.4530
REMARK 3 T TENSOR
REMARK 3 T11: 0.1865 T22: 0.1316
REMARK 3 T33: 0.2651 T12: -0.0007
REMARK 3 T13: 0.1635 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 2.8533 L22: 2.4852
REMARK 3 L33: 3.9912 L12: 0.3322
REMARK 3 L13: -0.0210 L23: -0.3178
REMARK 3 S TENSOR
REMARK 3 S11: -0.1094 S12: -0.1763 S13: -0.0514
REMARK 3 S21: -0.1731 S22: 0.0357 S23: 0.1912
REMARK 3 S31: 0.5086 S32: -0.2139 S33: 0.0737
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 273 A 434
REMARK 3 ORIGIN FOR THE GROUP (A): 330.7230 15.4170 20.8710
REMARK 3 T TENSOR
REMARK 3 T11: 0.0381 T22: 0.3771
REMARK 3 T33: 0.2066 T12: 0.0270
REMARK 3 T13: 0.0403 T23: -0.1225
REMARK 3 L TENSOR
REMARK 3 L11: 3.3719 L22: 2.1724
REMARK 3 L33: 2.9760 L12: -0.5331
REMARK 3 L13: 0.0695 L23: -0.9045
REMARK 3 S TENSOR
REMARK 3 S11: -0.0838 S12: -0.3530 S13: 0.3280
REMARK 3 S21: 0.0153 S22: -0.0832 S23: -0.0708
REMARK 3 S31: -0.1474 S32: 0.0445 S33: 0.1670
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 435 A 490
REMARK 3 ORIGIN FOR THE GROUP (A): 304.9400 28.4830 20.6050
REMARK 3 T TENSOR
REMARK 3 T11: 0.2305 T22: 0.5580
REMARK 3 T33: 0.4683 T12: 0.1807
REMARK 3 T13: 0.0603 T23: -0.2302
REMARK 3 L TENSOR
REMARK 3 L11: 2.7619 L22: 4.7146
REMARK 3 L33: 1.4772 L12: -0.7967
REMARK 3 L13: 0.1520 L23: 1.0230
REMARK 3 S TENSOR
REMARK 3 S11: -0.1044 S12: -0.1903 S13: 0.8182
REMARK 3 S21: -0.1816 S22: 0.0769 S23: -0.1072
REMARK 3 S31: -0.4477 S32: -0.3642 S33: 0.0275
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 491 A 724
REMARK 3 ORIGIN FOR THE GROUP (A): 296.9380 12.7920 15.6480
REMARK 3 T TENSOR
REMARK 3 T11: 0.1087 T22: 0.7386
REMARK 3 T33: 0.2547 T12: -0.0200
REMARK 3 T13: 0.0956 T23: -0.0806
REMARK 3 L TENSOR
REMARK 3 L11: 2.3667 L22: 1.5672
REMARK 3 L33: 2.7906 L12: -0.0862
REMARK 3 L13: 0.2481 L23: -0.4090
REMARK 3 S TENSOR
REMARK 3 S11: -0.0728 S12: -0.3289 S13: 0.1200
REMARK 3 S21: -0.0884 S22: 0.1233 S23: 0.2104
REMARK 3 S31: 0.2635 S32: -0.8578 S33: -0.0504
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 : B 5 B 124
REMARK 3 ORIGIN FOR THE GROUP (A): 302.7970 38.3500 -18.7160
REMARK 3 T TENSOR
REMARK 3 T11: 0.2584 T22: 0.3303
REMARK 3 T33: 0.1498 T12: -0.0005
REMARK 3 T13: 0.1380 T23: -0.0912
REMARK 3 L TENSOR
REMARK 3 L11: 4.3427 L22: 1.0923
REMARK 3 L33: 1.2513 L12: 0.1247
REMARK 3 L13: 0.5024 L23: -0.3887
REMARK 3 S TENSOR
REMARK 3 S11: 0.2152 S12: -0.2919 S13: -0.2470
REMARK 3 S21: 0.1273 S22: -0.1411 S23: 0.1240
REMARK 3 S31: -0.2203 S32: -0.2568 S33: -0.0742
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 125 B 272
REMARK 3 ORIGIN FOR THE GROUP (A): 325.9040 51.5190 -25.0510
REMARK 3 T TENSOR
REMARK 3 T11: 0.1032 T22: 0.1658
REMARK 3 T33: 0.2634 T12: -0.0092
REMARK 3 T13: 0.1436 T23: -0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 2.7546 L22: 2.7721
REMARK 3 L33: 5.0209 L12: -0.3339
REMARK 3 L13: 1.1676 L23: -0.4313
REMARK 3 S TENSOR
REMARK 3 S11: -0.0824 S12: 0.1047 S13: 0.1533
REMARK 3 S21: 0.2522 S22: 0.1114 S23: 0.1904
REMARK 3 S31: -0.2069 S32: -0.3172 S33: -0.0290
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 273 B 382
REMARK 3 ORIGIN FOR THE GROUP (A): 327.8430 41.6900 -44.5830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1056 T22: 0.6458
REMARK 3 T33: 0.1824 T12: -0.0304
REMARK 3 T13: 0.1075 T23: -0.0433
REMARK 3 L TENSOR
REMARK 3 L11: 2.9823 L22: 3.1410
REMARK 3 L33: 2.6905 L12: 0.4454
REMARK 3 L13: 0.5714 L23: -0.3043
REMARK 3 S TENSOR
REMARK 3 S11: -0.1282 S12: 0.8085 S13: 0.0546
REMARK 3 S21: -0.0961 S22: 0.0915 S23: -0.0516
REMARK 3 S31: -0.2411 S32: 0.4193 S33: 0.0367
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 383 B 440
REMARK 3 ORIGIN FOR THE GROUP (A): 323.8020 22.8550 -30.7240
REMARK 3 T TENSOR
REMARK 3 T11: 0.3009 T22: 0.3486
REMARK 3 T33: 0.3360 T12: 0.0552
REMARK 3 T13: 0.1159 T23: -0.1440
REMARK 3 L TENSOR
REMARK 3 L11: 9.3714 L22: 3.7888
REMARK 3 L33: 2.5198 L12: 4.3425
REMARK 3 L13: -2.1140 L23: -2.5837
REMARK 3 S TENSOR
REMARK 3 S11: 0.0345 S12: 0.0259 S13: -0.6794
REMARK 3 S21: 0.1632 S22: 0.0132 S23: -0.0438
REMARK 3 S31: 0.2597 S32: 0.1544 S33: -0.0477
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 441 B 625
REMARK 3 ORIGIN FOR THE GROUP (A): 297.7060 33.7460 -37.5550
REMARK 3 T TENSOR
REMARK 3 T11: 0.0483 T22: 0.4539
REMARK 3 T33: 0.1513 T12: 0.0158
REMARK 3 T13: 0.0713 T23: -0.0965
REMARK 3 L TENSOR
REMARK 3 L11: 3.3824 L22: 2.4585
REMARK 3 L33: 3.3228 L12: 0.4417
REMARK 3 L13: -0.2246 L23: -0.6609
REMARK 3 S TENSOR
REMARK 3 S11: 0.0700 S12: 0.3230 S13: -0.1637
REMARK 3 S21: 0.0532 S22: -0.0040 S23: 0.0480
REMARK 3 S31: -0.1135 S32: -0.0912 S33: -0.0661
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 626 B 724
REMARK 3 ORIGIN FOR THE GROUP (A): 288.7910 37.4520 -24.2770
REMARK 3 T TENSOR
REMARK 3 T11: 0.1653 T22: 0.4137
REMARK 3 T33: 0.2254 T12: 0.0050
REMARK 3 T13: 0.1279 T23: -0.0891
REMARK 3 L TENSOR
REMARK 3 L11: 1.7655 L22: 2.2197
REMARK 3 L33: 3.8583 L12: -0.3738
REMARK 3 L13: 0.2528 L23: -1.5841
REMARK 3 S TENSOR
REMARK 3 S11: 0.1322 S12: -0.3353 S13: 0.0101
REMARK 3 S21: 0.2449 S22: -0.0749 S23: -0.0404
REMARK 3 S31: -0.4943 S32: -0.2769 S33: -0.0573
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.00
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 5O3X 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_1200005109.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-15
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
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
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 : 44824
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 87.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.5000
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: 1QFS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12.2 MG/ML PCY1 IN 33% (W/V) PEG 2000,
REMARK 280 113.75 MM MG FORMATE AND 0.1 M NA CACODYLATE PH 7.0. FOR CRYO
REMARK 280 PROTECTION 10% (V/V) GLYCEROL WERE ADDED TO RESERVOIR SOLUTION.,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 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 3555 X+1/2,Y+1/2,Z
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 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 SMTRY1 3 1.000000 0.000000 0.000000 137.79000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.42500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 137.79000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.42500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 THR A 3
REMARK 465 SER A 4
REMARK 465 GLY A 5
REMARK 465 PHE A 6
REMARK 465 SER A 7
REMARK 465 GLY A 282
REMARK 465 ARG A 283
REMARK 465 GLU A 284
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 SER B 4
REMARK 465 LEU B 198
REMARK 465 LYS B 199
REMARK 465 GLU B 200
REMARK 465 GLY B 201
REMARK 465 GLU B 202
REMARK 465 ASP B 203
REMARK 465 HIS B 204
REMARK 465 MET B 205
REMARK 465 THR B 206
REMARK 465 ARG B 207
REMARK 465 ALA B 694
REMARK 465 HIS B 695
REMARK 465 TYR B 696
REMARK 465 GLY B 697
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 SER B 279 OG
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 -125.11 53.07
REMARK 500 ASP A 111 178.59 62.32
REMARK 500 GLU A 126 39.54 23.31
REMARK 500 TYR A 135 85.45 -154.78
REMARK 500 ASP A 165 17.37 -141.18
REMARK 500 TRP A 175 36.37 70.81
REMARK 500 LYS A 177 -83.66 -114.32
REMARK 500 PHE A 296 32.78 -98.67
REMARK 500 ALA A 318 78.88 -163.38
REMARK 500 LYS A 321 159.69 67.39
REMARK 500 GLU A 354 -52.59 64.74
REMARK 500 ASP A 423 56.90 -159.97
REMARK 500 TYR A 481 -71.66 -136.43
REMARK 500 PHE A 484 19.92 59.77
REMARK 500 ARG A 528 -135.86 51.14
REMARK 500 SER A 562 -108.42 57.85
REMARK 500 THR A 598 -121.75 53.21
REMARK 500 SER A 623 109.83 -46.84
REMARK 500 ARG A 655 -71.84 -72.43
REMARK 500 GLN A 681 98.43 -63.93
REMARK 500 ALA A 694 -166.27 -111.11
REMARK 500 ALA B 89 -125.92 53.65
REMARK 500 ASP B 111 178.77 62.59
REMARK 500 GLU B 126 34.40 27.45
REMARK 500 TYR B 135 85.96 -154.73
REMARK 500 ASP B 165 17.27 -140.66
REMARK 500 TRP B 175 37.15 72.19
REMARK 500 LYS B 177 -82.92 -113.70
REMARK 500 ALA B 209 72.37 9.74
REMARK 500 ASN B 275 -174.02 57.16
REMARK 500 ARG B 283 -90.66 -5.55
REMARK 500 GLU B 284 66.22 27.40
REMARK 500 SER B 286 135.54 71.61
REMARK 500 PHE B 296 34.24 -99.77
REMARK 500 ALA B 318 79.59 -162.75
REMARK 500 LYS B 321 160.18 67.03
REMARK 500 GLU B 354 -53.40 66.14
REMARK 500 GLN B 380 -56.41 -121.18
REMARK 500 TYR B 481 -70.55 -136.71
REMARK 500 PHE B 484 19.67 59.05
REMARK 500 ARG B 528 -135.21 52.43
REMARK 500 SER B 562 -107.89 57.64
REMARK 500 THR B 598 -120.74 51.72
REMARK 500 SER B 623 109.90 -47.23
REMARK 500 ARG B 655 -72.73 -73.53
REMARK 500 GLN B 681 98.48 -64.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY B 636 ASN B 637 -146.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAC A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CAC B 801
DBREF 5O3X A 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5O3X B 1 724 UNP R4P353 R4P353_9CARY 1 724
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 SER 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 SER 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
HET CAC A 801 5
HET CAC B 801 5
HETNAM CAC CACODYLATE ION
HETSYN CAC DIMETHYLARSINATE
FORMUL 3 CAC 2(C2 H6 AS O2 1-)
FORMUL 5 HOH *139(H2 O)
HELIX 1 AA1 TYR A 34 ASP A 39 5 6
HELIX 2 AA2 SER A 42 CYS A 63 1 22
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 GLY A 276 PHE A 280 5 5
HELIX 7 AA7 ASP A 439 SER A 441 5 3
HELIX 8 AA8 SER A 493 LEU A 503 1 11
HELIX 9 AA9 GLY A 519 ALA A 525 1 7
HELIX 10 AB1 GLY A 526 LYS A 530 5 5
HELIX 11 AB2 LYS A 531 SER A 548 1 18
HELIX 12 AB3 LYS A 552 ARG A 554 5 3
HELIX 13 AB4 SER 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 LEU A 718 1 20
HELIX 23 AC5 TYR B 34 ASP B 39 5 6
HELIX 24 AC6 SER B 42 CYS B 63 1 22
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 GLY B 276 ARG B 281 5 6
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 LYS B 530 5 5
HELIX 33 AD6 LYS B 531 SER B 548 1 18
HELIX 34 AD7 LYS B 552 ARG B 554 5 3
HELIX 35 AD8 SER 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 LEU B 718 1 20
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 30 N ASP A 23
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 ASP A 110 -1 O GLN A 107 N HIS A 94
SHEET 4 AA3 4 GLU A 117 TYR A 120 -1 O LEU A 119 N PHE A 106
SHEET 1 AA4 4 TYR A 135 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 TYR A 168 VAL A 176 -1 O LEU A 169 N ILE A 160
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 TYR A 254 N LYS A 241
SHEET 3 AA6 4 LYS A 264 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 326 N PHE A 310
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 SER A 363 -1 O ILE A 358 N HIS A 350
SHEET 3 AA8 4 LYS A 366 ASP A 373 -1 O VAL A 368 N TYR A 361
SHEET 4 AA8 4 LEU A 379 PRO A 384 -1 O LEU A 383 N LEU A 369
SHEET 1 AA9 4 SER A 389 ASP A 391 0
SHEET 2 AA9 4 VAL A 401 SER A 408 -1 O THR A 407 N SER A 389
SHEET 3 AA9 4 THR A 411 ASP A 419 -1 O TYR A 416 N PHE A 404
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 462 N LYS A 446
SHEET 3 AB1 8 VAL A 506 ALA A 510 -1 O LEU A 509 N PHE A 461
SHEET 4 AB1 8 CYS A 476 HIS A 479 1 N GLU A 477 O VAL A 506
SHEET 5 AB1 8 VAL A 556 GLY A 561 1 O ALA A 557 N MET A 478
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 ILE A 686 N THR A 645
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 30 N ASP B 23
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 ASP B 110 -1 O GLN B 107 N HIS B 94
SHEET 4 AB4 4 GLU B 117 TYR B 120 -1 O GLU B 117 N MET B 108
SHEET 1 AB5 4 TYR B 135 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 LEU B 169 N ILE B 160
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 TYR B 254 N LYS B 241
SHEET 3 AB7 4 LYS B 264 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 326 N PHE B 310
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 SER B 363 -1 O ILE B 358 N HIS B 350
SHEET 3 AB9 4 LYS B 366 ASP B 373 -1 O VAL B 368 N TYR B 361
SHEET 4 AB9 4 LEU B 379 PRO B 384 -1 O LEU B 383 N LEU B 369
SHEET 1 AC1 4 SER B 389 ASP B 391 0
SHEET 2 AC1 4 VAL B 401 SER B 408 -1 O THR B 407 N SER B 389
SHEET 3 AC1 4 THR B 411 ASP B 419 -1 O TYR B 416 N PHE B 404
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 462 N LYS B 446
SHEET 3 AC2 8 VAL B 506 ALA B 510 -1 O LEU B 509 N PHE B 461
SHEET 4 AC2 8 CYS B 476 HIS B 479 1 N GLU B 477 O VAL B 506
SHEET 5 AC2 8 VAL B 556 GLY B 561 1 O ALA B 557 N MET B 478
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 ILE B 686 N THR B 645
SITE 1 AC1 5 TYR A 481 SER A 562 ASN A 563 VAL A 588
SITE 2 AC1 5 TRP A 603
SITE 1 AC2 7 TYR B 481 PHE B 484 SER B 562 ASN B 563
SITE 2 AC2 7 TRP B 603 TYR B 607 ARG B 655
CRYST1 275.580 60.850 88.040 90.00 92.65 90.00 C 1 2 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 0.003629 0.000000 0.000168 0.00000
SCALE2 0.000000 0.016434 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011371 0.00000
TER 5748 ASP A 724
TER 11421 ASP B 724
MASTER 581 0 2 44 82 0 4 611563 2 10 112
END |