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HEADER HYDROLASE 25-MAY-17 5O3W
TITLE STRUCTURAL CHARACTERIZATION OF THE FAST AND PROMISCUOUS MACROCYCLASE
TITLE 2 FROM PLANT - PCY1-S562A BOUND TO PRESEGETALIN A1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEPTIDE CYCLASE 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PRESEGETALIN A1;
COMPND 8 CHAIN: W, X, Y, Z;
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 4 27-NOV-19 5O3W 1 REMARK
REVDAT 3 16-OCT-19 5O3W 1 REMARK
REVDAT 2 28-MAR-18 5O3W 1 JRNL
REVDAT 1 07-FEB-18 5O3W 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. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 77.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 183511
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) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 9515
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 13441
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.3310
REMARK 3 BIN FREE R VALUE SET COUNT : 689
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 23045
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 844
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.50000
REMARK 3 B22 (A**2) : -0.96000
REMARK 3 B33 (A**2) : -0.38000
REMARK 3 B12 (A**2) : -0.22000
REMARK 3 B13 (A**2) : -0.38000
REMARK 3 B23 (A**2) : -0.01000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.237
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.190
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.193
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.120
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 23675 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 21482 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 32074 ; 1.640 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 49925 ; 2.073 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2867 ; 6.883 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1180 ;34.387 ;24.017
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3976 ;13.936 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 149 ;17.007 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3404 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 26464 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 5033 ; 0.006 ; 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): 11480 ; 1.835 ; 1.304
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 11479 ; 1.835 ; 1.304
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14325 ; 2.871 ; 1.943
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 14326 ; 2.871 ; 1.943
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 12195 ; 1.920 ; 1.478
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 12187 ; 1.920 ; 1.476
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 17731 ; 2.985 ; 2.142
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 24679 ; 5.910 ;15.040
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 24653 ; 5.911 ;14.992
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 : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 6 724 B 6 724 44302 0.07 0.05
REMARK 3 2 A 6 724 C 6 724 44206 0.08 0.05
REMARK 3 3 A 6 724 D 6 724 44802 0.06 0.05
REMARK 3 4 B 6 724 C 6 724 46394 0.06 0.05
REMARK 3 5 B 6 724 D 6 724 43940 0.08 0.05
REMARK 3 6 C 6 724 D 6 724 43836 0.08 0.05
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
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 107
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0130 -55.9210-294.9430
REMARK 3 T TENSOR
REMARK 3 T11: 0.2359 T22: 0.0278
REMARK 3 T33: 0.3649 T12: 0.0327
REMARK 3 T13: 0.0747 T23: 0.0425
REMARK 3 L TENSOR
REMARK 3 L11: 0.4845 L22: 1.0449
REMARK 3 L33: 2.4993 L12: 0.0569
REMARK 3 L13: -0.0161 L23: -0.1854
REMARK 3 S TENSOR
REMARK 3 S11: 0.0052 S12: -0.0376 S13: 0.0769
REMARK 3 S21: 0.3027 S22: -0.0071 S23: 0.0852
REMARK 3 S31: -0.0514 S32: -0.1747 S33: 0.0019
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 108 A 134
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3390 -52.1930-325.9120
REMARK 3 T TENSOR
REMARK 3 T11: 0.3460 T22: 0.1936
REMARK 3 T33: 0.4878 T12: 0.0865
REMARK 3 T13: 0.0516 T23: 0.1446
REMARK 3 L TENSOR
REMARK 3 L11: 3.7528 L22: 3.2162
REMARK 3 L33: 4.1517 L12: 1.8930
REMARK 3 L13: 2.3727 L23: 0.4332
REMARK 3 S TENSOR
REMARK 3 S11: -0.0789 S12: 0.2458 S13: 0.3286
REMARK 3 S21: -0.4720 S22: 0.0614 S23: -0.1546
REMARK 3 S31: -0.2344 S32: -0.0113 S33: 0.0175
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 290
REMARK 3 ORIGIN FOR THE GROUP (A): -12.5330 -64.0330-323.2700
REMARK 3 T TENSOR
REMARK 3 T11: 0.2064 T22: 0.0919
REMARK 3 T33: 0.3205 T12: -0.0187
REMARK 3 T13: 0.0072 T23: 0.0374
REMARK 3 L TENSOR
REMARK 3 L11: 1.8835 L22: 1.9770
REMARK 3 L33: 2.2144 L12: -0.3850
REMARK 3 L13: -0.3259 L23: -0.3623
REMARK 3 S TENSOR
REMARK 3 S11: 0.1246 S12: -0.1895 S13: 0.0062
REMARK 3 S21: -0.1485 S22: -0.0852 S23: 0.3037
REMARK 3 S31: 0.1647 S32: -0.2224 S33: -0.0394
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 291 A 420
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5650 -80.5710-321.2630
REMARK 3 T TENSOR
REMARK 3 T11: 0.3959 T22: 0.0352
REMARK 3 T33: 0.2570 T12: 0.0991
REMARK 3 T13: 0.0389 T23: 0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 1.0545 L22: 1.0654
REMARK 3 L33: 2.1906 L12: 0.0549
REMARK 3 L13: 0.9323 L23: 0.1106
REMARK 3 S TENSOR
REMARK 3 S11: 0.1299 S12: 0.1077 S13: -0.0467
REMARK 3 S21: -0.1547 S22: -0.0315 S23: -0.0283
REMARK 3 S31: 0.5346 S32: 0.2182 S33: -0.0984
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 421 A 724
REMARK 3 ORIGIN FOR THE GROUP (A): 7.9260 -68.7860-292.2780
REMARK 3 T TENSOR
REMARK 3 T11: 0.3381 T22: 0.0242
REMARK 3 T33: 0.2420 T12: 0.0132
REMARK 3 T13: 0.0365 T23: 0.0713
REMARK 3 L TENSOR
REMARK 3 L11: 1.0247 L22: 1.4066
REMARK 3 L33: 1.7943 L12: 0.0546
REMARK 3 L13: -0.0915 L23: 0.1736
REMARK 3 S TENSOR
REMARK 3 S11: -0.0060 S12: 0.0459 S13: 0.0980
REMARK 3 S21: 0.2907 S22: 0.0480 S23: 0.0141
REMARK 3 S31: 0.3306 S32: -0.0610 S33: -0.0420
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 : B 6 B 110
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9640 -33.8320-299.3240
REMARK 3 T TENSOR
REMARK 3 T11: 0.0928 T22: 0.0888
REMARK 3 T33: 0.3262 T12: 0.0235
REMARK 3 T13: 0.0462 T23: 0.1315
REMARK 3 L TENSOR
REMARK 3 L11: 1.6231 L22: 1.6319
REMARK 3 L33: 1.5440 L12: 0.0275
REMARK 3 L13: 0.2485 L23: 0.5816
REMARK 3 S TENSOR
REMARK 3 S11: 0.0573 S12: -0.2323 S13: -0.1377
REMARK 3 S21: 0.1614 S22: -0.0379 S23: 0.0513
REMARK 3 S31: 0.2596 S32: 0.0816 S33: -0.0194
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 111 B 266
REMARK 3 ORIGIN FOR THE GROUP (A): 39.9450 -34.2780-323.9750
REMARK 3 T TENSOR
REMARK 3 T11: 0.2005 T22: 0.0265
REMARK 3 T33: 0.3019 T12: 0.0515
REMARK 3 T13: 0.0568 T23: 0.0376
REMARK 3 L TENSOR
REMARK 3 L11: 1.2320 L22: 1.9070
REMARK 3 L33: 1.5320 L12: -0.0409
REMARK 3 L13: -0.4601 L23: 0.1681
REMARK 3 S TENSOR
REMARK 3 S11: 0.0696 S12: 0.0232 S13: -0.0888
REMARK 3 S21: -0.3203 S22: 0.0096 S23: -0.0817
REMARK 3 S31: -0.0863 S32: 0.0434 S33: -0.0792
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 267 B 416
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9520 -15.4700-329.5400
REMARK 3 T TENSOR
REMARK 3 T11: 0.4306 T22: 0.0741
REMARK 3 T33: 0.2858 T12: 0.0943
REMARK 3 T13: 0.0129 T23: 0.0959
REMARK 3 L TENSOR
REMARK 3 L11: 1.8104 L22: 1.1191
REMARK 3 L33: 1.6842 L12: 0.1539
REMARK 3 L13: -0.6829 L23: 0.4593
REMARK 3 S TENSOR
REMARK 3 S11: 0.0734 S12: 0.2226 S13: 0.0154
REMARK 3 S21: -0.5375 S22: -0.0662 S23: 0.0858
REMARK 3 S31: -0.3075 S32: -0.1271 S33: -0.0072
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 417 B 679
REMARK 3 ORIGIN FOR THE GROUP (A): 25.7230 -17.7440-299.4250
REMARK 3 T TENSOR
REMARK 3 T11: 0.0572 T22: 0.0281
REMARK 3 T33: 0.2580 T12: 0.0198
REMARK 3 T13: 0.0514 T23: 0.0588
REMARK 3 L TENSOR
REMARK 3 L11: 1.6457 L22: 1.6521
REMARK 3 L33: 1.3044 L12: -0.1334
REMARK 3 L13: -0.1109 L23: 0.1766
REMARK 3 S TENSOR
REMARK 3 S11: 0.0160 S12: -0.1262 S13: 0.0269
REMARK 3 S21: 0.0600 S22: -0.0034 S23: 0.1256
REMARK 3 S31: -0.0927 S32: -0.0465 S33: -0.0125
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 680 B 724
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8340 -32.3800-293.7450
REMARK 3 T TENSOR
REMARK 3 T11: 0.1301 T22: 0.0749
REMARK 3 T33: 0.3157 T12: 0.0076
REMARK 3 T13: 0.0680 T23: 0.1144
REMARK 3 L TENSOR
REMARK 3 L11: 0.9827 L22: 1.9520
REMARK 3 L33: 2.3394 L12: -0.0524
REMARK 3 L13: -0.2498 L23: 1.2257
REMARK 3 S TENSOR
REMARK 3 S11: -0.0182 S12: -0.2242 S13: -0.1932
REMARK 3 S21: 0.2254 S22: 0.0318 S23: 0.1162
REMARK 3 S31: 0.0826 S32: -0.0383 S33: -0.0136
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 : C 6 C 110
REMARK 3 ORIGIN FOR THE GROUP (A): -6.6700 -28.8380-388.3530
REMARK 3 T TENSOR
REMARK 3 T11: 0.1130 T22: 0.0855
REMARK 3 T33: 0.3182 T12: -0.0365
REMARK 3 T13: 0.0258 T23: 0.1136
REMARK 3 L TENSOR
REMARK 3 L11: 2.0391 L22: 1.9005
REMARK 3 L33: 2.0161 L12: -0.3166
REMARK 3 L13: -0.2900 L23: 0.8768
REMARK 3 S TENSOR
REMARK 3 S11: 0.0088 S12: 0.2558 S13: 0.1162
REMARK 3 S21: -0.1750 S22: -0.0162 S23: 0.0064
REMARK 3 S31: -0.2291 S32: 0.0884 S33: 0.0074
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 : C 111 C 262
REMARK 3 ORIGIN FOR THE GROUP (A): 3.0050 -27.8410-363.6840
REMARK 3 T TENSOR
REMARK 3 T11: 0.2220 T22: 0.0333
REMARK 3 T33: 0.3464 T12: -0.0390
REMARK 3 T13: -0.0208 T23: 0.0485
REMARK 3 L TENSOR
REMARK 3 L11: 1.1648 L22: 2.1037
REMARK 3 L33: 1.5783 L12: 0.3244
REMARK 3 L13: 0.4194 L23: 0.3398
REMARK 3 S TENSOR
REMARK 3 S11: 0.0318 S12: 0.0276 S13: 0.0366
REMARK 3 S21: 0.4683 S22: 0.0300 S23: -0.2041
REMARK 3 S31: 0.1420 S32: 0.0374 S33: -0.0618
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 : C 263 C 416
REMARK 3 ORIGIN FOR THE GROUP (A): -7.6370 -47.2770-358.2010
REMARK 3 T TENSOR
REMARK 3 T11: 0.5277 T22: 0.0697
REMARK 3 T33: 0.2963 T12: -0.0785
REMARK 3 T13: -0.0117 T23: 0.1062
REMARK 3 L TENSOR
REMARK 3 L11: 2.0227 L22: 1.4287
REMARK 3 L33: 1.7382 L12: -0.2624
REMARK 3 L13: 0.8101 L23: 0.3635
REMARK 3 S TENSOR
REMARK 3 S11: 0.0832 S12: -0.2097 S13: -0.0094
REMARK 3 S21: 0.7405 S22: -0.0669 S23: -0.0656
REMARK 3 S31: 0.4105 S32: -0.1657 S33: -0.0163
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 : C 417 C 678
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9030 -44.9850-388.2370
REMARK 3 T TENSOR
REMARK 3 T11: 0.0802 T22: 0.0389
REMARK 3 T33: 0.2793 T12: -0.0306
REMARK 3 T13: 0.0214 T23: 0.0518
REMARK 3 L TENSOR
REMARK 3 L11: 1.7068 L22: 1.7429
REMARK 3 L33: 1.3371 L12: -0.0201
REMARK 3 L13: 0.2213 L23: 0.2657
REMARK 3 S TENSOR
REMARK 3 S11: 0.0317 S12: 0.1148 S13: -0.0272
REMARK 3 S21: -0.0475 S22: 0.0108 S23: 0.0721
REMARK 3 S31: 0.1408 S32: -0.0116 S33: -0.0425
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 679 C 724
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6310 -30.5020-394.3020
REMARK 3 T TENSOR
REMARK 3 T11: 0.1121 T22: 0.0683
REMARK 3 T33: 0.3231 T12: -0.0378
REMARK 3 T13: 0.0171 T23: 0.0972
REMARK 3 L TENSOR
REMARK 3 L11: 0.7959 L22: 2.2752
REMARK 3 L33: 2.6314 L12: -0.0555
REMARK 3 L13: 0.1986 L23: 1.1344
REMARK 3 S TENSOR
REMARK 3 S11: -0.0608 S12: 0.1985 S13: 0.1689
REMARK 3 S21: -0.2150 S22: 0.0439 S23: 0.1097
REMARK 3 S31: 0.0042 S32: 0.0167 S33: 0.0169
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 6 D 107
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4080 -95.4420-392.8020
REMARK 3 T TENSOR
REMARK 3 T11: 0.2328 T22: 0.0391
REMARK 3 T33: 0.3880 T12: -0.0430
REMARK 3 T13: -0.0144 T23: 0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 0.5523 L22: 1.0060
REMARK 3 L33: 3.0213 L12: -0.0979
REMARK 3 L13: 0.2361 L23: -0.4899
REMARK 3 S TENSOR
REMARK 3 S11: -0.0340 S12: 0.0394 S13: -0.0516
REMARK 3 S21: -0.2424 S22: 0.0048 S23: 0.0850
REMARK 3 S31: -0.0462 S32: -0.1996 S33: 0.0292
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 : D 108 D 300
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8850 -87.3200-364.5840
REMARK 3 T TENSOR
REMARK 3 T11: 0.2351 T22: 0.0969
REMARK 3 T33: 0.2968 T12: 0.0177
REMARK 3 T13: 0.0357 T23: 0.0387
REMARK 3 L TENSOR
REMARK 3 L11: 1.4701 L22: 1.8981
REMARK 3 L33: 1.9372 L12: 0.4093
REMARK 3 L13: -0.0289 L23: -0.2970
REMARK 3 S TENSOR
REMARK 3 S11: 0.0910 S12: 0.1613 S13: -0.0518
REMARK 3 S21: 0.1674 S22: -0.0615 S23: 0.1856
REMARK 3 S31: -0.1956 S32: -0.1790 S33: -0.0295
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 : D 301 D 422
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6560 -71.1960-365.9850
REMARK 3 T TENSOR
REMARK 3 T11: 0.4558 T22: 0.0476
REMARK 3 T33: 0.2616 T12: -0.1212
REMARK 3 T13: -0.0091 T23: 0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 1.1907 L22: 1.2042
REMARK 3 L33: 2.2973 L12: -0.0268
REMARK 3 L13: -0.9393 L23: 0.1984
REMARK 3 S TENSOR
REMARK 3 S11: 0.0919 S12: -0.1138 S13: -0.0013
REMARK 3 S21: 0.2482 S22: -0.0249 S23: -0.0751
REMARK 3 S31: -0.5780 S32: 0.2294 S33: -0.0670
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 : D 423 D 691
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6090 -81.1880-395.8930
REMARK 3 T TENSOR
REMARK 3 T11: 0.3661 T22: 0.0360
REMARK 3 T33: 0.2598 T12: -0.0277
REMARK 3 T13: -0.0005 T23: 0.0691
REMARK 3 L TENSOR
REMARK 3 L11: 1.0079 L22: 1.3562
REMARK 3 L33: 2.0286 L12: -0.1257
REMARK 3 L13: 0.1471 L23: 0.0789
REMARK 3 S TENSOR
REMARK 3 S11: 0.0333 S12: -0.0402 S13: -0.0871
REMARK 3 S21: -0.2607 S22: 0.0080 S23: 0.0154
REMARK 3 S31: -0.4326 S32: -0.1252 S33: -0.0412
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 : D 692 D 724
REMARK 3 ORIGIN FOR THE GROUP (A): 37.4280 -96.8470-395.4910
REMARK 3 T TENSOR
REMARK 3 T11: 0.2073 T22: 0.0229
REMARK 3 T33: 0.3154 T12: -0.0391
REMARK 3 T13: 0.0284 T23: 0.0428
REMARK 3 L TENSOR
REMARK 3 L11: 4.7323 L22: 2.9617
REMARK 3 L33: 4.6436 L12: -0.2696
REMARK 3 L13: 0.7882 L23: -0.3124
REMARK 3 S TENSOR
REMARK 3 S11: 0.0081 S12: -0.2108 S13: -0.1451
REMARK 3 S21: -0.1528 S22: 0.0813 S23: 0.0170
REMARK 3 S31: -0.1139 S32: -0.0041 S33: -0.0894
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 : 0.70
REMARK 3 SHRINKAGE RADIUS : 0.70
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5O3W 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_1200005110.
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 : 183511
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 77.070
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.8000
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: APO PCY1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PCY1-S562A COMPLEX WITH PRESEGA1 WAS
REMARK 280 CRYSTALLIZED AT 13.3 MG/ML WITH 0.163 MM PRESEGA1 IN 28% (W/V)
REMARK 280 PEG 5000 MME, 140 MM MG ACETATE TETRAHYDRATE AND 0.1 M TRIS PH
REMARK 280 7.5. FOR CRYO PROTECTION 7% (V/V) GLYCEROL WERE ADDED TO
REMARK 280 RESERVOIR SOLUTION., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, W
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, X
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, Y
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, Z
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 125
REMARK 465 GLU A 126
REMARK 465 GLY A 127
REMARK 465 GLY A 128
REMARK 465 ARG A 129
REMARK 465 SER A 130
REMARK 465 ALA A 693
REMARK 465 ALA A 694
REMARK 465 HIS A 695
REMARK 465 TYR A 696
REMARK 465 GLY A 697
REMARK 465 ARG A 698
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 SER B 4
REMARK 465 GLY B 5
REMARK 465 ARG B 283
REMARK 465 GLU B 284
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 THR C 3
REMARK 465 SER C 4
REMARK 465 GLY C 5
REMARK 465 ARG C 283
REMARK 465 GLU C 284
REMARK 465 ASP C 285
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 THR D 3
REMARK 465 SER D 4
REMARK 465 GLY D 5
REMARK 465 LEU D 112
REMARK 465 ASP D 113
REMARK 465 GLY D 114
REMARK 465 LEU D 124
REMARK 465 ARG D 125
REMARK 465 GLU D 126
REMARK 465 GLY D 127
REMARK 465 GLY D 128
REMARK 465 ARG D 129
REMARK 465 ARG D 283
REMARK 465 GLU D 284
REMARK 465 ALA D 693
REMARK 465 ALA D 694
REMARK 465 HIS D 695
REMARK 465 TYR D 696
REMARK 465 GLY D 697
REMARK 465 ARG D 698
REMARK 465 MET W -29
REMARK 465 SER W -28
REMARK 465 PRO W -27
REMARK 465 ILE W -26
REMARK 465 LEU W -25
REMARK 465 ALA W -24
REMARK 465 HIS W -23
REMARK 465 ASP W -22
REMARK 465 VAL W -21
REMARK 465 VAL W -20
REMARK 465 LYS W -19
REMARK 465 PRO W -18
REMARK 465 GLN W -17
REMARK 465 GLY W -16
REMARK 465 VAL W -15
REMARK 465 PRO W -14
REMARK 465 VAL W -13
REMARK 465 TRP W -12
REMARK 465 ALA W -11
REMARK 465 PHE W -10
REMARK 465 GLN W -9
REMARK 465 ALA W -8
REMARK 465 LYS W -7
REMARK 465 ASP W -6
REMARK 465 VAL W -5
REMARK 465 MET X -29
REMARK 465 SER X -28
REMARK 465 PRO X -27
REMARK 465 ILE X -26
REMARK 465 LEU X -25
REMARK 465 ALA X -24
REMARK 465 HIS X -23
REMARK 465 ASP X -22
REMARK 465 VAL X -21
REMARK 465 VAL X -20
REMARK 465 LYS X -19
REMARK 465 PRO X -18
REMARK 465 GLN X -17
REMARK 465 GLY X -16
REMARK 465 VAL X -15
REMARK 465 PRO X -14
REMARK 465 VAL X -13
REMARK 465 TRP X -12
REMARK 465 ALA X -11
REMARK 465 PHE X -10
REMARK 465 GLN X -9
REMARK 465 ALA X -8
REMARK 465 LYS X -7
REMARK 465 ASP X -6
REMARK 465 VAL X -5
REMARK 465 GLU X -4
REMARK 465 MET Y -29
REMARK 465 SER Y -28
REMARK 465 PRO Y -27
REMARK 465 ILE Y -26
REMARK 465 LEU Y -25
REMARK 465 ALA Y -24
REMARK 465 HIS Y -23
REMARK 465 ASP Y -22
REMARK 465 VAL Y -21
REMARK 465 VAL Y -20
REMARK 465 LYS Y -19
REMARK 465 PRO Y -18
REMARK 465 GLN Y -17
REMARK 465 GLY Y -16
REMARK 465 VAL Y -15
REMARK 465 PRO Y -14
REMARK 465 VAL Y -13
REMARK 465 TRP Y -12
REMARK 465 ALA Y -11
REMARK 465 PHE Y -10
REMARK 465 GLN Y -9
REMARK 465 ALA Y -8
REMARK 465 LYS Y -7
REMARK 465 ASP Y -6
REMARK 465 VAL Y -5
REMARK 465 GLU Y -4
REMARK 465 MET Z -29
REMARK 465 SER Z -28
REMARK 465 PRO Z -27
REMARK 465 ILE Z -26
REMARK 465 LEU Z -25
REMARK 465 ALA Z -24
REMARK 465 HIS Z -23
REMARK 465 ASP Z -22
REMARK 465 VAL Z -21
REMARK 465 VAL Z -20
REMARK 465 LYS Z -19
REMARK 465 PRO Z -18
REMARK 465 GLN Z -17
REMARK 465 GLY Z -16
REMARK 465 VAL Z -15
REMARK 465 PRO Z -14
REMARK 465 VAL Z -13
REMARK 465 TRP Z -12
REMARK 465 ALA Z -11
REMARK 465 PHE Z -10
REMARK 465 GLN Z -9
REMARK 465 ALA Z -8
REMARK 465 LYS Z -7
REMARK 465 ASP Z -6
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH C 954 O HOH C 1032 1.62
REMARK 500 NZ LYS B 446 OH TYR B 550 1.95
REMARK 500 O HOH D 869 O HOH D 974 2.10
REMARK 500 O HOH C 1094 O HOH C 1134 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 166 CG - CD - NE ANGL. DEV. = -15.4 DEGREES
REMARK 500 ARG D 166 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG D 166 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP D 203 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 CYS D 259 CA - CB - SG ANGL. DEV. = 7.7 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 -119.86 44.34
REMARK 500 ASN A 123 66.27 -66.83
REMARK 500 LYS A 177 -83.02 -114.44
REMARK 500 ARG A 283 -100.19 85.63
REMARK 500 GLU A 284 72.49 56.95
REMARK 500 PHE A 296 40.77 -94.78
REMARK 500 ALA A 318 83.09 -155.05
REMARK 500 LYS A 321 163.27 64.20
REMARK 500 GLU A 354 -45.76 71.22
REMARK 500 THR A 425 -18.01 84.74
REMARK 500 TYR A 481 -81.47 -133.87
REMARK 500 ARG A 528 -116.81 48.46
REMARK 500 ALA A 562 -116.52 59.53
REMARK 500 THR A 598 -114.53 42.67
REMARK 500 ASP A 653 104.72 -165.36
REMARK 500 CYS A 673 -53.23 -126.69
REMARK 500 ASP A 678 58.71 -148.57
REMARK 500 ALA B 89 -118.90 42.67
REMARK 500 LYS B 177 -83.49 -113.99
REMARK 500 GLU B 200 -122.05 39.32
REMARK 500 ARG B 281 -38.13 -38.81
REMARK 500 SER B 286 137.55 91.66
REMARK 500 PHE B 296 42.67 -95.36
REMARK 500 ALA B 318 81.40 -156.41
REMARK 500 LYS B 321 163.06 66.56
REMARK 500 GLU B 354 -46.78 71.50
REMARK 500 TYR B 481 -80.77 -134.57
REMARK 500 ARG B 528 -117.13 50.14
REMARK 500 ALA B 562 -116.46 59.16
REMARK 500 THR B 598 -117.24 42.23
REMARK 500 CYS B 673 -53.65 -127.13
REMARK 500 ASP B 678 53.18 -144.39
REMARK 500 ALA B 694 -168.76 -104.95
REMARK 500 ALA C 89 -120.09 43.10
REMARK 500 LYS C 177 -84.45 -114.16
REMARK 500 GLU C 200 -121.58 38.75
REMARK 500 GLU C 278 -13.71 -49.06
REMARK 500 PHE C 296 43.90 -95.86
REMARK 500 ALA C 318 80.84 -156.14
REMARK 500 LYS C 321 163.53 64.87
REMARK 500 GLU C 354 -46.89 70.61
REMARK 500 TYR C 481 -80.76 -134.75
REMARK 500 ARG C 528 -116.99 49.81
REMARK 500 ALA C 562 -116.55 58.06
REMARK 500 THR C 598 -118.12 43.72
REMARK 500 CYS C 673 -55.12 -126.39
REMARK 500 ALA C 694 -168.97 -105.60
REMARK 500 ALA D 89 -119.44 42.47
REMARK 500 LYS D 177 -83.68 -115.76
REMARK 500 ARG D 281 -39.38 -39.61
REMARK 500
REMARK 500 THIS ENTRY HAS 61 RAMACHANDRAN OUTLIERS.
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 GLU A 284 ASP A 285 -118.29
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 B 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 912 O
REMARK 620 2 HOH B1074 O 91.0
REMARK 620 3 HOH B1065 O 171.4 94.3
REMARK 620 4 HOH B 952 O 81.3 96.1 91.4
REMARK 620 5 HOH B1003 O 90.3 172.8 83.6 77.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 913 O
REMARK 620 2 HOH C 914 O 96.9
REMARK 620 3 HOH C 905 O 97.2 79.2
REMARK 620 4 HOH C1024 O 171.2 81.0 90.8
REMARK 620 5 HOH C1119 O 93.9 168.4 95.1 88.9
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 B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 802
DBREF 5O3W A 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5O3W B 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5O3W C 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5O3W D 1 724 UNP R4P353 R4P353_9CARY 1 724
DBREF 5O3W W -29 2 UNP F6LNL5 F6LNL5_9CARY 1 32
DBREF 5O3W X -29 2 UNP F6LNL5 F6LNL5_9CARY 1 32
DBREF 5O3W Y -29 2 UNP F6LNL5 F6LNL5_9CARY 1 32
DBREF 5O3W Z -29 2 UNP F6LNL5 F6LNL5_9CARY 1 32
SEQADV 5O3W ALA A 562 UNP R4P353 SER 562 ENGINEERED MUTATION
SEQADV 5O3W ALA B 562 UNP R4P353 SER 562 ENGINEERED MUTATION
SEQADV 5O3W ALA C 562 UNP R4P353 SER 562 ENGINEERED MUTATION
SEQADV 5O3W ALA D 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 C 724 MET ALA THR SER GLY PHE SER LYS PRO LEU HIS TYR PRO
SEQRES 2 C 724 PRO VAL ARG ARG ASP GLU THR VAL VAL ASP ASP TYR PHE
SEQRES 3 C 724 GLY VAL LYS VAL ALA ASP PRO TYR ARG TRP LEU GLU ASP
SEQRES 4 C 724 PRO ASN SER GLU GLU THR LYS GLU PHE VAL ASP ASN GLN
SEQRES 5 C 724 GLU LYS LEU ALA ASN SER VAL LEU GLU GLU CYS GLU LEU
SEQRES 6 C 724 ILE ASP LYS PHE LYS GLN LYS ILE ILE ASP PHE VAL ASN
SEQRES 7 C 724 PHE PRO ARG CYS GLY VAL PRO PHE ARG ARG ALA ASN LYS
SEQRES 8 C 724 TYR PHE HIS PHE TYR ASN SER GLY LEU GLN ALA GLN ASN
SEQRES 9 C 724 VAL PHE GLN MET GLN ASP ASP LEU ASP GLY LYS PRO GLU
SEQRES 10 C 724 VAL LEU TYR ASP PRO ASN LEU ARG GLU GLY GLY ARG SER
SEQRES 11 C 724 GLY LEU SER LEU TYR SER VAL SER GLU ASP ALA LYS TYR
SEQRES 12 C 724 PHE ALA PHE GLY ILE HIS SER GLY LEU THR GLU TRP VAL
SEQRES 13 C 724 THR ILE LYS ILE LEU LYS THR GLU ASP ARG SER TYR LEU
SEQRES 14 C 724 PRO ASP THR LEU GLU TRP VAL LYS PHE SER PRO ALA ILE
SEQRES 15 C 724 TRP THR HIS ASP ASN LYS GLY PHE PHE TYR CYS PRO TYR
SEQRES 16 C 724 PRO PRO LEU LYS GLU GLY GLU ASP HIS MET THR ARG SER
SEQRES 17 C 724 ALA VAL ASN GLN GLU ALA ARG TYR HIS PHE LEU GLY THR
SEQRES 18 C 724 ASP GLN SER GLU ASP ILE LEU LEU TRP ARG ASP LEU GLU
SEQRES 19 C 724 ASN PRO ALA HIS HIS LEU LYS CYS GLN ILE THR ASP ASP
SEQRES 20 C 724 GLY LYS TYR PHE LEU LEU TYR ILE LEU ASP GLY CYS ASP
SEQRES 21 C 724 ASP ALA ASN LYS VAL TYR CYS LEU ASP LEU THR LYS LEU
SEQRES 22 C 724 PRO ASN GLY LEU GLU SER PHE ARG GLY ARG GLU ASP SER
SEQRES 23 C 724 ALA PRO PHE MET LYS LEU ILE ASP SER PHE ASP ALA SER
SEQRES 24 C 724 TYR THR ALA ILE ALA ASN ASP GLY SER VAL PHE THR PHE
SEQRES 25 C 724 GLN THR ASN LYS ASP ALA PRO ARG LYS LYS LEU VAL ARG
SEQRES 26 C 724 VAL ASP LEU ASN ASN PRO SER VAL TRP THR ASP LEU VAL
SEQRES 27 C 724 PRO GLU SER LYS LYS ASP LEU LEU GLU SER ALA HIS ALA
SEQRES 28 C 724 VAL ASN GLU ASN GLN LEU ILE LEU ARG TYR LEU SER ASP
SEQRES 29 C 724 VAL LYS HIS VAL LEU GLU ILE ARG ASP LEU GLU SER GLY
SEQRES 30 C 724 ALA LEU GLN HIS ARG LEU PRO ILE ASP ILE GLY SER VAL
SEQRES 31 C 724 ASP GLY ILE THR ALA ARG ARG ARG ASP SER VAL VAL PHE
SEQRES 32 C 724 PHE LYS PHE THR SER ILE LEU THR PRO GLY ILE VAL TYR
SEQRES 33 C 724 GLN CYS ASP LEU LYS ASN ASP PRO THR GLN LEU LYS ILE
SEQRES 34 C 724 PHE ARG GLU SER VAL VAL PRO ASP PHE ASP ARG SER GLU
SEQRES 35 C 724 PHE GLU VAL LYS GLN VAL PHE VAL PRO SER LYS ASP GLY
SEQRES 36 C 724 THR LYS ILE PRO ILE PHE ILE ALA ALA ARG LYS GLY ILE
SEQRES 37 C 724 SER LEU ASP GLY SER HIS PRO CYS GLU MET HIS GLY TYR
SEQRES 38 C 724 GLY GLY PHE GLY ILE ASN MET MET PRO THR PHE SER ALA
SEQRES 39 C 724 SER ARG ILE VAL PHE LEU LYS HIS LEU GLY GLY VAL PHE
SEQRES 40 C 724 CYS LEU ALA ASN ILE ARG GLY GLY GLY GLU TYR GLY GLU
SEQRES 41 C 724 GLU TRP HIS LYS ALA GLY PHE ARG ASP LYS LYS GLN ASN
SEQRES 42 C 724 VAL PHE ASP ASP PHE ILE SER ALA ALA GLU TYR LEU ILE
SEQRES 43 C 724 SER SER GLY TYR THR LYS ALA ARG ARG VAL ALA ILE GLU
SEQRES 44 C 724 GLY GLY ALA ASN GLY GLY LEU LEU VAL ALA ALA CYS ILE
SEQRES 45 C 724 ASN GLN ARG PRO ASP LEU PHE GLY CYS ALA GLU ALA ASN
SEQRES 46 C 724 CYS GLY VAL MET ASP MET LEU ARG PHE HIS LYS PHE THR
SEQRES 47 C 724 LEU GLY TYR LEU TRP THR GLY ASP TYR GLY CYS SER ASP
SEQRES 48 C 724 LYS GLU GLU GLU PHE LYS TRP LEU ILE LYS TYR SER PRO
SEQRES 49 C 724 ILE HIS ASN VAL ARG ARG PRO TRP GLU GLN PRO GLY ASN
SEQRES 50 C 724 GLU GLU THR GLN TYR PRO ALA THR MET ILE LEU THR ALA
SEQRES 51 C 724 ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER PHE LYS
SEQRES 52 C 724 LEU LEU ALA THR MET GLN HIS VAL LEU CYS THR SER LEU
SEQRES 53 C 724 GLU ASP SER PRO GLN LYS ASN PRO ILE ILE ALA ARG ILE
SEQRES 54 C 724 GLN ARG LYS ALA ALA HIS TYR GLY ARG ALA THR MET THR
SEQRES 55 C 724 GLN ILE ALA GLU VAL ALA ASP ARG TYR GLY PHE MET ALA
SEQRES 56 C 724 LYS ALA LEU GLU ALA PRO TRP ILE ASP
SEQRES 1 D 724 MET ALA THR SER GLY PHE SER LYS PRO LEU HIS TYR PRO
SEQRES 2 D 724 PRO VAL ARG ARG ASP GLU THR VAL VAL ASP ASP TYR PHE
SEQRES 3 D 724 GLY VAL LYS VAL ALA ASP PRO TYR ARG TRP LEU GLU ASP
SEQRES 4 D 724 PRO ASN SER GLU GLU THR LYS GLU PHE VAL ASP ASN GLN
SEQRES 5 D 724 GLU LYS LEU ALA ASN SER VAL LEU GLU GLU CYS GLU LEU
SEQRES 6 D 724 ILE ASP LYS PHE LYS GLN LYS ILE ILE ASP PHE VAL ASN
SEQRES 7 D 724 PHE PRO ARG CYS GLY VAL PRO PHE ARG ARG ALA ASN LYS
SEQRES 8 D 724 TYR PHE HIS PHE TYR ASN SER GLY LEU GLN ALA GLN ASN
SEQRES 9 D 724 VAL PHE GLN MET GLN ASP ASP LEU ASP GLY LYS PRO GLU
SEQRES 10 D 724 VAL LEU TYR ASP PRO ASN LEU ARG GLU GLY GLY ARG SER
SEQRES 11 D 724 GLY LEU SER LEU TYR SER VAL SER GLU ASP ALA LYS TYR
SEQRES 12 D 724 PHE ALA PHE GLY ILE HIS SER GLY LEU THR GLU TRP VAL
SEQRES 13 D 724 THR ILE LYS ILE LEU LYS THR GLU ASP ARG SER TYR LEU
SEQRES 14 D 724 PRO ASP THR LEU GLU TRP VAL LYS PHE SER PRO ALA ILE
SEQRES 15 D 724 TRP THR HIS ASP ASN LYS GLY PHE PHE TYR CYS PRO TYR
SEQRES 16 D 724 PRO PRO LEU LYS GLU GLY GLU ASP HIS MET THR ARG SER
SEQRES 17 D 724 ALA VAL ASN GLN GLU ALA ARG TYR HIS PHE LEU GLY THR
SEQRES 18 D 724 ASP GLN SER GLU ASP ILE LEU LEU TRP ARG ASP LEU GLU
SEQRES 19 D 724 ASN PRO ALA HIS HIS LEU LYS CYS GLN ILE THR ASP ASP
SEQRES 20 D 724 GLY LYS TYR PHE LEU LEU TYR ILE LEU ASP GLY CYS ASP
SEQRES 21 D 724 ASP ALA ASN LYS VAL TYR CYS LEU ASP LEU THR LYS LEU
SEQRES 22 D 724 PRO ASN GLY LEU GLU SER PHE ARG GLY ARG GLU ASP SER
SEQRES 23 D 724 ALA PRO PHE MET LYS LEU ILE ASP SER PHE ASP ALA SER
SEQRES 24 D 724 TYR THR ALA ILE ALA ASN ASP GLY SER VAL PHE THR PHE
SEQRES 25 D 724 GLN THR ASN LYS ASP ALA PRO ARG LYS LYS LEU VAL ARG
SEQRES 26 D 724 VAL ASP LEU ASN ASN PRO SER VAL TRP THR ASP LEU VAL
SEQRES 27 D 724 PRO GLU SER LYS LYS ASP LEU LEU GLU SER ALA HIS ALA
SEQRES 28 D 724 VAL ASN GLU ASN GLN LEU ILE LEU ARG TYR LEU SER ASP
SEQRES 29 D 724 VAL LYS HIS VAL LEU GLU ILE ARG ASP LEU GLU SER GLY
SEQRES 30 D 724 ALA LEU GLN HIS ARG LEU PRO ILE ASP ILE GLY SER VAL
SEQRES 31 D 724 ASP GLY ILE THR ALA ARG ARG ARG ASP SER VAL VAL PHE
SEQRES 32 D 724 PHE LYS PHE THR SER ILE LEU THR PRO GLY ILE VAL TYR
SEQRES 33 D 724 GLN CYS ASP LEU LYS ASN ASP PRO THR GLN LEU LYS ILE
SEQRES 34 D 724 PHE ARG GLU SER VAL VAL PRO ASP PHE ASP ARG SER GLU
SEQRES 35 D 724 PHE GLU VAL LYS GLN VAL PHE VAL PRO SER LYS ASP GLY
SEQRES 36 D 724 THR LYS ILE PRO ILE PHE ILE ALA ALA ARG LYS GLY ILE
SEQRES 37 D 724 SER LEU ASP GLY SER HIS PRO CYS GLU MET HIS GLY TYR
SEQRES 38 D 724 GLY GLY PHE GLY ILE ASN MET MET PRO THR PHE SER ALA
SEQRES 39 D 724 SER ARG ILE VAL PHE LEU LYS HIS LEU GLY GLY VAL PHE
SEQRES 40 D 724 CYS LEU ALA ASN ILE ARG GLY GLY GLY GLU TYR GLY GLU
SEQRES 41 D 724 GLU TRP HIS LYS ALA GLY PHE ARG ASP LYS LYS GLN ASN
SEQRES 42 D 724 VAL PHE ASP ASP PHE ILE SER ALA ALA GLU TYR LEU ILE
SEQRES 43 D 724 SER SER GLY TYR THR LYS ALA ARG ARG VAL ALA ILE GLU
SEQRES 44 D 724 GLY GLY ALA ASN GLY GLY LEU LEU VAL ALA ALA CYS ILE
SEQRES 45 D 724 ASN GLN ARG PRO ASP LEU PHE GLY CYS ALA GLU ALA ASN
SEQRES 46 D 724 CYS GLY VAL MET ASP MET LEU ARG PHE HIS LYS PHE THR
SEQRES 47 D 724 LEU GLY TYR LEU TRP THR GLY ASP TYR GLY CYS SER ASP
SEQRES 48 D 724 LYS GLU GLU GLU PHE LYS TRP LEU ILE LYS TYR SER PRO
SEQRES 49 D 724 ILE HIS ASN VAL ARG ARG PRO TRP GLU GLN PRO GLY ASN
SEQRES 50 D 724 GLU GLU THR GLN TYR PRO ALA THR MET ILE LEU THR ALA
SEQRES 51 D 724 ASP HIS ASP ASP ARG VAL VAL PRO LEU HIS SER PHE LYS
SEQRES 52 D 724 LEU LEU ALA THR MET GLN HIS VAL LEU CYS THR SER LEU
SEQRES 53 D 724 GLU ASP SER PRO GLN LYS ASN PRO ILE ILE ALA ARG ILE
SEQRES 54 D 724 GLN ARG LYS ALA ALA HIS TYR GLY ARG ALA THR MET THR
SEQRES 55 D 724 GLN ILE ALA GLU VAL ALA ASP ARG TYR GLY PHE MET ALA
SEQRES 56 D 724 LYS ALA LEU GLU ALA PRO TRP ILE ASP
SEQRES 1 W 32 MET SER PRO ILE LEU ALA HIS ASP VAL VAL LYS PRO GLN
SEQRES 2 W 32 GLY VAL PRO VAL TRP ALA PHE GLN ALA LYS ASP VAL GLU
SEQRES 3 W 32 ASN ALA SER ALA PRO VAL
SEQRES 1 X 32 MET SER PRO ILE LEU ALA HIS ASP VAL VAL LYS PRO GLN
SEQRES 2 X 32 GLY VAL PRO VAL TRP ALA PHE GLN ALA LYS ASP VAL GLU
SEQRES 3 X 32 ASN ALA SER ALA PRO VAL
SEQRES 1 Y 32 MET SER PRO ILE LEU ALA HIS ASP VAL VAL LYS PRO GLN
SEQRES 2 Y 32 GLY VAL PRO VAL TRP ALA PHE GLN ALA LYS ASP VAL GLU
SEQRES 3 Y 32 ASN ALA SER ALA PRO VAL
SEQRES 1 Z 32 MET SER PRO ILE LEU ALA HIS ASP VAL VAL LYS PRO GLN
SEQRES 2 Z 32 GLY VAL PRO VAL TRP ALA PHE GLN ALA LYS ASP VAL GLU
SEQRES 3 Z 32 ASN ALA SER ALA PRO VAL
HET MG B 801 1
HET SO4 B 802 5
HET MG C 801 1
HET SO4 C 802 5
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
FORMUL 9 MG 2(MG 2+)
FORMUL 10 SO4 2(O4 S 2-)
FORMUL 13 HOH *844(H2 O)
HELIX 1 AA1 TYR A 34 ASP A 39 5 6
HELIX 2 AA2 SER A 42 GLU A 61 1 20
HELIX 3 AA3 LEU A 65 ASN A 78 1 14
HELIX 4 AA4 ASP A 222 ASP A 226 5 5
HELIX 5 AA5 THR A 271 LEU A 273 5 3
HELIX 6 AA6 ASN A 275 ARG A 281 5 7
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 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 THR A 700 LEU A 718 1 19
HELIX 23 AC5 TYR B 34 ASP B 39 5 6
HELIX 24 AC6 SER B 42 GLU B 61 1 20
HELIX 25 AC7 LEU B 65 ASN B 78 1 14
HELIX 26 AC8 ASP B 121 ARG B 125 5 5
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 ASN B 275 ARG B 281 5 7
HELIX 30 AD3 ASP B 439 SER B 441 5 3
HELIX 31 AD4 SER B 493 LEU B 503 1 11
HELIX 32 AD5 GLY B 519 ALA B 525 1 7
HELIX 33 AD6 GLY B 526 LYS B 530 5 5
HELIX 34 AD7 LYS B 531 SER B 548 1 18
HELIX 35 AD8 LYS B 552 ARG B 554 5 3
HELIX 36 AD9 ALA B 562 ARG B 575 1 14
HELIX 37 AE1 PRO B 576 PHE B 579 5 4
HELIX 38 AE2 ARG B 593 PHE B 597 5 5
HELIX 39 AE3 LEU B 599 LEU B 602 5 4
HELIX 40 AE4 TRP B 603 GLY B 608 1 6
HELIX 41 AE5 LYS B 612 SER B 623 1 12
HELIX 42 AE6 PRO B 624 ASN B 627 5 4
HELIX 43 AE7 ARG B 630 GLN B 634 5 5
HELIX 44 AE8 PRO B 658 CYS B 673 1 16
HELIX 45 AE9 ALA B 699 LEU B 718 1 20
HELIX 46 AF1 TYR C 34 ASP C 39 5 6
HELIX 47 AF2 SER C 42 GLU C 61 1 20
HELIX 48 AF3 LEU C 65 ASN C 78 1 14
HELIX 49 AF4 ASP C 121 ARG C 125 5 5
HELIX 50 AF5 ASP C 222 ASP C 226 5 5
HELIX 51 AF6 THR C 271 LEU C 273 5 3
HELIX 52 AF7 ASP C 439 SER C 441 5 3
HELIX 53 AF8 SER C 493 LEU C 503 1 11
HELIX 54 AF9 GLY C 519 ALA C 525 1 7
HELIX 55 AG1 GLY C 526 LYS C 530 5 5
HELIX 56 AG2 LYS C 531 SER C 548 1 18
HELIX 57 AG3 LYS C 552 ARG C 554 5 3
HELIX 58 AG4 ALA C 562 ARG C 575 1 14
HELIX 59 AG5 PRO C 576 PHE C 579 5 4
HELIX 60 AG6 ARG C 593 PHE C 597 5 5
HELIX 61 AG7 LEU C 599 LEU C 602 5 4
HELIX 62 AG8 TRP C 603 GLY C 608 1 6
HELIX 63 AG9 LYS C 612 SER C 623 1 12
HELIX 64 AH1 PRO C 624 ASN C 627 5 4
HELIX 65 AH2 ARG C 630 GLN C 634 5 5
HELIX 66 AH3 PRO C 658 CYS C 673 1 16
HELIX 67 AH4 ALA C 699 LEU C 718 1 20
HELIX 68 AH5 TYR D 34 ASP D 39 5 6
HELIX 69 AH6 SER D 42 GLU D 61 1 20
HELIX 70 AH7 LEU D 65 ASN D 78 1 14
HELIX 71 AH8 ASP D 222 ASP D 226 5 5
HELIX 72 AH9 THR D 271 LEU D 273 5 3
HELIX 73 AI1 ASN D 275 ARG D 281 5 7
HELIX 74 AI2 ASP D 439 SER D 441 5 3
HELIX 75 AI3 SER D 493 LEU D 503 1 11
HELIX 76 AI4 GLY D 519 ALA D 525 1 7
HELIX 77 AI5 GLY D 526 LYS D 530 5 5
HELIX 78 AI6 LYS D 531 SER D 548 1 18
HELIX 79 AI7 LYS D 552 ARG D 554 5 3
HELIX 80 AI8 ALA D 562 ARG D 575 1 14
HELIX 81 AI9 PRO D 576 PHE D 579 5 4
HELIX 82 AJ1 ARG D 593 PHE D 597 5 5
HELIX 83 AJ2 LEU D 599 LEU D 602 5 4
HELIX 84 AJ3 TRP D 603 GLY D 608 1 6
HELIX 85 AJ4 LYS D 612 SER D 623 1 12
HELIX 86 AJ5 PRO D 624 ASN D 627 5 4
HELIX 87 AJ6 ARG D 630 GLN D 634 5 5
HELIX 88 AJ7 PRO D 658 CYS D 673 1 16
HELIX 89 AJ8 THR D 700 LEU D 718 1 19
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 ARG A 88 O LYS A 91
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 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 LEU A 132 VAL A 137 0
SHEET 2 AA4 4 TYR A 143 HIS A 149 -1 O GLY A 147 N SER A 133
SHEET 3 AA4 4 VAL A 156 LYS A 162 -1 O LEU A 161 N PHE A 144
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 HIS A 217 N PHE A 190
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 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 324 N PHE A 312
SHEET 4 AA7 4 ASN A 330 VAL A 338 -1 O LEU A 337 N LEU A 323
SHEET 1 AA8 4 LEU A 345 VAL A 352 0
SHEET 2 AA8 4 GLN A 356 SER A 363 -1 O ARG A 360 N SER A 348
SHEET 3 AA8 4 LYS A 366 ASP A 373 -1 O ARG A 372 N LEU A 357
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 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 PHE A 430 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 GLU A 477 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 LEU A 648 N ALA A 584
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 ARG B 88 O LYS B 91
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 GLN B 107 N HIS B 94
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 LEU B 161 N PHE B 144
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 HIS B 217 N PHE B 190
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 LEU B 337 N LEU B 323
SHEET 1 AB9 4 LEU B 345 VAL B 352 0
SHEET 2 AB9 4 GLN B 356 SER B 363 -1 O ARG B 360 N SER B 348
SHEET 3 AB9 4 LYS B 366 ASP B 373 -1 O ARG B 372 N LEU B 357
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 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 PHE B 430 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 GLU B 477 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 LEU B 648 N ALA B 584
SHEET 8 AC2 8 ILE B 685 GLN B 690 1 O GLN B 690 N THR B 649
SHEET 1 AC3 2 VAL C 22 TYR C 25 0
SHEET 2 AC3 2 VAL C 28 ALA C 31 -1 O VAL C 28 N TYR C 25
SHEET 1 AC4 3 ARG C 81 CYS C 82 0
SHEET 2 AC4 3 LYS C 91 ASN C 97 -1 O ASN C 97 N ARG C 81
SHEET 3 AC4 3 PHE C 86 ARG C 88 -1 N ARG C 88 O LYS C 91
SHEET 1 AC5 4 ARG C 81 CYS C 82 0
SHEET 2 AC5 4 LYS C 91 ASN C 97 -1 O ASN C 97 N ARG C 81
SHEET 3 AC5 4 VAL C 105 GLN C 109 -1 O GLN C 107 N HIS C 94
SHEET 4 AC5 4 GLU C 117 TYR C 120 -1 O LEU C 119 N PHE C 106
SHEET 1 AC6 4 LEU C 134 VAL C 137 0
SHEET 2 AC6 4 TYR C 143 ILE C 148 -1 O ALA C 145 N SER C 136
SHEET 3 AC6 4 VAL C 156 LYS C 162 -1 O LEU C 161 N PHE C 144
SHEET 4 AC6 4 TYR C 168 VAL C 176 -1 O VAL C 176 N VAL C 156
SHEET 1 AC7 4 ILE C 182 TRP C 183 0
SHEET 2 AC7 4 GLY C 189 TYR C 192 -1 O PHE C 191 N ILE C 182
SHEET 3 AC7 4 ALA C 214 PHE C 218 -1 O HIS C 217 N PHE C 190
SHEET 4 AC7 4 ILE C 227 TRP C 230 -1 O LEU C 229 N ALA C 214
SHEET 1 AC8 4 HIS C 239 ILE C 244 0
SHEET 2 AC8 4 TYR C 250 LEU C 256 -1 O LEU C 252 N GLN C 243
SHEET 3 AC8 4 ASN C 263 ASP C 269 -1 O TYR C 266 N LEU C 253
SHEET 4 AC8 4 MET C 290 ILE C 293 -1 O MET C 290 N CYS C 267
SHEET 1 AC9 4 TYR C 300 ASP C 306 0
SHEET 2 AC9 4 VAL C 309 THR C 314 -1 O THR C 311 N ILE C 303
SHEET 3 AC9 4 LYS C 322 ASP C 327 -1 O VAL C 324 N PHE C 312
SHEET 4 AC9 4 ASN C 330 VAL C 338 -1 O LEU C 337 N LEU C 323
SHEET 1 AD1 4 LEU C 345 VAL C 352 0
SHEET 2 AD1 4 GLN C 356 SER C 363 -1 O ARG C 360 N SER C 348
SHEET 3 AD1 4 LYS C 366 ASP C 373 -1 O ARG C 372 N LEU C 357
SHEET 4 AD1 4 LEU C 379 PRO C 384 -1 O GLN C 380 N ILE C 371
SHEET 1 AD2 4 SER C 389 ASP C 391 0
SHEET 2 AD2 4 VAL C 401 SER C 408 -1 O LYS C 405 N ASP C 391
SHEET 3 AD2 4 THR C 411 ASP C 419 -1 O ILE C 414 N PHE C 406
SHEET 4 AD2 4 LYS C 428 GLU C 432 -1 O PHE C 430 N VAL C 415
SHEET 1 AD3 8 PHE C 443 PRO C 451 0
SHEET 2 AD3 8 LYS C 457 ARG C 465 -1 O ILE C 458 N VAL C 450
SHEET 3 AD3 8 VAL C 506 ALA C 510 -1 O PHE C 507 N ALA C 463
SHEET 4 AD3 8 CYS C 476 HIS C 479 1 N GLU C 477 O CYS C 508
SHEET 5 AD3 8 VAL C 556 GLY C 561 1 O ALA C 557 N CYS C 476
SHEET 6 AD3 8 CYS C 581 ASN C 585 1 O ASN C 585 N GLY C 560
SHEET 7 AD3 8 ALA C 644 ALA C 650 1 O LEU C 648 N ALA C 584
SHEET 8 AD3 8 ILE C 685 GLN C 690 1 O GLN C 690 N THR C 649
SHEET 1 AD4 2 VAL D 22 TYR D 25 0
SHEET 2 AD4 2 VAL D 28 ALA D 31 -1 O VAL D 28 N TYR D 25
SHEET 1 AD5 3 ARG D 81 CYS D 82 0
SHEET 2 AD5 3 LYS D 91 ASN D 97 -1 O ASN D 97 N ARG D 81
SHEET 3 AD5 3 PHE D 86 ARG D 88 -1 N PHE D 86 O PHE D 93
SHEET 1 AD6 4 ARG D 81 CYS D 82 0
SHEET 2 AD6 4 LYS D 91 ASN D 97 -1 O ASN D 97 N ARG D 81
SHEET 3 AD6 4 VAL D 105 ASP D 110 -1 O GLN D 107 N HIS D 94
SHEET 4 AD6 4 GLU D 117 TYR D 120 -1 O LEU D 119 N PHE D 106
SHEET 1 AD7 4 LEU D 132 VAL D 137 0
SHEET 2 AD7 4 TYR D 143 HIS D 149 -1 O GLY D 147 N SER D 133
SHEET 3 AD7 4 VAL D 156 LYS D 162 -1 O LEU D 161 N PHE D 144
SHEET 4 AD7 4 LEU D 173 VAL D 176 -1 O VAL D 176 N VAL D 156
SHEET 1 AD8 4 ILE D 182 TRP D 183 0
SHEET 2 AD8 4 GLY D 189 TYR D 192 -1 O PHE D 191 N ILE D 182
SHEET 3 AD8 4 ALA D 214 PHE D 218 -1 O HIS D 217 N PHE D 190
SHEET 4 AD8 4 ILE D 227 TRP D 230 -1 O LEU D 229 N ALA D 214
SHEET 1 AD9 4 HIS D 239 ILE D 244 0
SHEET 2 AD9 4 TYR D 250 LEU D 256 -1 O LEU D 252 N GLN D 243
SHEET 3 AD9 4 ASN D 263 ASP D 269 -1 O TYR D 266 N LEU D 253
SHEET 4 AD9 4 MET D 290 ILE D 293 -1 O MET D 290 N CYS D 267
SHEET 1 AE1 4 TYR D 300 ASP D 306 0
SHEET 2 AE1 4 VAL D 309 THR D 314 -1 O THR D 311 N ILE D 303
SHEET 3 AE1 4 LYS D 322 ASP D 327 -1 O VAL D 324 N PHE D 312
SHEET 4 AE1 4 ASN D 330 VAL D 338 -1 O LEU D 337 N LEU D 323
SHEET 1 AE2 4 LEU D 345 VAL D 352 0
SHEET 2 AE2 4 GLN D 356 LEU D 362 -1 O ARG D 360 N SER D 348
SHEET 3 AE2 4 HIS D 367 ASP D 373 -1 O ARG D 372 N LEU D 357
SHEET 4 AE2 4 LEU D 379 PRO D 384 -1 O LEU D 383 N LEU D 369
SHEET 1 AE3 4 SER D 389 ASP D 391 0
SHEET 2 AE3 4 VAL D 401 SER D 408 -1 O LYS D 405 N ASP D 391
SHEET 3 AE3 4 THR D 411 ASP D 419 -1 O ILE D 414 N PHE D 406
SHEET 4 AE3 4 LYS D 428 GLU D 432 -1 O PHE D 430 N VAL D 415
SHEET 1 AE4 8 PHE D 443 PRO D 451 0
SHEET 2 AE4 8 LYS D 457 ARG D 465 -1 O ILE D 458 N VAL D 450
SHEET 3 AE4 8 VAL D 506 ALA D 510 -1 O PHE D 507 N ALA D 463
SHEET 4 AE4 8 CYS D 476 HIS D 479 1 N GLU D 477 O CYS D 508
SHEET 5 AE4 8 VAL D 556 GLY D 561 1 O ALA D 557 N CYS D 476
SHEET 6 AE4 8 CYS D 581 ASN D 585 1 O ASN D 585 N GLY D 560
SHEET 7 AE4 8 ALA D 644 ALA D 650 1 O LEU D 648 N ALA D 584
SHEET 8 AE4 8 ILE D 685 GLN D 690 1 O GLN D 690 N THR D 649
LINK MG MG B 801 O HOH B 912 1555 1555 2.12
LINK MG MG B 801 O HOH B1074 1555 1555 1.86
LINK MG MG B 801 O HOH B1065 1555 1555 1.81
LINK MG MG B 801 O HOH B 952 1555 1555 1.92
LINK MG MG B 801 O HOH B1003 1555 1555 2.08
LINK MG MG C 801 O HOH C 913 1555 1555 2.33
LINK MG MG C 801 O HOH C 914 1555 1555 2.21
LINK MG MG C 801 O HOH C 905 1555 1555 2.26
LINK MG MG C 801 O HOH C1024 1555 1555 2.00
LINK MG MG C 801 O HOH C1119 1555 1555 2.04
SITE 1 AC1 6 HIS B 652 HOH B 912 HOH B 952 HOH B1003
SITE 2 AC1 6 HOH B1065 HOH B1074
SITE 1 AC2 6 GLY B 151 LEU B 152 THR B 153 HOH B 912
SITE 2 AC2 6 HOH B1000 HOH B1074
SITE 1 AC3 6 HIS C 652 HOH C 905 HOH C 913 HOH C 914
SITE 2 AC3 6 HOH C1024 HOH C1119
SITE 1 AC4 7 GLY C 151 LEU C 152 THR C 153 HOH C 914
SITE 2 AC4 7 HOH C1014 HOH C1021 HOH C1024
CRYST1 60.080 88.600 144.950 93.00 99.32 90.05 P 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 0.016644 0.000015 0.002736 0.00000
SCALE2 0.000000 0.011287 0.000601 0.00000
SCALE3 0.000000 0.000000 0.007001 0.00000
TER 5704 ASP A 724
TER 11478 ASP B 724
TER 17244 ASP C 724
TER 22896 ASP D 724
TER 22945 VAL W 2
TER 22985 VAL X 2
TER 23025 VAL Y 2
TER 23081 VAL Z 2
MASTER 953 0 4 89 164 0 8 623901 8 24 236
END |