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HEADER HYDROLASE 27-JUL-10 3O4H
TITLE STRUCTURE AND CATALYSIS OF ACYLAMINOACYL PEPTIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACYLAMINO-ACID-RELEASING ENZYME;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: AARE, ACYL-PEPTIDE HYDROLASE, APH, ACYLAMINOACYL-PEPTIDASE;
COMPND 5 EC: 3.4.19.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AEROPYRUM PERNIX;
SOURCE 3 ORGANISM_TAXID: 56636;
SOURCE 4 GENE: APE_1547.1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS ALPHA/BETA HYDROLASE FOLD, BETA PROPELLER, HYDROLASE, OLIGOPEPTIDASE,
KEYWDS 2 SIZE SELECTIVITY
EXPDTA X-RAY DIFFRACTION
AUTHOR V.HARMAT,K.DOMOKOS,D.K.MENYHARD,A.PALLO,Z.SZELTNER,I.SZAMOSI,T.BEKE-
AUTHOR 2 SOMFAI,G.NARAY-SZABO,L.POLGAR
REVDAT 1 17-NOV-10 3O4H 0
JRNL AUTH V.HARMAT,K.DOMOKOS,D.K.MENYHARD,A.PALLO,Z.SZELTNER,
JRNL AUTH 2 I.SZAMOSI,T.BEKE-SOMFAI,G.NARAY-SZABO,L.POLGAR
JRNL TITL STRUCTURE AND CATALYSIS OF ACYLAMINOACYL PEPTIDASE: CLOSED
JRNL TITL 2 AND OPEN SUBUNITS OF A DIMER OLIGOPEPTIDASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 196431
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10388
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.82
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 14326
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.08
REMARK 3 BIN R VALUE (WORKING SET) : 0.3300
REMARK 3 BIN FREE R VALUE SET COUNT : 737
REMARK 3 BIN FREE R VALUE : 0.3460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17118
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 928
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.09000
REMARK 3 B33 (A**2) : -0.03000
REMARK 3 B12 (A**2) : 0.03000
REMARK 3 B13 (A**2) : 0.04000
REMARK 3 B23 (A**2) : 0.06000
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): 0.134
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.118
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.964
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17614 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 11984 ; 0.008 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 23937 ; 1.722 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 29051 ; 1.426 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2322 ; 6.335 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 692 ;33.218 ;22.442
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2720 ;15.420 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 152 ;21.006 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2694 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19995 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3712 ; 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): 11413 ; 0.775 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4756 ; 0.483 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 18228 ; 1.157 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6201 ; 2.026 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5699 ; 2.924 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 4
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 6 A 10 3
REMARK 3 1 C 6 C 10 3
REMARK 3 2 A 12 A 21 3
REMARK 3 2 C 12 C 21 3
REMARK 3 3 A 322 A 344 3
REMARK 3 3 C 322 C 344 3
REMARK 3 4 A 346 A 430 3
REMARK 3 4 C 346 C 430 3
REMARK 3 5 A 432 A 434 3
REMARK 3 5 C 432 C 434 3
REMARK 3 6 A 436 A 541 3
REMARK 3 6 C 436 C 541 3
REMARK 3 7 A 543 A 580 3
REMARK 3 7 C 543 C 580 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1553 ; 0.060 ; 0.050
REMARK 3 LOOSE POSITIONAL 1 A (A): 1739 ; 0.160 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 1553 ; 0.260 ; 0.500
REMARK 3 LOOSE THERMAL 1 A (A**2): 1739 ; 0.220 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 6
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 7 B 21 3
REMARK 3 1 D 7 D 21 3
REMARK 3 2 B 322 B 341 3
REMARK 3 2 D 322 D 341 3
REMARK 3 3 B 343 B 344 3
REMARK 3 3 D 343 D 344 3
REMARK 3 4 B 346 B 427 3
REMARK 3 4 D 346 D 427 3
REMARK 3 5 B 429 B 430 3
REMARK 3 5 D 429 D 430 3
REMARK 3 6 B 433 B 579 3
REMARK 3 6 D 433 D 579 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 1566 ; 0.070 ; 0.050
REMARK 3 LOOSE POSITIONAL 2 B (A): 1745 ; 0.170 ; 5.000
REMARK 3 TIGHT THERMAL 2 B (A**2): 1566 ; 0.230 ; 0.500
REMARK 3 LOOSE THERMAL 2 B (A**2): 1745 ; 0.190 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 27 A 40 3
REMARK 3 1 C 27 C 40 3
REMARK 3 2 A 42 A 317 3
REMARK 3 2 C 42 C 317 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 1680 ; 0.060 ; 0.050
REMARK 3 LOOSE POSITIONAL 3 A (A): 1814 ; 0.140 ; 5.000
REMARK 3 TIGHT THERMAL 3 A (A**2): 1680 ; 0.200 ; 0.500
REMARK 3 LOOSE THERMAL 3 A (A**2): 1814 ; 0.190 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 4
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 25 B 71 3
REMARK 3 1 D 25 D 71 3
REMARK 3 2 B 73 B 97 3
REMARK 3 2 D 73 D 97 3
REMARK 3 3 B 99 B 158 3
REMARK 3 3 D 99 D 158 3
REMARK 3 4 B 160 B 317 3
REMARK 3 4 D 160 D 317 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 B (A): 1680 ; 0.100 ; 0.050
REMARK 3 LOOSE POSITIONAL 4 B (A): 1793 ; 0.170 ; 5.000
REMARK 3 TIGHT THERMAL 4 B (A**2): 1680 ; 0.230 ; 0.500
REMARK 3 LOOSE THERMAL 4 B (A**2): 1793 ; 0.190 ;10.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 6 A 23
REMARK 3 RESIDUE RANGE : A 319 A 581
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1077 -6.6514 -0.0263
REMARK 3 T TENSOR
REMARK 3 T11: 0.1881 T22: 0.0898
REMARK 3 T33: 0.1993 T12: 0.1188
REMARK 3 T13: -0.0993 T23: -0.0528
REMARK 3 L TENSOR
REMARK 3 L11: 0.8710 L22: 1.1408
REMARK 3 L33: 1.3810 L12: 0.4496
REMARK 3 L13: 0.4164 L23: 0.0098
REMARK 3 S TENSOR
REMARK 3 S11: -0.1367 S12: -0.1196 S13: 0.1605
REMARK 3 S21: -0.0977 S22: -0.0923 S23: 0.1540
REMARK 3 S31: -0.3306 S32: -0.2206 S33: 0.2291
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 7 B 23
REMARK 3 RESIDUE RANGE : B 319 B 580
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1847 6.0457 2.3542
REMARK 3 T TENSOR
REMARK 3 T11: 0.2311 T22: 0.2671
REMARK 3 T33: 0.2174 T12: 0.1552
REMARK 3 T13: -0.0811 T23: -0.1262
REMARK 3 L TENSOR
REMARK 3 L11: 1.6888 L22: 1.3908
REMARK 3 L33: 2.9427 L12: 1.3034
REMARK 3 L13: 0.8425 L23: 1.1548
REMARK 3 S TENSOR
REMARK 3 S11: 0.1373 S12: 0.3967 S13: -0.1774
REMARK 3 S21: -0.0747 S22: 0.3300 S23: -0.1340
REMARK 3 S31: 0.3112 S32: 0.6555 S33: -0.4673
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 5 C 23
REMARK 3 RESIDUE RANGE : C 319 C 581
REMARK 3 ORIGIN FOR THE GROUP (A): -18.5147 31.2688 -29.4688
REMARK 3 T TENSOR
REMARK 3 T11: 0.0400 T22: 0.0698
REMARK 3 T33: 0.1201 T12: 0.0112
REMARK 3 T13: 0.0358 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 0.9555 L22: 3.0101
REMARK 3 L33: 2.1834 L12: 0.6262
REMARK 3 L13: 0.8288 L23: 0.5827
REMARK 3 S TENSOR
REMARK 3 S11: -0.0007 S12: 0.1874 S13: -0.2160
REMARK 3 S21: 0.0715 S22: 0.1576 S23: -0.1798
REMARK 3 S31: 0.0083 S32: 0.2972 S33: -0.1570
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 7 D 23
REMARK 3 RESIDUE RANGE : D 319 D 581
REMARK 3 ORIGIN FOR THE GROUP (A): -23.8525 2.9426 -49.5696
REMARK 3 T TENSOR
REMARK 3 T11: 0.0629 T22: 0.1121
REMARK 3 T33: 0.1885 T12: -0.0038
REMARK 3 T13: 0.0538 T23: -0.0506
REMARK 3 L TENSOR
REMARK 3 L11: 1.0119 L22: 3.2599
REMARK 3 L33: 2.6193 L12: 0.1335
REMARK 3 L13: 0.8112 L23: 1.9555
REMARK 3 S TENSOR
REMARK 3 S11: -0.0723 S12: -0.0019 S13: 0.0392
REMARK 3 S21: 0.0289 S22: 0.3581 S23: -0.4862
REMARK 3 S31: 0.0498 S32: 0.3254 S33: -0.2858
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 24 A 318
REMARK 3 ORIGIN FOR THE GROUP (A): -12.4343 -34.1199 -2.1774
REMARK 3 T TENSOR
REMARK 3 T11: 0.0762 T22: 0.0521
REMARK 3 T33: 0.0860 T12: -0.0032
REMARK 3 T13: 0.0302 T23: 0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 0.7919 L22: 0.8188
REMARK 3 L33: 1.4908 L12: 0.2050
REMARK 3 L13: 0.1902 L23: 0.2134
REMARK 3 S TENSOR
REMARK 3 S11: 0.0184 S12: -0.0775 S13: -0.0039
REMARK 3 S21: -0.1318 S22: -0.0825 S23: 0.0523
REMARK 3 S31: 0.0654 S32: -0.1502 S33: 0.0642
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 24 B 318
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6059 32.6061 21.4787
REMARK 3 T TENSOR
REMARK 3 T11: 0.0715 T22: 0.1563
REMARK 3 T33: 0.0834 T12: -0.0194
REMARK 3 T13: 0.0623 T23: -0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 1.3053 L22: 1.5333
REMARK 3 L33: 0.9326 L12: -0.1577
REMARK 3 L13: 0.3020 L23: -0.3468
REMARK 3 S TENSOR
REMARK 3 S11: 0.0573 S12: 0.1708 S13: -0.0306
REMARK 3 S21: 0.0105 S22: -0.0403 S23: 0.1297
REMARK 3 S31: -0.0806 S32: 0.0987 S33: -0.0169
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 : C 24 C 318
REMARK 3 ORIGIN FOR THE GROUP (A): 0.8813 46.5323 -43.0351
REMARK 3 T TENSOR
REMARK 3 T11: 0.1450 T22: 0.1835
REMARK 3 T33: 0.2742 T12: -0.0511
REMARK 3 T13: -0.0593 T23: 0.0486
REMARK 3 L TENSOR
REMARK 3 L11: 2.2174 L22: 1.6436
REMARK 3 L33: 1.7293 L12: 0.2116
REMARK 3 L13: 0.5260 L23: 0.2123
REMARK 3 S TENSOR
REMARK 3 S11: 0.2139 S12: 0.1949 S13: -0.3610
REMARK 3 S21: 0.2212 S22: -0.0918 S23: -0.4789
REMARK 3 S31: 0.0681 S32: 0.3851 S33: -0.1221
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 : D 24 D 318
REMARK 3 ORIGIN FOR THE GROUP (A): -55.1609 -5.3036 -48.2023
REMARK 3 T TENSOR
REMARK 3 T11: 0.1277 T22: 0.3122
REMARK 3 T33: 0.0973 T12: -0.0627
REMARK 3 T13: 0.0704 T23: 0.0376
REMARK 3 L TENSOR
REMARK 3 L11: 1.7861 L22: 2.1145
REMARK 3 L33: 1.5290 L12: 0.1057
REMARK 3 L13: 0.1661 L23: 0.1583
REMARK 3 S TENSOR
REMARK 3 S11: 0.0097 S12: -0.5459 S13: 0.0153
REMARK 3 S21: 0.3101 S22: -0.0051 S23: 0.1806
REMARK 3 S31: 0.1309 S32: -0.2821 S33: -0.0047
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3O4H COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-10.
REMARK 100 THE RCSB ID CODE IS RCSB060653.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8148
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111),
REMARK 200 HORIZONTALLY FOCUSSING
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : FLAT PANEL
REMARK 200 DETECTOR MANUFACTURER : MAR555 FLAT PANEL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 206854
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 1.880
REMARK 200 R MERGE (I) : 0.02800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.7200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.88
REMARK 200 R MERGE FOR SHELL (I) : 0.60600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.260
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: HYDROLASE AND PROPELLER DOMAINS OF PDB ENTRY 2HU5.
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 78MM SODIUM ACETATE, 0.44MM EDTA,
REMARK 280 6.7MM DITHIOTHREITOL, 2.4% PEG 4000 , PH 5.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS HOMODIMER. ONE DIMER CONSISTS OF
REMARK 300 CHAINS A AND B, AND THE OTHER DIMER CONSISTS OF CHAINS C AND D.
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: 3450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
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 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: 3100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 ILE A 3
REMARK 465 ILE A 4
REMARK 465 MET A 5
REMARK 465 ARG A 582
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 ILE B 3
REMARK 465 ILE B 4
REMARK 465 MET B 5
REMARK 465 PRO B 6
REMARK 465 ARG B 581
REMARK 465 ARG B 582
REMARK 465 MET C 1
REMARK 465 ARG C 2
REMARK 465 ILE C 3
REMARK 465 ILE C 4
REMARK 465 ARG C 582
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 ILE D 3
REMARK 465 ILE D 4
REMARK 465 MET D 5
REMARK 465 PRO D 6
REMARK 465 ARG D 582
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 GLU A 8 OE1 OE2
REMARK 470 GLU A 43 CG CD OE1 OE2
REMARK 470 LYS A 85 CE NZ
REMARK 470 LYS A 94 CD CE NZ
REMARK 470 GLU A 131 CD OE1 OE2
REMARK 470 ARG A 216 CZ NH1 NH2
REMARK 470 GLU A 217 CG CD OE1 OE2
REMARK 470 ARG A 226 CD NE CZ NH1 NH2
REMARK 470 LYS A 238 CG CD CE NZ
REMARK 470 ARG A 244 NE CZ NH1 NH2
REMARK 470 LYS A 294 CD CE NZ
REMARK 470 ARG A 327 CZ NH1 NH2
REMARK 470 PHE A 341 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 352 CG CD OE1 OE2
REMARK 470 GLU A 479 CG CD OE1 OE2
REMARK 470 LYS A 530 NZ
REMARK 470 ARG A 581 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 7 CG1 CG2
REMARK 470 ASP B 52 CG OD1 OD2
REMARK 470 GLU B 55 CG CD OE1 OE2
REMARK 470 ARG B 61 CZ NH1 NH2
REMARK 470 LYS B 85 CG CD CE NZ
REMARK 470 GLU B 88 CG CD OE1 OE2
REMARK 470 GLN B 104 CD OE1 NE2
REMARK 470 ARG B 113 NH1 NH2
REMARK 470 GLU B 131 CG CD OE1 OE2
REMARK 470 ARG B 149 NE CZ NH1 NH2
REMARK 470 ARG B 174 CZ NH1 NH2
REMARK 470 GLU B 194 CG CD OE1 OE2
REMARK 470 ARG B 216 CZ NH1 NH2
REMARK 470 GLU B 217 CD OE1 OE2
REMARK 470 GLU B 234 CG CD OE1 OE2
REMARK 470 ASP B 325 CG OD1 OD2
REMARK 470 GLU B 406 CG CD OE1 OE2
REMARK 470 LYS B 410 CE NZ
REMARK 470 ARG B 431 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 463 NZ
REMARK 470 ARG B 486 CD NE CZ NH1 NH2
REMARK 470 ASN B 487 CG OD1 ND2
REMARK 470 GLU B 490 CG CD OE1 OE2
REMARK 470 GLN B 491 CG CD OE1 NE2
REMARK 470 SER B 496 OG
REMARK 470 GLU B 498 CG CD OE1 OE2
REMARK 470 ILE B 499 CD1
REMARK 470 ARG B 501 CD NE CZ NH1 NH2
REMARK 470 ASP B 510 CG OD1 OD2
REMARK 470 ARG B 511 NE CZ NH1 NH2
REMARK 470 LYS B 513 CD CE NZ
REMARK 470 ARG B 526 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 530 CD CE NZ
REMARK 470 GLU B 538 CD OE1 OE2
REMARK 470 ARG B 542 CZ NH1 NH2
REMARK 470 ILE B 558 CD1
REMARK 470 ILE B 567 CD1
REMARK 470 GLU B 580 CB CG CD OE1 OE2
REMARK 470 MET C 5 SD CE
REMARK 470 GLU C 8 CG CD OE1 OE2
REMARK 470 ASP C 32 CG OD1 OD2
REMARK 470 GLU C 43 CG CD OE1 OE2
REMARK 470 ARG C 61 CZ NH1 NH2
REMARK 470 LYS C 85 CE NZ
REMARK 470 GLN C 89 CD OE1 NE2
REMARK 470 LYS C 94 CD CE NZ
REMARK 470 ARG C 99 CD NE CZ NH1 NH2
REMARK 470 GLN C 104 CG CD OE1 NE2
REMARK 470 GLU C 107 CD OE1 OE2
REMARK 470 LYS C 110 CG CD CE NZ
REMARK 470 GLU C 131 CG CD OE1 OE2
REMARK 470 ARG C 133 CZ NH1 NH2
REMARK 470 ARG C 149 CD NE CZ NH1 NH2
REMARK 470 ARG C 188 NE CZ NH1 NH2
REMARK 470 LYS C 207 CE NZ
REMARK 470 GLU C 217 CG CD OE1 OE2
REMARK 470 GLU C 234 CG CD OE1 OE2
REMARK 470 ARG C 244 CD NE CZ NH1 NH2
REMARK 470 GLU C 279 OE1 OE2
REMARK 470 LYS C 294 NZ
REMARK 470 ARG C 328 CZ NH1 NH2
REMARK 470 GLU C 432 CG CD OE1 OE2
REMARK 470 GLU C 479 CD OE1 OE2
REMARK 470 LEU C 480 CG CD1 CD2
REMARK 470 ARG C 486 NE CZ NH1 NH2
REMARK 470 ARG C 497 CZ NH1 NH2
REMARK 470 GLU C 498 CG CD OE1 OE2
REMARK 470 ARG C 501 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 530 CG CD CE NZ
REMARK 470 ILE C 551 CD1
REMARK 470 THR C 560 CG2
REMARK 470 GLU C 562 CG CD OE1 OE2
REMARK 470 ARG C 581 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 35 CE NZ
REMARK 470 GLU D 55 CG CD OE1 OE2
REMARK 470 VAL D 83 CG1 CG2
REMARK 470 SER D 84 OG
REMARK 470 LYS D 85 CG CD CE NZ
REMARK 470 GLU D 88 CG CD OE1 OE2
REMARK 470 GLN D 89 CG CD OE1 NE2
REMARK 470 LYS D 94 NZ
REMARK 470 ARG D 99 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 110 CG CD CE NZ
REMARK 470 GLU D 131 CB CG CD OE1 OE2
REMARK 470 ASP D 132 CG OD1 OD2
REMARK 470 ARG D 133 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 134 CG1 CG2
REMARK 470 ARG D 149 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 181 CG OD1 ND2
REMARK 470 GLU D 194 OE1 OE2
REMARK 470 ARG D 216 NE CZ NH1 NH2
REMARK 470 GLU D 324 CG CD OE1 OE2
REMARK 470 ARG D 328 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 490 CG CD OE1 OE2
REMARK 470 GLN D 491 CD OE1 NE2
REMARK 470 ARG D 511 CD NE CZ NH1 NH2
REMARK 470 LYS D 513 CE NZ
REMARK 470 SER D 525 OG
REMARK 470 LYS D 530 CE NZ
REMARK 470 GLU D 580 CD OE1 OE2
REMARK 470 ARG D 581 CG CD NE CZ NH1 NH2
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 N SER A 199 O HOH A 840 2.04
REMARK 500 CE MET C 561 CG2 VAL C 565 2.18
REMARK 500 O HOH B 770 O HOH B 771 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PHE A 9 CG PHE A 9 CD2 -0.143
REMARK 500 PHE A 9 CG PHE A 9 CD1 -0.152
REMARK 500 PHE A 9 CE1 PHE A 9 CZ -0.215
REMARK 500 PHE A 9 CZ PHE A 9 CE2 -0.239
REMARK 500 GLU A 17 CB GLU A 17 CG -0.222
REMARK 500 ASP A 140 CB ASP A 140 CG -0.152
REMARK 500 ARG A 268 CZ ARG A 268 NH1 -0.132
REMARK 500 ARG A 268 CZ ARG A 268 NH2 -0.138
REMARK 500 ARG A 287 CZ ARG A 287 NH1 -0.183
REMARK 500 ARG A 292 CZ ARG A 292 NH1 -0.139
REMARK 500 ARG A 292 CZ ARG A 292 NH2 -0.132
REMARK 500 TYR A 444 CG TYR A 444 CD2 -0.159
REMARK 500 TYR A 444 CG TYR A 444 CD1 -0.174
REMARK 500 TYR A 444 CE1 TYR A 444 CZ -0.191
REMARK 500 TYR A 444 CZ TYR A 444 CE2 -0.202
REMARK 500 LEU A 455 CG LEU A 455 CD1 -0.230
REMARK 500 ARG B 105 CZ ARG B 105 NH1 -0.175
REMARK 500 ARG B 160 CZ ARG B 160 NH1 -0.166
REMARK 500 ARG B 160 CZ ARG B 160 NH2 -0.101
REMARK 500 ARG B 265 CZ ARG B 265 NH1 -0.176
REMARK 500 ARG B 292 CZ ARG B 292 NH1 -0.111
REMARK 500 ARG B 292 CZ ARG B 292 NH2 -0.123
REMARK 500 GLU B 339 C GLU B 339 O 0.149
REMARK 500 TYR B 444 CG TYR B 444 CD2 -0.158
REMARK 500 TYR B 444 CG TYR B 444 CD1 -0.166
REMARK 500 TYR B 444 CE1 TYR B 444 CZ -0.188
REMARK 500 TYR B 444 CZ TYR B 444 CE2 -0.198
REMARK 500 PHE B 485 CG PHE B 485 CD2 -0.153
REMARK 500 PHE B 485 CG PHE B 485 CD1 -0.133
REMARK 500 PHE B 485 CE1 PHE B 485 CZ -0.266
REMARK 500 PHE B 485 CZ PHE B 485 CE2 -0.232
REMARK 500 PHE C 9 CG PHE C 9 CD2 -0.162
REMARK 500 PHE C 9 CG PHE C 9 CD1 -0.161
REMARK 500 PHE C 9 CE1 PHE C 9 CZ -0.230
REMARK 500 PHE C 9 CZ PHE C 9 CE2 -0.221
REMARK 500 GLU C 17 CB GLU C 17 CG -0.215
REMARK 500 GLU C 55 CD GLU C 55 OE1 -0.075
REMARK 500 GLU C 55 CD GLU C 55 OE2 -0.072
REMARK 500 ARG C 268 CZ ARG C 268 NH1 -0.123
REMARK 500 ARG C 268 CZ ARG C 268 NH2 -0.131
REMARK 500 ARG C 287 CZ ARG C 287 NH1 -0.167
REMARK 500 ARG C 292 CZ ARG C 292 NH1 -0.132
REMARK 500 ARG C 292 CZ ARG C 292 NH2 -0.120
REMARK 500 TYR C 444 CG TYR C 444 CD2 -0.154
REMARK 500 TYR C 444 CG TYR C 444 CD1 -0.152
REMARK 500 TYR C 444 CE1 TYR C 444 CZ -0.185
REMARK 500 TYR C 444 CZ TYR C 444 CE2 -0.186
REMARK 500 ARG D 105 CZ ARG D 105 NH1 -0.165
REMARK 500 ARG D 160 CZ ARG D 160 NH1 -0.142
REMARK 500 ARG D 160 CZ ARG D 160 NH2 -0.088
REMARK 500
REMARK 500 THIS ENTRY HAS 66 BOND DEVIATIONS.
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 ASP A 34 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 52 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 61 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 GLU A 102 OE1 - CD - OE2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ASP A 140 N - CA - CB ANGL. DEV. = -15.9 DEGREES
REMARK 500 ASP A 140 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 140 CB - CG - OD2 ANGL. DEV. = -11.0 DEGREES
REMARK 500 ARG A 268 NH1 - CZ - NH2 ANGL. DEV. = -14.1 DEGREES
REMARK 500 ARG A 268 NE - CZ - NH1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 ARG A 268 NE - CZ - NH2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG A 287 CG - CD - NE ANGL. DEV. = 14.7 DEGREES
REMARK 500 ARG A 287 NH1 - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG A 287 NE - CZ - NH1 ANGL. DEV. = -4.7 DEGREES
REMARK 500 ARG A 287 NE - CZ - NH2 ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG A 292 NH1 - CZ - NH2 ANGL. DEV. = -16.3 DEGREES
REMARK 500 ARG A 292 NE - CZ - NH1 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ARG A 292 NE - CZ - NH2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 TYR A 444 CB - CG - CD1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 LEU A 492 CB - CG - CD2 ANGL. DEV. = 10.8 DEGREES
REMARK 500 GLU A 538 CA - CB - CG ANGL. DEV. = 14.1 DEGREES
REMARK 500 GLU B 62 OE1 - CD - OE2 ANGL. DEV. = -8.9 DEGREES
REMARK 500 ARG B 105 NH1 - CZ - NH2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 ARG B 105 NE - CZ - NH2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 ARG B 160 NH1 - CZ - NH2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 ARG B 160 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG B 265 NE - CZ - NH1 ANGL. DEV. = -14.2 DEGREES
REMARK 500 ARG B 265 NE - CZ - NH2 ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG B 292 NH1 - CZ - NH2 ANGL. DEV. = -11.7 DEGREES
REMARK 500 ARG B 292 NE - CZ - NH1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ARG B 292 NE - CZ - NH2 ANGL. DEV. = 3.3 DEGREES
REMARK 500 GLU B 315 OE1 - CD - OE2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ARG B 428 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 LEU B 455 CB - CG - CD2 ANGL. DEV. = 13.1 DEGREES
REMARK 500 ARG B 497 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP B 553 CB - CG - OD1 ANGL. DEV. = 8.5 DEGREES
REMARK 500 LEU B 569 CB - CG - CD1 ANGL. DEV. = 14.7 DEGREES
REMARK 500 PRO C 6 C - N - CA ANGL. DEV. = 11.8 DEGREES
REMARK 500 PRO C 6 C - N - CD ANGL. DEV. = -14.0 DEGREES
REMARK 500 GLU C 55 OE1 - CD - OE2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 GLU C 122 OE1 - CD - OE2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 GLU C 122 CG - CD - OE2 ANGL. DEV. = -15.5 DEGREES
REMARK 500 ASP C 140 CB - CG - OD2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 ARG C 268 NH1 - CZ - NH2 ANGL. DEV. = -15.3 DEGREES
REMARK 500 ARG C 268 NE - CZ - NH1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG C 268 NE - CZ - NH2 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG C 287 CG - CD - NE ANGL. DEV. = 13.2 DEGREES
REMARK 500 ARG C 287 NH1 - CZ - NH2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ARG C 287 NE - CZ - NH1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG C 287 NE - CZ - NH2 ANGL. DEV. = 12.5 DEGREES
REMARK 500 ARG C 292 NH1 - CZ - NH2 ANGL. DEV. = -16.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 73 ANGLE DEVIATIONS.
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 ASP A 32 -141.21 41.50
REMARK 500 ARG A 61 -82.13 -101.64
REMARK 500 ALA A 148 148.76 -171.77
REMARK 500 PRO A 151 44.93 -82.05
REMARK 500 THR A 214 -169.96 -101.63
REMARK 500 ARG A 216 10.19 -142.72
REMARK 500 SER A 445 -129.92 63.05
REMARK 500 ASP B 32 -139.74 59.21
REMARK 500 ASP B 34 45.78 79.51
REMARK 500 ASP B 52 50.30 -140.43
REMARK 500 ARG B 61 -83.40 -95.71
REMARK 500 ASP B 140 -159.96 -136.79
REMARK 500 ARG B 216 -113.42 -125.07
REMARK 500 ASP B 342 -15.91 -48.84
REMARK 500 ASP B 414 48.42 -140.56
REMARK 500 SER B 445 -130.34 65.46
REMARK 500 ASN B 523 39.67 -144.80
REMARK 500 ARG C 61 -81.73 -102.23
REMARK 500 ALA C 148 149.65 -170.64
REMARK 500 PRO C 151 46.81 -77.73
REMARK 500 THR C 214 -167.80 -103.03
REMARK 500 ASP C 414 45.04 -140.69
REMARK 500 SER C 445 -125.12 65.53
REMARK 500 ASP D 34 53.28 -170.81
REMARK 500 ARG D 61 -84.26 -93.82
REMARK 500 SER D 66 -177.65 -170.72
REMARK 500 GLU D 88 -6.67 66.69
REMARK 500 THR D 130 -169.12 -110.35
REMARK 500 ARG D 216 -112.21 -127.66
REMARK 500 SER D 340 -160.71 -107.95
REMARK 500 ASP D 342 3.55 53.73
REMARK 500 ASP D 414 48.44 -140.22
REMARK 500 SER D 445 -131.46 66.42
REMARK 500 ASN D 523 40.66 -146.22
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 VAL C 31 ASP C 32 -148.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASP A 140 46.0 L L OUTSIDE RANGE
REMARK 500 ALA D 87 23.2 L L OUTSIDE RANGE
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 NA D 583 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D 667 O
REMARK 620 2 HOH D 691 O 94.6
REMARK 620 3 HOH D 587 O 94.1 171.2
REMARK 620 4 ASP D 374 OD1 94.9 92.8 85.4
REMARK 620 5 HOH D 604 O 108.0 90.1 88.2 156.6
REMARK 620 6 HOH D 608 O 170.3 85.3 86.3 94.7 62.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 583 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 690 O
REMARK 620 2 HOH B 907 O 89.6
REMARK 620 3 HOH B 655 O 97.8 171.4
REMARK 620 4 ASP B 374 OD1 89.2 89.2 86.5
REMARK 620 5 HOH B 687 O 113.0 89.0 92.2 157.7
REMARK 620 6 HOH B 717 O 173.2 88.0 85.2 97.1 60.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 583
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 584
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 583
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 584
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 583
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 584
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 585
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O4G RELATED DB: PDB
REMARK 900 RELATED ID: 3O4I RELATED DB: PDB
REMARK 900 RELATED ID: 3O4J RELATED DB: PDB
DBREF 3O4H A 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 3O4H B 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 3O4H C 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 3O4H D 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
SEQADV 3O4H ALA A 524 UNP Q9YBQ2 ASP 524 ENGINEERED
SEQADV 3O4H ALA B 524 UNP Q9YBQ2 ASP 524 ENGINEERED
SEQADV 3O4H ALA C 524 UNP Q9YBQ2 ASP 524 ENGINEERED
SEQADV 3O4H ALA D 524 UNP Q9YBQ2 ASP 524 ENGINEERED
SEQRES 1 A 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 A 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 A 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 A 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 A 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 A 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 A 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 A 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 A 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 A 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 A 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 A 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 A 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 A 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 A 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 A 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 A 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 A 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 A 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 A 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 A 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 A 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 A 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 A 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 A 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 A 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 A 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 A 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 A 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 A 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 A 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 A 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 A 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 A 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 A 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 A 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 A 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 A 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 A 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 A 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 A 582 PRO GLN ASN ALA SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 A 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 A 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 A 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 A 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
SEQRES 1 B 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 B 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 B 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 B 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 B 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 B 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 B 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 B 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 B 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 B 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 B 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 B 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 B 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 B 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 B 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 B 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 B 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 B 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 B 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 B 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 B 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 B 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 B 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 B 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 B 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 B 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 B 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 B 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 B 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 B 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 B 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 B 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 B 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 B 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 B 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 B 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 B 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 B 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 B 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 B 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 B 582 PRO GLN ASN ALA SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 B 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 B 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 B 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 B 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
SEQRES 1 C 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 C 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 C 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 C 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 C 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 C 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 C 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 C 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 C 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 C 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 C 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 C 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 C 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 C 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 C 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 C 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 C 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 C 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 C 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 C 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 C 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 C 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 C 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 C 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 C 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 C 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 C 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 C 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 C 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 C 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 C 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 C 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 C 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 C 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 C 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 C 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 C 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 C 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 C 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 C 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 C 582 PRO GLN ASN ALA SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 C 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 C 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 C 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 C 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
SEQRES 1 D 582 MET ARG ILE ILE MET PRO VAL GLU PHE SER ARG ILE VAL
SEQRES 2 D 582 ARG ASP VAL GLU ARG LEU ILE ALA VAL GLU LYS TYR SER
SEQRES 3 D 582 LEU GLN GLY VAL VAL ASP GLY ASP LYS LEU LEU VAL VAL
SEQRES 4 D 582 GLY PHE SER GLU GLY SER VAL ASN ALA TYR LEU TYR ASP
SEQRES 5 D 582 GLY GLY GLU THR VAL LYS LEU ASN ARG GLU PRO ILE ASN
SEQRES 6 D 582 SER VAL LEU ASP PRO HIS TYR GLY VAL GLY ARG VAL ILE
SEQRES 7 D 582 LEU VAL ARG ASP VAL SER LYS GLY ALA GLU GLN HIS ALA
SEQRES 8 D 582 LEU PHE LYS VAL ASN THR SER ARG PRO GLY GLU GLU GLN
SEQRES 9 D 582 ARG LEU GLU ALA VAL LYS PRO MET ARG ILE LEU SER GLY
SEQRES 10 D 582 VAL ASP THR GLY GLU ALA VAL VAL PHE THR GLY ALA THR
SEQRES 11 D 582 GLU ASP ARG VAL ALA LEU TYR ALA LEU ASP GLY GLY GLY
SEQRES 12 D 582 LEU ARG GLU LEU ALA ARG LEU PRO GLY PHE GLY PHE VAL
SEQRES 13 D 582 SER ASP ILE ARG GLY ASP LEU ILE ALA GLY LEU GLY PHE
SEQRES 14 D 582 PHE GLY GLY GLY ARG VAL SER LEU PHE THR SER ASN LEU
SEQRES 15 D 582 SER SER GLY GLY LEU ARG VAL PHE ASP SER GLY GLU GLY
SEQRES 16 D 582 SER PHE SER SER ALA SER ILE SER PRO GLY MET LYS VAL
SEQRES 17 D 582 THR ALA GLY LEU GLU THR ALA ARG GLU ALA ARG LEU VAL
SEQRES 18 D 582 THR VAL ASP PRO ARG ASP GLY SER VAL GLU ASP LEU GLU
SEQRES 19 D 582 LEU PRO SER LYS ASP PHE SER SER TYR ARG PRO THR ALA
SEQRES 20 D 582 ILE THR TRP LEU GLY TYR LEU PRO ASP GLY ARG LEU ALA
SEQRES 21 D 582 VAL VAL ALA ARG ARG GLU GLY ARG SER ALA VAL PHE ILE
SEQRES 22 D 582 ASP GLY GLU ARG VAL GLU ALA PRO GLN GLY ASN HIS GLY
SEQRES 23 D 582 ARG VAL VAL LEU TRP ARG GLY LYS LEU VAL THR SER HIS
SEQRES 24 D 582 THR SER LEU SER THR PRO PRO ARG ILE VAL SER LEU PRO
SEQRES 25 D 582 SER GLY GLU PRO LEU LEU GLU GLY GLY LEU PRO GLU ASP
SEQRES 26 D 582 LEU ARG ARG SER ILE ALA GLY SER ARG LEU VAL TRP VAL
SEQRES 27 D 582 GLU SER PHE ASP GLY SER ARG VAL PRO THR TYR VAL LEU
SEQRES 28 D 582 GLU SER GLY ARG ALA PRO THR PRO GLY PRO THR VAL VAL
SEQRES 29 D 582 LEU VAL HIS GLY GLY PRO PHE ALA GLU ASP SER ASP SER
SEQRES 30 D 582 TRP ASP THR PHE ALA ALA SER LEU ALA ALA ALA GLY PHE
SEQRES 31 D 582 HIS VAL VAL MET PRO ASN TYR ARG GLY SER THR GLY TYR
SEQRES 32 D 582 GLY GLU GLU TRP ARG LEU LYS ILE ILE GLY ASP PRO CYS
SEQRES 33 D 582 GLY GLY GLU LEU GLU ASP VAL SER ALA ALA ALA ARG TRP
SEQRES 34 D 582 ALA ARG GLU SER GLY LEU ALA SER GLU LEU TYR ILE MET
SEQRES 35 D 582 GLY TYR SER TYR GLY GLY TYR MET THR LEU CYS ALA LEU
SEQRES 36 D 582 THR MET LYS PRO GLY LEU PHE LYS ALA GLY VAL ALA GLY
SEQRES 37 D 582 ALA SER VAL VAL ASP TRP GLU GLU MET TYR GLU LEU SER
SEQRES 38 D 582 ASP ALA ALA PHE ARG ASN PHE ILE GLU GLN LEU THR GLY
SEQRES 39 D 582 GLY SER ARG GLU ILE MET ARG SER ARG SER PRO ILE ASN
SEQRES 40 D 582 HIS VAL ASP ARG ILE LYS GLU PRO LEU ALA LEU ILE HIS
SEQRES 41 D 582 PRO GLN ASN ALA SER ARG THR PRO LEU LYS PRO LEU LEU
SEQRES 42 D 582 ARG LEU MET GLY GLU LEU LEU ALA ARG GLY LYS THR PHE
SEQRES 43 D 582 GLU ALA HIS ILE ILE PRO ASP ALA GLY HIS ALA ILE ASN
SEQRES 44 D 582 THR MET GLU ASP ALA VAL LYS ILE LEU LEU PRO ALA VAL
SEQRES 45 D 582 PHE PHE LEU ALA THR GLN ARG GLU ARG ARG
HET GOL A 583 12
HET GOL A 584 6
HET NA B 583 1
HET GOL B 584 6
HET NA D 583 1
HET GOL D 584 6
HET GOL D 585 6
HETNAM GOL GLYCEROL
HETNAM NA SODIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 5(C3 H8 O3)
FORMUL 7 NA 2(NA 1+)
FORMUL 12 HOH *928(H2 O)
HELIX 1 1 GLU A 8 VAL A 22 1 15
HELIX 2 2 LYS A 238 ARG A 244 1 7
HELIX 3 3 PRO A 323 SER A 329 1 7
HELIX 4 4 ASP A 379 ALA A 388 1 10
HELIX 5 5 GLY A 404 LYS A 410 1 7
HELIX 6 6 GLY A 417 SER A 433 1 17
HELIX 7 7 SER A 445 LYS A 458 1 14
HELIX 8 8 ASP A 473 LEU A 480 1 8
HELIX 9 9 ASP A 482 THR A 493 1 12
HELIX 10 10 SER A 496 ARG A 503 1 8
HELIX 11 11 SER A 504 ILE A 512 5 9
HELIX 12 12 PRO A 528 ARG A 542 1 15
HELIX 13 13 THR A 560 GLU A 580 1 21
HELIX 14 14 GLU B 8 VAL B 22 1 15
HELIX 15 15 LYS B 238 ARG B 244 1 7
HELIX 16 16 PRO B 323 SER B 329 1 7
HELIX 17 17 ASP B 379 ALA B 388 1 10
HELIX 18 18 GLY B 404 LYS B 410 1 7
HELIX 19 19 GLY B 417 SER B 433 1 17
HELIX 20 20 SER B 445 LYS B 458 1 14
HELIX 21 21 ASP B 473 SER B 481 1 9
HELIX 22 22 ASP B 482 THR B 493 1 12
HELIX 23 23 SER B 496 ARG B 503 1 8
HELIX 24 24 SER B 504 ILE B 512 5 9
HELIX 25 25 LEU B 529 ARG B 542 1 14
HELIX 26 26 THR B 560 LEU B 568 1 9
HELIX 27 27 LEU B 568 GLU B 580 1 13
HELIX 28 28 GLU C 8 VAL C 22 1 15
HELIX 29 29 LYS C 238 ARG C 244 1 7
HELIX 30 30 PRO C 323 SER C 329 1 7
HELIX 31 31 ASP C 379 ALA C 388 1 10
HELIX 32 32 GLY C 404 LYS C 410 1 7
HELIX 33 33 GLY C 417 SER C 433 1 17
HELIX 34 34 SER C 445 LYS C 458 1 14
HELIX 35 35 ASP C 473 SER C 481 1 9
HELIX 36 36 ASP C 482 GLY C 494 1 13
HELIX 37 37 SER C 496 ARG C 503 1 8
HELIX 38 38 SER C 504 ILE C 512 5 9
HELIX 39 39 LEU C 529 ARG C 542 1 14
HELIX 40 40 THR C 560 ARG C 581 1 22
HELIX 41 41 GLU D 8 VAL D 22 1 15
HELIX 42 42 LYS D 238 ARG D 244 1 7
HELIX 43 43 PRO D 323 SER D 329 1 7
HELIX 44 44 PHE D 341 GLY D 343 5 3
HELIX 45 45 ASP D 379 ALA D 388 1 10
HELIX 46 46 GLY D 404 LYS D 410 1 7
HELIX 47 47 GLY D 417 SER D 433 1 17
HELIX 48 48 SER D 445 LYS D 458 1 14
HELIX 49 49 ASP D 473 SER D 481 1 9
HELIX 50 50 ASP D 482 THR D 493 1 12
HELIX 51 51 SER D 496 ARG D 503 1 8
HELIX 52 52 SER D 504 ILE D 512 5 9
HELIX 53 53 PRO D 528 ARG D 542 1 15
HELIX 54 54 THR D 560 LEU D 568 1 9
HELIX 55 55 LEU D 568 ARG D 581 1 14
SHEET 1 A 4 LYS A 24 VAL A 31 0
SHEET 2 A 4 LYS A 35 SER A 42 -1 O PHE A 41 N LYS A 24
SHEET 3 A 4 SER A 45 ASP A 52 -1 O TYR A 49 N VAL A 38
SHEET 4 A 4 GLU A 55 LYS A 58 -1 O VAL A 57 N LEU A 50
SHEET 1 B 4 SER A 66 VAL A 67 0
SHEET 2 B 4 ARG A 76 ASP A 82 -1 O VAL A 80 N SER A 66
SHEET 3 B 4 HIS A 90 ASN A 96 -1 O PHE A 93 N LEU A 79
SHEET 4 B 4 GLN A 104 ARG A 105 -1 O GLN A 104 N LYS A 94
SHEET 1 C 5 ASP A 69 PRO A 70 0
SHEET 2 C 5 ARG A 113 ASP A 119 1 O ASP A 119 N ASP A 69
SHEET 3 C 5 VAL A 124 ALA A 129 -1 O VAL A 125 N VAL A 118
SHEET 4 C 5 VAL A 134 ASP A 140 -1 O TYR A 137 N PHE A 126
SHEET 5 C 5 GLY A 143 LEU A 150 -1 O ARG A 145 N ALA A 138
SHEET 1 D 4 GLY A 154 ARG A 160 0
SHEET 2 D 4 LEU A 163 GLY A 171 -1 O ALA A 165 N ASP A 158
SHEET 3 D 4 ARG A 174 ASN A 181 -1 O SER A 176 N GLY A 168
SHEET 4 D 4 ARG A 188 PHE A 190 -1 O PHE A 190 N LEU A 177
SHEET 1 E 4 SER A 196 ILE A 202 0
SHEET 2 E 4 VAL A 208 GLU A 213 -1 O GLU A 213 N SER A 196
SHEET 3 E 4 ALA A 218 VAL A 223 -1 O VAL A 223 N VAL A 208
SHEET 4 E 4 VAL A 230 ASP A 232 -1 O GLU A 231 N THR A 222
SHEET 1 F 4 ALA A 247 TYR A 253 0
SHEET 2 F 4 LEU A 259 ARG A 265 -1 O VAL A 262 N TRP A 250
SHEET 3 F 4 ARG A 268 ILE A 273 -1 O PHE A 272 N VAL A 261
SHEET 4 F 4 GLU A 276 VAL A 278 -1 O VAL A 278 N VAL A 271
SHEET 1 G 4 ASN A 284 TRP A 291 0
SHEET 2 G 4 LYS A 294 SER A 301 -1 O LYS A 294 N TRP A 291
SHEET 3 G 4 THR A 304 LEU A 311 -1 O VAL A 309 N THR A 297
SHEET 4 G 4 PRO A 316 LEU A 318 -1 O LEU A 318 N ILE A 308
SHEET 1 H16 ILE A 330 GLU A 339 0
SHEET 2 H16 ARG A 345 SER A 353 -1 O VAL A 346 N VAL A 338
SHEET 3 H16 HIS A 391 PRO A 395 -1 O MET A 394 N TYR A 349
SHEET 4 H16 GLY A 360 VAL A 366 1 N VAL A 363 O HIS A 391
SHEET 5 H16 ALA A 436 TYR A 444 1 O TYR A 440 N VAL A 364
SHEET 6 H16 GLY A 465 GLY A 468 1 O GLY A 468 N GLY A 443
SHEET 7 H16 LEU A 516 PRO A 521 1 O ALA A 517 N ALA A 467
SHEET 8 H16 PHE A 546 ILE A 551 1 O GLU A 547 N LEU A 518
SHEET 9 H16 PHE B 546 ILE B 551 -1 O ILE B 550 N ALA A 548
SHEET 10 H16 LEU B 516 PRO B 521 1 N HIS B 520 O HIS B 549
SHEET 11 H16 ALA B 464 GLY B 468 1 N ALA B 467 O ALA B 517
SHEET 12 H16 ALA B 436 TYR B 444 1 N GLY B 443 O GLY B 468
SHEET 13 H16 GLY B 360 VAL B 366 1 N VAL B 364 O TYR B 440
SHEET 14 H16 HIS B 391 PRO B 395 1 O HIS B 391 N VAL B 363
SHEET 15 H16 ARG B 345 SER B 353 -1 N TYR B 349 O MET B 394
SHEET 16 H16 ILE B 330 GLU B 339 -1 N VAL B 338 O VAL B 346
SHEET 1 I 4 LYS B 24 VAL B 31 0
SHEET 2 I 4 LYS B 35 PHE B 41 -1 O LEU B 37 N GLN B 28
SHEET 3 I 4 VAL B 46 TYR B 51 -1 O TYR B 49 N VAL B 38
SHEET 4 I 4 THR B 56 LYS B 58 -1 O VAL B 57 N LEU B 50
SHEET 1 J 4 SER B 66 VAL B 67 0
SHEET 2 J 4 ARG B 76 ASP B 82 -1 O VAL B 80 N SER B 66
SHEET 3 J 4 HIS B 90 ASN B 96 -1 O PHE B 93 N LEU B 79
SHEET 4 J 4 GLU B 103 ARG B 105 -1 O GLN B 104 N LYS B 94
SHEET 1 K 5 ASP B 69 PRO B 70 0
SHEET 2 K 5 ARG B 113 ASP B 119 1 O ASP B 119 N ASP B 69
SHEET 3 K 5 VAL B 124 ALA B 129 -1 O VAL B 125 N VAL B 118
SHEET 4 K 5 VAL B 134 ASP B 140 -1 O TYR B 137 N PHE B 126
SHEET 5 K 5 GLY B 143 LEU B 150 -1 O LEU B 150 N VAL B 134
SHEET 1 L 4 GLY B 154 ARG B 160 0
SHEET 2 L 4 LEU B 163 GLY B 168 -1 O ALA B 165 N ASP B 158
SHEET 3 L 4 SER B 176 ASN B 181 -1 O SER B 176 N GLY B 168
SHEET 4 L 4 ARG B 188 PHE B 190 -1 O PHE B 190 N LEU B 177
SHEET 1 M 4 SER B 196 ILE B 202 0
SHEET 2 M 4 VAL B 208 GLU B 213 -1 O GLU B 213 N SER B 196
SHEET 3 M 4 ARG B 219 VAL B 223 -1 O ARG B 219 N LEU B 212
SHEET 4 M 4 VAL B 230 ASP B 232 -1 O GLU B 231 N THR B 222
SHEET 1 N 4 ALA B 247 TYR B 253 0
SHEET 2 N 4 LEU B 259 ARG B 265 -1 O ARG B 264 N ALA B 247
SHEET 3 N 4 ARG B 268 ILE B 273 -1 O PHE B 272 N VAL B 261
SHEET 4 N 4 GLU B 276 VAL B 278 -1 O VAL B 278 N VAL B 271
SHEET 1 O 4 ASN B 284 TRP B 291 0
SHEET 2 O 4 LYS B 294 SER B 301 -1 O LYS B 294 N TRP B 291
SHEET 3 O 4 THR B 304 LEU B 311 -1 O LEU B 311 N LEU B 295
SHEET 4 O 4 PRO B 316 LEU B 318 -1 O LEU B 317 N ILE B 308
SHEET 1 P 4 LYS C 24 VAL C 31 0
SHEET 2 P 4 LYS C 35 SER C 42 -1 O VAL C 39 N SER C 26
SHEET 3 P 4 SER C 45 ASP C 52 -1 O TYR C 49 N VAL C 38
SHEET 4 P 4 GLU C 55 LYS C 58 -1 O GLU C 55 N ASP C 52
SHEET 1 Q 4 SER C 66 VAL C 67 0
SHEET 2 Q 4 ARG C 76 ASP C 82 -1 O VAL C 80 N SER C 66
SHEET 3 Q 4 HIS C 90 ASN C 96 -1 O PHE C 93 N LEU C 79
SHEET 4 Q 4 GLN C 104 ARG C 105 -1 O GLN C 104 N LYS C 94
SHEET 1 R 5 ASP C 69 PRO C 70 0
SHEET 2 R 5 ARG C 113 ASP C 119 1 O ASP C 119 N ASP C 69
SHEET 3 R 5 VAL C 124 ALA C 129 -1 O VAL C 125 N VAL C 118
SHEET 4 R 5 VAL C 134 ASP C 140 -1 O TYR C 137 N PHE C 126
SHEET 5 R 5 GLY C 143 LEU C 150 -1 O ARG C 145 N ALA C 138
SHEET 1 S 4 GLY C 154 ARG C 160 0
SHEET 2 S 4 LEU C 163 GLY C 171 -1 O ALA C 165 N ASP C 158
SHEET 3 S 4 ARG C 174 ASN C 181 -1 O SER C 176 N GLY C 168
SHEET 4 S 4 ARG C 188 PHE C 190 -1 O PHE C 190 N LEU C 177
SHEET 1 T 4 GLY C 195 ILE C 202 0
SHEET 2 T 4 VAL C 208 THR C 214 -1 O GLU C 213 N SER C 196
SHEET 3 T 4 ALA C 218 VAL C 223 -1 O VAL C 223 N VAL C 208
SHEET 4 T 4 VAL C 230 ASP C 232 -1 O GLU C 231 N THR C 222
SHEET 1 U 4 ALA C 247 TYR C 253 0
SHEET 2 U 4 LEU C 259 ARG C 265 -1 O VAL C 262 N TRP C 250
SHEET 3 U 4 ARG C 268 ILE C 273 -1 O PHE C 272 N VAL C 261
SHEET 4 U 4 GLU C 276 VAL C 278 -1 O VAL C 278 N VAL C 271
SHEET 1 V 4 ASN C 284 TRP C 291 0
SHEET 2 V 4 LYS C 294 SER C 301 -1 O LYS C 294 N TRP C 291
SHEET 3 V 4 THR C 304 LEU C 311 -1 O LEU C 311 N LEU C 295
SHEET 4 V 4 PRO C 316 LEU C 318 -1 O LEU C 318 N ILE C 308
SHEET 1 W16 ILE C 330 GLU C 339 0
SHEET 2 W16 ARG C 345 SER C 353 -1 O THR C 348 N VAL C 336
SHEET 3 W16 HIS C 391 PRO C 395 -1 O VAL C 392 N LEU C 351
SHEET 4 W16 GLY C 360 VAL C 366 1 N VAL C 363 O HIS C 391
SHEET 5 W16 ALA C 436 TYR C 444 1 O TYR C 440 N VAL C 364
SHEET 6 W16 GLY C 465 GLY C 468 1 O GLY C 468 N GLY C 443
SHEET 7 W16 LEU C 516 PRO C 521 1 O ALA C 517 N ALA C 467
SHEET 8 W16 PHE C 546 ILE C 551 1 O HIS C 549 N HIS C 520
SHEET 9 W16 PHE D 546 ILE D 551 -1 O ILE D 550 N ALA C 548
SHEET 10 W16 LEU D 516 PRO D 521 1 N HIS D 520 O HIS D 549
SHEET 11 W16 ALA D 464 GLY D 468 1 N ALA D 467 O ALA D 517
SHEET 12 W16 ALA D 436 TYR D 444 1 N GLY D 443 O GLY D 468
SHEET 13 W16 GLY D 360 VAL D 366 1 N VAL D 364 O TYR D 440
SHEET 14 W16 HIS D 391 PRO D 395 1 O HIS D 391 N VAL D 363
SHEET 15 W16 ARG D 345 SER D 353 -1 N TYR D 349 O MET D 394
SHEET 16 W16 ILE D 330 GLU D 339 -1 N VAL D 336 O THR D 348
SHEET 1 X 4 LYS D 24 VAL D 31 0
SHEET 2 X 4 LYS D 35 PHE D 41 -1 O LEU D 37 N GLN D 28
SHEET 3 X 4 VAL D 46 ASP D 52 -1 O TYR D 49 N VAL D 38
SHEET 4 X 4 GLU D 55 LYS D 58 -1 O VAL D 57 N LEU D 50
SHEET 1 Y 4 SER D 66 VAL D 67 0
SHEET 2 Y 4 ARG D 76 ASP D 82 -1 O VAL D 80 N SER D 66
SHEET 3 Y 4 HIS D 90 ASN D 96 -1 O PHE D 93 N LEU D 79
SHEET 4 Y 4 GLU D 103 ARG D 105 -1 O GLN D 104 N LYS D 94
SHEET 1 Z 5 ASP D 69 PRO D 70 0
SHEET 2 Z 5 ARG D 113 ASP D 119 1 O ASP D 119 N ASP D 69
SHEET 3 Z 5 VAL D 124 ALA D 129 -1 O VAL D 125 N VAL D 118
SHEET 4 Z 5 VAL D 134 ASP D 140 -1 O TYR D 137 N PHE D 126
SHEET 5 Z 5 GLY D 143 LEU D 150 -1 O ALA D 148 N LEU D 136
SHEET 1 AA 4 GLY D 154 ARG D 160 0
SHEET 2 AA 4 LEU D 163 GLY D 168 -1 O ALA D 165 N ASP D 158
SHEET 3 AA 4 SER D 176 ASN D 181 -1 O SER D 176 N GLY D 168
SHEET 4 AA 4 ARG D 188 PHE D 190 -1 O PHE D 190 N LEU D 177
SHEET 1 AB 4 SER D 196 ILE D 202 0
SHEET 2 AB 4 VAL D 208 GLU D 213 -1 O THR D 209 N SER D 201
SHEET 3 AB 4 ARG D 219 VAL D 223 -1 O ARG D 219 N LEU D 212
SHEET 4 AB 4 VAL D 230 ASP D 232 -1 O GLU D 231 N THR D 222
SHEET 1 AC 4 ALA D 247 TYR D 253 0
SHEET 2 AC 4 LEU D 259 ARG D 265 -1 O ALA D 260 N GLY D 252
SHEET 3 AC 4 ARG D 268 ILE D 273 -1 O PHE D 272 N VAL D 261
SHEET 4 AC 4 GLU D 276 VAL D 278 -1 O VAL D 278 N VAL D 271
SHEET 1 AD 4 ASN D 284 TRP D 291 0
SHEET 2 AD 4 LYS D 294 SER D 301 -1 O LYS D 294 N TRP D 291
SHEET 3 AD 4 THR D 304 LEU D 311 -1 O LEU D 311 N LEU D 295
SHEET 4 AD 4 PRO D 316 LEU D 318 -1 O LEU D 317 N ILE D 308
LINK NA NA D 583 O HOH D 667 1555 1555 2.21
LINK NA NA B 583 O HOH B 690 1555 1555 2.28
LINK NA NA D 583 O HOH D 691 1555 1555 2.33
LINK NA NA B 583 O HOH B 907 1555 1555 2.36
LINK NA NA B 583 O HOH B 655 1555 1555 2.41
LINK NA NA D 583 O HOH D 587 1555 1555 2.53
LINK OD1 ASP B 374 NA NA B 583 1555 1555 2.53
LINK NA NA B 583 O HOH B 687 1555 1555 2.58
LINK OD1 ASP D 374 NA NA D 583 1555 1555 2.60
LINK NA NA D 583 O HOH D 604 1555 1555 2.70
LINK NA NA D 583 O HOH D 608 1555 1555 2.74
LINK NA NA B 583 O HOH B 717 1555 1555 2.76
CISPEP 1 LEU A 311 PRO A 312 0 4.45
CISPEP 2 THR A 358 PRO A 359 0 -0.42
CISPEP 3 GLY A 369 PRO A 370 0 12.22
CISPEP 4 LEU B 311 PRO B 312 0 5.11
CISPEP 5 THR B 358 PRO B 359 0 4.47
CISPEP 6 GLY B 369 PRO B 370 0 9.30
CISPEP 7 LEU C 311 PRO C 312 0 6.03
CISPEP 8 THR C 358 PRO C 359 0 -2.12
CISPEP 9 GLY C 369 PRO C 370 0 13.65
CISPEP 10 LEU D 311 PRO D 312 0 6.29
CISPEP 11 THR D 358 PRO D 359 0 2.79
CISPEP 12 GLY D 369 PRO D 370 0 9.83
SITE 1 AC1 6 GLY A 369 SER A 445 MET A 477 PHE A 488
SITE 2 AC1 6 ARG A 526 THR A 527
SITE 1 AC2 2 ARG A 345 TYR A 403
SITE 1 AC3 6 ASP B 374 HOH B 655 HOH B 687 HOH B 690
SITE 2 AC3 6 HOH B 717 HOH B 907
SITE 1 AC4 3 SER B 445 VAL B 471 PHE B 488
SITE 1 AC5 6 ASP D 374 HOH D 587 HOH D 604 HOH D 608
SITE 2 AC5 6 HOH D 667 HOH D 691
SITE 1 AC6 4 TYR D 444 ALA D 469 GLY D 555 HOH D 711
SITE 1 AC7 5 SER D 445 VAL D 471 PHE D 488 HOH D 713
SITE 2 AC7 5 HOH D 714
CRYST1 71.405 97.979 98.797 105.69 103.52 100.36 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 0.014005 0.002560 0.004447 0.00000
SCALE2 0.000000 0.010375 0.003586 0.00000
SCALE3 0.000000 0.000000 0.011014 0.00000
TER 4351 ARG A 581
TER 8607 GLU B 580
TER 12917 ARG C 581
TER 17205 ARG D 581
MASTER 914 0 7 55 148 0 11 618078 4 52 180
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