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HEADER HYDROLASE 27-JUL-10 3O4J
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 3O4J 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. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 141856
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7519
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10589
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.3450
REMARK 3 BIN FREE R VALUE SET COUNT : 519
REMARK 3 BIN FREE R VALUE : 0.4120
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17452
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 535
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : 0.11000
REMARK 3 B33 (A**2) : -0.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.02000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.217
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.170
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.687
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17965 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 12417 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 24378 ; 1.748 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 30039 ; 1.120 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2330 ; 6.245 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 760 ;34.229 ;22.487
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2874 ;15.887 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 174 ;19.254 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2705 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 20338 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3816 ; 0.004 ; 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): 11445 ; 0.642 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4770 ; 0.354 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 18333 ; 1.065 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6520 ; 1.855 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6033 ; 2.818 ; 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 : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 6 A 21 3
REMARK 3 1 C 6 C 21 3
REMARK 3 2 A 322 A 580 3
REMARK 3 2 C 322 C 580 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1606 ; 0.040 ; 0.050
REMARK 3 LOOSE POSITIONAL 1 A (A): 1965 ; 0.100 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 1606 ; 0.160 ; 0.500
REMARK 3 LOOSE THERMAL 1 A (A**2): 1965 ; 0.160 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 3
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 6 B 21 3
REMARK 3 1 D 6 D 21 3
REMARK 3 2 B 322 B 340 3
REMARK 3 2 D 322 D 340 3
REMARK 3 3 B 342 B 580 3
REMARK 3 3 D 342 D 580 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 1581 ; 0.050 ; 0.050
REMARK 3 LOOSE POSITIONAL 2 B (A): 1878 ; 0.130 ; 5.000
REMARK 3 TIGHT THERMAL 2 B (A**2): 1581 ; 0.160 ; 0.500
REMARK 3 LOOSE THERMAL 2 B (A**2): 1878 ; 0.160 ;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 25 A 187 3
REMARK 3 1 C 25 C 187 3
REMARK 3 2 A 189 A 317 4
REMARK 3 2 C 189 C 317 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 939 ; 0.080 ; 0.050
REMARK 3 MEDIUM POSITIONAL 3 A (A): 1667 ; 0.120 ; 0.500
REMARK 3 LOOSE POSITIONAL 3 A (A): 1062 ; 0.220 ; 5.000
REMARK 3 TIGHT THERMAL 3 A (A**2): 939 ; 0.670 ; 0.500
REMARK 3 MEDIUM THERMAL 3 A (A**2): 1667 ; 0.800 ; 2.000
REMARK 3 LOOSE THERMAL 3 A (A**2): 1062 ; 0.960 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 25 B 317 3
REMARK 3 1 D 25 D 317 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 B (A): 1700 ; 0.040 ; 0.050
REMARK 3 LOOSE POSITIONAL 4 B (A): 1984 ; 0.080 ; 5.000
REMARK 3 TIGHT THERMAL 4 B (A**2): 1700 ; 0.160 ; 0.500
REMARK 3 LOOSE THERMAL 4 B (A**2): 1984 ; 0.150 ;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 4 A 23
REMARK 3 RESIDUE RANGE : A 319 A 581
REMARK 3 ORIGIN FOR THE GROUP (A): -38.7161 -12.1574 -39.1660
REMARK 3 T TENSOR
REMARK 3 T11: 0.2268 T22: 0.2845
REMARK 3 T33: 0.1339 T12: -0.2145
REMARK 3 T13: -0.0306 T23: -0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 1.4875 L22: 1.8152
REMARK 3 L33: 2.0207 L12: 0.3444
REMARK 3 L13: -0.6158 L23: -0.1209
REMARK 3 S TENSOR
REMARK 3 S11: -0.1320 S12: 0.1256 S13: 0.0044
REMARK 3 S21: -0.3521 S22: 0.1681 S23: 0.1767
REMARK 3 S31: 0.0804 S32: -0.3727 S33: -0.0361
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 6 B 23
REMARK 3 RESIDUE RANGE : B 319 B 581
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9995 11.4554 -21.6441
REMARK 3 T TENSOR
REMARK 3 T11: 0.0326 T22: 0.1068
REMARK 3 T33: 0.1005 T12: -0.0191
REMARK 3 T13: -0.0169 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 1.6748 L22: 2.1468
REMARK 3 L33: 2.6850 L12: 0.9444
REMARK 3 L13: -0.6865 L23: 0.6791
REMARK 3 S TENSOR
REMARK 3 S11: -0.1758 S12: 0.1998 S13: 0.0472
REMARK 3 S21: -0.2323 S22: 0.1961 S23: 0.0316
REMARK 3 S31: 0.0220 S32: -0.0717 S33: -0.0203
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 4 C 23
REMARK 3 RESIDUE RANGE : C 319 C 582
REMARK 3 ORIGIN FOR THE GROUP (A): 33.8684 0.4366 -37.2396
REMARK 3 T TENSOR
REMARK 3 T11: 0.1157 T22: 0.1457
REMARK 3 T33: 0.0775 T12: 0.0830
REMARK 3 T13: 0.0115 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 1.4050 L22: 1.7691
REMARK 3 L33: 1.1558 L12: -0.1534
REMARK 3 L13: -0.0750 L23: -0.1530
REMARK 3 S TENSOR
REMARK 3 S11: 0.0751 S12: 0.0482 S13: -0.0637
REMARK 3 S21: -0.2044 S22: -0.0610 S23: -0.0574
REMARK 3 S31: 0.2717 S32: 0.1542 S33: -0.0141
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 6 D 23
REMARK 3 RESIDUE RANGE : D 319 D 581
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0992 -22.5570 -17.1486
REMARK 3 T TENSOR
REMARK 3 T11: 0.1151 T22: 0.1799
REMARK 3 T33: 0.2842 T12: 0.0930
REMARK 3 T13: 0.0118 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 1.5289 L22: 3.0698
REMARK 3 L33: 2.7182 L12: 0.5073
REMARK 3 L13: 0.8146 L23: -1.1158
REMARK 3 S TENSOR
REMARK 3 S11: -0.1191 S12: 0.0415 S13: -0.2188
REMARK 3 S21: -0.2851 S22: 0.2159 S23: 0.3703
REMARK 3 S31: 0.0191 S32: -0.1221 S33: -0.0968
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): -23.5215 -35.5086 -38.2769
REMARK 3 T TENSOR
REMARK 3 T11: 0.4546 T22: 0.2243
REMARK 3 T33: 0.2621 T12: -0.1362
REMARK 3 T13: 0.1464 T23: -0.1266
REMARK 3 L TENSOR
REMARK 3 L11: 1.3218 L22: 1.9723
REMARK 3 L33: 2.2087 L12: 0.5079
REMARK 3 L13: -0.6168 L23: -0.2233
REMARK 3 S TENSOR
REMARK 3 S11: -0.2507 S12: 0.1211 S13: -0.2325
REMARK 3 S21: -0.5058 S22: 0.1453 S23: -0.3095
REMARK 3 S31: 0.6878 S32: 0.1316 S33: 0.1054
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): -40.7160 31.3309 -5.5020
REMARK 3 T TENSOR
REMARK 3 T11: 0.0655 T22: 0.1223
REMARK 3 T33: 0.1407 T12: 0.0569
REMARK 3 T13: -0.0483 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 1.7000 L22: 2.6938
REMARK 3 L33: 1.4631 L12: -0.5429
REMARK 3 L13: 0.4474 L23: -0.1785
REMARK 3 S TENSOR
REMARK 3 S11: 0.0508 S12: 0.0776 S13: 0.0004
REMARK 3 S21: -0.3148 S22: -0.0276 S23: 0.3380
REMARK 3 S31: -0.1494 S32: -0.2214 S33: -0.0232
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): 19.3873 24.2480 -34.3941
REMARK 3 T TENSOR
REMARK 3 T11: 0.0277 T22: 0.0866
REMARK 3 T33: 0.0830 T12: 0.0146
REMARK 3 T13: -0.0109 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 1.4061 L22: 1.1378
REMARK 3 L33: 1.6703 L12: 0.1335
REMARK 3 L13: 0.3455 L23: -0.2657
REMARK 3 S TENSOR
REMARK 3 S11: -0.0141 S12: 0.0444 S13: 0.1014
REMARK 3 S21: -0.1434 S22: -0.0221 S23: 0.0291
REMARK 3 S31: -0.0774 S32: -0.0335 S33: 0.0363
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): 39.2274 -42.9765 -4.5539
REMARK 3 T TENSOR
REMARK 3 T11: 0.1676 T22: 0.1294
REMARK 3 T33: 0.1803 T12: 0.1143
REMARK 3 T13: -0.0195 T23: 0.0705
REMARK 3 L TENSOR
REMARK 3 L11: 1.7032 L22: 2.9293
REMARK 3 L33: 1.7656 L12: -0.7392
REMARK 3 L13: -0.5782 L23: 0.4437
REMARK 3 S TENSOR
REMARK 3 S11: 0.1303 S12: 0.1050 S13: -0.0039
REMARK 3 S21: -0.0971 S22: 0.0145 S23: -0.0790
REMARK 3 S31: 0.0537 S32: 0.0631 S33: -0.1447
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 3O4J 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 RCSB060655.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
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 : 149375
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
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 (%) : 96.8
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.4300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.64200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.480
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 (%): 72.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 170MM SODIUM ACETATE, 0.4MM EDTA, 10%
REMARK 280 DIMETHYL SULPHOXIDE, 2.5% PEG 4000 , PH 5.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 92.13500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 113.76200
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 92.13500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 113.76200
REMARK 290 SMTRY3 4 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: 2950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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: 3590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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 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 GLY B 555
REMARK 465 HIS B 556
REMARK 465 ARG B 582
REMARK 465 MET C 1
REMARK 465 ARG C 2
REMARK 465 ILE C 3
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 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 ILE A 4 CG1 CG2 CD1
REMARK 470 MET A 5 SD CE
REMARK 470 ARG A 11 CD NE CZ NH1 NH2
REMARK 470 GLU A 43 CD OE1 OE2
REMARK 470 LYS A 94 CE NZ
REMARK 470 LYS A 207 NZ
REMARK 470 ARG A 428 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 85 CG CD CE NZ
REMARK 470 GLU B 88 CD OE1 OE2
REMARK 470 GLU B 131 CG CD OE1 OE2
REMARK 470 ILE B 159 CD1
REMARK 470 ARG B 174 CD NE CZ NH1 NH2
REMARK 470 LYS B 207 NZ
REMARK 470 ARG B 428 NE CZ NH1 NH2
REMARK 470 GLU B 498 CD OE1 OE2
REMARK 470 GLU B 562 CD OE1 OE2
REMARK 470 GLU B 580 CD OE1 OE2
REMARK 470 ILE C 4 CG1 CG2 CD1
REMARK 470 ARG C 11 CZ NH1 NH2
REMARK 470 LYS C 110 CD CE NZ
REMARK 470 ARG C 216 CZ NH1 NH2
REMARK 470 ARG C 428 CG CD NE CZ NH1 NH2
REMARK 470 ILE C 558 CD1
REMARK 470 ARG C 582 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS D 85 CG CD CE NZ
REMARK 470 GLU D 131 CG CD OE1 OE2
REMARK 470 ARG D 174 CZ NH1 NH2
REMARK 470 LYS D 207 NZ
REMARK 470 ARG D 216 CZ NH1 NH2
REMARK 470 ARG D 428 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 479 CG CD OE1 OE2
REMARK 470 LEU D 480 CG CD1 CD2
REMARK 470 ARG D 486 NE CZ NH1 NH2
REMARK 470 ARG D 497 CZ NH1 NH2
REMARK 470 ASP D 510 CG OD1 OD2
REMARK 470 ARG D 526 CG CD NE CZ NH1 NH2
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 OE1 GLU C 43 O HOH C 756 1.97
REMARK 500 OE1 GLU C 498 NH2 ARG C 501 2.09
REMARK 500 O HIS D 556 CG2 ILE D 558 2.14
REMARK 500 OD2 ASP B 482 NH1 ARG B 526 2.19
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 GLU A 373 CD GLU A 373 OE1 -0.071
REMARK 500 ASP A 510 CB ASP A 510 CG -0.173
REMARK 500 ASP B 82 CB ASP B 82 CG 0.127
REMARK 500 ARG B 428 CB ARG B 428 CG 0.213
REMARK 500 GLU B 432 CG GLU B 432 CD 0.119
REMARK 500 TYR B 444 CG TYR B 444 CD2 -0.146
REMARK 500 TYR B 444 CG TYR B 444 CD1 -0.155
REMARK 500 TYR B 444 CE1 TYR B 444 CZ -0.170
REMARK 500 TYR B 444 CZ TYR B 444 CE2 -0.172
REMARK 500 GLU B 514 CD GLU B 514 OE1 0.075
REMARK 500 VAL C 13 CB VAL C 13 CG1 -0.140
REMARK 500 GLU C 373 CD GLU C 373 OE2 -0.070
REMARK 500 GLU C 432 CG GLU C 432 CD 0.102
REMARK 500 GLU C 498 CG GLU C 498 CD 0.121
REMARK 500 ASP C 510 CB ASP C 510 CG -0.143
REMARK 500 GLU D 234 CG GLU D 234 CD 0.123
REMARK 500 TYR D 444 CG TYR D 444 CD2 -0.174
REMARK 500 TYR D 444 CG TYR D 444 CD1 -0.159
REMARK 500 TYR D 444 CE1 TYR D 444 CZ -0.214
REMARK 500 TYR D 444 CZ TYR D 444 CE2 -0.153
REMARK 500 GLU D 580 CG GLU D 580 CD 0.097
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 A 133 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 GLU A 373 OE1 - CD - OE2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ASP A 510 CB - CG - OD1 ANGL. DEV. = -7.4 DEGREES
REMARK 500 GLU A 580 OE1 - CD - OE2 ANGL. DEV. = -8.2 DEGREES
REMARK 500 PHE B 41 CB - CG - CD2 ANGL. DEV. = 7.5 DEGREES
REMARK 500 PHE B 41 CB - CG - CD1 ANGL. DEV. = -8.8 DEGREES
REMARK 500 ASP B 82 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG B 265 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ASP B 325 CB - CG - OD1 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ARG C 268 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 GLU C 373 OE1 - CD - OE2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 ASP C 510 CB - CG - OD1 ANGL. DEV. = -10.9 DEGREES
REMARK 500 GLU C 580 OE1 - CD - OE2 ANGL. DEV. = -8.7 DEGREES
REMARK 500 GLU D 8 CG - CD - OE1 ANGL. DEV. = 13.4 DEGREES
REMARK 500 PHE D 41 CB - CG - CD1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ASP D 69 CB - CG - OD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 ASP D 191 CB - CG - OD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP D 325 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 ASP D 325 CB - CG - OD1 ANGL. DEV. = -8.5 DEGREES
REMARK 500 ASP D 325 CB - CG - OD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 TYR D 444 CB - CG - CD2 ANGL. DEV. = 3.6 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 GLU A 8 72.55 -100.28
REMARK 500 ASP A 32 -144.09 56.53
REMARK 500 ARG A 61 -80.01 -104.18
REMARK 500 ARG A 133 161.64 177.33
REMARK 500 ALA A 148 149.07 -177.00
REMARK 500 MET A 206 33.53 71.17
REMARK 500 ASP A 414 47.22 -141.53
REMARK 500 SER A 445 -130.22 64.97
REMARK 500 ASP B 32 -149.00 61.69
REMARK 500 ARG B 61 -81.66 -101.08
REMARK 500 SER B 66 170.43 179.35
REMARK 500 ALA B 87 157.94 -41.60
REMARK 500 THR B 214 -169.12 -126.11
REMARK 500 ARG B 216 -88.08 -138.62
REMARK 500 ALA B 331 -158.78 -85.94
REMARK 500 ASP B 414 50.20 -145.34
REMARK 500 SER B 445 -129.22 54.57
REMARK 500 ASN B 523 26.52 -150.62
REMARK 500 SER B 525 3.96 -68.15
REMARK 500 ASP C 32 -139.98 56.05
REMARK 500 ASP C 52 141.49 -173.47
REMARK 500 ARG C 61 -82.70 -96.25
REMARK 500 SER C 116 168.80 178.00
REMARK 500 ASP C 227 -12.71 -140.32
REMARK 500 SER C 445 -124.07 61.86
REMARK 500 ASP D 32 -146.26 65.17
REMARK 500 ARG D 61 -83.04 -102.12
REMARK 500 ALA D 87 157.25 -43.02
REMARK 500 THR D 214 -167.18 -129.22
REMARK 500 ARG D 216 -88.24 -141.34
REMARK 500 ALA D 331 -159.33 -84.74
REMARK 500 ASP D 414 50.95 -144.67
REMARK 500 SER D 445 -122.26 54.44
REMARK 500 HIS D 508 31.40 -141.85
REMARK 500 ASN D 523 24.69 -147.69
REMARK 500 ALA D 557 115.70 -29.61
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 ILE C 567 23.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D 588 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH B 617 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH B 621 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH C 642 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH A 651 DISTANCE = 5.64 ANGSTROMS
REMARK 525 HOH A 655 DISTANCE = 5.37 ANGSTROMS
REMARK 525 HOH B 729 DISTANCE = 5.27 ANGSTROMS
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 B 586 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 184 OG
REMARK 620 2 GLY B 185 O 99.0
REMARK 620 3 ASN B 181 OD1 122.3 99.3
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 583
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 584
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 585
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 586
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 584
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 583
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 584
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O4G RELATED DB: PDB
REMARK 900 RELATED ID: 3O4H RELATED DB: PDB
REMARK 900 RELATED ID: 3O4I RELATED DB: PDB
DBREF 3O4J A 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 3O4J B 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 3O4J C 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 3O4J D 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
SEQADV 3O4J ASN A 524 UNP Q9YBQ2 ASP 524 ENGINEERED
SEQADV 3O4J ASN B 524 UNP Q9YBQ2 ASP 524 ENGINEERED
SEQADV 3O4J ASN C 524 UNP Q9YBQ2 ASP 524 ENGINEERED
SEQADV 3O4J ASN 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 ASN 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 ASN 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 ASN 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 ASN 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 B 583 6
HET CL B 584 1
HET CL B 585 1
HET NA B 586 1
HET GOL C 583 6
HET GOL C 584 6
HET GOL D 583 6
HET GOL D 584 6
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETNAM NA SODIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 5(C3 H8 O3)
FORMUL 6 CL 2(CL 1-)
FORMUL 8 NA NA 1+
FORMUL 13 HOH *535(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 GLY A 494 1 13
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 LEU A 529 ARG A 542 1 14
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 ARG B 581 1 14
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 LEU C 480 1 8
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 GLU C 580 1 21
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 ASP D 379 ALA D 388 1 10
HELIX 45 45 GLY D 404 LYS D 410 1 7
HELIX 46 46 GLY D 417 SER D 433 1 17
HELIX 47 47 SER D 445 LYS D 458 1 14
HELIX 48 48 ASP D 473 SER D 481 1 9
HELIX 49 49 ASP D 482 THR D 493 1 12
HELIX 50 50 SER D 496 ARG D 503 1 8
HELIX 51 51 SER D 504 ILE D 512 5 9
HELIX 52 52 LEU D 529 ARG D 542 1 14
HELIX 53 53 THR D 560 LEU D 568 1 9
HELIX 54 54 LEU D 568 ARG D 579 1 12
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 LEU A 167 N PHE A 155
SHEET 3 D 4 ARG A 174 ASN A 181 -1 O PHE A 178 N GLY A 166
SHEET 4 D 4 GLY A 185 PHE A 190 -1 O PHE A 190 N LEU A 177
SHEET 1 E 4 GLY A 195 ILE A 202 0
SHEET 2 E 4 VAL A 208 THR A 214 -1 O GLU A 213 N SER A 196
SHEET 3 E 4 ALA A 218 VAL A 223 -1 O ARG A 219 N LEU A 212
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 ARG A 268 N ARG A 265
SHEET 4 F 4 GLU A 276 VAL A 278 -1 O GLU A 276 N ILE A 273
SHEET 1 G 4 ASN A 284 TRP A 291 0
SHEET 2 G 4 LYS A 294 THR A 300 -1 O LYS A 294 N TRP A 291
SHEET 3 G 4 ARG A 307 LEU A 311 -1 O LEU A 311 N LEU A 295
SHEET 4 G 4 PRO A 316 LEU A 318 -1 O LEU A 317 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 GLY A 465
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 ALA B 548 N ILE A 550
SHEET 10 H16 LEU B 516 PRO B 521 1 N LEU B 518 O GLU B 547
SHEET 11 H16 GLY B 465 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 SER B 42 -1 O LEU B 37 N GLY B 29
SHEET 3 I 4 SER B 45 ASP B 52 -1 O TYR B 49 N VAL B 38
SHEET 4 I 4 GLU B 55 LYS B 58 -1 O GLU B 55 N ASP B 52
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 GLN B 104 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 ALA B 123 THR B 130 -1 O VAL B 125 N VAL B 118
SHEET 4 K 5 ARG B 133 ASP B 140 -1 O TYR B 137 N PHE B 126
SHEET 5 K 5 GLY B 143 LEU B 150 -1 O ARG B 145 N ALA B 138
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 SER B 157
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 3 SER B 196 PHE B 197 0
SHEET 2 M 3 VAL B 208 GLU B 213 -1 O GLU B 213 N SER B 196
SHEET 3 M 3 SER B 201 ILE B 202 -1 N SER B 201 O THR B 209
SHEET 1 N 4 SER B 196 PHE B 197 0
SHEET 2 N 4 VAL B 208 GLU B 213 -1 O GLU B 213 N SER B 196
SHEET 3 N 4 ARG B 219 VAL B 223 -1 O ARG B 219 N LEU B 212
SHEET 4 N 4 VAL B 230 ASP B 232 -1 O GLU B 231 N THR B 222
SHEET 1 O 4 ALA B 247 TYR B 253 0
SHEET 2 O 4 LEU B 259 ARG B 265 -1 O ALA B 260 N GLY B 252
SHEET 3 O 4 ARG B 268 ILE B 273 -1 O PHE B 272 N VAL B 261
SHEET 4 O 4 GLU B 276 VAL B 278 -1 O GLU B 276 N ILE B 273
SHEET 1 P 4 ASN B 284 TRP B 291 0
SHEET 2 P 4 LYS B 294 SER B 301 -1 O LYS B 294 N TRP B 291
SHEET 3 P 4 THR B 304 LEU B 311 -1 O VAL B 309 N THR B 297
SHEET 4 P 4 PRO B 316 LEU B 318 -1 O LEU B 318 N ILE B 308
SHEET 1 Q 4 LYS C 24 VAL C 31 0
SHEET 2 Q 4 LYS C 35 SER C 42 -1 O LYS C 35 N VAL C 31
SHEET 3 Q 4 SER C 45 ASP C 52 -1 O TYR C 49 N VAL C 38
SHEET 4 Q 4 GLU C 55 LYS C 58 -1 O GLU C 55 N ASP C 52
SHEET 1 R 4 SER C 66 VAL C 67 0
SHEET 2 R 4 ARG C 76 ASP C 82 -1 O VAL C 80 N SER C 66
SHEET 3 R 4 HIS C 90 ASN C 96 -1 O PHE C 93 N LEU C 79
SHEET 4 R 4 GLN C 104 ARG C 105 -1 O GLN C 104 N LYS C 94
SHEET 1 S 5 ASP C 69 PRO C 70 0
SHEET 2 S 5 ARG C 113 ASP C 119 1 O ASP C 119 N ASP C 69
SHEET 3 S 5 ALA C 123 ALA C 129 -1 O THR C 127 N LEU C 115
SHEET 4 S 5 VAL C 134 ASP C 140 -1 O LEU C 139 N VAL C 124
SHEET 5 S 5 GLY C 143 LEU C 150 -1 O ALA C 148 N LEU C 136
SHEET 1 T 4 GLY C 154 ARG C 160 0
SHEET 2 T 4 LEU C 163 GLY C 171 -1 O ALA C 165 N ASP C 158
SHEET 3 T 4 ARG C 174 ASN C 181 -1 O PHE C 178 N GLY C 166
SHEET 4 T 4 GLY C 185 PHE C 190 -1 O PHE C 190 N LEU C 177
SHEET 1 U 4 GLY C 195 ILE C 202 0
SHEET 2 U 4 VAL C 208 THR C 214 -1 O GLU C 213 N SER C 196
SHEET 3 U 4 ALA C 218 VAL C 223 -1 O ARG C 219 N LEU C 212
SHEET 4 U 4 VAL C 230 ASP C 232 -1 O GLU C 231 N THR C 222
SHEET 1 V 4 ALA C 247 TYR C 253 0
SHEET 2 V 4 LEU C 259 ARG C 265 -1 O VAL C 262 N TRP C 250
SHEET 3 V 4 ARG C 268 ILE C 273 -1 O ALA C 270 N ALA C 263
SHEET 4 V 4 GLU C 276 VAL C 278 -1 O GLU C 276 N ILE C 273
SHEET 1 W 4 ASN C 284 TRP C 291 0
SHEET 2 W 4 LYS C 294 SER C 301 -1 O LYS C 294 N TRP C 291
SHEET 3 W 4 THR C 304 LEU C 311 -1 O LEU C 311 N LEU C 295
SHEET 4 W 4 PRO C 316 LEU C 318 -1 O LEU C 317 N ILE C 308
SHEET 1 X16 ILE C 330 GLU C 339 0
SHEET 2 X16 ARG C 345 SER C 353 -1 O VAL C 346 N VAL C 338
SHEET 3 X16 HIS C 391 PRO C 395 -1 O MET C 394 N TYR C 349
SHEET 4 X16 GLY C 360 VAL C 366 1 N VAL C 363 O HIS C 391
SHEET 5 X16 ALA C 436 TYR C 444 1 O TYR C 440 N VAL C 364
SHEET 6 X16 GLY C 465 GLY C 468 1 O GLY C 468 N GLY C 443
SHEET 7 X16 LEU C 516 PRO C 521 1 O ALA C 517 N GLY C 465
SHEET 8 X16 PHE C 546 ILE C 551 1 O GLU C 547 N LEU C 518
SHEET 9 X16 PHE D 546 ILE D 551 -1 O ILE D 550 N ALA C 548
SHEET 10 X16 LEU D 516 PRO D 521 1 N HIS D 520 O HIS D 549
SHEET 11 X16 GLY D 465 GLY D 468 1 N ALA D 467 O ALA D 517
SHEET 12 X16 ALA D 436 TYR D 444 1 N GLY D 443 O GLY D 468
SHEET 13 X16 GLY D 360 VAL D 366 1 N GLY D 360 O SER D 437
SHEET 14 X16 HIS D 391 PRO D 395 1 O HIS D 391 N VAL D 363
SHEET 15 X16 ARG D 345 SER D 353 -1 N TYR D 349 O MET D 394
SHEET 16 X16 ILE D 330 GLU D 339 -1 N VAL D 338 O VAL D 346
SHEET 1 Y 4 LYS D 24 VAL D 31 0
SHEET 2 Y 4 LYS D 35 SER D 42 -1 O LEU D 37 N GLY D 29
SHEET 3 Y 4 SER D 45 ASP D 52 -1 O TYR D 49 N VAL D 38
SHEET 4 Y 4 GLU D 55 LYS D 58 -1 O VAL D 57 N LEU D 50
SHEET 1 Z 4 SER D 66 VAL D 67 0
SHEET 2 Z 4 ARG D 76 ASP D 82 -1 O VAL D 80 N SER D 66
SHEET 3 Z 4 HIS D 90 ASN D 96 -1 O PHE D 93 N LEU D 79
SHEET 4 Z 4 GLN D 104 ARG D 105 -1 O GLN D 104 N LYS D 94
SHEET 1 AA 5 ASP D 69 PRO D 70 0
SHEET 2 AA 5 ARG D 113 ASP D 119 1 O ASP D 119 N ASP D 69
SHEET 3 AA 5 ALA D 123 THR D 130 -1 O VAL D 125 N VAL D 118
SHEET 4 AA 5 ARG D 133 ASP D 140 -1 O TYR D 137 N PHE D 126
SHEET 5 AA 5 GLY D 143 LEU D 150 -1 O LEU D 147 N LEU D 136
SHEET 1 AB 4 GLY D 154 ARG D 160 0
SHEET 2 AB 4 LEU D 163 GLY D 168 -1 O LEU D 167 N PHE D 155
SHEET 3 AB 4 SER D 176 ASN D 181 -1 O SER D 176 N GLY D 168
SHEET 4 AB 4 ARG D 188 PHE D 190 -1 O PHE D 190 N LEU D 177
SHEET 1 AC 4 SER D 196 ILE D 202 0
SHEET 2 AC 4 VAL D 208 GLU D 213 -1 O GLU D 213 N SER D 196
SHEET 3 AC 4 ARG D 219 VAL D 223 -1 O ARG D 219 N LEU D 212
SHEET 4 AC 4 VAL D 230 ASP D 232 -1 O GLU D 231 N THR D 222
SHEET 1 AD 4 ALA D 247 TYR D 253 0
SHEET 2 AD 4 LEU D 259 ARG D 265 -1 O ARG D 264 N ALA D 247
SHEET 3 AD 4 ARG D 268 ILE D 273 -1 O PHE D 272 N VAL D 261
SHEET 4 AD 4 GLU D 276 VAL D 278 -1 O VAL D 278 N VAL D 271
SHEET 1 AE 4 ASN D 284 TRP D 291 0
SHEET 2 AE 4 LYS D 294 SER D 301 -1 O LYS D 294 N TRP D 291
SHEET 3 AE 4 THR D 304 LEU D 311 -1 O ARG D 307 N HIS D 299
SHEET 4 AE 4 PRO D 316 LEU D 318 -1 O LEU D 318 N ILE D 308
LINK OG SER B 184 NA NA B 586 1555 1555 2.07
LINK O GLY B 185 NA NA B 586 1555 1555 2.59
LINK OD1 ASN B 181 NA NA B 586 1555 1555 3.02
CISPEP 1 LEU A 311 PRO A 312 0 9.97
CISPEP 2 THR A 358 PRO A 359 0 -3.51
CISPEP 3 GLY A 369 PRO A 370 0 16.44
CISPEP 4 LEU B 311 PRO B 312 0 2.47
CISPEP 5 THR B 358 PRO B 359 0 0.22
CISPEP 6 GLY B 369 PRO B 370 0 7.45
CISPEP 7 LEU C 311 PRO C 312 0 4.71
CISPEP 8 THR C 358 PRO C 359 0 -1.29
CISPEP 9 GLY C 369 PRO C 370 0 15.42
CISPEP 10 LEU D 311 PRO D 312 0 1.59
CISPEP 11 THR D 358 PRO D 359 0 0.26
CISPEP 12 GLY D 369 PRO D 370 0 4.18
SITE 1 AC1 3 VAL B 565 PHE B 573 HOH B 685
SITE 1 AC2 1 SER B 183
SITE 1 AC3 2 LEU B 187 SER D 183
SITE 1 AC4 6 ASN B 181 SER B 184 GLY B 185 ASN D 181
SITE 2 AC4 6 SER D 184 GLY D 185
SITE 1 AC5 4 SER C 66 LEU C 115 HOH C 593 HOH C 638
SITE 1 AC6 4 LEU D 27 THR D 249 ARG D 287 HOH D 652
SITE 1 AC7 2 HIS D 549 PHE D 573
CRYST1 184.270 227.524 110.684 90.00 100.37 90.00 C 1 2 1 16
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 0.005427 0.000000 0.000993 0.00000
SCALE2 0.000000 0.004395 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009185 0.00000
TER 4395 ARG A 581
TER 8753 ARG B 581
TER 13185 ARG C 582
TER 17557 ARG D 581
MASTER 753 0 8 54 151 0 8 618020 4 34 180
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