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HEADER HYDROLASE 27-JUL-10 3O4G
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
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 3O4G 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) : 19.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 84232
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4439
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) : 6206
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.3340
REMARK 3 BIN FREE R VALUE SET COUNT : 321
REMARK 3 BIN FREE R VALUE : 0.3720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17159
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 340
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.06000
REMARK 3 B12 (A**2) : 0.01000
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): 0.309
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.268
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.672
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17544 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 11949 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 23818 ; 1.218 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 28983 ; 0.861 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2298 ; 6.157 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 689 ;33.298 ;22.642
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2735 ;15.958 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 147 ;18.081 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2681 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19864 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3658 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 11374 ; 0.316 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4744 ; 0.138 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 18157 ; 0.538 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6170 ; 0.947 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5661 ; 1.472 ; 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 : 3
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 510 3
REMARK 3 2 C 322 C 510 3
REMARK 3 3 A 512 A 580 3
REMARK 3 3 C 512 C 580 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1602 ; 0.030 ; 0.050
REMARK 3 LOOSE POSITIONAL 1 A (A): 1912 ; 0.030 ; 5.000
REMARK 3 TIGHT THERMAL 1 A (A**2): 1602 ; 0.070 ; 0.500
REMARK 3 LOOSE THERMAL 1 A (A**2): 1912 ; 0.070 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 8 B 21 3
REMARK 3 1 D 8 D 21 3
REMARK 3 2 B 322 B 580 3
REMARK 3 2 D 322 D 580 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 1592 ; 0.030 ; 0.050
REMARK 3 LOOSE POSITIONAL 2 B (A): 1770 ; 0.040 ; 5.000
REMARK 3 TIGHT THERMAL 2 B (A**2): 1592 ; 0.060 ; 0.500
REMARK 3 LOOSE THERMAL 2 B (A**2): 1770 ; 0.060 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 25 A 317 3
REMARK 3 1 C 25 C 317 3
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 A (A): 1704 ; 0.020 ; 0.050
REMARK 3 LOOSE POSITIONAL 3 A (A): 1932 ; 0.060 ; 5.000
REMARK 3 TIGHT THERMAL 3 A (A**2): 1704 ; 0.060 ; 0.500
REMARK 3 LOOSE THERMAL 3 A (A**2): 1932 ; 0.060 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 25 B 95 3
REMARK 3 1 D 25 D 95 3
REMARK 3 2 B 97 B 317 4
REMARK 3 2 D 97 D 317 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 B (A): 415 ; 0.080 ; 0.050
REMARK 3 MEDIUM POSITIONAL 4 B (A): 2715 ; 0.120 ; 0.500
REMARK 3 LOOSE POSITIONAL 4 B (A): 426 ; 0.140 ; 5.000
REMARK 3 TIGHT THERMAL 4 B (A**2): 415 ; 0.260 ; 0.500
REMARK 3 MEDIUM THERMAL 4 B (A**2): 2715 ; 0.350 ; 2.000
REMARK 3 LOOSE THERMAL 4 B (A**2): 426 ; 0.380 ;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 5 A 23
REMARK 3 RESIDUE RANGE : A 319 A 581
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0746 5.9527 -2.4570
REMARK 3 T TENSOR
REMARK 3 T11: 0.0793 T22: 0.0935
REMARK 3 T33: 0.0788 T12: 0.1027
REMARK 3 T13: 0.0394 T23: 0.0162
REMARK 3 L TENSOR
REMARK 3 L11: 1.5042 L22: 1.3738
REMARK 3 L33: 2.0104 L12: 0.4890
REMARK 3 L13: -0.2716 L23: -0.0297
REMARK 3 S TENSOR
REMARK 3 S11: -0.1755 S12: -0.1030 S13: -0.1303
REMARK 3 S21: 0.0517 S22: -0.0493 S23: -0.0429
REMARK 3 S31: 0.2831 S32: 0.3908 S33: 0.2249
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 581
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4219 -6.0817 -0.0964
REMARK 3 T TENSOR
REMARK 3 T11: 0.0827 T22: 0.1831
REMARK 3 T33: 0.2083 T12: 0.0846
REMARK 3 T13: 0.0601 T23: 0.0756
REMARK 3 L TENSOR
REMARK 3 L11: 1.9603 L22: 2.0656
REMARK 3 L33: 3.6305 L12: 1.1558
REMARK 3 L13: -0.4675 L23: -1.9132
REMARK 3 S TENSOR
REMARK 3 S11: -0.0769 S12: 0.4474 S13: 0.1266
REMARK 3 S21: -0.0794 S22: 0.4564 S23: 0.2186
REMARK 3 S31: -0.0065 S32: -0.4025 S33: -0.3795
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 6 C 23
REMARK 3 RESIDUE RANGE : C 319 C 581
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0607 -0.4296 59.8544
REMARK 3 T TENSOR
REMARK 3 T11: 0.0921 T22: 0.0091
REMARK 3 T33: 0.0360 T12: -0.0142
REMARK 3 T13: -0.0408 T23: -0.0242
REMARK 3 L TENSOR
REMARK 3 L11: 1.1219 L22: 2.0848
REMARK 3 L33: 1.7826 L12: 0.0661
REMARK 3 L13: -0.2498 L23: -0.3812
REMARK 3 S TENSOR
REMARK 3 S11: 0.0522 S12: -0.0342 S13: 0.0652
REMARK 3 S21: 0.1236 S22: -0.0406 S23: -0.1396
REMARK 3 S31: 0.0920 S32: -0.0164 S33: -0.0116
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): -23.9060 27.2165 39.1140
REMARK 3 T TENSOR
REMARK 3 T11: 0.0422 T22: 0.0263
REMARK 3 T33: 0.0944 T12: 0.0135
REMARK 3 T13: -0.0502 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 2.8535 L22: 2.1908
REMARK 3 L33: 1.5103 L12: 0.4334
REMARK 3 L13: -0.6104 L23: -1.0400
REMARK 3 S TENSOR
REMARK 3 S11: 0.0706 S12: -0.2313 S13: 0.0000
REMARK 3 S21: 0.1252 S22: 0.0621 S23: 0.0918
REMARK 3 S31: -0.0692 S32: -0.0727 S33: -0.1326
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): 13.1310 33.7540 -4.1532
REMARK 3 T TENSOR
REMARK 3 T11: 0.1621 T22: 0.0477
REMARK 3 T33: 0.0605 T12: -0.0190
REMARK 3 T13: -0.0305 T23: -0.0299
REMARK 3 L TENSOR
REMARK 3 L11: 1.3690 L22: 1.2308
REMARK 3 L33: 1.6387 L12: 0.6178
REMARK 3 L13: 0.1708 L23: 0.1483
REMARK 3 S TENSOR
REMARK 3 S11: -0.0159 S12: 0.1277 S13: 0.2136
REMARK 3 S21: -0.1683 S22: 0.0523 S23: 0.1500
REMARK 3 S31: -0.3913 S32: 0.2003 S33: -0.0363
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): -15.9137 -32.8839 19.7980
REMARK 3 T TENSOR
REMARK 3 T11: 0.1207 T22: 0.0344
REMARK 3 T33: 0.0857 T12: 0.0047
REMARK 3 T13: -0.0333 T23: 0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 1.7403 L22: 2.0904
REMARK 3 L33: 1.1146 L12: -0.0448
REMARK 3 L13: -0.5011 L23: 0.5609
REMARK 3 S TENSOR
REMARK 3 S11: 0.0760 S12: 0.2015 S13: 0.0238
REMARK 3 S21: 0.1029 S22: -0.0661 S23: -0.2859
REMARK 3 S31: 0.2237 S32: -0.0985 S33: -0.0099
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): -48.5318 -15.5807 46.8990
REMARK 3 T TENSOR
REMARK 3 T11: 0.0810 T22: 0.2245
REMARK 3 T33: 0.0886 T12: -0.0978
REMARK 3 T13: 0.0029 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 0.9937 L22: 2.1193
REMARK 3 L33: 1.3283 L12: -0.1764
REMARK 3 L13: -0.1650 L23: -0.2022
REMARK 3 S TENSOR
REMARK 3 S11: 0.0433 S12: 0.1544 S13: 0.1645
REMARK 3 S21: 0.0456 S22: -0.0672 S23: 0.1734
REMARK 3 S31: 0.2882 S32: -0.5008 S33: 0.0240
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): 8.0290 35.5933 41.2192
REMARK 3 T TENSOR
REMARK 3 T11: 0.0983 T22: 0.2312
REMARK 3 T33: 0.1576 T12: -0.0789
REMARK 3 T13: -0.0594 T23: 0.0778
REMARK 3 L TENSOR
REMARK 3 L11: 1.4238 L22: 2.5245
REMARK 3 L33: 2.0449 L12: 0.8932
REMARK 3 L13: -0.1235 L23: 0.1554
REMARK 3 S TENSOR
REMARK 3 S11: 0.1179 S12: -0.4881 S13: -0.3405
REMARK 3 S21: 0.3064 S22: -0.2310 S23: -0.3112
REMARK 3 S31: -0.2351 S32: 0.3831 S33: 0.1131
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 3O4G 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 RCSB060652.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X12
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111),
REMARK 200 HORIZONTALLY FOCUSSING
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88675
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.1
REMARK 200 DATA REDUNDANCY : 1.990
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.5500
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) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.9
REMARK 200 DATA REDUNDANCY IN SHELL : 1.99
REMARK 200 R MERGE FOR SHELL (I) : 0.59500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.010
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 (%): 55.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
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: 3290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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: 2630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 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 GLY B 555
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 MET C 5
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 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 MET A 5 CG SD CE
REMARK 470 VAL A 7 CG1 CG2
REMARK 470 GLU A 8 CG CD OE1 OE2
REMARK 470 ARG A 11 CD NE CZ NH1 NH2
REMARK 470 ASP A 34 CG OD1 OD2
REMARK 470 ARG A 61 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 69 CG OD1 OD2
REMARK 470 LYS A 110 NZ
REMARK 470 ARG A 149 NE CZ NH1 NH2
REMARK 470 ARG A 188 NE CZ NH1 NH2
REMARK 470 ARG A 216 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 217 CD OE1 OE2
REMARK 470 GLU A 324 CD OE1 OE2
REMARK 470 ARG A 327 CZ NH1 NH2
REMARK 470 ARG A 428 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 431 NH1 NH2
REMARK 470 VAL B 7 CG1 CG2
REMARK 470 GLU B 8 OE1 OE2
REMARK 470 ARG B 11 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 17 OE2
REMARK 470 GLU B 23 CG CD OE1 OE2
REMARK 470 PHE B 41 CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU B 55 CG CD OE1 OE2
REMARK 470 LYS B 85 CG CD CE NZ
REMARK 470 GLN B 89 CG CD OE1 NE2
REMARK 470 GLU B 131 CD OE1 OE2
REMARK 470 ARG B 149 CD NE CZ NH1 NH2
REMARK 470 ARG B 174 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 194 CG CD OE1 OE2
REMARK 470 ARG B 216 NE CZ NH1 NH2
REMARK 470 GLU B 217 CG CD OE1 OE2
REMARK 470 GLU B 234 CG CD OE1 OE2
REMARK 470 GLU B 324 CG CD OE1 OE2
REMARK 470 ARG B 327 NE CZ NH1 NH2
REMARK 470 ARG B 328 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 346 CG1 CG2
REMARK 470 GLU B 406 OE1 OE2
REMARK 470 ARG B 428 CD NE CZ NH1 NH2
REMARK 470 GLU B 479 CG CD OE1 OE2
REMARK 470 ASP B 482 CG OD1 OD2
REMARK 470 ARG B 486 CZ NH1 NH2
REMARK 470 ASN B 487 CG OD1 ND2
REMARK 470 PHE B 488 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN B 491 CD OE1 NE2
REMARK 470 LEU B 492 CD1 CD2
REMARK 470 ARG B 497 CZ NH1 NH2
REMARK 470 GLU B 498 CG CD OE1 OE2
REMARK 470 LYS B 513 CE NZ
REMARK 470 ARG B 526 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 553 CG OD1 OD2
REMARK 470 HIS B 556 ND1 CD2 CE1 NE2
REMARK 470 MET B 561 CE
REMARK 470 LYS B 566 CE NZ
REMARK 470 VAL C 7 CG1 CG2
REMARK 470 ARG C 11 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 61 CZ NH1 NH2
REMARK 470 ARG C 99 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 110 CD CE NZ
REMARK 470 GLU C 122 CG CD OE1 OE2
REMARK 470 ARG C 149 CD NE CZ NH1 NH2
REMARK 470 ARG C 188 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 194 CG CD OE1 OE2
REMARK 470 ARG C 216 CZ NH1 NH2
REMARK 470 GLU C 324 CD OE1 OE2
REMARK 470 ARG C 327 CD NE CZ NH1 NH2
REMARK 470 ARG C 431 CZ NH1 NH2
REMARK 470 GLU C 498 CD OE1 OE2
REMARK 470 ARG C 501 CD NE CZ NH1 NH2
REMARK 470 ASP C 510 CG OD1 OD2
REMARK 470 VAL D 7 CG1 CG2
REMARK 470 PHE D 9 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D 11 NE CZ NH1 NH2
REMARK 470 LYS D 24 CE NZ
REMARK 470 GLU D 55 CG CD OE1 OE2
REMARK 470 ARG D 61 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 85 CG CD CE NZ
REMARK 470 GLN D 89 CD OE1 NE2
REMARK 470 LYS D 94 CG CD CE NZ
REMARK 470 ARG D 99 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 103 CG CD OE1 OE2
REMARK 470 GLU D 122 CD OE1 OE2
REMARK 470 GLU D 131 CG CD OE1 OE2
REMARK 470 LEU D 139 CG CD1 CD2
REMARK 470 ARG D 149 CD NE CZ NH1 NH2
REMARK 470 ARG D 174 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 194 CD OE1 OE2
REMARK 470 ARG D 216 CD NE CZ NH1 NH2
REMARK 470 GLU D 217 CG CD OE1 OE2
REMARK 470 ARG D 244 CZ NH1 NH2
REMARK 470 LYS D 294 NZ
REMARK 470 GLU D 324 CG CD OE1 OE2
REMARK 470 ARG D 328 CD NE CZ NH1 NH2
REMARK 470 ASP D 342 CG OD1 OD2
REMARK 470 ARG D 486 CZ NH1 NH2
REMARK 470 GLU D 490 CG CD OE1 OE2
REMARK 470 GLU D 498 CG CD OE1 OE2
REMARK 470 ARG D 501 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 526 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 553 CG OD1 OD2
REMARK 470 HIS D 556 CG ND1 CD2 CE1 NE2
REMARK 470 ILE D 558 CD1
REMARK 470 GLU D 562 CG CD OE1 OE2
REMARK 470 LYS D 566 CG CD CE NZ
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 43 39.36 39.19
REMARK 500 ARG A 61 -78.83 -102.26
REMARK 500 SER A 66 -163.00 -170.64
REMARK 500 ALA A 148 143.17 -170.47
REMARK 500 PHE A 153 128.10 -39.94
REMARK 500 ARG A 216 20.04 -141.21
REMARK 500 SER A 445 -127.09 60.25
REMARK 500 ARG B 61 -79.19 -93.02
REMARK 500 SER B 84 25.88 -148.10
REMARK 500 ARG B 216 -114.67 -131.54
REMARK 500 ASP B 227 1.78 -152.22
REMARK 500 PRO B 306 125.97 -39.82
REMARK 500 ILE B 330 67.88 -105.07
REMARK 500 ASP B 414 60.49 -156.34
REMARK 500 SER B 445 -116.14 57.46
REMARK 500 HIS B 508 25.57 -143.14
REMARK 500 ASN B 523 49.37 -146.92
REMARK 500 GLU B 580 48.49 -97.14
REMARK 500 ARG C 61 -80.49 -104.64
REMARK 500 SER C 66 -162.29 -172.08
REMARK 500 ALA C 148 143.04 -171.40
REMARK 500 PHE C 153 131.39 -39.67
REMARK 500 ARG C 216 19.00 -141.31
REMARK 500 ASP C 414 44.46 -141.13
REMARK 500 SER C 445 -127.47 60.16
REMARK 500 ARG D 61 -86.51 -82.68
REMARK 500 TYR D 72 124.62 -39.21
REMARK 500 SER D 84 22.50 -148.59
REMARK 500 ALA D 148 143.85 -176.93
REMARK 500 ARG D 216 -109.14 -127.30
REMARK 500 TRP D 250 146.98 -171.70
REMARK 500 PRO D 306 132.10 -39.89
REMARK 500 ILE D 330 66.06 -102.95
REMARK 500 TYR D 403 33.30 -140.21
REMARK 500 ASP D 414 58.19 -157.04
REMARK 500 SER D 445 -117.59 59.33
REMARK 500 HIS D 508 26.96 -142.29
REMARK 500 ASN D 523 51.34 -146.23
REMARK 500 THR D 527 68.02 -150.15
REMARK 500 ALA D 554 31.27 -95.23
REMARK 500 GLU D 580 51.74 -96.28
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 612 DISTANCE = 5.44 ANGSTROMS
REMARK 525 HOH D 613 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH B 617 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH D 624 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH B 627 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH B 630 DISTANCE = 7.57 ANGSTROMS
REMARK 525 HOH C 630 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B 636 DISTANCE = 7.90 ANGSTROMS
REMARK 525 HOH C 638 DISTANCE = 6.92 ANGSTROMS
REMARK 525 HOH C 640 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH C 642 DISTANCE = 5.29 ANGSTROMS
REMARK 525 HOH A 646 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH C 645 DISTANCE = 7.81 ANGSTROMS
REMARK 525 HOH A 649 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH B 651 DISTANCE = 5.44 ANGSTROMS
REMARK 525 HOH B 673 DISTANCE = 5.01 ANGSTROMS
REMARK 525 HOH D 655 DISTANCE = 5.56 ANGSTROMS
REMARK 525 HOH C 659 DISTANCE = 5.23 ANGSTROMS
REMARK 525 HOH A 663 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A 677 DISTANCE = 7.27 ANGSTROMS
REMARK 525 HOH A 687 DISTANCE = 5.32 ANGSTROMS
REMARK 525 HOH A 691 DISTANCE = 7.42 ANGSTROMS
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 GOL B 583
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 583
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O4H RELATED DB: PDB
REMARK 900 RELATED ID: 3O4I RELATED DB: PDB
REMARK 900 RELATED ID: 3O4J RELATED DB: PDB
DBREF 3O4G A 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 3O4G B 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 3O4G C 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
DBREF 3O4G D 1 582 UNP Q9YBQ2 APEH_AERPE 1 582
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 ASP 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 ASP 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 ASP 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 ASP 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 6
HET GOL A 584 6
HET GOL B 583 6
HET GOL C 583 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 9 HOH *340(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 ARG A 328 1 6
HELIX 4 4 ASP A 379 GLY A 389 1 11
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 ARG A 581 1 22
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 ILE B 330 1 8
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 LEU B 480 1 8
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 579 1 12
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 ARG C 328 1 6
HELIX 31 31 ASP C 379 GLY C 389 1 11
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 PRO C 528 ARG C 542 1 15
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 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 LEU D 480 1 8
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 GLU A 103 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 GLY A 117 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 ALA A 148 N LEU A 136
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 SER A 176 N GLY A 168
SHEET 4 D 4 GLY A 185 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 THR A 209 N SER A 201
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 THR A 300 -1 O VAL A 296 N VAL A 289
SHEET 3 G 4 ARG A 307 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 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 THR A 348 N VAL A 336
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 VAL A 466 N ILE A 441
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 HIS A 549 N HIS A 520
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 ALA B 464 GLY B 468 1 N GLY B 465 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 LEU B 351 -1 N TYR B 349 O MET B 394
SHEET 16 H16 SER B 333 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 ASN B 47 N GLY B 40
SHEET 4 I 4 GLU B 55 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 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 VAL B 124 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 ALA B 148 N LEU B 136
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 PHE B 178 N GLY B 166
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 THR B 209 N SER B 201
SHEET 3 M 4 ARG B 219 VAL B 223 -1 O VAL B 223 N VAL B 208
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 VAL B 309 N THR B 297
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 VAL C 57 N LEU C 50
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 GLU C 103 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 THR C 127 N LEU C 115
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 ALA C 148 N LEU C 136
SHEET 1 S 4 GLY C 154 ARG C 160 0
SHEET 2 S 4 LEU C 163 GLY C 171 -1 O LEU C 167 N PHE C 155
SHEET 3 S 4 ARG C 174 ASN C 181 -1 O SER C 176 N GLY C 168
SHEET 4 S 4 GLY C 185 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 THR C 300 -1 O LYS C 294 N TRP C 291
SHEET 3 V 4 ARG C 307 LEU C 311 -1 O VAL C 309 N THR C 297
SHEET 4 V 4 PRO C 316 LEU C 318 -1 O LEU C 317 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 MET C 394 N TYR C 349
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 ALA C 464 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 GLY C 465
SHEET 8 W16 PHE C 546 ILE C 551 1 O GLU C 547 N LEU C 518
SHEET 9 W16 PHE D 546 ILE D 551 -1 O ALA D 548 N ILE C 550
SHEET 10 W16 LEU D 516 PRO D 521 1 N LEU D 516 O GLU D 547
SHEET 11 W16 ALA D 464 GLY D 468 1 N GLY D 465 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 366 O MET D 442
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 338 O VAL D 346
SHEET 1 X 4 LYS D 24 VAL D 31 0
SHEET 2 X 4 LYS D 35 SER D 42 -1 O PHE D 41 N LYS D 24
SHEET 3 X 4 SER D 45 ASP D 52 -1 O ASN D 47 N GLY D 40
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 GLN D 104 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 THR D 130 -1 O VAL D 125 N VAL D 118
SHEET 4 Z 5 ARG D 133 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 LEU D 167 N PHE D 155
SHEET 3 AA 4 SER D 176 ASN D 181 -1 O SER D 180 N ILE D 164
SHEET 4 AA 4 ARG D 188 PHE D 190 -1 O PHE D 190 N LEU D 177
SHEET 1 AB 4 GLY D 195 ILE D 202 0
SHEET 2 AB 4 VAL D 208 THR D 214 -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 VAL D 262 N TRP D 250
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 ARG D 307 N HIS D 299
SHEET 4 AD 4 PRO D 316 LEU D 318 -1 O LEU D 317 N ILE D 308
CISPEP 1 LEU A 311 PRO A 312 0 5.57
CISPEP 2 THR A 358 PRO A 359 0 3.26
CISPEP 3 GLY A 369 PRO A 370 0 4.85
CISPEP 4 LEU B 311 PRO B 312 0 0.66
CISPEP 5 THR B 358 PRO B 359 0 -2.32
CISPEP 6 GLY B 369 PRO B 370 0 6.87
CISPEP 7 LEU C 311 PRO C 312 0 7.14
CISPEP 8 THR C 358 PRO C 359 0 -0.03
CISPEP 9 GLY C 369 PRO C 370 0 8.92
CISPEP 10 LEU D 311 PRO D 312 0 4.81
CISPEP 11 THR D 358 PRO D 359 0 -3.60
CISPEP 12 GLY D 369 PRO D 370 0 8.60
SITE 1 AC1 2 SER A 66 ILE A 114
SITE 1 AC2 6 ASP A 473 GLU A 475 GLU A 476 GLU A 479
SITE 2 AC2 6 GLU C 421 LYS C 458
SITE 1 AC3 2 HIS B 285 SER B 298
SITE 1 AC4 4 THR C 249 ARG C 264 ASN C 284 THR C 401
CRYST1 71.212 97.016 109.494 89.01 109.20 100.21 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 0.014043 0.002528 0.005008 0.00000
SCALE2 0.000000 0.010473 0.000463 0.00000
SCALE3 0.000000 0.000000 0.009681 0.00000
TER 4339 ARG A 581
TER 8583 ARG B 581
TER 12908 ARG C 581
TER 17163 ARG D 581
MASTER 698 0 4 54 148 0 5 617523 4 24 180
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