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HEADER HYDROLASE 27-APR-11 2YH2
TITLE PYROBACULUM CALIDIFONTIS ESTERASE MONOCLINIC FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ALPH-BETA HYDROLASE;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROBACULUM CALIDIFONTIS;
SOURCE 3 ORGANISM_TAXID: 181486;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS HYPERTHERMOPHILIC ENZYME, HYDROLASE, TERTIARY ALCOHOL, ALPHA/BETA
KEYWDS 2 HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR G.PALM,X.BOGDANOVIC,W.HINRICHS
REVDAT 1 18-MAY-11 2YH2 0
JRNL AUTH G.J.PALM,E.FERNANDEZ-ALVARO,X.BOGDANOVIC,S.BARTSCH,
JRNL AUTH 2 J.SCZODROK,R.K.SINGH,D.BOETTCHER,H.ATOMI,U.T.BORNSCHEUER,
JRNL AUTH 3 W.HINRICHS
JRNL TITL THE CRYSTAL STRUCTURE OF AN ESTERASE FOM THE
JRNL TITL 2 HYPERTHERMOPHILIC MICROORGANISM PYROBACULUM CALIDIFONTIS
JRNL TITL 3 VA1 SUPPORTS EXPLANATION OF ITS ENANTIOSELECTIVITY.
JRNL REF APPL.MICROBIOL.BIOTECHNOL. 2011
JRNL REFN ESSN 1432-0614
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.HOTTA,S.EZAKI,H.ATOMI,T.IMANAKA
REMARK 1 TITL EXTREMELY STABLE AND VERSATILE CARBOXYLESTERASE FROM A
REMARK 1 TITL 2 HYPERTHERMOPHILIC ARCHAEON.
REMARK 1 REF APPL.ENVIRON.MICROBIOL. V. 68 3925 2002
REMARK 1 REFN ISSN 0099-2240
REMARK 1 PMID 12147492
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 141.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.82
REMARK 3 NUMBER OF REFLECTIONS : 47721
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) : 0.16668
REMARK 3 R VALUE (WORKING SET) : 0.16416
REMARK 3 FREE R VALUE : 0.21370
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 2550
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) : 2.198
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.255
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1716
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 41.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.167
REMARK 3 BIN FREE R VALUE SET COUNT : 89
REMARK 3 BIN FREE R VALUE : 0.252
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9580
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 368
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.6
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.688
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.21
REMARK 3 B22 (A**2) : -2.08
REMARK 3 B33 (A**2) : -0.13
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.32
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.435
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.231
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.135
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.584
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9813 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 6674 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13367 ; 1.198 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16179 ; 0.873 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1240 ; 5.663 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 441 ;30.566 ;22.834
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1550 ;13.996 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 88 ;16.220 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1489 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11049 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2059 ; 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): 6159 ; 0.432 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2486 ; 0.097 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9934 ; 0.810 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3654 ; 1.402 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3425 ; 2.310 ; 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 : NULL
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 : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 27
REMARK 3 ORIGIN FOR THE GROUP (A): 35.6880 12.0590 42.7390
REMARK 3 T TENSOR
REMARK 3 T11: 0.1655 T22: 0.2383
REMARK 3 T33: 0.3198 T12: -0.0618
REMARK 3 T13: 0.1284 T23: -0.0666
REMARK 3 L TENSOR
REMARK 3 L11: -0.4006 L22: 9.4239
REMARK 3 L33: 2.5264 L12: -1.0369
REMARK 3 L13: -0.1761 L23: 1.1932
REMARK 3 S TENSOR
REMARK 3 S11: 0.0232 S12: -0.0230 S13: 0.0862
REMARK 3 S21: -0.7006 S22: 0.2327 S23: -0.9512
REMARK 3 S31: -0.1943 S32: 0.5669 S33: -0.2559
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 28 A 313
REMARK 3 ORIGIN FOR THE GROUP (A): 20.0180 1.1470 52.0500
REMARK 3 T TENSOR
REMARK 3 T11: 0.1434 T22: 0.0625
REMARK 3 T33: 0.0285 T12: 0.0045
REMARK 3 T13: 0.0310 T23: 0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 0.5083 L22: 0.5735
REMARK 3 L33: 0.6160 L12: -0.0389
REMARK 3 L13: 0.0609 L23: 0.0470
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: 0.0173 S13: -0.0465
REMARK 3 S21: -0.0259 S22: -0.0148 S23: -0.0150
REMARK 3 S31: 0.0384 S32: 0.0318 S33: 0.0149
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 27
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5310 27.6770 45.7740
REMARK 3 T TENSOR
REMARK 3 T11: 0.1353 T22: 0.3894
REMARK 3 T33: 0.4221 T12: 0.0189
REMARK 3 T13: 0.0134 T23: 0.0359
REMARK 3 L TENSOR
REMARK 3 L11: 1.5680 L22: 19.6498
REMARK 3 L33: 4.1502 L12: -5.3996
REMARK 3 L13: -0.2600 L23: 4.9003
REMARK 3 S TENSOR
REMARK 3 S11: 0.2370 S12: 0.2551 S13: -0.5263
REMARK 3 S21: -0.8971 S22: -0.8627 S23: 2.1343
REMARK 3 S31: -0.2545 S32: -0.6488 S33: 0.6257
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 28 B 313
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5410 32.1480 59.3640
REMARK 3 T TENSOR
REMARK 3 T11: 0.1414 T22: 0.0692
REMARK 3 T33: 0.0260 T12: 0.0040
REMARK 3 T13: 0.0347 T23: -0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 0.4397 L22: 0.6685
REMARK 3 L33: 0.6034 L12: 0.0802
REMARK 3 L13: -0.1130 L23: 0.0198
REMARK 3 S TENSOR
REMARK 3 S11: 0.0121 S12: -0.0030 S13: 0.0102
REMARK 3 S21: -0.0142 S22: -0.0213 S23: 0.0218
REMARK 3 S31: -0.0536 S32: -0.0239 S33: 0.0092
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 : C 2 C 27
REMARK 3 ORIGIN FOR THE GROUP (A): 36.3260 27.3750 25.7890
REMARK 3 T TENSOR
REMARK 3 T11: 0.4717 T22: 0.5972
REMARK 3 T33: 0.8825 T12: 0.2289
REMARK 3 T13: -0.0611 T23: -0.1827
REMARK 3 L TENSOR
REMARK 3 L11: 0.5498 L22: 39.4352
REMARK 3 L33: 0.9447 L12: 9.2624
REMARK 3 L13: 0.1556 L23: 0.5998
REMARK 3 S TENSOR
REMARK 3 S11: 0.3535 S12: 0.0217 S13: -0.5905
REMARK 3 S21: 1.5238 S22: 0.0273 S23: -3.8482
REMARK 3 S31: 0.6422 S32: 0.8277 S33: -0.3808
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 : C 28 C 313
REMARK 3 ORIGIN FOR THE GROUP (A): 20.8990 41.3030 18.9040
REMARK 3 T TENSOR
REMARK 3 T11: 0.1595 T22: 0.0686
REMARK 3 T33: 0.0237 T12: -0.0049
REMARK 3 T13: 0.0461 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.4072 L22: 0.8220
REMARK 3 L33: 0.7968 L12: 0.0512
REMARK 3 L13: -0.0627 L23: 0.0371
REMARK 3 S TENSOR
REMARK 3 S11: -0.0042 S12: 0.0174 S13: 0.0251
REMARK 3 S21: -0.0170 S22: -0.0014 S23: -0.0328
REMARK 3 S31: -0.0974 S32: 0.0371 S33: 0.0056
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 : D 2 D 27
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4710 16.4550 24.8310
REMARK 3 T TENSOR
REMARK 3 T11: 0.1565 T22: 0.3973
REMARK 3 T33: 0.2274 T12: -0.0117
REMARK 3 T13: 0.1068 T23: 0.0603
REMARK 3 L TENSOR
REMARK 3 L11: 2.9433 L22: 17.6537
REMARK 3 L33: 4.4234 L12: 6.6180
REMARK 3 L13: 0.7541 L23: 4.3619
REMARK 3 S TENSOR
REMARK 3 S11: 0.5105 S12: -0.3871 S13: 0.3556
REMARK 3 S21: 1.1795 S22: -0.8178 S23: 1.3065
REMARK 3 S31: 0.2499 S32: -0.9048 S33: 0.3074
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 28 D 313
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2650 10.5970 11.7310
REMARK 3 T TENSOR
REMARK 3 T11: 0.1437 T22: 0.0678
REMARK 3 T33: 0.0110 T12: -0.0020
REMARK 3 T13: 0.0209 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.5170 L22: 0.6499
REMARK 3 L33: 1.2238 L12: -0.0439
REMARK 3 L13: 0.1389 L23: -0.0238
REMARK 3 S TENSOR
REMARK 3 S11: 0.0517 S12: 0.0167 S13: -0.0211
REMARK 3 S21: -0.0056 S22: 0.0107 S23: 0.0265
REMARK 3 S31: 0.1399 S32: -0.0669 S33: -0.0624
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2YH2 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-APR-11.
REMARK 100 THE PDBE ID CODE IS EBI-48083.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : 0.97784
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM 7.0.4
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50355
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.20
REMARK 200 RESOLUTION RANGE LOW (A) : 10.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.0
REMARK 200 DATA REDUNDANCY : 5
REMARK 200 R MERGE (I) : 0.10
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 47.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.6
REMARK 200 R MERGE FOR SHELL (I) : 0.20
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.50
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2WIR
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 4000, 30% MPD, 0.1 M
REMARK 280 IMIDAZOLE PH 8.0; SOAKED IN 10% PEG 4000, 4% DMSO, 0.1 M
REMARK 280 IMIDAZOLE PH 8.0, 0.01 M PHENYLBUTANOIC ACID ETHYL ESTER.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 36.16750
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 ALA A 15
REMARK 465 ALA A 16
REMARK 465 GLN A 17
REMARK 465 LEU A 18
REMARK 465 GLN A 19
REMARK 465 MET B 1
REMARK 465 LEU B 14
REMARK 465 ALA B 15
REMARK 465 ALA B 16
REMARK 465 GLN B 17
REMARK 465 LEU B 18
REMARK 465 MET C 1
REMARK 465 GLN C 17
REMARK 465 LEU C 18
REMARK 465 GLN C 19
REMARK 465 PHE C 20
REMARK 465 ARG C 21
REMARK 465 PRO C 22
REMARK 465 ASP C 23
REMARK 465 MET D 1
REMARK 465 ALA D 15
REMARK 465 ALA D 16
REMARK 465 GLN D 17
REMARK 465 LEU D 18
REMARK 465 GLN D 19
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 GLN A 12 29.69 -72.49
REMARK 500 SER A 91 -177.10 -172.77
REMARK 500 SER A 157 -117.72 61.84
REMARK 500 TYR A 185 66.20 28.09
REMARK 500 VAL A 207 -61.69 68.63
REMARK 500 TYR A 253 68.35 -105.97
REMARK 500 GLN B 12 89.62 -65.78
REMARK 500 SER B 157 -116.08 67.26
REMARK 500 TYR B 185 62.96 30.09
REMARK 500 VAL B 207 -59.03 67.72
REMARK 500 TYR B 253 57.77 -104.64
REMARK 500 LEU C 14 -36.57 -165.99
REMARK 500 ALA C 15 -72.80 -60.35
REMARK 500 ASN C 45 59.17 38.82
REMARK 500 SER C 157 -116.34 65.06
REMARK 500 TYR C 185 63.06 33.15
REMARK 500 VAL C 207 -62.50 65.11
REMARK 500 TYR C 253 60.49 -106.72
REMARK 500 SER D 157 -117.74 63.82
REMARK 500 TYR D 185 65.27 27.97
REMARK 500 VAL D 207 -56.84 64.70
REMARK 500 TYR D 253 53.95 -105.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1314
REMARK 800
REMARK 800 SITE_IDENTIFIER: ASA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD IN MONOMER A
REMARK 800
REMARK 800 SITE_IDENTIFIER: ASB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD IN MONOMER B
REMARK 800
REMARK 800 SITE_IDENTIFIER: ASC
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD IN MONOMER C
REMARK 800
REMARK 800 SITE_IDENTIFIER: ASD
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD IN MONOMER D
DBREF 2YH2 A 1 313 UNP Q8NKS0 Q8NKS0_9CREN 1 313
DBREF 2YH2 B 1 313 UNP Q8NKS0 Q8NKS0_9CREN 1 313
DBREF 2YH2 C 1 313 UNP Q8NKS0 Q8NKS0_9CREN 1 313
DBREF 2YH2 D 1 313 UNP Q8NKS0 Q8NKS0_9CREN 1 313
SEQRES 1 A 313 MET PRO LEU SER PRO ILE LEU ARG GLN ILE LEU GLN GLN
SEQRES 2 A 313 LEU ALA ALA GLN LEU GLN PHE ARG PRO ASP MET ASP VAL
SEQRES 3 A 313 LYS THR VAL ARG GLU GLN PHE GLU LYS SER SER LEU ILE
SEQRES 4 A 313 LEU VAL LYS MET ALA ASN GLU PRO ILE HIS ARG VAL GLU
SEQRES 5 A 313 ASP ILE THR ILE PRO GLY ARG GLY GLY PRO ILE ARG ALA
SEQRES 6 A 313 ARG VAL TYR ARG PRO ARG ASP GLY GLU ARG LEU PRO ALA
SEQRES 7 A 313 VAL VAL TYR TYR HIS GLY GLY GLY PHE VAL LEU GLY SER
SEQRES 8 A 313 VAL GLU THR HIS ASP HIS VAL CYS ARG ARG LEU ALA ASN
SEQRES 9 A 313 LEU SER GLY ALA VAL VAL VAL SER VAL ASP TYR ARG LEU
SEQRES 10 A 313 ALA PRO GLU HIS LYS PHE PRO ALA ALA VAL GLU ASP ALA
SEQRES 11 A 313 TYR ASP ALA ALA LYS TRP VAL ALA ASP ASN TYR ASP LYS
SEQRES 12 A 313 LEU GLY VAL ASP ASN GLY LYS ILE ALA VAL ALA GLY ASP
SEQRES 13 A 313 SER ALA GLY GLY ASN LEU ALA ALA VAL THR ALA ILE MET
SEQRES 14 A 313 ALA ARG ASP ARG GLY GLU SER PHE VAL LYS TYR GLN VAL
SEQRES 15 A 313 LEU ILE TYR PRO ALA VAL ASN LEU THR GLY SER PRO THR
SEQRES 16 A 313 VAL SER ARG VAL GLU TYR SER GLY PRO GLU TYR VAL ILE
SEQRES 17 A 313 LEU THR ALA ASP LEU MET ALA TRP PHE GLY ARG GLN TYR
SEQRES 18 A 313 PHE SER LYS PRO GLN ASP ALA LEU SER PRO TYR ALA SER
SEQRES 19 A 313 PRO ILE PHE ALA ASP LEU SER ASN LEU PRO PRO ALA LEU
SEQRES 20 A 313 VAL ILE THR ALA GLU TYR ASP PRO LEU ARG ASP GLU GLY
SEQRES 21 A 313 GLU LEU TYR ALA HIS LEU LEU LYS THR ARG GLY VAL ARG
SEQRES 22 A 313 ALA VAL ALA VAL ARG TYR ASN GLY VAL ILE HIS GLY PHE
SEQRES 23 A 313 VAL ASN PHE TYR PRO ILE LEU GLU GLU GLY ARG GLU ALA
SEQRES 24 A 313 VAL SER GLN ILE ALA ALA SER ILE LYS SER MET ALA VAL
SEQRES 25 A 313 ALA
SEQRES 1 B 313 MET PRO LEU SER PRO ILE LEU ARG GLN ILE LEU GLN GLN
SEQRES 2 B 313 LEU ALA ALA GLN LEU GLN PHE ARG PRO ASP MET ASP VAL
SEQRES 3 B 313 LYS THR VAL ARG GLU GLN PHE GLU LYS SER SER LEU ILE
SEQRES 4 B 313 LEU VAL LYS MET ALA ASN GLU PRO ILE HIS ARG VAL GLU
SEQRES 5 B 313 ASP ILE THR ILE PRO GLY ARG GLY GLY PRO ILE ARG ALA
SEQRES 6 B 313 ARG VAL TYR ARG PRO ARG ASP GLY GLU ARG LEU PRO ALA
SEQRES 7 B 313 VAL VAL TYR TYR HIS GLY GLY GLY PHE VAL LEU GLY SER
SEQRES 8 B 313 VAL GLU THR HIS ASP HIS VAL CYS ARG ARG LEU ALA ASN
SEQRES 9 B 313 LEU SER GLY ALA VAL VAL VAL SER VAL ASP TYR ARG LEU
SEQRES 10 B 313 ALA PRO GLU HIS LYS PHE PRO ALA ALA VAL GLU ASP ALA
SEQRES 11 B 313 TYR ASP ALA ALA LYS TRP VAL ALA ASP ASN TYR ASP LYS
SEQRES 12 B 313 LEU GLY VAL ASP ASN GLY LYS ILE ALA VAL ALA GLY ASP
SEQRES 13 B 313 SER ALA GLY GLY ASN LEU ALA ALA VAL THR ALA ILE MET
SEQRES 14 B 313 ALA ARG ASP ARG GLY GLU SER PHE VAL LYS TYR GLN VAL
SEQRES 15 B 313 LEU ILE TYR PRO ALA VAL ASN LEU THR GLY SER PRO THR
SEQRES 16 B 313 VAL SER ARG VAL GLU TYR SER GLY PRO GLU TYR VAL ILE
SEQRES 17 B 313 LEU THR ALA ASP LEU MET ALA TRP PHE GLY ARG GLN TYR
SEQRES 18 B 313 PHE SER LYS PRO GLN ASP ALA LEU SER PRO TYR ALA SER
SEQRES 19 B 313 PRO ILE PHE ALA ASP LEU SER ASN LEU PRO PRO ALA LEU
SEQRES 20 B 313 VAL ILE THR ALA GLU TYR ASP PRO LEU ARG ASP GLU GLY
SEQRES 21 B 313 GLU LEU TYR ALA HIS LEU LEU LYS THR ARG GLY VAL ARG
SEQRES 22 B 313 ALA VAL ALA VAL ARG TYR ASN GLY VAL ILE HIS GLY PHE
SEQRES 23 B 313 VAL ASN PHE TYR PRO ILE LEU GLU GLU GLY ARG GLU ALA
SEQRES 24 B 313 VAL SER GLN ILE ALA ALA SER ILE LYS SER MET ALA VAL
SEQRES 25 B 313 ALA
SEQRES 1 C 313 MET PRO LEU SER PRO ILE LEU ARG GLN ILE LEU GLN GLN
SEQRES 2 C 313 LEU ALA ALA GLN LEU GLN PHE ARG PRO ASP MET ASP VAL
SEQRES 3 C 313 LYS THR VAL ARG GLU GLN PHE GLU LYS SER SER LEU ILE
SEQRES 4 C 313 LEU VAL LYS MET ALA ASN GLU PRO ILE HIS ARG VAL GLU
SEQRES 5 C 313 ASP ILE THR ILE PRO GLY ARG GLY GLY PRO ILE ARG ALA
SEQRES 6 C 313 ARG VAL TYR ARG PRO ARG ASP GLY GLU ARG LEU PRO ALA
SEQRES 7 C 313 VAL VAL TYR TYR HIS GLY GLY GLY PHE VAL LEU GLY SER
SEQRES 8 C 313 VAL GLU THR HIS ASP HIS VAL CYS ARG ARG LEU ALA ASN
SEQRES 9 C 313 LEU SER GLY ALA VAL VAL VAL SER VAL ASP TYR ARG LEU
SEQRES 10 C 313 ALA PRO GLU HIS LYS PHE PRO ALA ALA VAL GLU ASP ALA
SEQRES 11 C 313 TYR ASP ALA ALA LYS TRP VAL ALA ASP ASN TYR ASP LYS
SEQRES 12 C 313 LEU GLY VAL ASP ASN GLY LYS ILE ALA VAL ALA GLY ASP
SEQRES 13 C 313 SER ALA GLY GLY ASN LEU ALA ALA VAL THR ALA ILE MET
SEQRES 14 C 313 ALA ARG ASP ARG GLY GLU SER PHE VAL LYS TYR GLN VAL
SEQRES 15 C 313 LEU ILE TYR PRO ALA VAL ASN LEU THR GLY SER PRO THR
SEQRES 16 C 313 VAL SER ARG VAL GLU TYR SER GLY PRO GLU TYR VAL ILE
SEQRES 17 C 313 LEU THR ALA ASP LEU MET ALA TRP PHE GLY ARG GLN TYR
SEQRES 18 C 313 PHE SER LYS PRO GLN ASP ALA LEU SER PRO TYR ALA SER
SEQRES 19 C 313 PRO ILE PHE ALA ASP LEU SER ASN LEU PRO PRO ALA LEU
SEQRES 20 C 313 VAL ILE THR ALA GLU TYR ASP PRO LEU ARG ASP GLU GLY
SEQRES 21 C 313 GLU LEU TYR ALA HIS LEU LEU LYS THR ARG GLY VAL ARG
SEQRES 22 C 313 ALA VAL ALA VAL ARG TYR ASN GLY VAL ILE HIS GLY PHE
SEQRES 23 C 313 VAL ASN PHE TYR PRO ILE LEU GLU GLU GLY ARG GLU ALA
SEQRES 24 C 313 VAL SER GLN ILE ALA ALA SER ILE LYS SER MET ALA VAL
SEQRES 25 C 313 ALA
SEQRES 1 D 313 MET PRO LEU SER PRO ILE LEU ARG GLN ILE LEU GLN GLN
SEQRES 2 D 313 LEU ALA ALA GLN LEU GLN PHE ARG PRO ASP MET ASP VAL
SEQRES 3 D 313 LYS THR VAL ARG GLU GLN PHE GLU LYS SER SER LEU ILE
SEQRES 4 D 313 LEU VAL LYS MET ALA ASN GLU PRO ILE HIS ARG VAL GLU
SEQRES 5 D 313 ASP ILE THR ILE PRO GLY ARG GLY GLY PRO ILE ARG ALA
SEQRES 6 D 313 ARG VAL TYR ARG PRO ARG ASP GLY GLU ARG LEU PRO ALA
SEQRES 7 D 313 VAL VAL TYR TYR HIS GLY GLY GLY PHE VAL LEU GLY SER
SEQRES 8 D 313 VAL GLU THR HIS ASP HIS VAL CYS ARG ARG LEU ALA ASN
SEQRES 9 D 313 LEU SER GLY ALA VAL VAL VAL SER VAL ASP TYR ARG LEU
SEQRES 10 D 313 ALA PRO GLU HIS LYS PHE PRO ALA ALA VAL GLU ASP ALA
SEQRES 11 D 313 TYR ASP ALA ALA LYS TRP VAL ALA ASP ASN TYR ASP LYS
SEQRES 12 D 313 LEU GLY VAL ASP ASN GLY LYS ILE ALA VAL ALA GLY ASP
SEQRES 13 D 313 SER ALA GLY GLY ASN LEU ALA ALA VAL THR ALA ILE MET
SEQRES 14 D 313 ALA ARG ASP ARG GLY GLU SER PHE VAL LYS TYR GLN VAL
SEQRES 15 D 313 LEU ILE TYR PRO ALA VAL ASN LEU THR GLY SER PRO THR
SEQRES 16 D 313 VAL SER ARG VAL GLU TYR SER GLY PRO GLU TYR VAL ILE
SEQRES 17 D 313 LEU THR ALA ASP LEU MET ALA TRP PHE GLY ARG GLN TYR
SEQRES 18 D 313 PHE SER LYS PRO GLN ASP ALA LEU SER PRO TYR ALA SER
SEQRES 19 D 313 PRO ILE PHE ALA ASP LEU SER ASN LEU PRO PRO ALA LEU
SEQRES 20 D 313 VAL ILE THR ALA GLU TYR ASP PRO LEU ARG ASP GLU GLY
SEQRES 21 D 313 GLU LEU TYR ALA HIS LEU LEU LYS THR ARG GLY VAL ARG
SEQRES 22 D 313 ALA VAL ALA VAL ARG TYR ASN GLY VAL ILE HIS GLY PHE
SEQRES 23 D 313 VAL ASN PHE TYR PRO ILE LEU GLU GLU GLY ARG GLU ALA
SEQRES 24 D 313 VAL SER GLN ILE ALA ALA SER ILE LYS SER MET ALA VAL
SEQRES 25 D 313 ALA
HET SO4 A1314 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 O4 S 2-
FORMUL 6 HOH *368(H2 O)
HELIX 1 1 SER A 4 GLN A 12 1 9
HELIX 2 2 ASP A 25 ASN A 45 1 21
HELIX 3 3 HIS A 95 GLY A 107 1 13
HELIX 4 4 PRO A 124 ASN A 140 1 17
HELIX 5 5 ASN A 140 GLY A 145 1 6
HELIX 6 6 SER A 157 ARG A 173 1 17
HELIX 7 7 THR A 195 TYR A 201 1 7
HELIX 8 8 GLY A 203 VAL A 207 5 5
HELIX 9 9 THR A 210 PHE A 222 1 13
HELIX 10 10 LYS A 224 SER A 230 5 7
HELIX 11 11 SER A 234 ALA A 238 5 5
HELIX 12 12 LEU A 256 ARG A 270 1 15
HELIX 13 13 GLY A 285 TYR A 290 5 6
HELIX 14 14 LEU A 293 MET A 310 1 18
HELIX 15 15 SER B 4 GLN B 12 1 9
HELIX 16 16 ASP B 25 ASN B 45 1 21
HELIX 17 17 HIS B 95 GLY B 107 1 13
HELIX 18 18 PRO B 124 ASN B 140 1 17
HELIX 19 19 ASN B 140 GLY B 145 1 6
HELIX 20 20 SER B 157 ARG B 173 1 17
HELIX 21 21 THR B 195 TYR B 201 1 7
HELIX 22 22 GLY B 203 VAL B 207 5 5
HELIX 23 23 THR B 210 PHE B 222 1 13
HELIX 24 24 LYS B 224 SER B 230 5 7
HELIX 25 25 SER B 234 ALA B 238 5 5
HELIX 26 26 LEU B 256 ARG B 270 1 15
HELIX 27 27 GLY B 285 TYR B 290 5 6
HELIX 28 28 LEU B 293 MET B 310 1 18
HELIX 29 29 SER C 4 ALA C 16 1 13
HELIX 30 30 ASP C 25 ASN C 45 1 21
HELIX 31 31 VAL C 92 THR C 94 5 3
HELIX 32 32 HIS C 95 GLY C 107 1 13
HELIX 33 33 PRO C 124 ASN C 140 1 17
HELIX 34 34 ASN C 140 GLY C 145 1 6
HELIX 35 35 SER C 157 ARG C 173 1 17
HELIX 36 36 THR C 195 TYR C 201 1 7
HELIX 37 37 GLY C 203 VAL C 207 5 5
HELIX 38 38 THR C 210 PHE C 222 1 13
HELIX 39 39 LYS C 224 SER C 230 5 7
HELIX 40 40 SER C 234 ALA C 238 5 5
HELIX 41 41 LEU C 256 ARG C 270 1 15
HELIX 42 42 GLY C 285 TYR C 290 5 6
HELIX 43 43 LEU C 293 MET C 310 1 18
HELIX 44 44 SER D 4 GLN D 13 1 10
HELIX 45 45 ASP D 25 ASN D 45 1 21
HELIX 46 46 VAL D 92 THR D 94 5 3
HELIX 47 47 HIS D 95 GLY D 107 1 13
HELIX 48 48 PRO D 124 ASN D 140 1 17
HELIX 49 49 ASN D 140 GLY D 145 1 6
HELIX 50 50 SER D 157 ARG D 173 1 17
HELIX 51 51 THR D 195 TYR D 201 1 7
HELIX 52 52 GLY D 203 VAL D 207 5 5
HELIX 53 53 THR D 210 PHE D 222 1 13
HELIX 54 54 LYS D 224 SER D 230 5 7
HELIX 55 55 SER D 234 ALA D 238 5 5
HELIX 56 56 LEU D 256 ARG D 270 1 15
HELIX 57 57 GLY D 285 TYR D 290 5 6
HELIX 58 58 LEU D 293 MET D 310 1 18
SHEET 1 AA16 ARG A 50 GLY A 58 0
SHEET 2 AA16 GLY A 61 ARG A 69 -1 O GLY A 61 N GLY A 58
SHEET 3 AA16 VAL A 109 ASP A 114 -1 O VAL A 110 N TYR A 68
SHEET 4 AA16 ALA A 78 TYR A 82 1 O VAL A 79 N VAL A 111
SHEET 5 AA16 ILE A 151 ASP A 156 1 O ALA A 152 N VAL A 80
SHEET 6 AA16 VAL A 178 ILE A 184 1 N LYS A 179 O ILE A 151
SHEET 7 AA16 ALA A 246 TYR A 253 1 O LEU A 247 N LEU A 183
SHEET 8 AA16 ALA A 274 ILE A 283 1 O VAL A 275 N VAL A 248
SHEET 9 AA16 ALA B 274 ILE B 283 -1 O ALA B 276 N ASN A 280
SHEET 10 AA16 ALA B 246 TYR B 253 1 O ALA B 246 N VAL B 275
SHEET 11 AA16 TYR B 180 ILE B 184 1 O GLN B 181 N LEU B 247
SHEET 12 AA16 VAL B 146 ASP B 156 1 O VAL B 153 N VAL B 182
SHEET 13 AA16 LEU B 76 TYR B 82 1 O LEU B 76 N ASP B 147
SHEET 14 AA16 VAL B 109 ASP B 114 1 O VAL B 109 N VAL B 79
SHEET 15 AA16 GLY B 61 ARG B 69 -1 O ARG B 64 N ASP B 114
SHEET 16 AA16 ARG B 50 GLY B 58 -1 O ARG B 50 N ARG B 69
SHEET 1 CA16 ARG C 50 GLY C 58 0
SHEET 2 CA16 GLY C 61 ARG C 69 -1 O GLY C 61 N GLY C 58
SHEET 3 CA16 VAL C 109 ASP C 114 -1 O VAL C 110 N TYR C 68
SHEET 4 CA16 LEU C 76 TYR C 82 1 O PRO C 77 N VAL C 109
SHEET 5 CA16 VAL C 146 ASP C 156 1 N ASP C 147 O LEU C 76
SHEET 6 CA16 VAL C 178 ILE C 184 1 N LYS C 179 O ILE C 151
SHEET 7 CA16 ALA C 246 TYR C 253 1 O LEU C 247 N LEU C 183
SHEET 8 CA16 ALA C 274 ILE C 283 1 O VAL C 275 N VAL C 248
SHEET 9 CA16 ALA D 274 ILE D 283 -1 O ALA D 276 N ASN C 280
SHEET 10 CA16 ALA D 246 TYR D 253 1 O ALA D 246 N VAL D 275
SHEET 11 CA16 TYR D 180 ILE D 184 1 O GLN D 181 N LEU D 247
SHEET 12 CA16 VAL D 146 ASP D 156 1 O VAL D 153 N VAL D 182
SHEET 13 CA16 LEU D 76 TYR D 82 1 O LEU D 76 N ASP D 147
SHEET 14 CA16 VAL D 109 ASP D 114 1 O VAL D 109 N VAL D 79
SHEET 15 CA16 GLY D 61 ARG D 69 -1 O ARG D 64 N ASP D 114
SHEET 16 CA16 ARG D 50 GLY D 58 -1 O ARG D 50 N ARG D 69
CISPEP 1 ALA A 118 PRO A 119 0 4.69
CISPEP 2 PHE A 123 PRO A 124 0 6.69
CISPEP 3 ALA B 118 PRO B 119 0 1.11
CISPEP 4 PHE B 123 PRO B 124 0 7.85
CISPEP 5 ALA C 118 PRO C 119 0 3.83
CISPEP 6 PHE C 123 PRO C 124 0 5.22
CISPEP 7 ALA D 118 PRO D 119 0 5.77
CISPEP 8 PHE D 123 PRO D 124 0 10.21
SITE 1 AC1 5 ASP A 139 ASN A 140 TYR A 141 ASP A 142
SITE 2 AC1 5 LYS A 143
SITE 1 ASA 3 SER A 157 HIS A 284 ASP A 254
SITE 1 ASB 3 SER B 157 HIS B 284 ASP B 254
SITE 1 ASC 3 SER C 157 HIS C 284 ASP C 254
SITE 1 ASD 3 SER D 157 HIS D 284 ASP D 254
CRYST1 57.282 72.335 141.873 90.00 90.19 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.017457 0.000000 0.000058 0.00000
SCALE2 0.000000 0.013825 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007049 0.00000
MTRIX1 1 -0.999790 0.001800 -0.020320 29.56792 1
MTRIX2 1 0.007480 -0.894290 -0.447420 56.28368 1
MTRIX3 1 -0.018980 -0.447480 0.894090 13.51402 1
MTRIX1 2 0.998730 -0.044320 -0.023980 2.20997 1
MTRIX2 2 -0.044070 -0.998970 0.010710 42.67968 1
MTRIX3 2 -0.024430 -0.009640 -0.999660 71.47411 1
MTRIX1 3 -0.999550 0.029840 0.001030 28.20140 1
MTRIX2 3 0.027270 0.898150 0.438850 -13.72702 1
MTRIX3 3 0.012170 0.438680 -0.898560 57.84884 1
MTRIX1 4 -0.998200 0.056630 -0.019830 28.74554 1
MTRIX2 4 0.041340 0.888680 0.456670 -14.69877 1
MTRIX3 4 0.043480 0.455020 -0.889420 56.58555 1
MTRIX1 5 0.999410 -0.033600 0.006500 0.47794 1
MTRIX2 5 -0.033540 -0.999390 -0.009510 43.63300 1
MTRIX3 5 0.006820 0.009290 -0.999930 70.62668 1
MTRIX1 6 -0.999620 0.014850 0.023190 28.12387 1
MTRIX2 6 -0.023670 -0.893520 -0.448390 56.49620 1
MTRIX3 6 0.014060 -0.448770 0.893540 13.09818 1
TER 2407 ALA A 313
TER 4826 ALA B 313
TER 7186 ALA C 313
TER 9584 ALA D 313
MASTER 470 0 1 58 32 0 6 24 9953 4 5 100
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