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HEADER HYDROLASE 04-MAR-16 5IKX
TITLE CRYSTAL STRUCTURE OF THE ALPHA-ESTERASE-7 CARBOXYL ESTERASE (DIMER),
TITLE 2 E3, FROM LUCILIA CUPRINA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LUCILIA CUPRINA;
SOURCE 3 ORGANISM_COMMON: GREEN BOTTLE FLY;
SOURCE 4 ORGANISM_TAXID: 7375;
SOURCE 5 GENE: LCAE7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ORGANOPHOSPHATE, CARBOXYLESTERASE, OLIGERMERIZATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.JACKSON,N.FRASER
REVDAT 1 22-JUN-16 5IKX 0
SPRSDE 22-JUN-16 5IKX 4FG5
JRNL AUTH N.J.FRASER,J.W.LIU,P.D.MABBITT,G.J.CORREY,C.W.COPPIN,
JRNL AUTH 2 M.LETHIER,M.A.PERUGINI,J.M.MURPHY,J.G.OAKESHOTT,M.WEIK,
JRNL AUTH 3 C.J.JACKSON
JRNL TITL EVOLUTION OF PROTEIN QUATERNARY STRUCTURE IN RESPONSE TO
JRNL TITL 2 SELECTIVE PRESSURE FOR INCREASED THERMOSTABILITY.
JRNL REF J.MOL.BIOL. V. 428 2359 2016
JRNL REFN ESSN 1089-8638
JRNL PMID 27016206
JRNL DOI 10.1016/J.JMB.2016.03.014
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 58544
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 3276
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) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3419
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.2370
REMARK 3 BIN FREE R VALUE SET COUNT : 172
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9140
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 376
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.72000
REMARK 3 B22 (A**2) : 14.12000
REMARK 3 B33 (A**2) : -25.84000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -15.41000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.055
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.040
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.142
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.304
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9372 ; 0.007 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12685 ; 1.155 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1136 ; 5.887 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 444 ;37.563 ;24.324
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1634 ;17.695 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;15.816 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1353 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7153 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 6
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 2 A 66
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8150 -4.7350 -5.6640
REMARK 3 T TENSOR
REMARK 3 T11: 0.1335 T22: 0.1499
REMARK 3 T33: 0.2252 T12: 0.0533
REMARK 3 T13: 0.1183 T23: -0.0302
REMARK 3 L TENSOR
REMARK 3 L11: 0.2579 L22: 0.1936
REMARK 3 L33: 1.2130 L12: -0.1835
REMARK 3 L13: -0.2810 L23: 0.3400
REMARK 3 S TENSOR
REMARK 3 S11: 0.0256 S12: 0.0639 S13: 0.0284
REMARK 3 S21: 0.0397 S22: -0.0666 S23: 0.0204
REMARK 3 S31: 0.2067 S32: 0.0574 S33: 0.0410
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 67 A 347
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0060 2.9250 11.0190
REMARK 3 T TENSOR
REMARK 3 T11: 0.1211 T22: 0.1521
REMARK 3 T33: 0.2303 T12: 0.0198
REMARK 3 T13: 0.0958 T23: 0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 0.3809 L22: 0.2588
REMARK 3 L33: 0.4881 L12: 0.1415
REMARK 3 L13: -0.2266 L23: 0.1802
REMARK 3 S TENSOR
REMARK 3 S11: -0.0472 S12: 0.0114 S13: -0.0216
REMARK 3 S21: 0.0229 S22: 0.0483 S23: 0.0104
REMARK 3 S31: 0.0482 S32: 0.0223 S33: -0.0010
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 348 A 570
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9000 22.8480 -0.5770
REMARK 3 T TENSOR
REMARK 3 T11: 0.1725 T22: 0.1025
REMARK 3 T33: 0.1909 T12: 0.0302
REMARK 3 T13: 0.1150 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.8219 L22: 0.2843
REMARK 3 L33: 0.8247 L12: -0.1377
REMARK 3 L13: -0.5586 L23: 0.4247
REMARK 3 S TENSOR
REMARK 3 S11: 0.1167 S12: 0.1049 S13: 0.0369
REMARK 3 S21: -0.0914 S22: -0.0557 S23: -0.0182
REMARK 3 S31: -0.2097 S32: -0.0875 S33: -0.0610
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 2 B 66
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0400 3.5520 -51.9860
REMARK 3 T TENSOR
REMARK 3 T11: 0.1974 T22: 0.1561
REMARK 3 T33: 0.2070 T12: 0.0611
REMARK 3 T13: 0.0738 T23: 0.0293
REMARK 3 L TENSOR
REMARK 3 L11: 0.1943 L22: 0.9427
REMARK 3 L33: 0.9989 L12: -0.3038
REMARK 3 L13: -0.3944 L23: 0.7009
REMARK 3 S TENSOR
REMARK 3 S11: -0.0560 S12: -0.0298 S13: 0.0077
REMARK 3 S21: -0.0718 S22: 0.0382 S23: 0.0008
REMARK 3 S31: -0.0618 S32: 0.0217 S33: 0.0179
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 : B 67 B 347
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4350 -3.9740 -34.9470
REMARK 3 T TENSOR
REMARK 3 T11: 0.0843 T22: 0.1580
REMARK 3 T33: 0.2303 T12: -0.0093
REMARK 3 T13: 0.1141 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 0.3550 L22: 0.0373
REMARK 3 L33: 0.7911 L12: -0.0542
REMARK 3 L13: 0.0859 L23: 0.0030
REMARK 3 S TENSOR
REMARK 3 S11: -0.0659 S12: 0.0231 S13: -0.0125
REMARK 3 S21: -0.0071 S22: 0.0523 S23: -0.0018
REMARK 3 S31: -0.0277 S32: 0.0554 S33: 0.0136
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 348 B 570
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3290 -24.1270 -46.1850
REMARK 3 T TENSOR
REMARK 3 T11: 0.2388 T22: 0.1173
REMARK 3 T33: 0.1952 T12: 0.0300
REMARK 3 T13: 0.0926 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 0.3100 L22: 0.3414
REMARK 3 L33: 0.8386 L12: -0.2460
REMARK 3 L13: 0.1467 L23: -0.0331
REMARK 3 S TENSOR
REMARK 3 S11: -0.0249 S12: 0.0239 S13: -0.0021
REMARK 3 S21: -0.0747 S22: 0.0232 S23: 0.0150
REMARK 3 S31: 0.2323 S32: 0.1215 S33: 0.0017
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 5IKX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218989.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.82655
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62125
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 46.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.31
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.43900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4FNG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, 20% PEG 2K MME, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 292K
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 54.47800
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 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 -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 MET B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
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 LYS A 306 CG CD CE NZ
REMARK 470 VAL A 366 CG1 CG2
REMARK 470 LYS B 46 CG CD CE NZ
REMARK 470 MET B 308 CB CG SD CE
REMARK 470 ARG B 385 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 405 CG CD OE1 OE2
REMARK 470 THR B 436 OG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O TRP B 337 OG SER B 340 2.18
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 LEU B 114 CA - CB - CG ANGL. DEV. = 13.9 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 ILE A 101 -55.69 -121.59
REMARK 500 ASN A 120 116.26 -162.63
REMARK 500 GLU A 142 -175.38 -171.24
REMARK 500 ILE A 154 1.09 -69.71
REMARK 500 SER A 218 -110.68 66.59
REMARK 500 LYS A 270 -78.43 139.60
REMARK 500 ASP A 273 85.94 -66.97
REMARK 500 ASN A 305 7.51 -69.44
REMARK 500 TYR A 350 62.04 -154.48
REMARK 500 PRO A 377 125.72 -37.69
REMARK 500 PHE A 421 -62.44 -125.64
REMARK 500 SER A 437 41.42 -107.86
REMARK 500 ASP A 447 30.70 -142.21
REMARK 500 THR A 472 -22.64 109.00
REMARK 500 SER A 542 -134.60 -129.20
REMARK 500 SER B 218 -120.16 57.65
REMARK 500 LYS B 270 50.31 91.92
REMARK 500 CYS B 372 39.87 -95.47
REMARK 500 PHE B 421 -67.98 -134.79
REMARK 500 HIS B 435 -0.35 -147.03
REMARK 500 PRO B 440 155.60 -48.09
REMARK 500 THR B 472 -24.68 99.52
REMARK 500 ASN B 523 20.93 81.14
REMARK 500 SER B 542 -145.45 -117.35
REMARK 500 HIS B 566 58.03 -119.18
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5IKX A 1 570 UNP Q25252 Q25252_LUCCU 1 570
DBREF 5IKX B 1 570 UNP Q25252 Q25252_LUCCU 1 570
SEQADV 5IKX MET A -6 UNP Q25252 INITIATING METHIONINE
SEQADV 5IKX HIS A -5 UNP Q25252 EXPRESSION TAG
SEQADV 5IKX HIS A -4 UNP Q25252 EXPRESSION TAG
SEQADV 5IKX HIS A -3 UNP Q25252 EXPRESSION TAG
SEQADV 5IKX HIS A -2 UNP Q25252 EXPRESSION TAG
SEQADV 5IKX HIS A -1 UNP Q25252 EXPRESSION TAG
SEQADV 5IKX HIS A 0 UNP Q25252 EXPRESSION TAG
SEQADV 5IKX ALA A 83 UNP Q25252 ASP 83 CONFLICT
SEQADV 5IKX LEU A 364 UNP Q25252 MET 364 CONFLICT
SEQADV 5IKX PHE A 419 UNP Q25252 ILE 419 CONFLICT
SEQADV 5IKX THR A 472 UNP Q25252 ALA 472 CONFLICT
SEQADV 5IKX THR A 505 UNP Q25252 ILE 505 CONFLICT
SEQADV 5IKX GLU A 530 UNP Q25252 LYS 530 CONFLICT
SEQADV 5IKX GLY A 554 UNP Q25252 ASP 554 CONFLICT
SEQADV 5IKX MET B -6 UNP Q25252 INITIATING METHIONINE
SEQADV 5IKX HIS B -5 UNP Q25252 EXPRESSION TAG
SEQADV 5IKX HIS B -4 UNP Q25252 EXPRESSION TAG
SEQADV 5IKX HIS B -3 UNP Q25252 EXPRESSION TAG
SEQADV 5IKX HIS B -2 UNP Q25252 EXPRESSION TAG
SEQADV 5IKX HIS B -1 UNP Q25252 EXPRESSION TAG
SEQADV 5IKX HIS B 0 UNP Q25252 EXPRESSION TAG
SEQADV 5IKX ALA B 83 UNP Q25252 ASP 83 CONFLICT
SEQADV 5IKX LEU B 364 UNP Q25252 MET 364 CONFLICT
SEQADV 5IKX PHE B 419 UNP Q25252 ILE 419 CONFLICT
SEQADV 5IKX THR B 472 UNP Q25252 ALA 472 CONFLICT
SEQADV 5IKX THR B 505 UNP Q25252 ILE 505 CONFLICT
SEQADV 5IKX GLU B 530 UNP Q25252 LYS 530 CONFLICT
SEQADV 5IKX GLY B 554 UNP Q25252 ASP 554 CONFLICT
SEQRES 1 A 577 MET HIS HIS HIS HIS HIS HIS MET ASN PHE ASN VAL SER
SEQRES 2 A 577 LEU MET GLU LYS LEU LYS TRP LYS ILE LYS CYS ILE GLU
SEQRES 3 A 577 ASN LYS PHE LEU ASN TYR ARG LEU THR THR ASN GLU THR
SEQRES 4 A 577 VAL VAL ALA GLU THR GLU TYR GLY LYS VAL LYS GLY VAL
SEQRES 5 A 577 LYS ARG LEU THR VAL TYR ASP ASP SER TYR TYR SER PHE
SEQRES 6 A 577 GLU GLY ILE PRO TYR ALA GLN PRO PRO VAL GLY GLU LEU
SEQRES 7 A 577 ARG PHE LYS ALA PRO GLN ARG PRO THR PRO TRP ALA GLY
SEQRES 8 A 577 VAL ARG ASP CYS CYS ASN HIS LYS ASP LYS SER VAL GLN
SEQRES 9 A 577 VAL ASP PHE ILE THR GLY LYS VAL CYS GLY SER GLU ASP
SEQRES 10 A 577 CYS LEU TYR LEU SER VAL TYR THR ASN ASN LEU ASN PRO
SEQRES 11 A 577 GLU THR LYS ARG PRO VAL LEU VAL TYR ILE HIS GLY GLY
SEQRES 12 A 577 GLY PHE ILE ILE GLY GLU ASN HIS ARG ASP MET TYR GLY
SEQRES 13 A 577 PRO ASP TYR PHE ILE LYS LYS ASP VAL VAL LEU ILE ASN
SEQRES 14 A 577 ILE GLN TYR ARG LEU GLY ALA LEU GLY PHE LEU SER LEU
SEQRES 15 A 577 ASN SER GLU ASP LEU ASN VAL PRO GLY ASN ALA GLY LEU
SEQRES 16 A 577 LYS ASP GLN VAL MET ALA LEU ARG TRP ILE LYS ASN ASN
SEQRES 17 A 577 CYS ALA ASN PHE GLY GLY ASN PRO ASP ASN ILE THR VAL
SEQRES 18 A 577 PHE GLY GLU SER ALA GLY ALA ALA SER THR HIS TYR MET
SEQRES 19 A 577 MET LEU THR GLU GLN THR ARG GLY LEU PHE HIS ARG GLY
SEQRES 20 A 577 ILE LEU MET SER GLY ASN ALA ILE CYS PRO TRP ALA ASN
SEQRES 21 A 577 THR GLN CYS GLN HIS ARG ALA PHE THR LEU ALA LYS LEU
SEQRES 22 A 577 ALA GLY TYR LYS GLY GLU ASP ASN ASP LYS ASP VAL LEU
SEQRES 23 A 577 GLU PHE LEU MET LYS ALA LYS PRO GLN ASP LEU ILE LYS
SEQRES 24 A 577 LEU GLU GLU LYS VAL LEU THR LEU GLU GLU ARG THR ASN
SEQRES 25 A 577 LYS VAL MET PHE PRO PHE GLY PRO THR VAL GLU PRO TYR
SEQRES 26 A 577 GLN THR ALA ASP CYS VAL LEU PRO LYS HIS PRO ARG GLU
SEQRES 27 A 577 MET VAL LYS THR ALA TRP GLY ASN SER ILE PRO THR MET
SEQRES 28 A 577 MET GLY ASN THR SER TYR GLU GLY LEU PHE PHE THR SER
SEQRES 29 A 577 ILE LEU LYS GLN MET PRO LEU LEU VAL LYS GLU LEU GLU
SEQRES 30 A 577 THR CYS VAL ASN PHE VAL PRO SER GLU LEU ALA ASP ALA
SEQRES 31 A 577 GLU ARG THR ALA PRO GLU THR LEU GLU MET GLY ALA LYS
SEQRES 32 A 577 ILE LYS LYS ALA HIS VAL THR GLY GLU THR PRO THR ALA
SEQRES 33 A 577 ASP ASN PHE MET ASP LEU CYS SER HIS PHE TYR PHE TRP
SEQRES 34 A 577 PHE PRO MET HIS ARG LEU LEU GLN LEU ARG PHE ASN HIS
SEQRES 35 A 577 THR SER GLY THR PRO VAL TYR LEU TYR ARG PHE ASP PHE
SEQRES 36 A 577 ASP SER GLU ASP LEU ILE ASN PRO TYR ARG ILE MET ARG
SEQRES 37 A 577 SER GLY ARG GLY VAL LYS GLY VAL SER HIS THR ASP GLU
SEQRES 38 A 577 LEU THR TYR PHE PHE TRP ASN GLN LEU ALA LYS ARG MET
SEQRES 39 A 577 PRO LYS GLU SER ARG GLU TYR LYS THR ILE GLU ARG MET
SEQRES 40 A 577 THR GLY ILE TRP THR GLN PHE ALA THR THR GLY ASN PRO
SEQRES 41 A 577 TYR SER ASN GLU ILE GLU GLY MET GLU ASN VAL SER TRP
SEQRES 42 A 577 ASP PRO ILE GLU LYS SER ASP GLU VAL TYR LYS CYS LEU
SEQRES 43 A 577 ASN ILE SER ASP GLU LEU LYS MET ILE ASP VAL PRO GLU
SEQRES 44 A 577 MET GLY LYS ILE LYS GLN TRP GLU SER MET PHE GLU LYS
SEQRES 45 A 577 HIS ARG ASP LEU PHE
SEQRES 1 B 577 MET HIS HIS HIS HIS HIS HIS MET ASN PHE ASN VAL SER
SEQRES 2 B 577 LEU MET GLU LYS LEU LYS TRP LYS ILE LYS CYS ILE GLU
SEQRES 3 B 577 ASN LYS PHE LEU ASN TYR ARG LEU THR THR ASN GLU THR
SEQRES 4 B 577 VAL VAL ALA GLU THR GLU TYR GLY LYS VAL LYS GLY VAL
SEQRES 5 B 577 LYS ARG LEU THR VAL TYR ASP ASP SER TYR TYR SER PHE
SEQRES 6 B 577 GLU GLY ILE PRO TYR ALA GLN PRO PRO VAL GLY GLU LEU
SEQRES 7 B 577 ARG PHE LYS ALA PRO GLN ARG PRO THR PRO TRP ALA GLY
SEQRES 8 B 577 VAL ARG ASP CYS CYS ASN HIS LYS ASP LYS SER VAL GLN
SEQRES 9 B 577 VAL ASP PHE ILE THR GLY LYS VAL CYS GLY SER GLU ASP
SEQRES 10 B 577 CYS LEU TYR LEU SER VAL TYR THR ASN ASN LEU ASN PRO
SEQRES 11 B 577 GLU THR LYS ARG PRO VAL LEU VAL TYR ILE HIS GLY GLY
SEQRES 12 B 577 GLY PHE ILE ILE GLY GLU ASN HIS ARG ASP MET TYR GLY
SEQRES 13 B 577 PRO ASP TYR PHE ILE LYS LYS ASP VAL VAL LEU ILE ASN
SEQRES 14 B 577 ILE GLN TYR ARG LEU GLY ALA LEU GLY PHE LEU SER LEU
SEQRES 15 B 577 ASN SER GLU ASP LEU ASN VAL PRO GLY ASN ALA GLY LEU
SEQRES 16 B 577 LYS ASP GLN VAL MET ALA LEU ARG TRP ILE LYS ASN ASN
SEQRES 17 B 577 CYS ALA ASN PHE GLY GLY ASN PRO ASP ASN ILE THR VAL
SEQRES 18 B 577 PHE GLY GLU SER ALA GLY ALA ALA SER THR HIS TYR MET
SEQRES 19 B 577 MET LEU THR GLU GLN THR ARG GLY LEU PHE HIS ARG GLY
SEQRES 20 B 577 ILE LEU MET SER GLY ASN ALA ILE CYS PRO TRP ALA ASN
SEQRES 21 B 577 THR GLN CYS GLN HIS ARG ALA PHE THR LEU ALA LYS LEU
SEQRES 22 B 577 ALA GLY TYR LYS GLY GLU ASP ASN ASP LYS ASP VAL LEU
SEQRES 23 B 577 GLU PHE LEU MET LYS ALA LYS PRO GLN ASP LEU ILE LYS
SEQRES 24 B 577 LEU GLU GLU LYS VAL LEU THR LEU GLU GLU ARG THR ASN
SEQRES 25 B 577 LYS VAL MET PHE PRO PHE GLY PRO THR VAL GLU PRO TYR
SEQRES 26 B 577 GLN THR ALA ASP CYS VAL LEU PRO LYS HIS PRO ARG GLU
SEQRES 27 B 577 MET VAL LYS THR ALA TRP GLY ASN SER ILE PRO THR MET
SEQRES 28 B 577 MET GLY ASN THR SER TYR GLU GLY LEU PHE PHE THR SER
SEQRES 29 B 577 ILE LEU LYS GLN MET PRO LEU LEU VAL LYS GLU LEU GLU
SEQRES 30 B 577 THR CYS VAL ASN PHE VAL PRO SER GLU LEU ALA ASP ALA
SEQRES 31 B 577 GLU ARG THR ALA PRO GLU THR LEU GLU MET GLY ALA LYS
SEQRES 32 B 577 ILE LYS LYS ALA HIS VAL THR GLY GLU THR PRO THR ALA
SEQRES 33 B 577 ASP ASN PHE MET ASP LEU CYS SER HIS PHE TYR PHE TRP
SEQRES 34 B 577 PHE PRO MET HIS ARG LEU LEU GLN LEU ARG PHE ASN HIS
SEQRES 35 B 577 THR SER GLY THR PRO VAL TYR LEU TYR ARG PHE ASP PHE
SEQRES 36 B 577 ASP SER GLU ASP LEU ILE ASN PRO TYR ARG ILE MET ARG
SEQRES 37 B 577 SER GLY ARG GLY VAL LYS GLY VAL SER HIS THR ASP GLU
SEQRES 38 B 577 LEU THR TYR PHE PHE TRP ASN GLN LEU ALA LYS ARG MET
SEQRES 39 B 577 PRO LYS GLU SER ARG GLU TYR LYS THR ILE GLU ARG MET
SEQRES 40 B 577 THR GLY ILE TRP THR GLN PHE ALA THR THR GLY ASN PRO
SEQRES 41 B 577 TYR SER ASN GLU ILE GLU GLY MET GLU ASN VAL SER TRP
SEQRES 42 B 577 ASP PRO ILE GLU LYS SER ASP GLU VAL TYR LYS CYS LEU
SEQRES 43 B 577 ASN ILE SER ASP GLU LEU LYS MET ILE ASP VAL PRO GLU
SEQRES 44 B 577 MET GLY LYS ILE LYS GLN TRP GLU SER MET PHE GLU LYS
SEQRES 45 B 577 HIS ARG ASP LEU PHE
FORMUL 3 HOH *376(H2 O)
HELIX 1 AA1 SER A 6 LEU A 27 1 22
HELIX 2 AA2 VAL A 68 ARG A 72 5 5
HELIX 3 AA3 TYR A 152 LYS A 156 5 5
HELIX 4 AA4 LEU A 167 LEU A 173 1 7
HELIX 5 AA5 ASN A 185 CYS A 202 1 18
HELIX 6 AA6 ALA A 203 PHE A 205 5 3
HELIX 7 AA7 SER A 218 THR A 230 1 13
HELIX 8 AA8 GLU A 231 ARG A 234 5 4
HELIX 9 AA9 HIS A 258 ALA A 267 1 10
HELIX 10 AB1 ASN A 274 ALA A 285 1 12
HELIX 11 AB2 LYS A 286 GLU A 294 1 9
HELIX 12 AB3 GLU A 295 VAL A 297 5 3
HELIX 13 AB4 THR A 299 ASN A 305 1 7
HELIX 14 AB5 HIS A 328 LYS A 334 1 7
HELIX 15 AB6 ALA A 336 ILE A 341 5 6
HELIX 16 AB7 TYR A 350 PHE A 354 5 5
HELIX 17 AB8 PHE A 355 MET A 362 1 8
HELIX 18 AB9 PRO A 363 THR A 371 5 9
HELIX 19 AC1 CYS A 372 VAL A 376 5 5
HELIX 20 AC2 ALA A 387 VAL A 402 1 16
HELIX 21 AC3 THR A 408 PHE A 421 1 14
HELIX 22 AC4 PHE A 421 HIS A 435 1 15
HELIX 23 AC5 ASN A 455 ARG A 461 1 7
HELIX 24 AC6 THR A 472 PHE A 478 5 7
HELIX 25 AC7 SER A 491 GLY A 511 1 21
HELIX 26 AC8 GLU A 552 SER A 561 1 10
HELIX 27 AC9 MET A 562 GLU A 564 5 3
HELIX 28 AD1 HIS A 566 PHE A 570 5 5
HELIX 29 AD2 SER B 6 LEU B 27 1 22
HELIX 30 AD3 VAL B 68 ARG B 72 5 5
HELIX 31 AD4 TYR B 152 LYS B 156 5 5
HELIX 32 AD5 LEU B 167 LEU B 173 1 7
HELIX 33 AD6 SER B 177 ASN B 181 5 5
HELIX 34 AD7 ASN B 185 CYS B 202 1 18
HELIX 35 AD8 ALA B 203 PHE B 205 5 3
HELIX 36 AD9 SER B 218 THR B 230 1 13
HELIX 37 AE1 GLU B 231 ARG B 234 5 4
HELIX 38 AE2 CYS B 249 ASN B 253 5 5
HELIX 39 AE3 HIS B 258 ALA B 267 1 10
HELIX 40 AE4 ASN B 274 MET B 283 1 10
HELIX 41 AE5 LYS B 286 GLU B 294 1 9
HELIX 42 AE6 GLU B 295 VAL B 297 5 3
HELIX 43 AE7 THR B 299 ASN B 305 1 7
HELIX 44 AE8 HIS B 328 LYS B 334 1 7
HELIX 45 AE9 THR B 335 ILE B 341 5 7
HELIX 46 AF1 TYR B 350 PHE B 354 5 5
HELIX 47 AF2 PHE B 355 MET B 362 1 8
HELIX 48 AF3 PRO B 363 GLU B 370 5 8
HELIX 49 AF4 CYS B 372 VAL B 376 5 5
HELIX 50 AF5 ALA B 387 VAL B 402 1 16
HELIX 51 AF6 THR B 408 PHE B 421 1 14
HELIX 52 AF7 PHE B 421 THR B 436 1 16
HELIX 53 AF8 PRO B 456 ARG B 461 1 6
HELIX 54 AF9 THR B 472 PHE B 478 5 7
HELIX 55 AG1 SER B 491 GLY B 511 1 21
HELIX 56 AG2 GLU B 552 MET B 562 1 11
SHEET 1 AA1 3 THR A 28 ALA A 35 0
SHEET 2 AA1 3 LYS A 41 LEU A 48 -1 O LYS A 46 N GLU A 31
SHEET 3 AA1 3 VAL A 85 ASP A 87 1 O ARG A 86 N LYS A 43
SHEET 1 AA212 THR A 28 ALA A 35 0
SHEET 2 AA212 LYS A 41 LEU A 48 -1 O LYS A 46 N GLU A 31
SHEET 3 AA212 SER A 54 PRO A 62 -1 O SER A 57 N VAL A 45
SHEET 4 AA212 TYR A 113 THR A 118 -1 O THR A 118 N TYR A 56
SHEET 5 AA212 VAL A 159 ILE A 163 -1 O LEU A 160 N TYR A 117
SHEET 6 AA212 ARG A 127 ILE A 133 1 N LEU A 130 O VAL A 159
SHEET 7 AA212 GLY A 207 GLU A 217 1 O THR A 213 N VAL A 129
SHEET 8 AA212 ARG A 239 MET A 243 1 O ARG A 239 N VAL A 214
SHEET 9 AA212 THR A 343 THR A 348 1 O MET A 344 N LEU A 242
SHEET 10 AA212 TYR A 442 PHE A 446 1 O TYR A 442 N MET A 345
SHEET 11 AA212 LYS A 537 ILE A 541 1 O ILE A 541 N ARG A 445
SHEET 12 AA212 LEU A 545 ASP A 549 -1 O LYS A 546 N ASN A 540
SHEET 1 AA3 2 GLN A 97 VAL A 98 0
SHEET 2 AA3 2 VAL A 105 CYS A 106 -1 O CYS A 106 N GLN A 97
SHEET 1 AA4 3 THR B 28 ALA B 35 0
SHEET 2 AA4 3 LYS B 41 LEU B 48 -1 O GLY B 44 N VAL B 33
SHEET 3 AA4 3 VAL B 85 ASP B 87 1 O ARG B 86 N LYS B 41
SHEET 1 AA512 THR B 28 ALA B 35 0
SHEET 2 AA512 LYS B 41 LEU B 48 -1 O GLY B 44 N VAL B 33
SHEET 3 AA512 SER B 54 PRO B 62 -1 O TYR B 55 N ARG B 47
SHEET 4 AA512 TYR B 113 THR B 118 -1 O THR B 118 N TYR B 56
SHEET 5 AA512 VAL B 159 ILE B 163 -1 O LEU B 160 N TYR B 117
SHEET 6 AA512 ARG B 127 ILE B 133 1 N LEU B 130 O VAL B 159
SHEET 7 AA512 GLY B 207 GLU B 217 1 O THR B 213 N VAL B 129
SHEET 8 AA512 ARG B 239 MET B 243 1 O ARG B 239 N VAL B 214
SHEET 9 AA512 THR B 343 THR B 348 1 O MET B 344 N LEU B 242
SHEET 10 AA512 VAL B 441 PHE B 446 1 O TYR B 442 N MET B 345
SHEET 11 AA512 LYS B 537 ILE B 541 1 O ILE B 541 N ARG B 445
SHEET 12 AA512 LEU B 545 ASP B 549 -1 O LYS B 546 N ASN B 540
SHEET 1 AA6 2 GLN B 97 VAL B 98 0
SHEET 2 AA6 2 VAL B 105 CYS B 106 -1 O CYS B 106 N GLN B 97
CISPEP 1 TYR A 269 LYS A 270 0 -8.36
CISPEP 2 TYR B 269 LYS B 270 0 -13.73
CRYST1 61.767 108.956 92.172 90.00 90.36 90.00 P 1 21 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 0.016190 0.000000 0.000101 0.00000
SCALE2 0.000000 0.009178 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010849 0.00000
TER 4578 PHE A 570
TER 9142 PHE B 570
MASTER 445 0 0 56 34 0 0 6 9516 2 0 90
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