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HEADER HYDROLASE 27-FEB-13 4JEI
TITLE NONGLYCOSYLATED YARROWIA LIPOLYTICA LIP2 LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 34-334;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: YARROWIA LIPOLYTICA;
SOURCE 3 ORGANISM_TAXID: 4952;
SOURCE 4 GENE: LIP2;
SOURCE 5 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ALPHA BETA HYDROLASE FOLD, LIPOLYTIC ENZYME, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.ALOULOU,A.BENAROUCHE,D.PUCCINELLI,S.SPINELLI,J.-F.CAVALIER,
AUTHOR 2 C.CAMBILLAU,F.CARRIERE
REVDAT 1 13-MAR-13 4JEI 0
JRNL AUTH A.ALOULOU,A.BENAROUCHE,D.PUCCINELLI,S.SPINELLI,
JRNL AUTH 2 J.-F.CAVALIER,C.CAMBILLAU,F.CARRIERE
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF
JRNL TITL 2 NON-GLYCOSYLATED YARROWIA LIPOLYTICA LIP2 LIPASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 21618
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) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 1112
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 11
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.73
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.51
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2797
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2641
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2650
REMARK 3 BIN R VALUE (WORKING SET) : 0.2636
REMARK 3 BIN FREE R VALUE : 0.2734
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.26
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 147
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2334
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 67.97
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -13.41770
REMARK 3 B22 (A**2) : -13.41770
REMARK 3 B33 (A**2) : 26.83540
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.37
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.28
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.22
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.26
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.22
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.880
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.842
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2399 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3272 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 788 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 65 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 349 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2399 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 310 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2960 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.15
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.93
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 22.22
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: {A|2 - A|30}
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5216 48.2069 22.4226
REMARK 3 T TENSOR
REMARK 3 T11: -0.0059 T22: -0.0021
REMARK 3 T33: 0.0026 T12: 0.0063
REMARK 3 T13: 0.0297 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.4040 L22: 0.0142
REMARK 3 L33: 0.0000 L12: -0.1876
REMARK 3 L13: -0.0147 L23: 0.0916
REMARK 3 S TENSOR
REMARK 3 S11: -0.0018 S12: 0.0008 S13: 0.0002
REMARK 3 S21: 0.0000 S22: 0.0023 S23: 0.0021
REMARK 3 S31: 0.0073 S32: -0.0068 S33: -0.0005
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: {A|31 - A|60}
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7613 59.4022 33.7561
REMARK 3 T TENSOR
REMARK 3 T11: -0.0006 T22: 0.0091
REMARK 3 T33: -0.0125 T12: 0.0102
REMARK 3 T13: 0.0056 T23: -0.0059
REMARK 3 L TENSOR
REMARK 3 L11: 0.0174 L22: 0.0315
REMARK 3 L33: 0.0958 L12: -0.0071
REMARK 3 L13: 0.0321 L23: 0.1218
REMARK 3 S TENSOR
REMARK 3 S11: -0.0005 S12: 0.0004 S13: 0.0041
REMARK 3 S21: 0.0011 S22: 0.0009 S23: -0.0024
REMARK 3 S31: -0.0039 S32: 0.0019 S33: -0.0004
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: {A|61 - A|90}
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7682 54.1969 24.9924
REMARK 3 T TENSOR
REMARK 3 T11: -0.0072 T22: 0.0009
REMARK 3 T33: -0.0142 T12: 0.0090
REMARK 3 T13: 0.0144 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 0.2986 L22: 0.1189
REMARK 3 L33: 0.0449 L12: -0.2047
REMARK 3 L13: -0.0143 L23: 0.1102
REMARK 3 S TENSOR
REMARK 3 S11: -0.0030 S12: 0.0000 S13: 0.0015
REMARK 3 S21: 0.0023 S22: 0.0036 S23: -0.0038
REMARK 3 S31: 0.0010 S32: 0.0036 S33: -0.0006
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: {A|91 - A|120}
REMARK 3 ORIGIN FOR THE GROUP (A): 24.7949 49.2930 8.2665
REMARK 3 T TENSOR
REMARK 3 T11: -0.0002 T22: 0.0056
REMARK 3 T33: -0.0006 T12: 0.0054
REMARK 3 T13: 0.0047 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 0.1865 L22: -0.0739
REMARK 3 L33: 0.1473 L12: -0.0443
REMARK 3 L13: -0.2829 L23: 0.0434
REMARK 3 S TENSOR
REMARK 3 S11: 0.0009 S12: 0.0000 S13: -0.0005
REMARK 3 S21: -0.0012 S22: -0.0001 S23: -0.0010
REMARK 3 S31: 0.0003 S32: 0.0039 S33: -0.0008
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: {A|121 - A|150}
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6356 46.6851 19.3255
REMARK 3 T TENSOR
REMARK 3 T11: -0.0098 T22: 0.0101
REMARK 3 T33: -0.0140 T12: 0.0096
REMARK 3 T13: 0.0181 T23: -0.0024
REMARK 3 L TENSOR
REMARK 3 L11: 0.5024 L22: -0.4097
REMARK 3 L33: 0.0000 L12: -0.3169
REMARK 3 L13: -0.0522 L23: 0.1762
REMARK 3 S TENSOR
REMARK 3 S11: -0.0015 S12: -0.0026 S13: -0.0056
REMARK 3 S21: 0.0039 S22: 0.0027 S23: -0.0119
REMARK 3 S31: 0.0019 S32: 0.0041 S33: -0.0011
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: {A|151 - A|180}
REMARK 3 ORIGIN FOR THE GROUP (A): 21.4088 43.7213 24.0350
REMARK 3 T TENSOR
REMARK 3 T11: -0.0045 T22: 0.0066
REMARK 3 T33: -0.0058 T12: 0.0168
REMARK 3 T13: 0.0190 T23: 0.0031
REMARK 3 L TENSOR
REMARK 3 L11: 0.2262 L22: -0.0558
REMARK 3 L33: 0.1258 L12: -0.1797
REMARK 3 L13: -0.2817 L23: -0.0493
REMARK 3 S TENSOR
REMARK 3 S11: 0.0027 S12: -0.0055 S13: -0.0068
REMARK 3 S21: 0.0051 S22: -0.0017 S23: -0.0046
REMARK 3 S31: 0.0050 S32: 0.0003 S33: -0.0009
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: {A|181 - A|210}
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7880 39.4067 13.5100
REMARK 3 T TENSOR
REMARK 3 T11: -0.0014 T22: -0.0083
REMARK 3 T33: -0.0017 T12: 0.0125
REMARK 3 T13: 0.0171 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.1145 L22: -0.0304
REMARK 3 L33: 0.0360 L12: -0.0904
REMARK 3 L13: -0.1904 L23: -0.0107
REMARK 3 S TENSOR
REMARK 3 S11: -0.0011 S12: 0.0033 S13: -0.0049
REMARK 3 S21: -0.0007 S22: 0.0024 S23: 0.0015
REMARK 3 S31: 0.0024 S32: -0.0007 S33: -0.0013
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: {A|211 - A|240}
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8161 45.5791 12.9869
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: -0.0017
REMARK 3 T33: -0.0041 T12: 0.0069
REMARK 3 T13: 0.0177 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 0.1872 L22: 0.1278
REMARK 3 L33: 0.0673 L12: -0.1948
REMARK 3 L13: -0.1215 L23: 0.2549
REMARK 3 S TENSOR
REMARK 3 S11: -0.0028 S12: 0.0059 S13: -0.0043
REMARK 3 S21: -0.0036 S22: 0.0017 S23: 0.0048
REMARK 3 S31: -0.0005 S32: 0.0002 S33: 0.0011
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: {A|241 - A|270}
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8354 48.3098 14.3453
REMARK 3 T TENSOR
REMARK 3 T11: -0.0115 T22: -0.0012
REMARK 3 T33: -0.0066 T12: 0.0048
REMARK 3 T13: 0.0174 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: -0.0628 L22: 0.0839
REMARK 3 L33: 0.0000 L12: 0.0303
REMARK 3 L13: -0.1428 L23: -0.0990
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: 0.0005 S13: -0.0058
REMARK 3 S21: -0.0014 S22: 0.0010 S23: 0.0011
REMARK 3 S31: 0.0009 S32: -0.0052 S33: -0.0008
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: {A|271 - A|300}
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3320 58.0454 12.6490
REMARK 3 T TENSOR
REMARK 3 T11: 0.0191 T22: 0.0192
REMARK 3 T33: 0.0248 T12: 0.0083
REMARK 3 T13: -0.0055 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.7983 L22: 0.6325
REMARK 3 L33: 0.2286 L12: -0.2559
REMARK 3 L13: -0.3366 L23: -0.0398
REMARK 3 S TENSOR
REMARK 3 S11: -0.0033 S12: 0.0153 S13: 0.0114
REMARK 3 S21: -0.0122 S22: 0.0045 S23: 0.0087
REMARK 3 S31: -0.0038 S32: -0.0053 S33: -0.0013
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4JEI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-FEB-13.
REMARK 100 THE RCSB ID CODE IS RCSB077944.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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) : 0.931
REMARK 200 MONOCHROMATOR : BENT CYLINDRICAL MIRROR
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21708
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 12.000
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 10.00
REMARK 200 R MERGE FOR SHELL (I) : 56.00000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.700
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: 1DTE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 75.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M LI2SO4, 2% PEG 8000 (PH 6.5).,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z
REMARK 290 10555 -Y,-X,-Z+1/2
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/2
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 85.13600
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 85.13600
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 85.13600
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 85.13600
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 85.13600
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 85.13600
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 VAL A 1
REMARK 465 ILE A 301
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 GLN A 281 CG CD OE1 NE2
REMARK 470 GLN A 282 CG CD OE1 NE2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 36 NZ
REMARK 480 LEU A 45 CB CG CD1 CD2
REMARK 480 ASP A 93 CG
REMARK 480 GLU A 149 OE1 OE2
REMARK 480 ILE A 173 CD1
REMARK 480 LYS A 215 NZ
REMARK 480 LYS A 271 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 PHE A 41 68.19 -166.57
REMARK 500 CYS A 43 23.59 -147.64
REMARK 500 LEU A 45 30.54 -88.74
REMARK 500 LYS A 79 61.23 60.55
REMARK 500 ILE A 100 58.46 -113.30
REMARK 500 ALA A 103 75.58 -113.60
REMARK 500 SER A 162 -124.64 59.67
REMARK 500 ASN A 178 32.35 -89.73
REMARK 500 CYS A 273 -142.26 -114.77
REMARK 500 GLN A 282 65.37 -106.94
REMARK 500 PHE A 293 -50.99 67.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 LEU A 45 23.8 L L OUTSIDE RANGE
REMARK 500 ARG A 63 23.6 L L OUTSIDE RANGE
REMARK 500 ILE A 100 24.4 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 442 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH A 444 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH A 445 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH A 461 DISTANCE = 10.77 ANGSTROMS
REMARK 525 HOH A 475 DISTANCE = 10.01 ANGSTROMS
REMARK 525 HOH A 487 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH A 495 DISTANCE = 5.63 ANGSTROMS
REMARK 525 HOH A 505 DISTANCE = 7.23 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3O0D RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THR88 AND THR96 ARE VARIENTS OF THE PROTEIN.
DBREF 4JEI A 1 301 UNP E0A7J0 E0A7J0_YARLL 34 334
SEQADV 4JEI THR A 88 UNP E0A7J0 ILE 121 SEE REMARK 999
SEQADV 4JEI THR A 96 UNP E0A7J0 SER 129 SEE REMARK 999
SEQADV 4JEI GLN A 113 UNP E0A7J0 ASN 146 ENGINEERED MUTATION
SEQADV 4JEI GLN A 134 UNP E0A7J0 ASN 167 ENGINEERED MUTATION
SEQRES 1 A 301 VAL TYR THR SER THR GLU THR SER HIS ILE ASP GLN GLU
SEQRES 2 A 301 SER TYR ASN PHE PHE GLU LYS TYR ALA ARG LEU ALA ASN
SEQRES 3 A 301 ILE GLY TYR CYS VAL GLY PRO GLY THR LYS ILE PHE LYS
SEQRES 4 A 301 PRO PHE ASN CYS GLY LEU GLN CYS ALA HIS PHE PRO ASN
SEQRES 5 A 301 VAL GLU LEU ILE GLU GLU PHE HIS ASP PRO ARG LEU ILE
SEQRES 6 A 301 PHE ASP VAL SER GLY TYR LEU ALA VAL ASP HIS ALA SER
SEQRES 7 A 301 LYS GLN ILE TYR LEU VAL ILE ARG GLY THR HIS SER LEU
SEQRES 8 A 301 GLU ASP VAL ILE THR ASP ILE ARG ILE MET GLN ALA PRO
SEQRES 9 A 301 LEU THR ASN PHE ASP LEU ALA ALA GLN ILE SER SER THR
SEQRES 10 A 301 ALA THR CYS ASP ASP CYS LEU VAL HIS ASN GLY PHE ILE
SEQRES 11 A 301 GLN SER TYR GLN ASN THR TYR ASN GLN ILE GLY PRO LYS
SEQRES 12 A 301 LEU ASP SER VAL ILE GLU GLN TYR PRO ASP TYR GLN ILE
SEQRES 13 A 301 ALA VAL THR GLY HIS SER LEU GLY GLY ALA ALA ALA LEU
SEQRES 14 A 301 LEU PHE GLY ILE ASN LEU LYS VAL ASN GLY HIS ASP PRO
SEQRES 15 A 301 LEU VAL VAL THR LEU GLY GLN PRO ILE VAL GLY ASN ALA
SEQRES 16 A 301 GLY PHE ALA ASN TRP VAL ASP LYS LEU PHE PHE GLY GLN
SEQRES 17 A 301 GLU ASN PRO ASP VAL SER LYS VAL SER LYS ASP ARG LYS
SEQRES 18 A 301 LEU TYR ARG ILE THR HIS ARG GLY ASP ILE VAL PRO GLN
SEQRES 19 A 301 VAL PRO PHE TRP ASP GLY TYR GLN HIS CYS SER GLY GLU
SEQRES 20 A 301 VAL PHE ILE ASP TRP PRO LEU ILE HIS PRO PRO LEU SER
SEQRES 21 A 301 ASN VAL VAL MET CYS GLN GLY GLN SER ASN LYS GLN CYS
SEQRES 22 A 301 SER ALA GLY ASN THR LEU LEU GLN GLN VAL ASN VAL ILE
SEQRES 23 A 301 GLY ASN HIS LEU GLN TYR PHE VAL THR GLU GLY VAL CYS
SEQRES 24 A 301 GLY ILE
FORMUL 2 HOH *110(H2 O)
HELIX 1 1 ASP A 11 GLY A 28 1 18
HELIX 2 2 TYR A 29 VAL A 31 5 3
HELIX 3 3 GLN A 46 PHE A 50 5 5
HELIX 4 4 SER A 90 ILE A 100 1 11
HELIX 5 5 ASP A 109 ALA A 111 5 3
HELIX 6 6 ASN A 127 TYR A 151 1 25
HELIX 7 7 SER A 162 ASN A 178 1 17
HELIX 8 8 ASN A 194 GLY A 207 1 14
HELIX 9 9 ILE A 231 VAL A 235 5 5
HELIX 10 10 PRO A 258 SER A 260 5 3
HELIX 11 11 CYS A 273 ASN A 277 5 5
HELIX 12 12 ASN A 284 GLN A 291 1 8
SHEET 1 A10 VAL A 53 HIS A 60 0
SHEET 2 A10 VAL A 68 ASP A 75 -1 O VAL A 74 N GLU A 54
SHEET 3 A10 GLN A 80 GLY A 87 -1 O TYR A 82 N ALA A 73
SHEET 4 A10 GLN A 155 HIS A 161 1 O ALA A 157 N ILE A 81
SHEET 5 A10 LEU A 183 LEU A 187 1 O LEU A 183 N VAL A 158
SHEET 6 A10 LEU A 222 HIS A 227 1 O ILE A 225 N THR A 186
SHEET 7 A10 GLU A 247 ILE A 250 1 O VAL A 248 N THR A 226
SHEET 8 A10 VAL A 262 GLY A 267 -1 O VAL A 263 N PHE A 249
SHEET 9 A10 THR A 3 SER A 8 -1 N SER A 8 O MET A 264
SHEET 10 A10 SER A 269 ASN A 270 1 O SER A 269 N SER A 4
SHEET 1 B 2 LEU A 105 ASN A 107 0
SHEET 2 B 2 LEU A 124 HIS A 126 -1 O VAL A 125 N THR A 106
SSBOND 1 CYS A 30 CYS A 299 1555 1555 2.03
SSBOND 2 CYS A 43 CYS A 47 1555 1555 2.03
SSBOND 3 CYS A 120 CYS A 123 1555 1555 2.04
SSBOND 4 CYS A 265 CYS A 273 1555 1555 2.03
CISPEP 1 LYS A 39 PRO A 40 0 2.61
CISPEP 2 VAL A 235 PRO A 236 0 1.43
CISPEP 3 SER A 245 GLY A 246 0 0.40
CRYST1 116.693 116.693 170.272 90.00 90.00 120.00 P 63 2 2 12
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 0.008569 0.004948 0.000000 0.00000
SCALE2 0.000000 0.009895 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005873 0.00000
TER 2335 GLY A 300
MASTER 510 0 0 12 12 0 0 6 2444 1 8 24
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