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HEADER HYDROLASE 13-MAY-11 2YIJ
TITLE CRYSTAL STRUCTURE OF PHOSPHOLIPASE A1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOLIPASE A1-IIGAMMA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DAD1-LIKE SEEDLING ESTABLISHMENT-RELATED LIPASE, ATDSEL,
COMPND 5 PHOSPHOLIPASE DSEL, AT4G18550, LIPASE-LIKE PROTEIN;
COMPND 6 EC: 3.1.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_TAXID: 3702;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS HYDROLASE, PHOSPHOLIPASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.LEE
REVDAT 1 30-MAY-12 2YIJ 0
JRNL AUTH I.LEE
JRNL TITL CRYSTAL STRUCTURE OF PHOSPHOLIPASE A1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.00
REMARK 3 NUMBER OF REFLECTIONS : 1264
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) : 0.26344
REMARK 3 R VALUE (WORKING SET) : 0.23112
REMARK 3 FREE R VALUE : 0.26403
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 98.2
REMARK 3 FREE R VALUE TEST SET COUNT : 67394
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) : 2.000
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.051
REMARK 3 REFLECTION IN BIN (WORKING SET) : 87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.240
REMARK 3 BIN FREE R VALUE SET COUNT : 4842
REMARK 3 BIN FREE R VALUE : 0.321
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6190
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 406
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.831
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.06
REMARK 3 B22 (A**2) : 0.01
REMARK 3 B33 (A**2) : -0.03
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.15
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 3.999
REMARK 3 ESU BASED ON FREE R VALUE (A): 4.568
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.000
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.003
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.912
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.887
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED 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 : NULL
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 2YIJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-MAY-11.
REMARK 100 THE PDBE ID CODE IS EBI-48210.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979632, 0.979454,
REMARK 200 0.971679
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 114783
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.70
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 200 DATA REDUNDANCY : 4.4
REMARK 200 R MERGE (I) : 0.11
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.39
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.8
REMARK 200 DATA REDUNDANCY IN SHELL : 8.2
REMARK 200 R MERGE FOR SHELL (I) : 0.27
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.45
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 47.92700
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.3 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 MSE A 1
REMARK 465 LYS A 2
REMARK 465 ARG A 3
REMARK 465 LYS A 4
REMARK 465 LYS A 5
REMARK 465 LYS A 6
REMARK 465 GLU A 7
REMARK 465 GLU A 8
REMARK 465 GLU A 9
REMARK 465 GLU A 10
REMARK 465 GLU A 11
REMARK 465 LYS A 12
REMARK 465 LEU A 13
REMARK 465 ILE A 14
REMARK 465 VAL A 15
REMARK 465 THR A 16
REMARK 465 ARG A 17
REMARK 465 GLU A 18
REMARK 465 ARG A 120
REMARK 465 GLU A 121
REMARK 465 GLY A 122
REMARK 465 LEU A 160
REMARK 465 GLU A 161
REMARK 465 TRP A 162
REMARK 465 VAL A 163
REMARK 465 GLU A 164
REMARK 465 ASP A 165
REMARK 465 ASP A 418
REMARK 465 PHE A 419
REMARK 465 MSE B 1
REMARK 465 LYS B 2
REMARK 465 ARG B 3
REMARK 465 LYS B 4
REMARK 465 LYS B 5
REMARK 465 LYS B 6
REMARK 465 GLU B 7
REMARK 465 GLU B 8
REMARK 465 GLU B 9
REMARK 465 GLU B 10
REMARK 465 GLU B 11
REMARK 465 LYS B 12
REMARK 465 LEU B 13
REMARK 465 ILE B 14
REMARK 465 VAL B 15
REMARK 465 THR B 16
REMARK 465 ARG B 17
REMARK 465 GLU B 18
REMARK 465 PHE B 19
REMARK 465 ALA B 20
REMARK 465 LYS B 21
REMARK 465 GLN B 158
REMARK 465 PRO B 159
REMARK 465 LEU B 160
REMARK 465 GLU B 161
REMARK 465 TRP B 162
REMARK 465 VAL B 163
REMARK 465 GLU B 164
REMARK 465 ASP B 165
REMARK 465 PHE B 166
REMARK 465 GLU B 167
REMARK 465 PHE B 168
REMARK 465 PHE B 419
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 THR A 93 57.30 -92.37
REMARK 500 VAL A 157 -162.86 -106.64
REMARK 500 GLN A 158 -133.12 37.82
REMARK 500 GLU A 167 66.31 38.59
REMARK 500 SER A 236 -124.65 57.75
REMARK 500 ASN A 255 36.30 -91.05
REMARK 500 SER B 236 -123.20 58.22
REMARK 500 ASN B 255 32.87 -90.76
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2YIJ A 1 419 UNP O49523 O49523_ARATH 1 419
DBREF 2YIJ B 1 419 UNP O49523 O49523_ARATH 1 419
SEQRES 1 A 419 MSE LYS ARG LYS LYS LYS GLU GLU GLU GLU GLU LYS LEU
SEQRES 2 A 419 ILE VAL THR ARG GLU PHE ALA LYS ARG TRP ARG ASP LEU
SEQRES 3 A 419 SER GLY GLN ASN HIS TRP LYS GLY MSE LEU GLN PRO LEU
SEQRES 4 A 419 ASP GLN ASP LEU ARG GLU TYR ILE ILE HIS TYR GLY GLU
SEQRES 5 A 419 MSE ALA GLN ALA GLY TYR ASP THR PHE ASN ILE ASN THR
SEQRES 6 A 419 GLU SER GLN PHE ALA GLY ALA SER ILE TYR SER ARG LYS
SEQRES 7 A 419 ASP PHE PHE ALA LYS VAL GLY LEU GLU ILE ALA HIS PRO
SEQRES 8 A 419 TYR THR LYS TYR LYS VAL THR LYS PHE ILE TYR ALA THR
SEQRES 9 A 419 SER ASP ILE HIS VAL PRO GLU SER PHE LEU LEU PHE PRO
SEQRES 10 A 419 ILE SER ARG GLU GLY TRP SER LYS GLU SER ASN TRP MSE
SEQRES 11 A 419 GLY TYR VAL ALA VAL THR ASP ASP GLN GLY THR ALA LEU
SEQRES 12 A 419 LEU GLY ARG ARG ASP ILE VAL VAL SER TRP ARG GLY SER
SEQRES 13 A 419 VAL GLN PRO LEU GLU TRP VAL GLU ASP PHE GLU PHE GLY
SEQRES 14 A 419 LEU VAL ASN ALA ILE LYS ILE PHE GLY GLU ARG ASN ASP
SEQRES 15 A 419 GLN VAL GLN ILE HIS GLN GLY TRP TYR SER ILE TYR MSE
SEQRES 16 A 419 SER GLN ASP GLU ARG SER PRO PHE THR LYS THR ASN ALA
SEQRES 17 A 419 ARG ASP GLN VAL LEU ARG GLU VAL GLY ARG LEU LEU GLU
SEQRES 18 A 419 LYS TYR LYS ASP GLU GLU VAL SER ILE THR ILE CYS GLY
SEQRES 19 A 419 HIS SER LEU GLY ALA ALA LEU ALA THR LEU SER ALA THR
SEQRES 20 A 419 ASP ILE VAL ALA ASN GLY TYR ASN ARG PRO LYS SER ARG
SEQRES 21 A 419 PRO ASP LYS SER CYS PRO VAL THR ALA PHE VAL PHE ALA
SEQRES 22 A 419 SER PRO ARG VAL GLY ASP SER ASP PHE ARG LYS LEU PHE
SEQRES 23 A 419 SER GLY LEU GLU ASP ILE ARG VAL LEU ARG THR ARG ASN
SEQRES 24 A 419 LEU PRO ASP VAL ILE PRO ILE TYR PRO PRO ILE GLY TYR
SEQRES 25 A 419 SER GLU VAL GLY ASP GLU PHE PRO ILE ASP THR ARG LYS
SEQRES 26 A 419 SER PRO TYR MSE LYS SER PRO GLY ASN LEU ALA THR PHE
SEQRES 27 A 419 HIS CYS LEU GLU GLY TYR LEU HIS GLY VAL ALA GLY THR
SEQRES 28 A 419 GLN GLY THR ASN LYS ALA ASP LEU PHE ARG LEU ASP VAL
SEQRES 29 A 419 GLU ARG ALA ILE GLY LEU VAL ASN LYS SER VAL ASP GLY
SEQRES 30 A 419 LEU LYS ASP GLU CYS MSE VAL PRO GLY LYS TRP ARG VAL
SEQRES 31 A 419 LEU LYS ASN LYS GLY MSE ALA GLN GLN ASP ASP GLY SER
SEQRES 32 A 419 TRP GLU LEU VAL ASP HIS GLU ILE ASP ASP ASN GLU ASP
SEQRES 33 A 419 LEU ASP PHE
SEQRES 1 B 419 MSE LYS ARG LYS LYS LYS GLU GLU GLU GLU GLU LYS LEU
SEQRES 2 B 419 ILE VAL THR ARG GLU PHE ALA LYS ARG TRP ARG ASP LEU
SEQRES 3 B 419 SER GLY GLN ASN HIS TRP LYS GLY MSE LEU GLN PRO LEU
SEQRES 4 B 419 ASP GLN ASP LEU ARG GLU TYR ILE ILE HIS TYR GLY GLU
SEQRES 5 B 419 MSE ALA GLN ALA GLY TYR ASP THR PHE ASN ILE ASN THR
SEQRES 6 B 419 GLU SER GLN PHE ALA GLY ALA SER ILE TYR SER ARG LYS
SEQRES 7 B 419 ASP PHE PHE ALA LYS VAL GLY LEU GLU ILE ALA HIS PRO
SEQRES 8 B 419 TYR THR LYS TYR LYS VAL THR LYS PHE ILE TYR ALA THR
SEQRES 9 B 419 SER ASP ILE HIS VAL PRO GLU SER PHE LEU LEU PHE PRO
SEQRES 10 B 419 ILE SER ARG GLU GLY TRP SER LYS GLU SER ASN TRP MSE
SEQRES 11 B 419 GLY TYR VAL ALA VAL THR ASP ASP GLN GLY THR ALA LEU
SEQRES 12 B 419 LEU GLY ARG ARG ASP ILE VAL VAL SER TRP ARG GLY SER
SEQRES 13 B 419 VAL GLN PRO LEU GLU TRP VAL GLU ASP PHE GLU PHE GLY
SEQRES 14 B 419 LEU VAL ASN ALA ILE LYS ILE PHE GLY GLU ARG ASN ASP
SEQRES 15 B 419 GLN VAL GLN ILE HIS GLN GLY TRP TYR SER ILE TYR MSE
SEQRES 16 B 419 SER GLN ASP GLU ARG SER PRO PHE THR LYS THR ASN ALA
SEQRES 17 B 419 ARG ASP GLN VAL LEU ARG GLU VAL GLY ARG LEU LEU GLU
SEQRES 18 B 419 LYS TYR LYS ASP GLU GLU VAL SER ILE THR ILE CYS GLY
SEQRES 19 B 419 HIS SER LEU GLY ALA ALA LEU ALA THR LEU SER ALA THR
SEQRES 20 B 419 ASP ILE VAL ALA ASN GLY TYR ASN ARG PRO LYS SER ARG
SEQRES 21 B 419 PRO ASP LYS SER CYS PRO VAL THR ALA PHE VAL PHE ALA
SEQRES 22 B 419 SER PRO ARG VAL GLY ASP SER ASP PHE ARG LYS LEU PHE
SEQRES 23 B 419 SER GLY LEU GLU ASP ILE ARG VAL LEU ARG THR ARG ASN
SEQRES 24 B 419 LEU PRO ASP VAL ILE PRO ILE TYR PRO PRO ILE GLY TYR
SEQRES 25 B 419 SER GLU VAL GLY ASP GLU PHE PRO ILE ASP THR ARG LYS
SEQRES 26 B 419 SER PRO TYR MSE LYS SER PRO GLY ASN LEU ALA THR PHE
SEQRES 27 B 419 HIS CYS LEU GLU GLY TYR LEU HIS GLY VAL ALA GLY THR
SEQRES 28 B 419 GLN GLY THR ASN LYS ALA ASP LEU PHE ARG LEU ASP VAL
SEQRES 29 B 419 GLU ARG ALA ILE GLY LEU VAL ASN LYS SER VAL ASP GLY
SEQRES 30 B 419 LEU LYS ASP GLU CYS MSE VAL PRO GLY LYS TRP ARG VAL
SEQRES 31 B 419 LEU LYS ASN LYS GLY MSE ALA GLN GLN ASP ASP GLY SER
SEQRES 32 B 419 TRP GLU LEU VAL ASP HIS GLU ILE ASP ASP ASN GLU ASP
SEQRES 33 B 419 LEU ASP PHE
MODRES 2YIJ MSE A 35 MET SELENOMETHIONINE
MODRES 2YIJ MSE A 53 MET SELENOMETHIONINE
MODRES 2YIJ MSE A 130 MET SELENOMETHIONINE
MODRES 2YIJ MSE A 195 MET SELENOMETHIONINE
MODRES 2YIJ MSE A 329 MET SELENOMETHIONINE
MODRES 2YIJ MSE A 383 MET SELENOMETHIONINE
MODRES 2YIJ MSE A 396 MET SELENOMETHIONINE
MODRES 2YIJ MSE B 35 MET SELENOMETHIONINE
MODRES 2YIJ MSE B 53 MET SELENOMETHIONINE
MODRES 2YIJ MSE B 130 MET SELENOMETHIONINE
MODRES 2YIJ MSE B 195 MET SELENOMETHIONINE
MODRES 2YIJ MSE B 329 MET SELENOMETHIONINE
MODRES 2YIJ MSE B 383 MET SELENOMETHIONINE
MODRES 2YIJ MSE B 396 MET SELENOMETHIONINE
HET MSE A 35 8
HET MSE A 53 8
HET MSE A 130 8
HET MSE A 195 8
HET MSE A 329 8
HET MSE A 383 8
HET MSE A 396 8
HET MSE B 35 8
HET MSE B 53 8
HET MSE B 130 8
HET MSE B 195 8
HET MSE B 329 8
HET MSE B 383 8
HET MSE B 396 8
HETNAM MSE SELENOMETHIONINE
FORMUL 3 MSE 14(C5 H11 N O2 SE)
FORMUL 4 HOH *406(H2 O)
HELIX 1 1 ARG A 22 SER A 27 1 6
HELIX 2 2 ASP A 40 THR A 60 1 21
HELIX 3 3 ASP A 79 VAL A 84 1 6
HELIX 4 4 ASP A 137 GLY A 145 1 9
HELIX 5 5 ALA A 173 GLY A 178 1 6
HELIX 6 6 GLU A 179 ASP A 182 5 4
HELIX 7 7 GLN A 188 SER A 196 1 9
HELIX 8 8 ASN A 207 TYR A 223 1 17
HELIX 9 9 SER A 236 ASN A 252 1 17
HELIX 10 10 ASP A 279 GLY A 288 1 10
HELIX 11 11 VAL A 303 TYR A 307 5 5
HELIX 12 12 ASP A 322 SER A 326 5 5
HELIX 13 13 ASN A 334 CYS A 340 1 7
HELIX 14 14 CYS A 340 THR A 351 1 12
HELIX 15 15 ALA A 367 SER A 374 5 8
HELIX 16 16 LYS A 379 MSE A 383 5 5
HELIX 17 17 LEU A 391 LYS A 394 5 4
HELIX 18 18 ARG B 22 SER B 27 1 6
HELIX 19 19 ASP B 40 PHE B 61 1 22
HELIX 20 20 ASP B 79 VAL B 84 1 6
HELIX 21 21 ASP B 137 GLY B 145 1 9
HELIX 22 22 ALA B 173 GLY B 178 1 6
HELIX 23 23 GLU B 179 ASP B 182 5 4
HELIX 24 24 GLN B 188 SER B 196 1 9
HELIX 25 25 ASN B 207 TYR B 223 1 17
HELIX 26 26 SER B 236 ASN B 252 1 17
HELIX 27 27 ASP B 279 GLY B 288 1 10
HELIX 28 28 VAL B 303 TYR B 307 5 5
HELIX 29 29 ASP B 322 SER B 326 5 5
HELIX 30 30 ASN B 334 CYS B 340 1 7
HELIX 31 31 CYS B 340 THR B 351 1 12
HELIX 32 32 ALA B 367 SER B 374 5 8
HELIX 33 33 LYS B 379 MSE B 383 5 5
HELIX 34 34 LEU B 391 LYS B 394 5 4
SHEET 1 AA 7 TYR A 95 ALA A 103 0
SHEET 2 AA 7 ASN A 128 THR A 136 -1 O ASN A 128 N ALA A 103
SHEET 3 AA 7 ARG A 147 TRP A 153 -1 O ASP A 148 N THR A 136
SHEET 4 AA 7 VAL A 228 HIS A 235 1 O SER A 229 N ILE A 149
SHEET 5 AA 7 VAL A 267 PHE A 272 1 O THR A 268 N ILE A 232
SHEET 6 AA 7 ILE A 292 ASN A 299 1 O ARG A 293 N ALA A 269
SHEET 7 AA 7 ASP A 317 ILE A 321 1 O ASP A 317 N ARG A 296
SHEET 1 AB 2 LEU A 170 ASN A 172 0
SHEET 2 AB 2 GLN A 185 HIS A 187 -1 O ILE A 186 N VAL A 171
SHEET 1 AC 2 MSE A 396 GLN A 398 0
SHEET 2 AC 2 TRP A 404 LEU A 406 -1 O GLU A 405 N ALA A 397
SHEET 1 BA 7 TYR B 95 ALA B 103 0
SHEET 2 BA 7 ASN B 128 THR B 136 -1 O ASN B 128 N ALA B 103
SHEET 3 BA 7 ARG B 147 TRP B 153 -1 O ASP B 148 N THR B 136
SHEET 4 BA 7 VAL B 228 HIS B 235 1 O SER B 229 N ILE B 149
SHEET 5 BA 7 VAL B 267 PHE B 272 1 O THR B 268 N ILE B 232
SHEET 6 BA 7 ILE B 292 ASN B 299 1 O ARG B 293 N ALA B 269
SHEET 7 BA 7 ASP B 317 ILE B 321 1 O ASP B 317 N ARG B 296
SHEET 1 BB 2 LEU B 170 ASN B 172 0
SHEET 2 BB 2 GLN B 185 HIS B 187 -1 O ILE B 186 N VAL B 171
SHEET 1 BC 2 MSE B 396 GLN B 398 0
SHEET 2 BC 2 TRP B 404 LEU B 406 -1 O GLU B 405 N ALA B 397
LINK C GLY A 34 N MSE A 35 1555 1555 1.31
LINK C MSE A 35 N LEU A 36 1555 1555 1.33
LINK C GLU A 52 N MSE A 53 1555 1555 1.33
LINK C MSE A 53 N ALA A 54 1555 1555 1.32
LINK C TRP A 129 N MSE A 130 1555 1555 1.29
LINK C MSE A 130 N GLY A 131 1555 1555 1.32
LINK C TYR A 194 N MSE A 195 1555 1555 1.32
LINK C MSE A 195 N SER A 196 1555 1555 1.31
LINK C TYR A 328 N MSE A 329 1555 1555 1.32
LINK C MSE A 329 N LYS A 330 1555 1555 1.32
LINK C CYS A 382 N MSE A 383 1555 1555 1.31
LINK C MSE A 383 N VAL A 384 1555 1555 1.31
LINK C GLY A 395 N MSE A 396 1555 1555 1.30
LINK C MSE A 396 N ALA A 397 1555 1555 1.32
LINK C GLY B 34 N MSE B 35 1555 1555 1.31
LINK C MSE B 35 N LEU B 36 1555 1555 1.32
LINK C GLU B 52 N MSE B 53 1555 1555 1.32
LINK C MSE B 53 N ALA B 54 1555 1555 1.32
LINK C TRP B 129 N MSE B 130 1555 1555 1.30
LINK C MSE B 130 N GLY B 131 1555 1555 1.30
LINK C TYR B 194 N MSE B 195 1555 1555 1.32
LINK C MSE B 195 N SER B 196 1555 1555 1.31
LINK C TYR B 328 N MSE B 329 1555 1555 1.32
LINK C MSE B 329 N LYS B 330 1555 1555 1.32
LINK C CYS B 382 N MSE B 383 1555 1555 1.31
LINK C MSE B 383 N VAL B 384 1555 1555 1.31
LINK C GLY B 395 N MSE B 396 1555 1555 1.31
LINK C MSE B 396 N ALA B 397 1555 1555 1.32
CISPEP 1 GLN A 37 PRO A 38 0 -0.30
CISPEP 2 TYR A 307 PRO A 308 0 -8.77
CISPEP 3 SER A 331 PRO A 332 0 0.83
CISPEP 4 GLN B 37 PRO B 38 0 -0.27
CISPEP 5 TYR B 307 PRO B 308 0 -16.86
CISPEP 6 SER B 331 PRO B 332 0 -0.94
CRYST1 73.223 95.854 78.891 90.00 105.31 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 0.013657 0.000000 0.003739 0.00000
SCALE2 0.000000 0.010433 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013142 0.00000
TER 3116 LEU A 417
TER 6192 ASP B 418
MASTER 318 0 14 34 22 0 0 6 6596 2 140 66
END |