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HEADER UNKNOWN FUNCTION 02-MAY-12 4EZI
TITLE CRYSTAL STRUCTURE OF A HYPOTHETICAL PROTEIN (LPG1103) FROM LEGIONELLA
TITLE 2 PNEUMOPHILA SUBSP. PNEUMOPHILA STR. PHILADELPHIA 1 AT 1.15 A
TITLE 3 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEGIONELLA PNEUMOPHILA SUBSP. PNEUMOPHILA STR.
SOURCE 3 PHILADELPHIA 1;
SOURCE 4 ORGANISM_TAXID: 272624;
SOURCE 5 STRAIN: PHILADELPHIA 1 / ATCC 33152 / DSM 7513;
SOURCE 6 GENE: LPG1103;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: PB1;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS ALPHA-BETA HYDROLASES FOLD, STRUCTURAL GENOMICS, JOINT CENTER FOR
KEYWDS 2 STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-
KEYWDS 3 BIOLOGY, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 27-JUN-12 4EZI 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF A HYPOTHETICAL PROTEIN (LPG1103) FROM
JRNL TITL 2 LEGIONELLA PNEUMOPHILA SUBSP. PNEUMOPHILA STR. PHILADELPHIA
JRNL TITL 3 1 AT 1.15 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 131826
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) : 0.137
REMARK 3 R VALUE (WORKING SET) : 0.135
REMARK 3 FREE R VALUE : 0.157
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6631
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) : 1.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9084
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE SET COUNT : 545
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2962
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 536
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 9.25
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.20000
REMARK 3 B22 (A**2) : -0.11000
REMARK 3 B33 (A**2) : -0.09000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.032
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.032
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.020
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.002
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.980
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.975
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3292 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2214 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4507 ; 1.428 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5439 ; 0.951 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 416 ; 5.845 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 160 ;37.149 ;24.563
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 541 ;11.786 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;21.892 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 485 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3696 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 680 ; 0.002 ; 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): 1972 ; 1.898 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 778 ; 1.390 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3221 ; 2.691 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1320 ; 3.642 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1269 ; 5.188 ;11.000
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 5506 ; 1.464 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 539 ; 6.748 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 5395 ; 3.568 ; 3.000
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. A MET-INHIBITION PROTOCOL WAS USED FOR
REMARK 3 SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75
REMARK 3 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 3. POLYETHYLENE GLYCOL (PEG) AND CHLORIDE (CL)
REMARK 3 FROM THE CRYSTALLIZATION SOLUTION HAVE BEEN MODELED INTO THE
REMARK 3 STRUCTURE.
REMARK 4
REMARK 4 4EZI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-12.
REMARK 100 THE RCSB ID CODE IS RCSB072264.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97916
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : VERTICAL FOCUSING MIRROR; DOUBLE
REMARK 200 CRYSTAL SI(111) MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 131916
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.150
REMARK 200 RESOLUTION RANGE LOW (A) : 28.637
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10600
REMARK 200 FOR THE DATA SET : 7.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.78700
REMARK 200 R SYM FOR SHELL (I) : 0.78700
REMARK 200 FOR SHELL : 1.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD,SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.20M SODIUM ACETATE, 30.00%
REMARK 280 POLYETHYLENE GLYCOL 4000, 0.1M TRIS HYDROCHLORIDE PH 8.5,
REMARK 280 NANODROP, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 25.43750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.27450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.74400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.27450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.43750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.74400
REMARK 290 SMTRY3 4 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: 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 GLY A 0
REMARK 465 ALA A 28
REMARK 465 LEU A 29
REMARK 465 GLU A 30
REMARK 465 HIS A 31
REMARK 465 LYS A 403
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 GLU A 32 CG CD OE1 OE2
REMARK 470 LYS A 53 CE NZ
REMARK 470 MSE A 401 CG SE CE
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 ASN A 120 62.78 37.89
REMARK 500 SER A 134 -64.05 -90.37
REMARK 500 TYR A 144 157.60 86.64
REMARK 500 SER A 195 -123.44 63.74
REMARK 500 PHE A 365 58.66 -91.35
REMARK 500 ALA A 374 -17.32 -140.12
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 PEG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: JCSG-418740 RELATED DB: TARGETTRACK
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT (RESIDUES 28-403) WAS EXPRESSED WITH A PURIFICATION
REMARK 999 TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 4EZI A 28 403 UNP Q5ZWI2 Q5ZWI2_LEGPH 28 403
SEQADV 4EZI GLY A 0 UNP Q5ZWI2 LEADER SEQUENCE
SEQRES 1 A 377 GLY ALA LEU GLU HIS GLU LYS LEU VAL ASN TYR ILE ALA
SEQRES 2 A 377 LEU GLY GLU PHE SER ARG GLU THR ALA GLU ILE ALA LEU
SEQRES 3 A 377 LYS LYS MSE PRO PRO LEU ASP THR LEU THR VAL HIS TYR
SEQRES 4 A 377 ASP LEU GLN LEU TYR LYS ILE ASN TYR LYS THR GLN SER
SEQRES 5 A 377 PRO ASP GLY ASN LEU THR ILE ALA SER GLY LEU VAL ALA
SEQRES 6 A 377 MSE PRO ILE HIS PRO VAL GLY GLN VAL GLY ILE ILE SER
SEQRES 7 A 377 TYR GLN HIS GLY THR ARG PHE GLU ARG ASN ASP VAL PRO
SEQRES 8 A 377 SER ARG ASN ASN GLU LYS ASN TYR ILE TYR LEU ALA ALA
SEQRES 9 A 377 TYR GLY ASN SER ALA GLY TYR MSE THR VAL MSE PRO ASP
SEQRES 10 A 377 TYR LEU GLY LEU GLY ASP ASN GLU LEU THR LEU HIS PRO
SEQRES 11 A 377 TYR VAL GLN ALA GLU THR LEU ALA SER SER SER ILE ASP
SEQRES 12 A 377 MSE LEU PHE ALA ALA LYS GLU LEU ALA ASN ARG LEU HIS
SEQRES 13 A 377 TYR PRO ILE SER ASP LYS LEU TYR LEU ALA GLY TYR SER
SEQRES 14 A 377 GLU GLY GLY PHE SER THR ILE VAL MSE PHE GLU MSE LEU
SEQRES 15 A 377 ALA LYS GLU TYR PRO ASP LEU PRO VAL SER ALA VAL ALA
SEQRES 16 A 377 PRO GLY SER ALA PRO TYR GLY TRP GLU GLU THR MSE HIS
SEQRES 17 A 377 PHE VAL MSE LEU GLU PRO GLY PRO ARG ALA THR ALA TYR
SEQRES 18 A 377 LEU ALA TYR PHE PHE TYR SER LEU GLN THR TYR LYS SER
SEQRES 19 A 377 TYR TRP SER GLY PHE ASP GLU ILE PHE ALA PRO PRO TYR
SEQRES 20 A 377 ASN THR LEU ILE PRO GLU LEU MSE ASP GLY TYR HIS ALA
SEQRES 21 A 377 VAL ASP GLU ILE LEU GLN ALA LEU PRO GLN ASP PRO LEU
SEQRES 22 A 377 LEU ILE PHE GLN PRO LYS PHE SER ASN GLY ILE ILE SER
SEQRES 23 A 377 LYS THR ASP ARG ASN THR GLU ILE LEU LYS ILE ASN PHE
SEQRES 24 A 377 ASN HIS TYR ASP PHE LYS PRO THR ALA PRO LEU LEU LEU
SEQRES 25 A 377 VAL GLY THR LYS GLY ASP ARG ASP VAL PRO TYR ALA GLY
SEQRES 26 A 377 ALA GLU MSE ALA TYR HIS SER PHE ARG LYS TYR SER ASP
SEQRES 27 A 377 PHE VAL TRP ILE LYS SER VAL SER ASP ALA LEU ASP HIS
SEQRES 28 A 377 VAL GLN ALA HIS PRO PHE VAL LEU LYS GLU GLN VAL ASP
SEQRES 29 A 377 PHE PHE LYS GLN PHE GLU ARG GLN GLU ALA MSE ASN LYS
MODRES 4EZI MSE A 55 MET SELENOMETHIONINE
MODRES 4EZI MSE A 92 MET SELENOMETHIONINE
MODRES 4EZI MSE A 138 MET SELENOMETHIONINE
MODRES 4EZI MSE A 141 MET SELENOMETHIONINE
MODRES 4EZI MSE A 170 MET SELENOMETHIONINE
MODRES 4EZI MSE A 204 MET SELENOMETHIONINE
MODRES 4EZI MSE A 207 MET SELENOMETHIONINE
MODRES 4EZI MSE A 233 MET SELENOMETHIONINE
MODRES 4EZI MSE A 237 MET SELENOMETHIONINE
MODRES 4EZI MSE A 281 MET SELENOMETHIONINE
MODRES 4EZI MSE A 354 MET SELENOMETHIONINE
MODRES 4EZI MSE A 401 MET SELENOMETHIONINE
HET MSE A 55 13
HET MSE A 92 8
HET MSE A 138 8
HET MSE A 141 8
HET MSE A 170 8
HET MSE A 204 8
HET MSE A 207 8
HET MSE A 233 8
HET MSE A 237 13
HET MSE A 281 8
HET MSE A 354 13
HET MSE A 401 5
HET PEG A 501 7
HET CL A 502 1
HETNAM MSE SELENOMETHIONINE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM CL CHLORIDE ION
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 2 PEG C4 H10 O3
FORMUL 3 CL CL 1-
FORMUL 4 HOH *536(H2 O)
HELIX 1 1 SER A 44 LYS A 54 1 11
HELIX 2 2 PRO A 57 LEU A 61 5 5
HELIX 3 3 VAL A 116 ASN A 120 5 5
HELIX 4 4 ASN A 121 LYS A 123 5 3
HELIX 5 5 ASN A 124 GLY A 132 1 9
HELIX 6 6 GLN A 159 LEU A 181 1 23
HELIX 7 7 SER A 195 TYR A 212 1 18
HELIX 8 8 GLY A 228 GLU A 239 1 12
HELIX 9 9 ARG A 243 SER A 260 1 18
HELIX 10 10 GLY A 264 PHE A 269 1 6
HELIX 11 11 PRO A 272 MSE A 281 1 10
HELIX 12 12 ALA A 286 LEU A 294 1 9
HELIX 13 13 ASP A 297 PHE A 302 5 6
HELIX 14 14 GLN A 303 SER A 312 1 10
HELIX 15 15 ASN A 317 ASN A 326 1 10
HELIX 16 16 PRO A 348 LYS A 361 1 14
HELIX 17 17 ALA A 380 ARG A 397 1 18
SHEET 1 A 7 LEU A 34 PHE A 43 0
SHEET 2 A 7 LEU A 67 GLN A 77 -1 O ASN A 73 N VAL A 35
SHEET 3 A 7 LEU A 83 PRO A 93 -1 O MSE A 92 N GLN A 68
SHEET 4 A 7 MSE A 138 PRO A 142 -1 O MSE A 141 N LEU A 89
SHEET 5 A 7 VAL A 100 GLN A 106 1 N ILE A 103 O VAL A 140
SHEET 6 A 7 ILE A 185 TYR A 194 1 O SER A 186 N VAL A 100
SHEET 7 A 7 ALA A 219 GLY A 223 1 O ALA A 221 N LEU A 191
SHEET 1 B 2 LEU A 336 GLY A 340 0
SHEET 2 B 2 VAL A 366 SER A 370 1 O TRP A 367 N LEU A 338
LINK C LYS A 54 N MSE A 55 1555 1555 1.34
LINK C MSE A 55 N PRO A 56 1555 1555 1.34
LINK C ALA A 91 N MSE A 92 1555 1555 1.34
LINK C MSE A 92 N PRO A 93 1555 1555 1.34
LINK C TYR A 137 N MSE A 138 1555 1555 1.33
LINK C MSE A 138 N THR A 139 1555 1555 1.33
LINK C VAL A 140 N MSE A 141 1555 1555 1.34
LINK C MSE A 141 N PRO A 142 1555 1555 1.34
LINK C ASP A 169 N MSE A 170 1555 1555 1.33
LINK C MSE A 170 N LEU A 171 1555 1555 1.32
LINK C VAL A 203 N MSE A 204 1555 1555 1.33
LINK C MSE A 204 N PHE A 205 1555 1555 1.32
LINK C GLU A 206 N MSE A 207 1555 1555 1.33
LINK C MSE A 207 N LEU A 208 1555 1555 1.32
LINK C THR A 232 N MSE A 233 1555 1555 1.33
LINK C MSE A 233 N HIS A 234 1555 1555 1.32
LINK C VAL A 236 N MSE A 237 1555 1555 1.34
LINK C MSE A 237 N LEU A 238 1555 1555 1.34
LINK C LEU A 280 N MSE A 281 1555 1555 1.34
LINK C MSE A 281 N ASP A 282 1555 1555 1.33
LINK C GLU A 353 N MSE A 354 1555 1555 1.33
LINK C MSE A 354 N ALA A 355 1555 1555 1.34
LINK C ALA A 400 N MSE A 401 1555 1555 1.34
LINK C MSE A 401 N ASN A 402 1555 1555 1.33
CISPEP 1 PRO A 56 PRO A 57 0 11.27
CISPEP 2 PRO A 271 PRO A 272 0 -2.42
SITE 1 AC1 4 TYR A 157 GLU A 196 PHE A 251 VAL A 347
SITE 1 AC2 3 GLU A 230 ASN A 326 HOH A 729
CRYST1 50.875 63.488 114.549 90.00 90.00 90.00 P 21 21 21 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 0.019656 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015751 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008730 0.00000
TER 3175 ASN A 402
MASTER 300 0 14 17 9 0 2 6 3506 1 139 29
END |