| content |
HEADER HYDROLASE 28-JAN-10 3LLC
TITLE CRYSTAL STRUCTURE OF PUTATIVE HYDROLASE (YP_002548124.1)
TITLE 2 FROM AGROBACTERIUM VITIS S4 AT 1.80 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AGROBACTERIUM VITIS;
SOURCE 3 ORGANISM_COMMON: RHIZOBIUM VITIS (STRAIN S4);
SOURCE 4 ORGANISM_TAXID: 311402;
SOURCE 5 STRAIN: S4 / ATCC BAA-846;
SOURCE 6 GENE: AVI_0199;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS PUTATIVE HYDROLASE, STRUCTURAL GENOMICS, JOINT CENTER FOR
KEYWDS 2 STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 3 PSI-2, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 23-MAR-10 3LLC 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE HYDROLASE
JRNL TITL 2 (YP_002548124.1) FROM AGROBACTERIUM VITIS S4 AT
JRNL TITL 3 1.80 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0053
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 35855
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1788
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2412
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE SET COUNT : 114
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2111
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 258
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.33
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.48000
REMARK 3 B22 (A**2) : -1.48000
REMARK 3 B33 (A**2) : 2.95000
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): 0.092
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.090
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.065
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.795
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2207 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1542 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3014 ; 1.436 ; 1.981
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3769 ; 0.951 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 307 ; 5.095 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 104 ;36.772 ;23.654
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 374 ;13.920 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;18.885 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 337 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2513 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 438 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1368 ; 1.724 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 553 ; 0.492 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2221 ; 2.766 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 839 ; 4.293 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 769 ; 6.401 ;11.000
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 : 1
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 6 A 266
REMARK 3 ORIGIN FOR THE GROUP (A): 31.8381 3.6172 -0.0326
REMARK 3 T TENSOR
REMARK 3 T11: 0.0494 T22: 0.0568
REMARK 3 T33: 0.0141 T12: -0.0072
REMARK 3 T13: -0.0054 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 2.2502 L22: 2.8390
REMARK 3 L33: 0.9559 L12: -0.5615
REMARK 3 L13: -0.1807 L23: -0.3919
REMARK 3 S TENSOR
REMARK 3 S11: 0.0035 S12: -0.0247 S13: -0.1553
REMARK 3 S21: -0.0064 S22: -0.0341 S23: -0.0437
REMARK 3 S31: 0.0686 S32: -0.0085 S33: 0.0306
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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.ATOM RECORDS CONTAIN RESIDUAL B FACTORS
REMARK 3 ONLY. 3.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
REMARK 3 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 4.PEG3350 FRAGMENTS (PEG AND PG4) AND CHLORIDE
REMARK 3 (CL) FROM THE CRYSTALLIZATION SOLUTION AND 1,2-ETHANEDIOL
REMARK 3 (EDO) FROM THE CRYOPROTECTANT SOLUTION HAVE BEEN MODELED IN
REMARK 3 THE SOLVENT STRUCTURE.
REMARK 4
REMARK 4 3LLC COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-10.
REMARK 100 THE RCSB ID CODE IS RCSB057418.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91162,0.97949,0.97934
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : FLAT COLLIMATING MIRROR,
REMARK 200 TOROID FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35908
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 28.763
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 7.107
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 12.1200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.70600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD, AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2000M NACL, 20.0000% PEG-3350, NO
REMARK 280 BUFFER PH 6.9, NANODROP, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 29.74850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 56.32600
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 56.32600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 14.87425
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 56.32600
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 56.32600
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 44.62275
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 56.32600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.32600
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 14.87425
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 56.32600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.32600
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 44.62275
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 29.74850
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 300 REMARK: CRYSTAL PACKING ANALYSIS SUPPORTS THE ASSIGNMENT OF A
REMARK 300 MONOMER AS THE SIGNIFICANT OLIGOMERIC FORM IN SOLUTION.
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 MSE A 1
REMARK 465 THR A 2
REMARK 465 ASN A 3
REMARK 465 VAL A 4
REMARK 465 GLY A 5
REMARK 465 PRO A 267
REMARK 465 ARG A 268
REMARK 465 PRO A 269
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 106 CE NZ
REMARK 470 ASP A 131 CG OD1 OD2
REMARK 470 GLU A 167 CG CD OE1 OE2
REMARK 470 GLU A 180 CD OE1 OE2
REMARK 470 ARG A 247 NE CZ NH1 NH2
REMARK 470 ARG A 262 CZ NH1 NH2
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 SER A 113 -115.28 57.38
REMARK 500 SER A 178 156.34 179.05
REMARK 500 ASP A 245 -167.94 -103.30
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 CL A 270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 271
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 277
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 401112 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.
DBREF 3LLC A 1 269 UNP B9JYM4 B9JYM4_AGRVS 1 269
SEQADV 3LLC GLY A 0 UNP B9JYM4 LEADER SEQUENCE
SEQRES 1 A 270 GLY MSE THR ASN VAL GLY ARG PRO ILE GLU THR HIS ALA
SEQRES 2 A 270 ILE THR VAL GLY GLN GLY SER ASP ALA ARG SER ILE ALA
SEQRES 3 A 270 ALA LEU VAL ARG ALA PRO ALA GLN ASP GLU ARG PRO THR
SEQRES 4 A 270 CYS ILE TRP LEU GLY GLY TYR ARG SER ASP MSE THR GLY
SEQRES 5 A 270 THR LYS ALA LEU GLU MSE ASP ASP LEU ALA ALA SER LEU
SEQRES 6 A 270 GLY VAL GLY ALA ILE ARG PHE ASP TYR SER GLY HIS GLY
SEQRES 7 A 270 ALA SER GLY GLY ALA PHE ARG ASP GLY THR ILE SER ARG
SEQRES 8 A 270 TRP LEU GLU GLU ALA LEU ALA VAL LEU ASP HIS PHE LYS
SEQRES 9 A 270 PRO GLU LYS ALA ILE LEU VAL GLY SER SER MSE GLY GLY
SEQRES 10 A 270 TRP ILE ALA LEU ARG LEU ILE GLN GLU LEU LYS ALA ARG
SEQRES 11 A 270 HIS ASP ASN PRO THR GLN VAL SER GLY MSE VAL LEU ILE
SEQRES 12 A 270 ALA PRO ALA PRO ASP PHE THR SER ASP LEU ILE GLU PRO
SEQRES 13 A 270 LEU LEU GLY ASP ARG GLU ARG ALA GLU LEU ALA GLU ASN
SEQRES 14 A 270 GLY TYR PHE GLU GLU VAL SER GLU TYR SER PRO GLU PRO
SEQRES 15 A 270 ASN ILE PHE THR ARG ALA LEU MSE GLU ASP GLY ARG ALA
SEQRES 16 A 270 ASN ARG VAL MSE ALA GLY MSE ILE ASP THR GLY CYS PRO
SEQRES 17 A 270 VAL HIS ILE LEU GLN GLY MSE ALA ASP PRO ASP VAL PRO
SEQRES 18 A 270 TYR GLN HIS ALA LEU LYS LEU VAL GLU HIS LEU PRO ALA
SEQRES 19 A 270 ASP ASP VAL VAL LEU THR LEU VAL ARG ASP GLY ASP HIS
SEQRES 20 A 270 ARG LEU SER ARG PRO GLN ASP ILE ASP ARG MSE ARG ASN
SEQRES 21 A 270 ALA ILE ARG ALA MSE ILE GLU PRO ARG PRO
MODRES 3LLC MSE A 49 MET SELENOMETHIONINE
MODRES 3LLC MSE A 57 MET SELENOMETHIONINE
MODRES 3LLC MSE A 114 MET SELENOMETHIONINE
MODRES 3LLC MSE A 139 MET SELENOMETHIONINE
MODRES 3LLC MSE A 189 MET SELENOMETHIONINE
MODRES 3LLC MSE A 198 MET SELENOMETHIONINE
MODRES 3LLC MSE A 201 MET SELENOMETHIONINE
MODRES 3LLC MSE A 214 MET SELENOMETHIONINE
MODRES 3LLC MSE A 257 MET SELENOMETHIONINE
MODRES 3LLC MSE A 264 MET SELENOMETHIONINE
HET MSE A 49 8
HET MSE A 57 8
HET MSE A 114 8
HET MSE A 139 13
HET MSE A 189 8
HET MSE A 198 8
HET MSE A 201 8
HET MSE A 214 8
HET MSE A 257 8
HET MSE A 264 8
HET CL A 270 1
HET EDO A 271 4
HET EDO A 272 4
HET EDO A 273 4
HET EDO A 274 4
HET EDO A 275 4
HET PEG A 276 7
HET PG4 A 277 13
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PG4 TETRAETHYLENE GLYCOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 10(C5 H11 N O2 SE)
FORMUL 2 CL CL 1-
FORMUL 3 EDO 5(C2 H6 O2)
FORMUL 8 PEG C4 H10 O3
FORMUL 9 PG4 C8 H18 O5
FORMUL 10 HOH *252(H2 O)
HELIX 1 1 GLN A 17 ALA A 21 5 5
HELIX 2 2 GLY A 51 GLY A 65 1 15
HELIX 3 3 ALA A 82 GLY A 86 5 5
HELIX 4 4 THR A 87 LYS A 103 1 17
HELIX 5 5 MSE A 114 ALA A 128 1 15
HELIX 6 6 ASP A 147 LEU A 152 1 6
HELIX 7 7 ILE A 153 LEU A 157 5 5
HELIX 8 8 GLY A 158 GLY A 169 1 12
HELIX 9 9 ARG A 186 ASN A 195 1 10
HELIX 10 10 PRO A 220 HIS A 230 1 11
HELIX 11 11 ARG A 250 GLU A 266 1 17
SHEET 1 A 8 ILE A 8 VAL A 15 0
SHEET 2 A 8 ARG A 22 ARG A 29 -1 O ILE A 24 N ILE A 13
SHEET 3 A 8 GLY A 67 PHE A 71 -1 O ALA A 68 N ARG A 29
SHEET 4 A 8 THR A 38 LEU A 42 1 N CYS A 39 O GLY A 67
SHEET 5 A 8 LYS A 106 SER A 112 1 O VAL A 110 N ILE A 40
SHEET 6 A 8 GLN A 135 ILE A 142 1 O VAL A 140 N LEU A 109
SHEET 7 A 8 VAL A 208 GLY A 213 1 O LEU A 211 N LEU A 141
SHEET 8 A 8 VAL A 236 VAL A 241 1 O THR A 239 N ILE A 210
SHEET 1 B 2 TYR A 170 GLU A 173 0
SHEET 2 B 2 ASN A 182 THR A 185 -1 O ASN A 182 N GLU A 173
LINK C ASP A 48 N MSE A 49 1555 1555 1.33
LINK C MSE A 49 N THR A 50 1555 1555 1.34
LINK C GLU A 56 N MSE A 57 1555 1555 1.32
LINK C MSE A 57 N ASP A 58 1555 1555 1.33
LINK C SER A 113 N MSE A 114 1555 1555 1.33
LINK C MSE A 114 N GLY A 115 1555 1555 1.33
LINK C GLY A 138 N MSE A 139 1555 1555 1.34
LINK C MSE A 139 N VAL A 140 1555 1555 1.35
LINK C LEU A 188 N MSE A 189 1555 1555 1.33
LINK C MSE A 189 N GLU A 190 1555 1555 1.33
LINK C VAL A 197 N MSE A 198 1555 1555 1.35
LINK C MSE A 198 N ALA A 199 1555 1555 1.33
LINK C GLY A 200 N MSE A 201 1555 1555 1.34
LINK C MSE A 201 N ILE A 202 1555 1555 1.33
LINK C GLY A 213 N MSE A 214 1555 1555 1.33
LINK C MSE A 214 N ALA A 215 1555 1555 1.33
LINK C ARG A 256 N MSE A 257 1555 1555 1.33
LINK C MSE A 257 N ARG A 258 1555 1555 1.32
LINK C ALA A 263 N MSE A 264 1555 1555 1.34
LINK C MSE A 264 N ILE A 265 1555 1555 1.34
SITE 1 AC1 4 THR A 52 LYS A 53 HOH A 319 HOH A 392
SITE 1 AC2 7 SER A 23 GLN A 124 VAL A 197 GLY A 200
SITE 2 AC2 7 MSE A 201 EDO A 272 HOH A 284
SITE 1 AC3 7 ARG A 121 GLN A 124 ALA A 194 ARG A 196
SITE 2 AC3 7 EDO A 271 HOH A 505 HOH A 511
SITE 1 AC4 6 ILE A 123 LEU A 126 ASN A 132 GLN A 135
SITE 2 AC4 6 VAL A 136 HOH A 434
SITE 1 AC5 3 VAL A 28 THR A 38 PRO A 104
SITE 1 AC6 1 GLU A 56
SITE 1 AC7 3 GLU A 9 THR A 10 HOH A 384
SITE 1 AC8 5 TYR A 45 SER A 113 MSE A 114 GLU A 173
SITE 2 AC8 5 ASP A 218
CRYST1 112.652 112.652 59.497 90.00 90.00 90.00 P 41 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008877 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008877 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016808 0.00000
TER 2112 GLU A 266
MASTER 365 0 18 11 10 0 12 6 2410 1 145 21
END |