HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 07-AUG-07 2QV5
TITLE CRYSTAL STRUCTURE OF UNCHARACTERIZED PROTEIN ATU2773 FROM
TITLE 2 AGROBACTERIUM TUMEFACIENS C58
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN ATU2773;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN: RESIDUES 149-398;
COMPND 5 SYNONYM: AGR_C_5032P;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AGROBACTERIUM TUMEFACIENS STR.;
SOURCE 3 ORGANISM_TAXID: 176299;
SOURCE 4 STRAIN: C58;
SOURCE 5 ATCC: 33970;
SOURCE 6 GENE: ATU2773, AGR_C_5032;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR: PET;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC)
KEYWDS STRUCTURAL GENOMICS, UNKNOWN FUNCTION, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS,
KEYWDS 3 NYSGXRC
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.PATSKOVSKY,J.B.BONANNO,S.SOJITRA,M.DICKEY,K.T.BAIN,M.IIZUKA,
AUTHOR 2 D.SMITH,L.RODGERS,S.WASSERMAN,J.M.SAUDER,S.K.BURLEY,S.C.ALMO,NEW
AUTHOR 3 YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)
REVDAT 7 30-AUG-23 2QV5 1 REMARK
REVDAT 6 03-FEB-21 2QV5 1 AUTHOR JRNL REMARK SEQADV
REVDAT 5 14-NOV-18 2QV5 1 AUTHOR
REVDAT 4 25-OCT-17 2QV5 1 REMARK
REVDAT 3 13-JUL-11 2QV5 1 VERSN
REVDAT 2 24-FEB-09 2QV5 1 VERSN
REVDAT 1 21-AUG-07 2QV5 0
JRNL AUTH Y.PATSKOVSKY,J.B.BONANNO,S.SOJITRA,M.DICKEY,D.SMITH,
JRNL AUTH 2 K.T.BAIN,M.IIZUKA,L.RODGERS,S.WASSERMAN,J.M.SAUDER,
JRNL AUTH 3 S.K.BURLEY,S.C.ALMO
JRNL TITL CRYSTAL STRUCTURE OF UNCHARACTERIZED PROTEIN ATU2773 FROM
JRNL TITL 2 AGROBACTERIUM TUMEFACIENS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0034
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 31951
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1037
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2212
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.3730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3662
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 6
REMARK 3 SOLVENT ATOMS : 298
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.44
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.33000
REMARK 3 B22 (A**2) : 0.40000
REMARK 3 B33 (A**2) : -0.36000
REMARK 3 B12 (A**2) : -0.64000
REMARK 3 B13 (A**2) : -0.21000
REMARK 3 B23 (A**2) : 0.37000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.175
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.164
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.121
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.077
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3832 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5203 ; 1.291 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 521 ; 5.323 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 163 ;32.431 ;22.883
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 654 ;14.323 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;14.085 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 580 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2935 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1748 ; 0.151 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2620 ; 0.299 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 466 ; 0.165 ; 0.500
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): 63 ; 0.101 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 27 ; 0.190 ; 0.500
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): 2538 ; 3.289 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3940 ; 4.351 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1445 ; 5.790 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1247 ; 8.375 ; 5.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 148 A 393 1
REMARK 3 1 B 148 B 393 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1784 ; 0.38 ; 0.05
REMARK 3 TIGHT THERMAL 1 B (A**2): 1784 ; 4.00 ; 2.50
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2QV5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000044094.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-MAY-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97958
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33092
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -0.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.11400
REMARK 200 R SYM (I) : 0.10400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.75000
REMARK 200 R SYM FOR SHELL (I) : 0.78000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
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: PDB ENTRY 2NLY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM SODIUM CACODYLATE PH 6.5, 400MM
REMARK 280 SODIUM ACETATE PH 4.6, 30% PEG8000, PH 5.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 146
REMARK 465 SER A 147
REMARK 465 SER A 394
REMARK 465 GLY A 395
REMARK 465 GLN A 396
REMARK 465 ALA A 397
REMARK 465 GLY A 398
REMARK 465 GLU A 399
REMARK 465 GLY A 400
REMARK 465 HIS A 401
REMARK 465 HIS A 402
REMARK 465 HIS A 403
REMARK 465 HIS A 404
REMARK 465 HIS A 405
REMARK 465 HIS A 406
REMARK 465 MET B 146
REMARK 465 SER B 147
REMARK 465 SER B 394
REMARK 465 GLY B 395
REMARK 465 GLN B 396
REMARK 465 ALA B 397
REMARK 465 GLY B 398
REMARK 465 GLU B 399
REMARK 465 GLY B 400
REMARK 465 HIS B 401
REMARK 465 HIS B 402
REMARK 465 HIS B 403
REMARK 465 HIS B 404
REMARK 465 HIS B 405
REMARK 465 HIS B 406
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 LEU A 278 -128.40 63.15
REMARK 500 LEU B 278 -138.22 57.57
REMARK 500 ALA B 364 49.74 -80.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU B 148 GLY B 149 -88.70
REMARK 500 TYR B 238 PRO B 239 42.96
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 GOL A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NYSGXRC-10097F RELATED DB: TARGETDB
DBREF 2QV5 A 149 398 UNP Q8UBS7 Q8UBS7_AGRT5 149 398
DBREF 2QV5 B 149 398 UNP Q8UBS7 Q8UBS7_AGRT5 149 398
SEQADV 2QV5 MET A 146 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 SER A 147 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 LEU A 148 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 GLU A 399 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 GLY A 400 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 HIS A 401 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 HIS A 402 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 HIS A 403 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 HIS A 404 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 HIS A 405 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 HIS A 406 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 MET B 146 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 SER B 147 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 LEU B 148 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 GLU B 399 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 GLY B 400 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 HIS B 401 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 HIS B 402 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 HIS B 403 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 HIS B 404 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 HIS B 405 UNP Q8UBS7 EXPRESSION TAG
SEQADV 2QV5 HIS B 406 UNP Q8UBS7 EXPRESSION TAG
SEQRES 1 A 261 MET SER LEU GLY GLN LEU PRO VAL VAL GLY ALA ASP GLY
SEQRES 2 A 261 LEU ARG PRO MET GLU GLN TYR ALA ARG PRO TRP SER GLY
SEQRES 3 A 261 ALA ARG GLY THR ARG VAL ALA ILE VAL VAL GLY GLY LEU
SEQRES 4 A 261 GLY LEU SER GLN THR GLY SER GLN LYS ALA ILE ARG ASP
SEQRES 5 A 261 LEU PRO PRO GLU VAL THR LEU GLY PHE ALA ALA SER GLY
SEQRES 6 A 261 ASN SER LEU GLN ARG TRP MET GLN ASP ALA ARG ARG GLU
SEQRES 7 A 261 GLY HIS GLU ILE LEU LEU GLN ILE PRO LEU GLU PRO PHE
SEQRES 8 A 261 GLY TYR PRO GLY THR ASN PRO GLY PRO ASP THR LEU LEU
SEQRES 9 A 261 ALA GLY ASP PRO ALA LYS VAL ASN ILE ASP ARG LEU HIS
SEQRES 10 A 261 ARG SER MET ALA LYS ILE THR ASN TYR THR GLY VAL MET
SEQRES 11 A 261 ASN TYR LEU GLY GLY ARG PHE LEU ALA GLU GLN SER ALA
SEQRES 12 A 261 LEU GLU PRO VAL MET ARG ASP ILE GLY LYS ARG GLY LEU
SEQRES 13 A 261 LEU PHE LEU ASP ASP GLY SER SER ALA GLN SER LEU SER
SEQRES 14 A 261 GLY GLY ILE ALA LYS ALA ILE SER ALA PRO GLN GLY PHE
SEQRES 15 A 261 ALA ASP VAL LEU LEU ASP GLY GLU VAL THR GLU ALA SER
SEQRES 16 A 261 ILE LEU ARG LYS LEU ASP ASP LEU GLU ARG ILE ALA ARG
SEQRES 17 A 261 ARG ASN GLY GLN ALA ILE GLY VAL ALA SER ALA PHE ASP
SEQRES 18 A 261 GLU SER ILE ALA ALA ILE SER LYS TRP SER ARG GLU ALA
SEQRES 19 A 261 GLY GLY ARG GLY ILE GLU ILE VAL GLY VAL SER ALA LEU
SEQRES 20 A 261 VAL SER GLY GLN ALA GLY GLU GLY HIS HIS HIS HIS HIS
SEQRES 21 A 261 HIS
SEQRES 1 B 261 MET SER LEU GLY GLN LEU PRO VAL VAL GLY ALA ASP GLY
SEQRES 2 B 261 LEU ARG PRO MET GLU GLN TYR ALA ARG PRO TRP SER GLY
SEQRES 3 B 261 ALA ARG GLY THR ARG VAL ALA ILE VAL VAL GLY GLY LEU
SEQRES 4 B 261 GLY LEU SER GLN THR GLY SER GLN LYS ALA ILE ARG ASP
SEQRES 5 B 261 LEU PRO PRO GLU VAL THR LEU GLY PHE ALA ALA SER GLY
SEQRES 6 B 261 ASN SER LEU GLN ARG TRP MET GLN ASP ALA ARG ARG GLU
SEQRES 7 B 261 GLY HIS GLU ILE LEU LEU GLN ILE PRO LEU GLU PRO PHE
SEQRES 8 B 261 GLY TYR PRO GLY THR ASN PRO GLY PRO ASP THR LEU LEU
SEQRES 9 B 261 ALA GLY ASP PRO ALA LYS VAL ASN ILE ASP ARG LEU HIS
SEQRES 10 B 261 ARG SER MET ALA LYS ILE THR ASN TYR THR GLY VAL MET
SEQRES 11 B 261 ASN TYR LEU GLY GLY ARG PHE LEU ALA GLU GLN SER ALA
SEQRES 12 B 261 LEU GLU PRO VAL MET ARG ASP ILE GLY LYS ARG GLY LEU
SEQRES 13 B 261 LEU PHE LEU ASP ASP GLY SER SER ALA GLN SER LEU SER
SEQRES 14 B 261 GLY GLY ILE ALA LYS ALA ILE SER ALA PRO GLN GLY PHE
SEQRES 15 B 261 ALA ASP VAL LEU LEU ASP GLY GLU VAL THR GLU ALA SER
SEQRES 16 B 261 ILE LEU ARG LYS LEU ASP ASP LEU GLU ARG ILE ALA ARG
SEQRES 17 B 261 ARG ASN GLY GLN ALA ILE GLY VAL ALA SER ALA PHE ASP
SEQRES 18 B 261 GLU SER ILE ALA ALA ILE SER LYS TRP SER ARG GLU ALA
SEQRES 19 B 261 GLY GLY ARG GLY ILE GLU ILE VAL GLY VAL SER ALA LEU
SEQRES 20 B 261 VAL SER GLY GLN ALA GLY GLU GLY HIS HIS HIS HIS HIS
SEQRES 21 B 261 HIS
HET GOL A 1 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *298(H2 O)
HELIX 1 1 ARG A 160 TYR A 165 1 6
HELIX 2 2 SER A 187 LEU A 198 1 12
HELIX 3 3 SER A 212 GLY A 224 1 13
HELIX 4 4 PRO A 253 ALA A 266 1 14
HELIX 5 5 ARG A 281 ALA A 284 5 4
HELIX 6 6 GLU A 285 ARG A 299 1 15
HELIX 7 7 LEU A 313 SER A 322 1 10
HELIX 8 8 THR A 337 GLY A 356 1 20
HELIX 9 9 PHE A 365 ALA A 379 1 15
HELIX 10 10 GLY A 380 ARG A 382 5 3
HELIX 11 11 GLY A 388 VAL A 393 1 6
HELIX 12 12 ARG B 160 TYR B 165 1 6
HELIX 13 13 SER B 187 LEU B 198 1 12
HELIX 14 14 SER B 212 GLY B 224 1 13
HELIX 15 15 PRO B 253 ALA B 266 1 14
HELIX 16 16 GLY B 279 ALA B 284 1 6
HELIX 17 17 GLU B 285 ARG B 299 1 15
HELIX 18 18 LEU B 313 SER B 322 1 10
HELIX 19 19 THR B 337 GLY B 356 1 20
HELIX 20 20 PHE B 365 GLY B 380 1 16
HELIX 21 21 GLY B 388 VAL B 393 1 6
SHEET 1 A 8 GLN A 325 PHE A 327 0
SHEET 2 A 8 LEU A 302 ASP A 305 1 N ASP A 305 O GLY A 326
SHEET 3 A 8 GLY A 273 LEU A 278 1 N VAL A 274 O LEU A 304
SHEET 4 A 8 ILE A 227 LEU A 233 1 N ILE A 231 O MET A 275
SHEET 5 A 8 THR A 203 ALA A 207 1 N PHE A 206 O GLN A 230
SHEET 6 A 8 THR A 175 LEU A 184 1 N LEU A 184 O ALA A 207
SHEET 7 A 8 GLN A 357 SER A 363 1 O ALA A 362 N GLY A 182
SHEET 8 A 8 VAL A 330 LEU A 331 1 N VAL A 330 O VAL A 361
SHEET 1 B 7 GLN A 325 PHE A 327 0
SHEET 2 B 7 LEU A 302 ASP A 305 1 N ASP A 305 O GLY A 326
SHEET 3 B 7 GLY A 273 LEU A 278 1 N VAL A 274 O LEU A 304
SHEET 4 B 7 ILE A 227 LEU A 233 1 N ILE A 231 O MET A 275
SHEET 5 B 7 THR A 203 ALA A 207 1 N PHE A 206 O GLN A 230
SHEET 6 B 7 THR A 175 LEU A 184 1 N LEU A 184 O ALA A 207
SHEET 7 B 7 ILE A 384 ILE A 386 1 O GLU A 385 N VAL A 177
SHEET 1 C 8 GLN B 325 PHE B 327 0
SHEET 2 C 8 LEU B 302 ASP B 305 1 N ASP B 305 O GLY B 326
SHEET 3 C 8 GLY B 273 LEU B 278 1 N VAL B 274 O LEU B 304
SHEET 4 C 8 ILE B 227 LEU B 233 1 N ILE B 231 O MET B 275
SHEET 5 C 8 THR B 203 ALA B 207 1 N PHE B 206 O GLN B 230
SHEET 6 C 8 THR B 175 LEU B 184 1 N VAL B 181 O GLY B 205
SHEET 7 C 8 GLN B 357 SER B 363 1 O ALA B 362 N GLY B 182
SHEET 8 C 8 VAL B 330 LEU B 331 1 N VAL B 330 O VAL B 361
SHEET 1 D 7 GLN B 325 PHE B 327 0
SHEET 2 D 7 LEU B 302 ASP B 305 1 N ASP B 305 O GLY B 326
SHEET 3 D 7 GLY B 273 LEU B 278 1 N VAL B 274 O LEU B 304
SHEET 4 D 7 ILE B 227 LEU B 233 1 N ILE B 231 O MET B 275
SHEET 5 D 7 THR B 203 ALA B 207 1 N PHE B 206 O GLN B 230
SHEET 6 D 7 THR B 175 LEU B 184 1 N VAL B 181 O GLY B 205
SHEET 7 D 7 ILE B 384 ILE B 386 1 O GLU B 385 N THR B 175
CISPEP 1 TYR A 238 PRO A 239 0 3.19
SITE 1 AC1 4 PRO A 168 TRP A 169 GLY A 171 HOH A 572
CRYST1 37.349 47.373 65.492 91.06 92.36 73.06 P 1 2
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 0.026774 -0.008155 0.001048 0.00000
SCALE2 0.000000 0.022067 0.000150 0.00000
SCALE3 0.000000 0.000000 0.015282 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
