HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 21-DEC-04 1YBM
TITLE X-RAY STRUCTURE OF SELENOMETHIONYL GENE PRODUCT FROM ARABIDOPSIS
TITLE 2 THALIANA AT5G02240 IN SPACE GROUP P21212
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNKNOWN PROTEIN AT5G02240;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: AT5G02240;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834 P(RARE2);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PVP-17
KEYWDS STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, CESG, PSI, CENTER
KEYWDS 2 FOR EUKARYOTIC STRUCTURAL GENOMICS, NADP, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR G.E.WESENBERG,D.W.SMITH,G.N.PHILLIPS JR.,E.BITTO,C.A.BINGMAN,
AUTHOR 2 S.T.M.ALLARD,CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS (CESG)
REVDAT 5 14-FEB-24 1YBM 1 REMARK SEQADV
REVDAT 4 11-OCT-17 1YBM 1 REMARK
REVDAT 3 24-FEB-09 1YBM 1 VERSN
REVDAT 2 12-FEB-08 1YBM 1 REMARK
REVDAT 1 18-JAN-05 1YBM 0
JRNL AUTH CENTER FOR EUKARYOTIC STRUCTURAL GENOMICS (CESG)
JRNL TITL X-RAY STRUCTURE OF SELENOMETHIONYL GENE PRODUCT FROM
JRNL TITL 2 ARABIDOPSIS THALIANA AT5G02240 IN SPACE GROUP P21212
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.2.0005
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.09
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 29855
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.108
REMARK 3 FREE R VALUE TEST SET COUNT : 1525
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1869
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.2360
REMARK 3 BIN FREE R VALUE SET COUNT : 99
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3672
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 369
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.53900
REMARK 3 B22 (A**2) : 1.58900
REMARK 3 B33 (A**2) : -0.05000
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): 0.245
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.219
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.161
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.058
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.916
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3834 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5196 ; 1.643 ; 2.007
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 482 ; 6.592 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 152 ;36.884 ;25.789
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 664 ;15.086 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;15.382 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 592 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2804 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1861 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2578 ; 0.299 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 339 ; 0.198 ; 0.200
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): 44 ; 0.179 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 35 ; 0.306 ; 0.200
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): 2486 ; 3.220 ; 4.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3848 ; 4.412 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1531 ; 6.383 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1348 ; 8.126 ;12.000
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 : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2 A 80 6
REMARK 3 1 B 2 B 80 6
REMARK 3 2 A 102 A 253 6
REMARK 3 2 B 102 B 253 6
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 LOOSE POSITIONAL 1 A (A): 1734 ; 0.39 ; 5.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 1734 ; 6.17 ; 10.00
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 BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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, MOLPROBITY USED TO ASSIST IN FINAL MODEL BUILDING
REMARK 4
REMARK 4 1YBM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031348.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-AUG-04
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 : APS
REMARK 200 BEAMLINE : 14-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97935, 0.97904, 0.96389
REMARK 200 MONOCHROMATOR : DIAMOND (111) DOUBLE-CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : BENT CYLINDRICAL SI-MIRROR (RH
REMARK 200 COATING)
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29937
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.096
REMARK 200 RESOLUTION RANGE LOW (A) : 29.087
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 11.70
REMARK 200 R MERGE (I) : 0.04700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.7450
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.3
REMARK 200 DATA REDUNDANCY IN SHELL : 9.30
REMARK 200 R MERGE FOR SHELL (I) : 0.28000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.125
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE 2.06, RESOLVE 2.06
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MG/ML PROTEIN, 24 PERCENT PEG 4K,
REMARK 280 0.136 M SODIUM MALONATE, 0.10 M BISTRIS, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 37.31700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.64300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.31700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.64300
REMARK 290 SMTRY3 4 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 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 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 PRO A 85
REMARK 465 GLY A 86
REMARK 465 PHE A 87
REMARK 465 ASP A 88
REMARK 465 PRO A 89
REMARK 465 THR A 90
REMARK 465 LYS A 91
REMARK 465 GLY A 92
REMARK 465 GLY A 93
REMARK 465 ARG A 94
REMARK 465 PRO B 85
REMARK 465 GLY B 86
REMARK 465 PHE B 87
REMARK 465 ASP B 88
REMARK 465 PRO B 89
REMARK 465 THR B 90
REMARK 465 LYS B 91
REMARK 465 GLY B 92
REMARK 465 GLY B 93
REMARK 465 ARG B 94
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER A 165 O HOH A 531 1.86
REMARK 500 O HOH B 445 O HOH B 503 1.97
REMARK 500 O HOH A 470 O HOH A 512 1.99
REMARK 500 O HOH B 470 O HOH B 557 2.05
REMARK 500 O HOH B 467 O HOH B 468 2.05
REMARK 500 OE1 GLN A 197 O HOH A 499 2.14
REMARK 500 O HOH B 472 O HOH B 596 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 512 O HOH B 567 3646 1.93
REMARK 500 O HOH A 466 O HOH B 566 3646 2.13
REMARK 500
REMARK 500 REMARK: NULL
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 28 30.52 -82.20
REMARK 500 GLU A 100 157.10 -48.02
REMARK 500 PRO A 105 -34.10 -37.05
REMARK 500 TRP A 110 -71.58 -83.91
REMARK 500 HIS A 141 131.89 -39.31
REMARK 500 TRP B 110 -73.47 -89.74
REMARK 500 THR B 200 57.35 -119.93
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 NAP A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XQ6 RELATED DB: PDB
REMARK 900 1XQ6 IS THE NATIVE STRUCTURE OF AT5G02240 IN SPACE GROUP P21
REMARK 900 RELATED ID: GO.23662 RELATED DB: TARGETDB
DBREF 1YBM A 2 253 UNP Q94EG6 Y5224_ARATH 2 253
DBREF 1YBM B 2 253 UNP Q94EG6 Y5224_ARATH 2 253
SEQADV 1YBM SER A 1 UNP Q94EG6 CLONING ARTIFACT
SEQADV 1YBM SER B 1 UNP Q94EG6 CLONING ARTIFACT
SEQRES 1 A 253 SER ALA ASN LEU PRO THR VAL LEU VAL THR GLY ALA SER
SEQRES 2 A 253 GLY ARG THR GLY GLN ILE VAL TYR LYS LYS LEU LYS GLU
SEQRES 3 A 253 GLY SER ASP LYS PHE VAL ALA LYS GLY LEU VAL ARG SER
SEQRES 4 A 253 ALA GLN GLY LYS GLU LYS ILE GLY GLY GLU ALA ASP VAL
SEQRES 5 A 253 PHE ILE GLY ASP ILE THR ASP ALA ASP SER ILE ASN PRO
SEQRES 6 A 253 ALA PHE GLN GLY ILE ASP ALA LEU VAL ILE LEU THR SER
SEQRES 7 A 253 ALA VAL PRO LYS MET LYS PRO GLY PHE ASP PRO THR LYS
SEQRES 8 A 253 GLY GLY ARG PRO GLU PHE ILE PHE GLU ASP GLY GLN TYR
SEQRES 9 A 253 PRO GLU GLN VAL ASP TRP ILE GLY GLN LYS ASN GLN ILE
SEQRES 10 A 253 ASP ALA ALA LYS VAL ALA GLY VAL LYS HIS ILE VAL VAL
SEQRES 11 A 253 VAL GLY SER MET GLY GLY THR ASN PRO ASP HIS PRO LEU
SEQRES 12 A 253 ASN LYS LEU GLY ASN GLY ASN ILE LEU VAL TRP LYS ARG
SEQRES 13 A 253 LYS ALA GLU GLN TYR LEU ALA ASP SER GLY THR PRO TYR
SEQRES 14 A 253 THR ILE ILE ARG ALA GLY GLY LEU LEU ASP LYS GLU GLY
SEQRES 15 A 253 GLY VAL ARG GLU LEU LEU VAL GLY LYS ASP ASP GLU LEU
SEQRES 16 A 253 LEU GLN THR ASP THR LYS THR VAL PRO ARG ALA ASP VAL
SEQRES 17 A 253 ALA GLU VAL CYS ILE GLN ALA LEU LEU PHE GLU GLU ALA
SEQRES 18 A 253 LYS ASN LYS ALA PHE ASP LEU GLY SER LYS PRO GLU GLY
SEQRES 19 A 253 THR SER THR PRO THR LYS ASP PHE LYS ALA LEU PHE SER
SEQRES 20 A 253 GLN VAL THR SER ARG PHE
SEQRES 1 B 253 SER ALA ASN LEU PRO THR VAL LEU VAL THR GLY ALA SER
SEQRES 2 B 253 GLY ARG THR GLY GLN ILE VAL TYR LYS LYS LEU LYS GLU
SEQRES 3 B 253 GLY SER ASP LYS PHE VAL ALA LYS GLY LEU VAL ARG SER
SEQRES 4 B 253 ALA GLN GLY LYS GLU LYS ILE GLY GLY GLU ALA ASP VAL
SEQRES 5 B 253 PHE ILE GLY ASP ILE THR ASP ALA ASP SER ILE ASN PRO
SEQRES 6 B 253 ALA PHE GLN GLY ILE ASP ALA LEU VAL ILE LEU THR SER
SEQRES 7 B 253 ALA VAL PRO LYS MET LYS PRO GLY PHE ASP PRO THR LYS
SEQRES 8 B 253 GLY GLY ARG PRO GLU PHE ILE PHE GLU ASP GLY GLN TYR
SEQRES 9 B 253 PRO GLU GLN VAL ASP TRP ILE GLY GLN LYS ASN GLN ILE
SEQRES 10 B 253 ASP ALA ALA LYS VAL ALA GLY VAL LYS HIS ILE VAL VAL
SEQRES 11 B 253 VAL GLY SER MET GLY GLY THR ASN PRO ASP HIS PRO LEU
SEQRES 12 B 253 ASN LYS LEU GLY ASN GLY ASN ILE LEU VAL TRP LYS ARG
SEQRES 13 B 253 LYS ALA GLU GLN TYR LEU ALA ASP SER GLY THR PRO TYR
SEQRES 14 B 253 THR ILE ILE ARG ALA GLY GLY LEU LEU ASP LYS GLU GLY
SEQRES 15 B 253 GLY VAL ARG GLU LEU LEU VAL GLY LYS ASP ASP GLU LEU
SEQRES 16 B 253 LEU GLN THR ASP THR LYS THR VAL PRO ARG ALA ASP VAL
SEQRES 17 B 253 ALA GLU VAL CYS ILE GLN ALA LEU LEU PHE GLU GLU ALA
SEQRES 18 B 253 LYS ASN LYS ALA PHE ASP LEU GLY SER LYS PRO GLU GLY
SEQRES 19 B 253 THR SER THR PRO THR LYS ASP PHE LYS ALA LEU PHE SER
SEQRES 20 B 253 GLN VAL THR SER ARG PHE
HET NAP A 400 48
HET NAP B 401 48
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 NAP 2(C21 H28 N7 O17 P3)
FORMUL 5 HOH *369(H2 O)
HELIX 1 1 GLY A 14 GLY A 27 1 14
HELIX 2 2 SER A 39 ILE A 46 1 8
HELIX 3 3 ASP A 59 GLN A 68 1 10
HELIX 4 4 TYR A 104 ASP A 109 1 6
HELIX 5 5 TRP A 110 ALA A 123 1 14
HELIX 6 6 HIS A 141 GLY A 149 5 9
HELIX 7 7 ASN A 150 SER A 165 1 16
HELIX 8 8 ASP A 193 THR A 198 5 6
HELIX 9 9 ARG A 205 PHE A 218 1 14
HELIX 10 10 GLU A 219 LYS A 222 5 4
HELIX 11 11 ASP A 241 GLN A 248 1 8
HELIX 12 12 GLY B 14 GLY B 27 1 14
HELIX 13 13 SER B 39 ILE B 46 1 8
HELIX 14 14 ASP B 59 SER B 62 5 4
HELIX 15 15 ILE B 63 GLN B 68 1 6
HELIX 16 16 TYR B 104 ASP B 109 1 6
HELIX 17 17 TRP B 110 ALA B 123 1 14
HELIX 18 18 HIS B 141 GLY B 149 5 9
HELIX 19 19 ASN B 150 ASP B 164 1 15
HELIX 20 20 ASP B 193 THR B 198 5 6
HELIX 21 21 ARG B 205 PHE B 218 1 14
HELIX 22 22 GLU B 219 LYS B 222 5 4
HELIX 23 23 ASP B 241 VAL B 249 1 9
SHEET 1 A 8 VAL A 52 ILE A 54 0
SHEET 2 A 8 VAL A 32 VAL A 37 1 N GLY A 35 O PHE A 53
SHEET 3 A 8 THR A 6 THR A 10 1 N VAL A 7 O VAL A 32
SHEET 4 A 8 ALA A 72 ILE A 75 1 O VAL A 74 N LEU A 8
SHEET 5 A 8 HIS A 127 SER A 133 1 O VAL A 129 N ILE A 75
SHEET 6 A 8 TYR A 169 ALA A 174 1 O ILE A 172 N GLY A 132
SHEET 7 A 8 LYS A 224 SER A 230 1 O PHE A 226 N ARG A 173
SHEET 8 A 8 LEU A 187 GLY A 190 -1 N GLY A 190 O ASP A 227
SHEET 1 B 2 LYS A 82 MET A 83 0
SHEET 2 B 2 PHE A 97 ILE A 98 -1 O ILE A 98 N LYS A 82
SHEET 1 C 2 GLY A 176 LEU A 178 0
SHEET 2 C 2 THR A 202 PRO A 204 1 O VAL A 203 N GLY A 176
SHEET 1 D 8 VAL B 52 ILE B 54 0
SHEET 2 D 8 VAL B 32 VAL B 37 1 N GLY B 35 O PHE B 53
SHEET 3 D 8 THR B 6 THR B 10 1 N VAL B 9 O LYS B 34
SHEET 4 D 8 ALA B 72 ILE B 75 1 O VAL B 74 N LEU B 8
SHEET 5 D 8 HIS B 127 SER B 133 1 O VAL B 129 N LEU B 73
SHEET 6 D 8 TYR B 169 ALA B 174 1 O ILE B 172 N GLY B 132
SHEET 7 D 8 LYS B 224 SER B 230 1 O PHE B 226 N ARG B 173
SHEET 8 D 8 LEU B 187 GLY B 190 -1 N GLY B 190 O ASP B 227
SHEET 1 E 2 LYS B 82 MET B 83 0
SHEET 2 E 2 PHE B 97 ILE B 98 -1 O ILE B 98 N LYS B 82
SHEET 1 F 2 GLY B 176 LEU B 178 0
SHEET 2 F 2 THR B 202 PRO B 204 1 O VAL B 203 N GLY B 176
SITE 1 AC1 26 SER A 13 GLY A 14 ARG A 15 THR A 16
SITE 2 AC1 26 ARG A 38 ASP A 56 ILE A 57 LEU A 76
SITE 3 AC1 26 THR A 77 SER A 78 VAL A 80 GLN A 103
SITE 4 AC1 26 VAL A 108 VAL A 131 GLY A 132 SER A 133
SITE 5 AC1 26 LYS A 155 ALA A 174 GLY A 175 GLY A 176
SITE 6 AC1 26 LEU A 177 ARG A 205 HOH A 403 HOH A 404
SITE 7 AC1 26 HOH A 409 HOH A 458
SITE 1 AC2 30 SER B 13 GLY B 14 ARG B 15 THR B 16
SITE 2 AC2 30 ARG B 38 ASP B 56 ILE B 57 LEU B 76
SITE 3 AC2 30 THR B 77 SER B 78 VAL B 80 GLN B 103
SITE 4 AC2 30 VAL B 131 GLY B 132 SER B 133 LYS B 155
SITE 5 AC2 30 ALA B 174 GLY B 175 GLY B 176 LEU B 177
SITE 6 AC2 30 ARG B 205 HOH B 402 HOH B 403 HOH B 404
SITE 7 AC2 30 HOH B 422 HOH B 434 HOH B 507 HOH B 510
SITE 8 AC2 30 HOH B 519 HOH B 540
CRYST1 74.634 77.286 92.864 90.00 90.00 90.00 P 21 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 0.013400 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012900 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010800 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
