HEADER HYDROLASE 14-NOV-07 3BDI
TITLE CRYSTAL STRUCTURE OF PREDICTED CIB-LIKE HYDROLASE (NP_393672.1) FROM
TITLE 2 THERMOPLASMA ACIDOPHILUM AT 1.45 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN TA0194;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOPLASMA ACIDOPHILUM DSM 1728;
SOURCE 3 ORGANISM_TAXID: 273075;
SOURCE 4 STRAIN: DSM 1728, AMRC-C165, IFO 15155, JCM 9062;
SOURCE 5 ATCC: 25905;
SOURCE 6 GENE: NP_393672.1, TA0194;
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 NP_393672.1, PREDICTED CIB-LIKE HYDROLASE, STRUCTURAL GENOMICS, JOINT
KEYWDS 2 CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 3 PSI-2, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 6 25-JAN-23 3BDI 1 REMARK SEQADV
REVDAT 5 24-JUL-19 3BDI 1 REMARK LINK
REVDAT 4 25-OCT-17 3BDI 1 REMARK
REVDAT 3 13-JUL-11 3BDI 1 VERSN
REVDAT 2 24-FEB-09 3BDI 1 VERSN
REVDAT 1 27-NOV-07 3BDI 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF PREDICTED CIB-LIKE HYDROLASE
JRNL TITL 2 (NP_393672.1) FROM THERMOPLASMA ACIDOPHILUM AT 1.45 A
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 37039
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1851
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) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2548
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.78
REMARK 3 BIN R VALUE (WORKING SET) : 0.1960
REMARK 3 BIN FREE R VALUE SET COUNT : 127
REMARK 3 BIN FREE R VALUE : 0.2670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1596
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 203
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 12.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.78000
REMARK 3 B22 (A**2) : -0.64000
REMARK 3 B33 (A**2) : -0.14000
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): 0.064
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.066
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.041
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.094
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1779 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1211 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2414 ; 1.622 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2953 ; 0.973 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 232 ; 6.481 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 75 ;40.007 ;23.867
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 301 ;12.771 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;12.993 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 260 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2038 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 373 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 366 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1255 ; 0.196 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 878 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 895 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 154 ; 0.219 ; 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): 8 ; 0.145 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 67 ; 0.292 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.115 ; 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): 1191 ; 1.847 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 453 ; 0.478 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1795 ; 2.415 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 752 ; 3.791 ; 7.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 619 ; 4.910 ; 9.000
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 : 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 0 A 206
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5682 26.7390 13.5602
REMARK 3 T TENSOR
REMARK 3 T11: -0.0013 T22: -0.0114
REMARK 3 T33: -0.0160 T12: -0.0016
REMARK 3 T13: 0.0182 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.2299 L22: 0.4640
REMARK 3 L33: 0.1473 L12: 0.1697
REMARK 3 L13: -0.0316 L23: -0.1047
REMARK 3 S TENSOR
REMARK 3 S11: -0.0213 S12: -0.0236 S13: -0.0248
REMARK 3 S21: -0.1118 S22: 0.0053 S23: -0.0359
REMARK 3 S31: -0.0081 S32: 0.0068 S33: 0.0161
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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:
REMARK 3 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
REMARK 3 2. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.
REMARK 3 3. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE
REMARK 3 INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY
REMARK 3 OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75
REMARK 3 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL
REMARK 3 S-MET INCORPORATION.
REMARK 3 4. POLYETHYLENE GLYCOL MOLECULES FROM THE CRYSTALLIZATION
REMARK 3 CONDITIONS WERE MODELED.
REMARK 4
REMARK 4 3BDI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000045385.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-07
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 : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.94939, 0.97939, 0.97953
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 OPTICS : ADJUSTABLE FOCUSING MIRRORS IN K
REMARK 200 -B GEOMETRY
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37089
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 27.338
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : 0.08700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.19400
REMARK 200 R SYM FOR SHELL (I) : 0.19400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NANODROP, 5.0% PEG 3000, 44.0% PEG
REMARK 280 400, 0.1M MES PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
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 21.69200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.82200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.14600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.82200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.69200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.14600
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 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 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 ASP A 23 CG OD1 OD2
REMARK 470 ARG A 26 CD NE CZ NH1 NH2
REMARK 470 ARG A 27 CZ NH1 NH2
REMARK 470 LYS A 83 CE NZ
REMARK 470 LYS A 94 CE NZ
REMARK 470 ARG A 100 CD NE CZ NH1 NH2
REMARK 470 LYS A 144 CG CD CE NZ
REMARK 470 ARG A 146 NH1 NH2
REMARK 470 LYS A 166 CD CE NZ
REMARK 470 GLU A 193 CD OE1 OE2
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 OE1 GLU A 87 O HOH A 318 2.14
REMARK 500 OE2 GLU A 87 OH TYR A 120 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 178 CD GLU A 178 OE2 -0.081
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 107 -122.66 62.67
REMARK 500 SER A 107 -119.55 62.67
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 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 209
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 388819 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 1. THE 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.
REMARK 999 2. DNA SEQUENCING OF THE CLONED CONSTRUCT REVEALS A GLU AT
REMARK 999 POSITION 190 INSTEAD OF LYS. THIS IS CONSISTENT WITH THE
REMARK 999 OBSERVED ELECTRON DENSITY AT THIS POSITION.
DBREF 3BDI A 11 206 UNP Q9HLN3 Q9HLN3_THEAC 2 197
SEQADV 3BDI GLY A 0 UNP Q9HLN3 EXPRESSION TAG
SEQADV 3BDI MSE A 1 UNP Q9HLN3 VARIANT
SEQADV 3BDI ALA A 2 UNP Q9HLN3 VARIANT
SEQADV 3BDI LEU A 3 UNP Q9HLN3 VARIANT
SEQADV 3BDI GLN A 4 UNP Q9HLN3 VARIANT
SEQADV 3BDI GLU A 5 UNP Q9HLN3 VARIANT
SEQADV 3BDI GLU A 6 UNP Q9HLN3 VARIANT
SEQADV 3BDI PHE A 7 UNP Q9HLN3 VARIANT
SEQADV 3BDI ILE A 8 UNP Q9HLN3 VARIANT
SEQADV 3BDI ASP A 9 UNP Q9HLN3 VARIANT
SEQADV 3BDI VAL A 10 UNP Q9HLN3 VARIANT
SEQADV 3BDI GLU A 190 UNP Q9HLN3 LYS 181 SEE REMARK 999
SEQRES 1 A 207 GLY MSE ALA LEU GLN GLU GLU PHE ILE ASP VAL ASN GLY
SEQRES 2 A 207 THR ARG VAL PHE GLN ARG LYS MSE VAL THR ASP SER ASN
SEQRES 3 A 207 ARG ARG SER ILE ALA LEU PHE HIS GLY TYR SER PHE THR
SEQRES 4 A 207 SER MSE ASP TRP ASP LYS ALA ASP LEU PHE ASN ASN TYR
SEQRES 5 A 207 SER LYS ILE GLY TYR ASN VAL TYR ALA PRO ASP TYR PRO
SEQRES 6 A 207 GLY PHE GLY ARG SER ALA SER SER GLU LYS TYR GLY ILE
SEQRES 7 A 207 ASP ARG GLY ASP LEU LYS HIS ALA ALA GLU PHE ILE ARG
SEQRES 8 A 207 ASP TYR LEU LYS ALA ASN GLY VAL ALA ARG SER VAL ILE
SEQRES 9 A 207 MSE GLY ALA SER MSE GLY GLY GLY MSE VAL ILE MSE THR
SEQRES 10 A 207 THR LEU GLN TYR PRO ASP ILE VAL ASP GLY ILE ILE ALA
SEQRES 11 A 207 VAL ALA PRO ALA TRP VAL GLU SER LEU LYS GLY ASP MSE
SEQRES 12 A 207 LYS LYS ILE ARG GLN LYS THR LEU LEU VAL TRP GLY SER
SEQRES 13 A 207 LYS ASP HIS VAL VAL PRO ILE ALA LEU SER LYS GLU TYR
SEQRES 14 A 207 ALA SER ILE ILE SER GLY SER ARG LEU GLU ILE VAL GLU
SEQRES 15 A 207 GLY SER GLY HIS PRO VAL TYR ILE GLU LYS PRO GLU GLU
SEQRES 16 A 207 PHE VAL ARG ILE THR VAL ASP PHE LEU ARG ASN LEU
MODRES 3BDI MSE A 1 MET SELENOMETHIONINE
MODRES 3BDI MSE A 20 MET SELENOMETHIONINE
MODRES 3BDI MSE A 40 MET SELENOMETHIONINE
MODRES 3BDI MSE A 104 MET SELENOMETHIONINE
MODRES 3BDI MSE A 108 MET SELENOMETHIONINE
MODRES 3BDI MSE A 112 MET SELENOMETHIONINE
MODRES 3BDI MSE A 115 MET SELENOMETHIONINE
MODRES 3BDI MSE A 142 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 20 8
HET MSE A 40 8
HET MSE A 104 16
HET MSE A 108 16
HET MSE A 112 8
HET MSE A 115 8
HET MSE A 142 8
HET PEG A 207 7
HET PEG A 208 7
HET PEG A 209 7
HETNAM MSE SELENOMETHIONINE
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 2 PEG 3(C4 H10 O3)
FORMUL 5 HOH *203(H2 O)
HELIX 1 1 THR A 38 ALA A 45 5 8
HELIX 2 2 ASP A 46 LYS A 53 1 8
HELIX 3 3 ASP A 81 ASN A 96 1 16
HELIX 4 4 SER A 107 TYR A 120 1 14
HELIX 5 5 VAL A 135 SER A 137 5 3
HELIX 6 6 LEU A 138 LYS A 143 1 6
HELIX 7 7 PRO A 161 ILE A 172 1 12
HELIX 8 8 PRO A 186 LYS A 191 1 6
HELIX 9 9 LYS A 191 ASN A 205 1 15
SHEET 1 A 8 GLN A 4 VAL A 10 0
SHEET 2 A 8 THR A 13 MSE A 20 -1 O GLN A 17 N GLU A 6
SHEET 3 A 8 TYR A 56 PRO A 61 -1 O VAL A 58 N MSE A 20
SHEET 4 A 8 ARG A 27 PHE A 32 1 N ARG A 27 O ASN A 57
SHEET 5 A 8 SER A 101 ALA A 106 1 O VAL A 102 N SER A 28
SHEET 6 A 8 VAL A 124 VAL A 130 1 O VAL A 130 N GLY A 105
SHEET 7 A 8 THR A 149 GLY A 154 1 O LEU A 150 N ALA A 129
SHEET 8 A 8 ARG A 176 VAL A 180 1 O ARG A 176 N LEU A 151
LINK C GLY A 0 N MSE A 1 1555 1555 1.34
LINK C MSE A 1 N ALA A 2 1555 1555 1.33
LINK C LYS A 19 N MSE A 20 1555 1555 1.33
LINK C MSE A 20 N VAL A 21 1555 1555 1.32
LINK C SER A 39 N MSE A 40 1555 1555 1.34
LINK C MSE A 40 N ASP A 41 1555 1555 1.33
LINK C ILE A 103 N AMSE A 104 1555 1555 1.33
LINK C ILE A 103 N BMSE A 104 1555 1555 1.33
LINK C AMSE A 104 N GLY A 105 1555 1555 1.33
LINK C BMSE A 104 N GLY A 105 1555 1555 1.33
LINK C SER A 107 N AMSE A 108 1555 1555 1.33
LINK C SER A 107 N BMSE A 108 1555 1555 1.34
LINK C AMSE A 108 N GLY A 109 1555 1555 1.34
LINK C BMSE A 108 N GLY A 109 1555 1555 1.33
LINK C GLY A 111 N MSE A 112 1555 1555 1.33
LINK C MSE A 112 N VAL A 113 1555 1555 1.34
LINK C ILE A 114 N MSE A 115 1555 1555 1.32
LINK C MSE A 115 N THR A 116 1555 1555 1.32
LINK C ASP A 141 N MSE A 142 1555 1555 1.33
LINK C MSE A 142 N LYS A 143 1555 1555 1.35
SITE 1 AC1 2 ASN A 11 LYS A 74
SITE 1 AC2 2 TYR A 35 GLY A 65
SITE 1 AC3 6 GLY A 67 ARG A 68 GLU A 190 LYS A 191
SITE 2 AC3 6 HOH A 366 HOH A 397
CRYST1 43.384 46.292 101.644 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 0.023050 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021602 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009838 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
