HEADER PHOSPHATE-BINDING PROTEIN 16-DEC-09 3L39
TITLE CRYSTAL STRUCTURE OF PUTATIVE PHOU-LIKE PHOSPHATE REGULATORY PROTEIN
TITLE 2 (BT4638) FROM BACTEROIDES THETAIOTAOMICRON VPI-5482 AT 1.93 A
TITLE 3 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE PHOU-LIKE PHOSPHATE REGULATORY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON;
SOURCE 3 ORGANISM_TAXID: 226186;
SOURCE 4 STRAIN: VPI-5482;
SOURCE 5 GENE: BT4638, BT_4638;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MH4A
KEYWDS BT4638, PUTATIVE PHOU-LIKE PHOSPHATE REGULATORY PROTEIN, STRUCTURAL
KEYWDS 2 GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, PSI-2, PHOSPHATE-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 5 20-SEP-23 3L39 1 REMARK
REVDAT 4 01-FEB-23 3L39 1 REMARK SEQADV
REVDAT 3 17-JUL-19 3L39 1 REMARK
REVDAT 2 01-NOV-17 3L39 1 REMARK
REVDAT 1 19-JAN-10 3L39 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE PHOU-LIKE PHOSPHATE REGULATORY
JRNL TITL 2 PROTEIN (BT4638) FROM BACTEROIDES THETAIOTAOMICRON VPI-5482
JRNL TITL 3 AT 1.93 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.93 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 18940
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.166
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 981
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) : 1.93
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 496
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE SET COUNT : 32
REMARK 3 BIN FREE R VALUE : 0.3680
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1672
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 187
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.51
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.33000
REMARK 3 B22 (A**2) : 0.33000
REMARK 3 B33 (A**2) : -0.49000
REMARK 3 B12 (A**2) : 0.16000
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): 0.147
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.133
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.679
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1867 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1262 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2562 ; 1.471 ; 2.005
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3140 ; 0.980 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 249 ; 3.075 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 91 ;35.174 ;25.495
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 360 ;11.840 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;15.928 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 291 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2063 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 342 ; 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): 1115 ; 0.869 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 435 ; 0.160 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1841 ; 1.526 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 752 ; 1.068 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 699 ; 1.840 ; 3.000
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 : 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. PHOSPHATES (PO4) FROM THE CRYSTALLIZATION
REMARK 3 SOLUTION WERE MODELED INTO THE STRUCTURE.
REMARK 4
REMARK 4 3L39 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-09.
REMARK 100 THE DEPOSITION ID IS D_1000056777.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-04
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 : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979245
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : FLAT COLLIMATING MIRROR, TOROID
REMARK 200 FOCUSING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18980
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.930
REMARK 200 RESOLUTION RANGE LOW (A) : 44.972
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.3
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 2IIU,1XWM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20.0% GLYCEROL, 1.6M NH4H2PO3, 0.1M
REMARK 280 TRIS PH 8.5, NANODROP, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 39.79350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 22.97479
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 79.12833
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 39.79350
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 22.97479
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 79.12833
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 39.79350
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 22.97479
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 79.12833
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 39.79350
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 22.97479
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 79.12833
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 39.79350
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 22.97479
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 79.12833
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 39.79350
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 22.97479
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 79.12833
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 45.94958
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 158.25667
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 45.94958
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 158.25667
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 45.94958
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 158.25667
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 45.94958
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 158.25667
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 45.94958
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 158.25667
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 45.94958
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 158.25667
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -159.0 KCAL/MOL
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 BIOMT1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 243 LIES ON A SPECIAL POSITION.
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 -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ILE A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 LYS A 2
REMARK 465 ASN A 3
REMARK 465 SER A 4
REMARK 465 PHE A 5
REMARK 465 PHE A 6
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 8 CG CD CE NZ
REMARK 470 LYS A 12 CG CD CE NZ
REMARK 470 GLU A 13 CG CD OE1 OE2
REMARK 470 LYS A 15 CE NZ
REMARK 470 LYS A 51 CD CE NZ
REMARK 470 ARG A 58 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 82 CG CD OE1 OE2
REMARK 470 LYS A 143 CG CD CE NZ
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 182 CG GLU A 182 CD 0.102
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 GLU A 13 71.42 -104.89
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 PO4 A 216
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 217
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 218
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 221
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 222
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 356900 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHH
REMARK 999 FOLLOWED BY THE TARGET SEQUENCE.
DBREF 3L39 A 1 215 UNP Q89YU3 Q89YU3_BACTN 1 215
SEQADV 3L39 MET A -11 UNP Q89YU3 EXPRESSION TAG
SEQADV 3L39 GLY A -10 UNP Q89YU3 EXPRESSION TAG
SEQADV 3L39 SER A -9 UNP Q89YU3 EXPRESSION TAG
SEQADV 3L39 ASP A -8 UNP Q89YU3 EXPRESSION TAG
SEQADV 3L39 LYS A -7 UNP Q89YU3 EXPRESSION TAG
SEQADV 3L39 ILE A -6 UNP Q89YU3 EXPRESSION TAG
SEQADV 3L39 HIS A -5 UNP Q89YU3 EXPRESSION TAG
SEQADV 3L39 HIS A -4 UNP Q89YU3 EXPRESSION TAG
SEQADV 3L39 HIS A -3 UNP Q89YU3 EXPRESSION TAG
SEQADV 3L39 HIS A -2 UNP Q89YU3 EXPRESSION TAG
SEQADV 3L39 HIS A -1 UNP Q89YU3 EXPRESSION TAG
SEQADV 3L39 HIS A 0 UNP Q89YU3 EXPRESSION TAG
SEQRES 1 A 227 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 A 227 LYS ASN SER PHE PHE SER LYS PHE THR PRO LYS GLU PRO
SEQRES 3 A 227 LYS PHE PHE PRO LEU LEU LYS GLN LEU SER ASP VAL LEU
SEQRES 4 A 227 SER ALA SER SER VAL LEU LEU VAL GLU SER MET GLU HIS
SEQRES 5 A 227 ASP LEU PRO THR GLU ARG ALA ASP TYR TYR LYS GLN ILE
SEQRES 6 A 227 LYS ASP MET GLU ARG GLU GLY ASP ARG LEU THR HIS LEU
SEQRES 7 A 227 ILE PHE ASP GLU LEU SER THR THR PHE ILE THR PRO PHE
SEQRES 8 A 227 ASP ARG GLU ASP ILE HIS ASP LEU ALA SER CYS MET ASP
SEQRES 9 A 227 ASP VAL ILE ASP GLY ILE ASN SER SER ALA LYS ARG ILE
SEQRES 10 A 227 VAL ILE TYR ASN PRO ARG PRO ILE SER GLU SER GLY LYS
SEQRES 11 A 227 GLU LEU SER ARG LEU ILE HIS GLU GLU ALA ILE ASN ILE
SEQRES 12 A 227 GLY LYS ALA MET ASP GLU LEU GLU THR PHE ARG LYS ASN
SEQRES 13 A 227 PRO LYS PRO LEU ARG ASP TYR CYS THR GLN LEU HIS ASP
SEQRES 14 A 227 ILE GLU ASN GLN ALA ASP ASP VAL TYR GLU LEU PHE ILE
SEQRES 15 A 227 THR LYS LEU PHE GLU GLU GLU LYS ASP CYS ILE GLU LEU
SEQRES 16 A 227 ILE LYS ILE LYS GLU ILE MET HIS GLU LEU GLU LYS THR
SEQRES 17 A 227 THR ASP ALA ALA GLU HIS VAL GLY LYS ILE LEU LYS ASN
SEQRES 18 A 227 LEU ILE VAL LYS TYR SER
HET PO4 A 216 5
HET PO4 A 217 5
HET PO4 A 218 5
HET PO4 A 219 5
HET PO4 A 220 5
HET PO4 A 221 5
HET PO4 A 222 5
HETNAM PO4 PHOSPHATE ION
FORMUL 2 PO4 7(O4 P 3-)
FORMUL 9 HOH *187(H2 O)
HELIX 1 1 LYS A 15 MET A 38 1 24
HELIX 2 2 LEU A 42 THR A 74 1 33
HELIX 3 3 ASP A 80 ASN A 109 1 30
HELIX 4 4 SER A 114 ASP A 136 1 23
HELIX 5 5 PRO A 145 GLU A 177 1 33
HELIX 6 6 ASP A 179 SER A 215 1 37
SITE 1 AC1 8 SER A 100 LYS A 103 ARG A 104 HIS A 191
SITE 2 AC1 8 GLU A 194 HOH A 253 HOH A 308 HOH A 348
SITE 1 AC2 5 ARG A 104 GLU A 188 HIS A 191 LYS A 195
SITE 2 AC2 5 HOH A 323
SITE 1 AC3 6 HIS A 156 GLU A 201 GLY A 204 LYS A 205
SITE 2 AC3 6 LYS A 208 HOH A 236
SITE 1 AC4 6 HIS A 40 ASP A 41 LEU A 42 GLU A 45
SITE 2 AC4 6 HOH A 381 HOH A 407
SITE 1 AC5 10 SER A 114 GLU A 115 SER A 116 GLU A 126
SITE 2 AC5 10 GLN A 154 GLN A 161 LYS A 172 HOH A 254
SITE 3 AC5 10 HOH A 256 HOH A 393
SITE 1 AC6 6 ARG A 111 GLU A 177 ASP A 179 HOH A 294
SITE 2 AC6 6 HOH A 324 HOH A 386
SITE 1 AC7 6 GLU A 39 GLU A 115 LYS A 118 ARG A 122
SITE 2 AC7 6 HOH A 280 HOH A 362
CRYST1 79.587 79.587 237.385 90.00 90.00 120.00 H 3 2 18
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 0.012565 0.007254 0.000000 0.00000
SCALE2 0.000000 0.014509 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004213 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
