HEADER TRANSCRIPTION 06-JAN-10 3LA7
TITLE CRYSTAL STRUCTURE OF NTCA IN APO-FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLOBAL NITROGEN REGULATOR;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DNA-BINDING PROTEIN VF1, NITROGEN-RESPONSIVE REGULATORY
COMPND 5 PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANABAENA;
SOURCE 3 ORGANISM_TAXID: 103690;
SOURCE 4 STRAIN: PCC 7120;
SOURCE 5 GENE: ALR4392, BIFA, NTCA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS NITROGEN REGULATOR, ACTIVATOR, DNA-BINDING, TRANSCRIPTION,
KEYWDS 2 TRANSCRIPTION REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.X.ZHAO,Y.L.JIANG,Y.X.HE,Y.F.CHEN,Y.B.TENG,C.C.ZHANG,Y.X.CHEN,
AUTHOR 2 C.Z.ZHOU
REVDAT 3 20-MAR-24 3LA7 1 HETSYN
REVDAT 2 29-JUL-20 3LA7 1 COMPND REMARK SEQADV HETNAM
REVDAT 2 2 1 SITE
REVDAT 1 01-SEP-10 3LA7 0
JRNL AUTH M.X.ZHAO,Y.L.JIANG,Y.X.HE,Y.F.CHEN,Y.B.TENG,Y.X.CHEN,
JRNL AUTH 2 C.C.ZHANG,C.Z.ZHOU
JRNL TITL STRUCTURAL BASIS FOR THE ALLOSTERIC CONTROL OF THE GLOBAL
JRNL TITL 2 TRANSCRIPTION FACTOR NTCA BY THE NITROGEN STARVATION SIGNAL
JRNL TITL 3 2-OXOGLUTARATE.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 12487 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20616047
JRNL DOI 10.1073/PNAS.1001556107
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
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) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 37279
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.215
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1972
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) : 2710
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 142
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3247
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 85.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.55000
REMARK 3 B22 (A**2) : 0.55000
REMARK 3 B33 (A**2) : -1.10000
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): 0.159
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.156
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.106
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.524
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3329 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4486 ; 1.410 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 413 ; 5.730 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 134 ;32.782 ;22.985
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 628 ;15.240 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;12.899 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 532 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2385 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2066 ; 1.048 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3346 ; 1.924 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1263 ; 2.641 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1140 ; 4.327 ; 4.500
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3LA7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JAN-10.
REMARK 100 THE DEPOSITION ID IS D_1000057027.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791, 0.9792, 0.9795, 0.9700
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39299
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 10.70
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.2000
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) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : 7.90
REMARK 200 R MERGE FOR SHELL (I) : 0.53400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30-40%(V/V) PEG 300, 0.1M NAAC PH4.5,
REMARK 280 0.2M NACL, 2MM DTT, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 85.97950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.97950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 33.75300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.81200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 33.75300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.81200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 85.97950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 33.75300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.81200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 85.97950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 33.75300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.81200
REMARK 290 SMTRY3 8 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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3330 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ILE A 2
REMARK 465 VAL A 3
REMARK 465 THR A 4
REMARK 465 GLN A 5
REMARK 465 PRO A 215
REMARK 465 VAL A 216
REMARK 465 THR A 217
REMARK 465 LEU A 218
REMARK 465 SER A 219
REMARK 465 ARG A 220
REMARK 465 GLN A 221
REMARK 465 PHE A 222
REMARK 465 THR A 223
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ILE B 2
REMARK 465 VAL B 3
REMARK 465 THR B 4
REMARK 465 GLN B 5
REMARK 465 ALA B 17
REMARK 465 THR B 18
REMARK 465 GLY B 19
REMARK 465 ALA B 20
REMARK 465 PHE B 21
REMARK 465 PRO B 22
REMARK 465 THR B 217
REMARK 465 LEU B 218
REMARK 465 SER B 219
REMARK 465 ARG B 220
REMARK 465 GLN B 221
REMARK 465 PHE B 222
REMARK 465 THR B 223
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 B 59 O HOH B 257 1.92
REMARK 500 NH1 ARG A 88 O HOH A 233 2.02
REMARK 500 OD2 ASP A 144 O HOH A 283 2.06
REMARK 500 O VAL B 12 O GLN B 15 2.07
REMARK 500 CB CYS B 164 O GLY B 167 2.18
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 NZ LYS B 49 OE1 GLU B 71 4555 1.25
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 ALA A 20 -127.39 -132.75
REMARK 500 ASN A 72 1.44 87.20
REMARK 500 THR A 82 -158.44 -99.01
REMARK 500 LYS A 85 -40.35 -136.28
REMARK 500 PHE A 160 11.19 -141.62
REMARK 500 ASP A 171 50.91 -90.36
REMARK 500 SER A 185 -167.18 -118.18
REMARK 500 ASN B 31 -3.11 76.43
REMARK 500 ASN B 72 2.67 82.81
REMARK 500 ASP B 87 98.04 -165.39
REMARK 500 GLU B 114 -60.71 -99.69
REMARK 500 PHE B 160 11.07 -141.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3LA2 RELATED DB: PDB
REMARK 900 RELATED ID: 3LA3 RELATED DB: PDB
DBREF 3LA7 A 1 223 UNP P0A4U6 NTCA_ANASP 1 223
DBREF 3LA7 B 1 223 UNP P0A4U6 NTCA_ANASP 1 223
SEQADV 3LA7 MET A -19 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 GLY A -18 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 SER A -17 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 SER A -16 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 HIS A -15 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 HIS A -14 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 HIS A -13 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 HIS A -12 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 HIS A -11 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 HIS A -10 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 SER A -9 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 SER A -8 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 GLY A -7 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 LEU A -6 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 VAL A -5 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 PRO A -4 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 ARG A -3 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 GLY A -2 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 SER A -1 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 HIS A 0 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 MET B -19 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 GLY B -18 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 SER B -17 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 SER B -16 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 HIS B -15 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 HIS B -14 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 HIS B -13 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 HIS B -12 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 HIS B -11 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 HIS B -10 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 SER B -9 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 SER B -8 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 GLY B -7 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 LEU B -6 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 VAL B -5 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 PRO B -4 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 ARG B -3 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 GLY B -2 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 SER B -1 UNP P0A4U6 EXPRESSION TAG
SEQADV 3LA7 HIS B 0 UNP P0A4U6 EXPRESSION TAG
SEQRES 1 A 243 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 243 LEU VAL PRO ARG GLY SER HIS MET ILE VAL THR GLN ASP
SEQRES 3 A 243 LYS ALA LEU ALA ASN VAL PHE ARG GLN MET ALA THR GLY
SEQRES 4 A 243 ALA PHE PRO PRO VAL VAL GLU THR PHE GLU ARG ASN LYS
SEQRES 5 A 243 THR ILE PHE PHE PRO GLY ASP PRO ALA GLU ARG VAL TYR
SEQRES 6 A 243 PHE LEU LEU LYS GLY ALA VAL LYS LEU SER ARG VAL TYR
SEQRES 7 A 243 GLU ALA GLY GLU GLU ILE THR VAL ALA LEU LEU ARG GLU
SEQRES 8 A 243 ASN SER VAL PHE GLY VAL LEU SER LEU LEU THR GLY ASN
SEQRES 9 A 243 LYS SER ASP ARG PHE TYR HIS ALA VAL ALA PHE THR PRO
SEQRES 10 A 243 VAL GLU LEU LEU SER ALA PRO ILE GLU GLN VAL GLU GLN
SEQRES 11 A 243 ALA LEU LYS GLU ASN PRO GLU LEU SER MET LEU MET LEU
SEQRES 12 A 243 ARG GLY LEU SER SER ARG ILE LEU GLN THR GLU MET MET
SEQRES 13 A 243 ILE GLU THR LEU ALA HIS ARG ASP MET GLY SER ARG LEU
SEQRES 14 A 243 VAL SER PHE LEU LEU ILE LEU CYS ARG ASP PHE GLY VAL
SEQRES 15 A 243 PRO CYS ALA ASP GLY ILE THR ILE ASP LEU LYS LEU SER
SEQRES 16 A 243 HIS GLN ALA ILE ALA GLU ALA ILE GLY SER THR ARG VAL
SEQRES 17 A 243 THR VAL THR ARG LEU LEU GLY ASP LEU ARG GLU LYS LYS
SEQRES 18 A 243 MET ILE SER ILE HIS LYS LYS LYS ILE THR VAL HIS LYS
SEQRES 19 A 243 PRO VAL THR LEU SER ARG GLN PHE THR
SEQRES 1 B 243 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 243 LEU VAL PRO ARG GLY SER HIS MET ILE VAL THR GLN ASP
SEQRES 3 B 243 LYS ALA LEU ALA ASN VAL PHE ARG GLN MET ALA THR GLY
SEQRES 4 B 243 ALA PHE PRO PRO VAL VAL GLU THR PHE GLU ARG ASN LYS
SEQRES 5 B 243 THR ILE PHE PHE PRO GLY ASP PRO ALA GLU ARG VAL TYR
SEQRES 6 B 243 PHE LEU LEU LYS GLY ALA VAL LYS LEU SER ARG VAL TYR
SEQRES 7 B 243 GLU ALA GLY GLU GLU ILE THR VAL ALA LEU LEU ARG GLU
SEQRES 8 B 243 ASN SER VAL PHE GLY VAL LEU SER LEU LEU THR GLY ASN
SEQRES 9 B 243 LYS SER ASP ARG PHE TYR HIS ALA VAL ALA PHE THR PRO
SEQRES 10 B 243 VAL GLU LEU LEU SER ALA PRO ILE GLU GLN VAL GLU GLN
SEQRES 11 B 243 ALA LEU LYS GLU ASN PRO GLU LEU SER MET LEU MET LEU
SEQRES 12 B 243 ARG GLY LEU SER SER ARG ILE LEU GLN THR GLU MET MET
SEQRES 13 B 243 ILE GLU THR LEU ALA HIS ARG ASP MET GLY SER ARG LEU
SEQRES 14 B 243 VAL SER PHE LEU LEU ILE LEU CYS ARG ASP PHE GLY VAL
SEQRES 15 B 243 PRO CYS ALA ASP GLY ILE THR ILE ASP LEU LYS LEU SER
SEQRES 16 B 243 HIS GLN ALA ILE ALA GLU ALA ILE GLY SER THR ARG VAL
SEQRES 17 B 243 THR VAL THR ARG LEU LEU GLY ASP LEU ARG GLU LYS LYS
SEQRES 18 B 243 MET ILE SER ILE HIS LYS LYS LYS ILE THR VAL HIS LYS
SEQRES 19 B 243 PRO VAL THR LEU SER ARG GLN PHE THR
HET BOG A 224 20
HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE
HETSYN BOG BETA-OCTYLGLUCOSIDE; OCTYL BETA-D-GLUCOSIDE; OCTYL D-
HETSYN 2 BOG GLUCOSIDE; OCTYL GLUCOSIDE
FORMUL 3 BOG C14 H28 O6
FORMUL 4 HOH *170(H2 O)
HELIX 1 1 ASP A 6 ALA A 17 1 12
HELIX 2 2 VAL A 77 THR A 82 1 6
HELIX 3 3 ILE A 105 LYS A 113 1 9
HELIX 4 4 ASN A 115 HIS A 142 1 28
HELIX 5 5 ASP A 144 PHE A 160 1 17
HELIX 6 6 SER A 175 GLY A 184 1 10
HELIX 7 7 THR A 186 LYS A 200 1 15
HELIX 8 8 ASP B 6 GLN B 15 1 10
HELIX 9 9 VAL B 77 THR B 82 1 6
HELIX 10 10 ILE B 105 ASN B 115 1 11
HELIX 11 11 PRO B 116 ALA B 141 1 26
HELIX 12 12 ASP B 144 PHE B 160 1 17
HELIX 13 13 SER B 175 GLY B 184 1 10
HELIX 14 14 THR B 186 LYS B 200 1 15
SHEET 1 A 4 VAL A 24 PHE A 28 0
SHEET 2 A 4 VAL A 98 PRO A 104 -1 O VAL A 98 N PHE A 28
SHEET 3 A 4 ARG A 43 LYS A 49 -1 N VAL A 44 O ALA A 103
SHEET 4 A 4 VAL A 74 PHE A 75 -1 O PHE A 75 N TYR A 45
SHEET 1 B 4 THR A 33 PHE A 35 0
SHEET 2 B 4 TYR A 90 ALA A 94 -1 O ALA A 92 N ILE A 34
SHEET 3 B 4 VAL A 52 VAL A 57 -1 N SER A 55 O HIS A 91
SHEET 4 B 4 GLU A 63 LEU A 69 -1 O ALA A 67 N LEU A 54
SHEET 1 C 4 GLY A 161 PRO A 163 0
SHEET 2 C 4 ILE A 168 ILE A 170 -1 O THR A 169 N VAL A 162
SHEET 3 C 4 LYS A 209 VAL A 212 -1 O ILE A 210 N ILE A 170
SHEET 4 C 4 ILE A 203 HIS A 206 -1 N SER A 204 O THR A 211
SHEET 1 D 4 VAL B 24 PHE B 28 0
SHEET 2 D 4 VAL B 98 PRO B 104 -1 O VAL B 98 N PHE B 28
SHEET 3 D 4 ARG B 43 LYS B 49 -1 N PHE B 46 O LEU B 101
SHEET 4 D 4 VAL B 74 PHE B 75 -1 O PHE B 75 N TYR B 45
SHEET 1 E 4 THR B 33 PHE B 35 0
SHEET 2 E 4 TYR B 90 ALA B 94 -1 O ALA B 92 N ILE B 34
SHEET 3 E 4 VAL B 52 VAL B 57 -1 N LYS B 53 O VAL B 93
SHEET 4 E 4 GLU B 63 LEU B 69 -1 O LEU B 69 N VAL B 52
SHEET 1 F 4 GLY B 161 PRO B 163 0
SHEET 2 F 4 ILE B 168 ILE B 170 -1 O THR B 169 N VAL B 162
SHEET 3 F 4 LYS B 209 VAL B 212 -1 O ILE B 210 N ILE B 170
SHEET 4 F 4 ILE B 203 HIS B 206 -1 N SER B 204 O THR B 211
CRYST1 67.506 85.624 171.959 90.00 90.00 90.00 C 2 2 21 16
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 0.014813 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011679 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005815 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
