HEADER TRANSCRIPTION 02-JUL-05 2A6C
TITLE CRYSTAL STRUCTURE OF A PUTATIVE TRANSCRIPTIONAL REGULATOR (NE_1354)
TITLE 2 FROM NITROSOMONAS EUROPAEA AT 1.90 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HELIX-TURN-HELIX MOTIF;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NITROSOMONAS EUROPAEA;
SOURCE 3 ORGANISM_TAXID: 915;
SOURCE 4 ATCC: 19718;
SOURCE 5 GENE: NP_841403.1;
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
KEYWDS PUTATIVE TRANSCRIPTIONAL REGULATOR, STRUCTURAL GENOMICS, JOINT CENTER
KEYWDS 2 FOR STRUCTURAL GENOMICS, JCSG, PROTEIN STRUCTURE INITIATIVE, PSI-2,
KEYWDS 3 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 5 25-JAN-23 2A6C 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 2A6C 1 VERSN
REVDAT 3 28-JUL-10 2A6C 1 HEADER TITLE KEYWDS
REVDAT 2 24-FEB-09 2A6C 1 VERSN
REVDAT 1 12-JUL-05 2A6C 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF (NP_841403.1) FROM NITROSOMONAS
JRNL TITL 2 EUROPAEA AT 1.90 A RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 12269
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) : 0.182
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 672
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) : 899
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.2100
REMARK 3 BIN FREE R VALUE SET COUNT : 52
REMARK 3 BIN FREE R VALUE : 0.2350
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1178
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 72
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.00000
REMARK 3 B22 (A**2) : 2.85000
REMARK 3 B33 (A**2) : -1.02000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.83000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.151
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.105
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.221
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1234 ; 0.018 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1186 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1659 ; 1.357 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2733 ; 0.844 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 154 ; 5.035 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 48 ;28.379 ;23.125
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 230 ;12.335 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;12.684 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 198 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1330 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 230 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 249 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1137 ; 0.173 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 602 ; 0.168 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 778 ; 0.081 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 46 ; 0.144 ; 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): 20 ; 0.247 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 101 ; 0.238 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.116 ; 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): 791 ; 2.347 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 318 ; 0.651 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1231 ; 2.861 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 475 ; 5.452 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 428 ; 7.442 ;11.000
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 : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 2A6C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033542.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
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) : 0.97929, 0.91162
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14998
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 26.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : 0.09500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.51600
REMARK 200 R SYM FOR SHELL (I) : 0.51600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
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 (%): 46.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40.0 % MPD, 0.1M PHOSPHATE CITRATE,
REMARK 280 VAPOR DIFFUSION,SITTING DROP,NANODROP, TEMPERATURE 273K, PH 4.2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 43.93100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.39400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 43.93100
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.39400
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, 3
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 -1.000000 0.000000 0.000000 61.30281
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 46.31870
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 87.86200
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 102 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 MSE A -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ALA A 70
REMARK 465 ALA A 71
REMARK 465 MSE B -11
REMARK 465 GLY B -10
REMARK 465 SER B -9
REMARK 465 ASP B -8
REMARK 465 LYS B -7
REMARK 465 ALA B 70
REMARK 465 ALA B 71
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 ILE A -6 CG1 CG2 CD1
REMARK 470 HIS A -5 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 2 CG CD CE NZ
REMARK 470 LYS A 62 CD CE NZ
REMARK 470 GLU A 64 CD OE1 OE2
REMARK 470 LYS A 68 CG CD CE NZ
REMARK 470 ASP A 69 CB CG OD1 OD2
REMARK 470 ILE B -6 CD1
REMARK 470 LYS B 24 CE NZ
REMARK 470 GLU B 27 CD OE1 OE2
REMARK 470 LYS B 62 CD CE NZ
REMARK 470 GLU B 64 CD OE1 OE2
REMARK 470 LYS B 68 CD CE NZ
REMARK 470 ASP B 69 CG OD1 OD2
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 MSE A 1 SE MSE A 1 CE -0.379
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 EDO A 72
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 72
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 73
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 74
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 358727 RELATED DB: TARGETDB
DBREF 2A6C A 1 71 UNP Q82UW4 Q82UW4_NITEU 1 71
DBREF 2A6C B 1 71 UNP Q82UW4 Q82UW4_NITEU 1 71
SEQADV 2A6C MSE A -11 UNP Q82UW4 MODIFIED RESIDUE
SEQADV 2A6C GLY A -10 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C SER A -9 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C ASP A -8 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C LYS A -7 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C ILE A -6 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C HIS A -5 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C HIS A -4 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C HIS A -3 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C HIS A -2 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C HIS A -1 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C HIS A 0 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C MSE A 1 UNP Q82UW4 MET 1 MODIFIED RESIDUE
SEQADV 2A6C MSE A 3 UNP Q82UW4 MET 3 MODIFIED RESIDUE
SEQADV 2A6C MSE A 40 UNP Q82UW4 MET 40 MODIFIED RESIDUE
SEQADV 2A6C MSE A 55 UNP Q82UW4 MET 55 MODIFIED RESIDUE
SEQADV 2A6C MSE B -11 UNP Q82UW4 MODIFIED RESIDUE
SEQADV 2A6C GLY B -10 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C SER B -9 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C ASP B -8 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C LYS B -7 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C ILE B -6 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C HIS B -5 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C HIS B -4 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C HIS B -3 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C HIS B -2 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C HIS B -1 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C HIS B 0 UNP Q82UW4 EXPRESSION TAG
SEQADV 2A6C MSE B 1 UNP Q82UW4 MET 1 MODIFIED RESIDUE
SEQADV 2A6C MSE B 3 UNP Q82UW4 MET 3 MODIFIED RESIDUE
SEQADV 2A6C MSE B 40 UNP Q82UW4 MET 40 MODIFIED RESIDUE
SEQADV 2A6C MSE B 55 UNP Q82UW4 MET 55 MODIFIED RESIDUE
SEQRES 1 A 83 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 A 83 LYS MSE ARG SER GLN LEU LEU ILE VAL LEU GLN GLU HIS
SEQRES 3 A 83 LEU ARG ASN SER GLY LEU THR GLN PHE LYS ALA ALA GLU
SEQRES 4 A 83 LEU LEU GLY VAL THR GLN PRO ARG VAL SER ASP LEU MSE
SEQRES 5 A 83 ARG GLY LYS ILE ASP LEU PHE SER LEU GLU SER LEU ILE
SEQRES 6 A 83 ASP MSE ILE THR SER ILE GLY LEU LYS VAL GLU ILE ASN
SEQRES 7 A 83 ILE LYS ASP ALA ALA
SEQRES 1 B 83 MSE GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE
SEQRES 2 B 83 LYS MSE ARG SER GLN LEU LEU ILE VAL LEU GLN GLU HIS
SEQRES 3 B 83 LEU ARG ASN SER GLY LEU THR GLN PHE LYS ALA ALA GLU
SEQRES 4 B 83 LEU LEU GLY VAL THR GLN PRO ARG VAL SER ASP LEU MSE
SEQRES 5 B 83 ARG GLY LYS ILE ASP LEU PHE SER LEU GLU SER LEU ILE
SEQRES 6 B 83 ASP MSE ILE THR SER ILE GLY LEU LYS VAL GLU ILE ASN
SEQRES 7 B 83 ILE LYS ASP ALA ALA
MODRES 2A6C MSE A 1 MET SELENOMETHIONINE
MODRES 2A6C MSE A 3 MET SELENOMETHIONINE
MODRES 2A6C MSE A 40 MET SELENOMETHIONINE
MODRES 2A6C MSE A 55 MET SELENOMETHIONINE
MODRES 2A6C MSE B 1 MET SELENOMETHIONINE
MODRES 2A6C MSE B 3 MET SELENOMETHIONINE
MODRES 2A6C MSE B 40 MET SELENOMETHIONINE
MODRES 2A6C MSE B 55 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 3 8
HET MSE A 40 8
HET MSE A 55 8
HET MSE B 1 8
HET MSE B 3 8
HET MSE B 40 8
HET MSE B 55 8
HET EDO A 72 4
HET CIT B 72 13
HET GOL B 73 6
HET GOL B 74 6
HETNAM MSE SELENOMETHIONINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CIT CITRIC ACID
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 3 EDO C2 H6 O2
FORMUL 4 CIT C6 H8 O7
FORMUL 5 GOL 2(C3 H8 O3)
FORMUL 7 HOH *72(H2 O)
HELIX 1 1 HIS A 0 ASN A 17 1 18
HELIX 2 2 THR A 21 GLY A 30 1 10
HELIX 3 3 THR A 32 ARG A 41 1 10
HELIX 4 4 LYS A 43 PHE A 47 5 5
HELIX 5 5 SER A 48 ILE A 59 1 12
HELIX 6 6 HIS B 0 ASN B 17 1 18
HELIX 7 7 THR B 21 GLY B 30 1 10
HELIX 8 8 THR B 32 ARG B 41 1 10
HELIX 9 9 LYS B 43 PHE B 47 5 5
HELIX 10 10 SER B 48 ILE B 59 1 12
LINK C HIS A 0 N MSE A 1 1555 1555 1.32
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C LYS A 2 N MSE A 3 1555 1555 1.31
LINK C MSE A 3 N ARG A 4 1555 1555 1.32
LINK C LEU A 39 N MSE A 40 1555 1555 1.33
LINK C MSE A 40 N ARG A 41 1555 1555 1.33
LINK C ASP A 54 N MSE A 55 1555 1555 1.32
LINK C MSE A 55 N ILE A 56 1555 1555 1.33
LINK C HIS B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N LYS B 2 1555 1555 1.33
LINK C LYS B 2 N MSE B 3 1555 1555 1.32
LINK C MSE B 3 N ARG B 4 1555 1555 1.32
LINK C LEU B 39 N MSE B 40 1555 1555 1.33
LINK C MSE B 40 N ARG B 41 1555 1555 1.33
LINK C ASP B 54 N MSE B 55 1555 1555 1.33
LINK C MSE B 55 N ILE B 56 1555 1555 1.33
SITE 1 AC1 1 SER A 18
SITE 1 AC2 10 HIS A -1 HIS B -1 HIS B -2 HIS B -5
SITE 2 AC2 10 HIS B -3 HIS B -4 HIS B 0 ARG B 4
SITE 3 AC2 10 GLU B 50 ASP B 54
SITE 1 AC3 5 HIS A -1 HIS A 0 HIS B -1 HIS B 0
SITE 2 AC3 5 HOH B 80
SITE 1 AC4 4 HIS B 14 LEU B 15 SER B 18 HOH B 111
CRYST1 87.862 40.788 53.393 90.00 119.83 90.00 C 1 2 1 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 0.011380 0.000000 0.006530 0.00000
SCALE2 0.000000 0.024520 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021590 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
