HEADER TRANSCRIPTION 03-FEB-09 3G3Z
TITLE THE STRUCTURE OF NMB1585, A MARR FAMILY REGULATOR FROM NEISSERIA
TITLE 2 MENINGITIDIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REGULATOR, MARR FAMILY;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NMB1585;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NEISSERIA MENINGITIDIS SEROGROUP B;
SOURCE 3 ORGANISM_TAXID: 491;
SOURCE 4 STRAIN: MC58;
SOURCE 5 GENE: NMB1585;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: OPPF160
KEYWDS MARR, NEISSERIA MENINGITIDIS, TRANSCRIPTION FACTOR, STRUCTURAL
KEYWDS 2 GENOMICS, OXFORD PROTEIN PRODUCTION FACILITY, OPPF, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.E.NICHOLS,S.SAINSBURY,J.REN,T.S.WALTER,A.VERMA,D.K.STAMMERS,
AUTHOR 2 N.J.SAUNDERS,R.J.OWENS,OXFORD PROTEIN PRODUCTION FACILITY (OPPF)
REVDAT 2 13-JUL-11 3G3Z 1 VERSN
REVDAT 1 14-APR-09 3G3Z 0
JRNL AUTH C.E.NICHOLS,S.SAINSBURY,J.REN,T.S.WALTER,A.VERMA,
JRNL AUTH 2 D.K.STAMMERS,N.J.SAUNDERS,R.J.OWENS
JRNL TITL THE STRUCTURE OF NMB1585, A MARR-FAMILY REGULATOR FROM
JRNL TITL 2 NEISSERIA MENINGITIDIS
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 65 204 2009
JRNL REFN ESSN 1744-3091
JRNL PMID 19255465
JRNL DOI 10.1107/S174430910900414X
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0047
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
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) : 27.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.6
REMARK 3 NUMBER OF REFLECTIONS : 13531
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 734
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) : 505
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 45.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 35
REMARK 3 BIN FREE R VALUE : 0.3590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2254
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 109
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 33.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.28000
REMARK 3 B22 (A**2) : 3.11000
REMARK 3 B33 (A**2) : -0.91000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.91000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.343
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.246
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.173
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.648
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2288 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3084 ; 1.043 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 282 ; 4.449 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 110 ;41.879 ;25.091
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 428 ;17.395 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ; 8.348 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 348 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1698 ; 0.004 ; 0.020
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): 1402 ; 1.515 ; 4.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2246 ; 2.535 ; 6.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 886 ; 3.477 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 838 ; 5.271 ;10.000
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 : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 75 5
REMARK 3 1 B 1 B 75 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 300 ; 0.220 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 A (A): 297 ; 0.450 ; 5.000
REMARK 3 MEDIUM THERMAL 1 A (A**2): 300 ; 2.710 ;20.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 297 ; 3.560 ;20.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 86 A 112 5
REMARK 3 1 B 86 B 112 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 108 ; 0.140 ; 0.500
REMARK 3 LOOSE POSITIONAL 2 A (A): 97 ; 0.340 ; 5.000
REMARK 3 MEDIUM THERMAL 2 A (A**2): 108 ; 2.490 ;20.000
REMARK 3 LOOSE THERMAL 2 A (A**2): 97 ; 3.810 ;20.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 121 A 142 5
REMARK 3 1 B 121 B 142 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 88 ; 0.300 ; 0.500
REMARK 3 LOOSE POSITIONAL 3 A (A): 85 ; 1.060 ; 5.000
REMARK 3 MEDIUM THERMAL 3 A (A**2): 88 ; 3.390 ;20.000
REMARK 3 LOOSE THERMAL 3 A (A**2): 85 ; 6.880 ;20.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 25
REMARK 3 RESIDUE RANGE : B 116 B 142
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0800 13.8440 23.9690
REMARK 3 T TENSOR
REMARK 3 T11: 0.1546 T22: 0.1192
REMARK 3 T33: 0.1192 T12: 0.0204
REMARK 3 T13: 0.0735 T23: -0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 4.5654 L22: 2.5793
REMARK 3 L33: 1.0450 L12: -2.2390
REMARK 3 L13: 1.8539 L23: -0.6594
REMARK 3 S TENSOR
REMARK 3 S11: -0.1873 S12: -0.1956 S13: -0.0388
REMARK 3 S21: 0.2344 S22: 0.1269 S23: 0.1795
REMARK 3 S31: -0.1090 S32: -0.0245 S33: 0.0603
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 25
REMARK 3 RESIDUE RANGE : A 116 A 142
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9490 9.2760 12.1300
REMARK 3 T TENSOR
REMARK 3 T11: 0.1473 T22: 0.1882
REMARK 3 T33: 0.1388 T12: 0.0138
REMARK 3 T13: 0.0049 T23: -0.0307
REMARK 3 L TENSOR
REMARK 3 L11: 0.5793 L22: 2.4625
REMARK 3 L33: 0.1766 L12: 0.7321
REMARK 3 L13: 0.0689 L23: -0.3941
REMARK 3 S TENSOR
REMARK 3 S11: -0.0714 S12: -0.0119 S13: -0.1088
REMARK 3 S21: -0.3129 S22: 0.0722 S23: -0.0223
REMARK 3 S31: 0.0528 S32: -0.0367 S33: -0.0008
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 26 A 115
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4660 -3.4220 15.1740
REMARK 3 T TENSOR
REMARK 3 T11: 0.0989 T22: 0.1057
REMARK 3 T33: 0.1868 T12: 0.0022
REMARK 3 T13: 0.0383 T23: -0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 2.8947 L22: 0.9088
REMARK 3 L33: 1.7857 L12: -0.8711
REMARK 3 L13: -0.2839 L23: 0.0787
REMARK 3 S TENSOR
REMARK 3 S11: -0.0615 S12: 0.2292 S13: -0.4258
REMARK 3 S21: -0.0658 S22: -0.0045 S23: 0.0267
REMARK 3 S31: 0.0825 S32: 0.0740 S33: 0.0659
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 26 B 115
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3290 31.3850 14.3880
REMARK 3 T TENSOR
REMARK 3 T11: 0.1950 T22: 0.1199
REMARK 3 T33: 0.0933 T12: 0.0070
REMARK 3 T13: -0.0184 T23: 0.0177
REMARK 3 L TENSOR
REMARK 3 L11: 0.9109 L22: 3.5873
REMARK 3 L33: 0.2436 L12: 0.8124
REMARK 3 L13: -0.2701 L23: 0.3848
REMARK 3 S TENSOR
REMARK 3 S11: -0.0417 S12: -0.0064 S13: -0.0537
REMARK 3 S21: -0.1407 S22: 0.0005 S23: -0.0671
REMARK 3 S31: -0.0738 S32: 0.0077 S33: 0.0412
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3G3Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-FEB-09.
REMARK 100 THE RCSB ID CODE IS RCSB051393.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90777, 0.97912, 0.97889
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14294
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.4
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4000
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) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 48.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.26400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
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 (%): 41.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 25%(W/V) PEG 3350, 0.2M
REMARK 280 AMMONIUM CHLORIDE, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 32.18350
REMARK 290 SMTRY3 2 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: 6000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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 GLY A -1
REMARK 465 PRO A 0
REMARK 465 LYS A 143
REMARK 465 GLY B -1
REMARK 465 PRO B 0
REMARK 465 LYS B 143
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 79 48.29 -92.01
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: OPTIC233 RELATED DB: TARGETDB
DBREF 3G3Z A 1 143 UNP Q9JYH5 Q9JYH5_NEIMB 1 143
DBREF 3G3Z B 1 143 UNP Q9JYH5 Q9JYH5_NEIMB 1 143
SEQADV 3G3Z GLY A -1 UNP Q9JYH5 EXPRESSION TAG
SEQADV 3G3Z PRO A 0 UNP Q9JYH5 EXPRESSION TAG
SEQADV 3G3Z GLY B -1 UNP Q9JYH5 EXPRESSION TAG
SEQADV 3G3Z PRO B 0 UNP Q9JYH5 EXPRESSION TAG
SEQRES 1 A 145 GLY PRO MSE ASN GLN LEU ASP GLN LEU GLY THR ARG ILE
SEQRES 2 A 145 ASN LEU ILE CYS ASN VAL PHE ASP LYS TRP ILE GLY GLN
SEQRES 3 A 145 GLN ASP LEU ASN TYR ASN LEU PHE ALA VAL LEU TYR THR
SEQRES 4 A 145 LEU ALA THR GLU GLY SER ARG THR GLN LYS HIS ILE GLY
SEQRES 5 A 145 GLU LYS TRP SER LEU PRO LYS GLN THR VAL SER GLY VAL
SEQRES 6 A 145 CYS LYS THR LEU ALA GLY GLN GLY LEU ILE GLU TRP GLN
SEQRES 7 A 145 GLU GLY GLU GLN ASP ARG ARG LYS ARG LEU LEU SER LEU
SEQRES 8 A 145 THR GLU THR GLY LYS ALA TYR ALA ALA PRO LEU THR GLU
SEQRES 9 A 145 SER ALA GLN GLU PHE SER ASP LYS VAL PHE ALA THR PHE
SEQRES 10 A 145 GLY ASP LYS ARG THR THR ARG LEU PHE ALA ASP LEU ASP
SEQRES 11 A 145 ALA LEU ALA GLU VAL MSE GLU LYS THR ILE SER GLU ASN
SEQRES 12 A 145 LYS LYS
SEQRES 1 B 145 GLY PRO MSE ASN GLN LEU ASP GLN LEU GLY THR ARG ILE
SEQRES 2 B 145 ASN LEU ILE CYS ASN VAL PHE ASP LYS TRP ILE GLY GLN
SEQRES 3 B 145 GLN ASP LEU ASN TYR ASN LEU PHE ALA VAL LEU TYR THR
SEQRES 4 B 145 LEU ALA THR GLU GLY SER ARG THR GLN LYS HIS ILE GLY
SEQRES 5 B 145 GLU LYS TRP SER LEU PRO LYS GLN THR VAL SER GLY VAL
SEQRES 6 B 145 CYS LYS THR LEU ALA GLY GLN GLY LEU ILE GLU TRP GLN
SEQRES 7 B 145 GLU GLY GLU GLN ASP ARG ARG LYS ARG LEU LEU SER LEU
SEQRES 8 B 145 THR GLU THR GLY LYS ALA TYR ALA ALA PRO LEU THR GLU
SEQRES 9 B 145 SER ALA GLN GLU PHE SER ASP LYS VAL PHE ALA THR PHE
SEQRES 10 B 145 GLY ASP LYS ARG THR THR ARG LEU PHE ALA ASP LEU ASP
SEQRES 11 B 145 ALA LEU ALA GLU VAL MSE GLU LYS THR ILE SER GLU ASN
SEQRES 12 B 145 LYS LYS
MODRES 3G3Z MSE A 1 MET SELENOMETHIONINE
MODRES 3G3Z MSE A 134 MET SELENOMETHIONINE
MODRES 3G3Z MSE B 1 MET SELENOMETHIONINE
MODRES 3G3Z MSE B 134 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 134 8
HET MSE B 1 8
HET MSE B 134 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 3 HOH *109(H2 O)
HELIX 1 1 ASN A 2 GLN A 24 1 23
HELIX 2 2 ASN A 28 GLY A 42 1 15
HELIX 3 3 THR A 45 SER A 54 1 10
HELIX 4 4 PRO A 56 GLN A 70 1 15
HELIX 5 5 ASP A 81 ARG A 85 5 5
HELIX 6 6 THR A 90 GLY A 116 1 27
HELIX 7 7 GLY A 116 ASN A 141 1 26
HELIX 8 8 ASN B 2 GLN B 25 1 24
HELIX 9 9 ASN B 28 GLY B 42 1 15
HELIX 10 10 THR B 45 TRP B 53 1 9
HELIX 11 11 PRO B 56 GLN B 70 1 15
HELIX 12 12 ASP B 81 ARG B 85 5 5
HELIX 13 13 THR B 90 ALA B 113 1 24
HELIX 14 14 GLY B 116 LYS B 142 1 27
SHEET 1 A 2 ILE A 73 TRP A 75 0
SHEET 2 A 2 LEU A 87 LEU A 89 -1 O SER A 88 N GLU A 74
SHEET 1 B 2 ILE B 73 TRP B 75 0
SHEET 2 B 2 LEU B 87 LEU B 89 -1 O SER B 88 N GLU B 74
LINK C MSE A 1 N ASN A 2 1555 1555 1.33
LINK C VAL A 133 N MSE A 134 1555 1555 1.33
LINK C MSE A 134 N GLU A 135 1555 1555 1.34
LINK C MSE B 1 N ASN B 2 1555 1555 1.33
LINK C VAL B 133 N MSE B 134 1555 1555 1.33
LINK C MSE B 134 N GLU B 135 1555 1555 1.34
CRYST1 35.001 64.367 61.066 90.00 91.12 90.00 P 1 21 1 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 0.028571 0.000000 0.000561 0.00000
SCALE2 0.000000 0.015536 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016379 0.00000
HETATM 1 N MSE A 1 -7.966 26.540 19.492 1.00 57.20 N
HETATM 2 CA MSE A 1 -8.757 27.355 18.520 1.00 56.67 C
HETATM 3 C MSE A 1 -9.137 26.550 17.273 1.00 52.48 C
HETATM 4 O MSE A 1 -10.233 25.989 17.205 1.00 53.48 O
HETATM 5 CB MSE A 1 -8.013 28.646 18.151 1.00 59.08 C
HETATM 6 CG MSE A 1 -6.492 28.512 18.110 1.00 68.04 C
HETATM 7 SE MSE A 1 -5.581 30.184 17.662 1.00 84.17 SE
HETATM 8 CE MSE A 1 -6.383 31.370 19.004 1.00 78.83 C
(ATOM LINES ARE NOT SHOWN.)
END
