HEADER STRUCTURAL PROTEIN 26-FEB-09 3GFH
TITLE CRYSTAL STRUCTURE OF EUTL SHELL PROTEIN OF THE BACTERIAL ETHANOLAMINE
TITLE 2 MICROMPARTMENT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ETHANOLAMINE UTILIZATION PROTEIN EUTL;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: B2439, EUT-L, EUTL, JW2432, YFFJ;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K12;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET101
KEYWDS BACTERIAL MIRCOCOMPARTMENT, SHELL PROTEIN, ETHANOLAMINE, STRUCTURAL
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SAGERMANN,K.NIKOLAKAKIS,A.OHTAKI
REVDAT 3 03-APR-24 3GFH 1 REMARK
REVDAT 2 21-FEB-24 3GFH 1 REMARK SEQADV
REVDAT 1 21-JUL-09 3GFH 0
JRNL AUTH M.SAGERMANN,A.OHTAKI,K.NIKOLAKAKIS
JRNL TITL CRYSTAL STRUCTURE OF THE EUTL SHELL PROTEIN OF THE
JRNL TITL 2 ETHANOLAMINE AMMONIA LYASE MICROCOMPARTMENT
JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 8883 2009
JRNL REFN ISSN 0027-8424
JRNL PMID 19451619
JRNL DOI 10.1073/PNAS.0902324106
REMARK 2
REMARK 2 RESOLUTION. 2.20 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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 34866
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) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2944
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2503
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 215
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3118
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 171
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.85000
REMARK 3 B22 (A**2) : -10.85000
REMARK 3 B33 (A**2) : 21.70000
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): 0.034
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.033
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.228
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.162
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.906
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.866
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3200 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2944 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4383 ; 2.289 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6820 ; 0.879 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 428 ; 7.130 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 120 ;41.594 ;24.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 456 ;22.372 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;25.012 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 520 ; 0.116 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3646 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 604 ; 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): 2150 ; 0.935 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 862 ; 0.188 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3437 ; 1.606 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1050 ; 2.632 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 946 ; 4.162 ; 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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.575
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : K, H, -L
REMARK 3 TWIN FRACTION : 0.425
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS REFINED AGAINST
REMARK 3 TWINNED DATA AS PUBLISHED. THE DATA IS HEMOHEDRAL TWINNING WITH
REMARK 3 TWINNING OPERATORS: (H,-H-K,-L) AND CORRESPONDING TWINNED
REMARK 3 FRACTIONS: 0.575, 0.425. RESIDUES 2-216 COULD BE FITTED RELIABLY
REMARK 3 INTO THE ELECTRON DENSITY MAP. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 3GFH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-09.
REMARK 100 THE DEPOSITION ID IS D_1000051793.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : SI-MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AND XDS
REMARK 200 DATA SCALING SOFTWARE : AND SCALEIT
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51500
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 19.950
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 85.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
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) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.27800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.460
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: MODEL WAS DERIVED FROM FITTING INTO A 3.5 A SAD
REMARK 200 DENSITY DERIVED FROM TWO MERCURY ATOMS.
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M NACL, 100MM PHOSPHATE, MES BUFFER
REMARK 280 PH6.5, 5% PEG 400, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 3
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
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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 7310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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 33.69200
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 58.35626
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -33.69200
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 58.35626
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 7380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL
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 -0.500000 -0.866025 0.000000 67.38400
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 33.69200
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 58.35626
REMARK 350 BIOMT3 3 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 1
REMARK 465 ILE A 216
REMARK 465 GLN A 217
REMARK 465 ARG A 218
REMARK 465 ALA A 219
REMARK 465 HIS A 220
REMARK 465 HIS A 221
REMARK 465 HIS A 222
REMARK 465 HIS A 223
REMARK 465 HIS A 224
REMARK 465 HIS A 225
REMARK 465 MET B 1
REMARK 465 ILE B 216
REMARK 465 GLN B 217
REMARK 465 ARG B 218
REMARK 465 ALA B 219
REMARK 465 HIS B 220
REMARK 465 HIS B 221
REMARK 465 HIS B 222
REMARK 465 HIS B 223
REMARK 465 HIS B 224
REMARK 465 HIS B 225
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 O ILE B 142 O HOH B 268 1.77
REMARK 500 O TYR A 70 O GLU A 182 1.84
REMARK 500 O TYR B 70 O GLU B 182 1.90
REMARK 500 OE1 GLU A 62 OG SER A 134 2.03
REMARK 500 O PRO B 179 O TYR B 185 2.05
REMARK 500 CB PRO A 2 OD1 ASP A 5 2.10
REMARK 500 O CYS B 201 CG2 THR B 205 2.12
REMARK 500 O PRO A 179 O TYR A 185 2.12
REMARK 500 NE2 HIS A 127 O HOH A 290 2.14
REMARK 500 O VAL A 84 O HOH A 234 2.17
REMARK 500 O ALA A 98 OD2 ASP A 101 2.18
REMARK 500 O SER A 137 O HOH A 228 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 OE1 GLU A 27 CD1 LEU A 173 2665 1.09
REMARK 500 OE1 GLU B 27 CD1 LEU B 173 3665 1.38
REMARK 500 CD GLU B 27 CD1 LEU B 173 3665 1.61
REMARK 500 NH1 ARG B 15 CG1 ILE B 211 3665 1.61
REMARK 500 NH1 ARG A 15 CG1 ILE A 211 2665 1.65
REMARK 500 OE2 GLU B 27 CD1 LEU B 173 3665 1.72
REMARK 500 CD GLU A 27 CD1 LEU A 173 2665 1.84
REMARK 500 NH1 ARG A 15 CD1 ILE A 211 2665 1.86
REMARK 500 OE2 GLU B 27 CB LEU B 173 3665 1.88
REMARK 500 OE2 GLU B 27 CG LEU B 173 3665 1.99
REMARK 500 CA LYS A 29 NH2 ARG B 26 3675 2.03
REMARK 500 CZ ARG A 15 CD1 ILE A 211 2665 2.07
REMARK 500 CB ALA B 81 O HOH B 221 3665 2.14
REMARK 500 CZ ARG A 15 CG1 ILE A 211 2665 2.17
REMARK 500 NH1 ARG B 15 CD1 ILE B 211 3665 2.17
REMARK 500 O GLN A 58 O HOH A 273 2765 2.19
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 CYS A 201 CB CYS A 201 SG 0.303
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
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 ATM2 ATM3
REMARK 500 ASP A 23 CB - CG - OD1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 PRO A 179 C - N - CA ANGL. DEV. = 13.3 DEGREES
REMARK 500 CYS A 201 CA - CB - SG ANGL. DEV. = 9.0 DEGREES
REMARK 500 PRO B 79 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 PRO B 79 C - N - CD ANGL. DEV. = -30.7 DEGREES
REMARK 500 ASP B 118 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 PRO B 154 C - N - CA ANGL. DEV. = -9.7 DEGREES
REMARK 500 PRO B 179 C - N - CA ANGL. DEV. = 19.5 DEGREES
REMARK 500 PRO B 179 C - N - CD ANGL. DEV. = -17.5 DEGREES
REMARK 500 PRO B 180 C - N - CA ANGL. DEV. = -11.2 DEGREES
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 3 -92.29 -55.88
REMARK 500 GLU A 83 12.32 -147.96
REMARK 500 ASN A 109 55.42 -158.80
REMARK 500 PRO A 154 170.93 -53.24
REMARK 500 PRO A 179 -70.55 -3.49
REMARK 500 ASN A 184 10.64 87.95
REMARK 500 SER A 193 -150.95 -83.71
REMARK 500 ASN A 214 -84.70 -132.89
REMARK 500 ALA B 3 -98.95 -31.35
REMARK 500 ALA B 13 137.65 177.35
REMARK 500 LYS B 29 48.67 83.51
REMARK 500 ALA B 74 -70.12 -34.36
REMARK 500 SER B 78 -138.09 -87.90
REMARK 500 GLU B 83 18.55 -62.73
REMARK 500 ALA B 140 -172.15 62.67
REMARK 500 ASN B 214 -81.76 -126.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 SER B 78 PRO B 79 133.92
REMARK 500 GLY B 82 GLU B 83 -143.88
REMARK 500 ALA B 140 GLY B 141 -141.15
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 HG A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG B 800
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CGI RELATED DB: PDB
REMARK 900 CARBOXYSOMAL SHELL PROTEIN
REMARK 900 RELATED ID: 3BN4 RELATED DB: PDB
REMARK 900 CARBOXYSOMAL SHELL PROTEIN
DBREF 3GFH A 1 219 UNP P76541 EUTL_ECOLI 1 219
DBREF 3GFH B 1 219 UNP P76541 EUTL_ECOLI 1 219
SEQADV 3GFH HIS A 220 UNP P76541 EXPRESSION TAG
SEQADV 3GFH HIS A 221 UNP P76541 EXPRESSION TAG
SEQADV 3GFH HIS A 222 UNP P76541 EXPRESSION TAG
SEQADV 3GFH HIS A 223 UNP P76541 EXPRESSION TAG
SEQADV 3GFH HIS A 224 UNP P76541 EXPRESSION TAG
SEQADV 3GFH HIS A 225 UNP P76541 EXPRESSION TAG
SEQADV 3GFH HIS B 220 UNP P76541 EXPRESSION TAG
SEQADV 3GFH HIS B 221 UNP P76541 EXPRESSION TAG
SEQADV 3GFH HIS B 222 UNP P76541 EXPRESSION TAG
SEQADV 3GFH HIS B 223 UNP P76541 EXPRESSION TAG
SEQADV 3GFH HIS B 224 UNP P76541 EXPRESSION TAG
SEQADV 3GFH HIS B 225 UNP P76541 EXPRESSION TAG
SEQRES 1 A 225 MET PRO ALA LEU ASP LEU ILE ARG PRO SER VAL THR ALA
SEQRES 2 A 225 MET ARG VAL ILE ALA SER VAL ASN ALA ASP PHE ALA ARG
SEQRES 3 A 225 GLU LEU LYS LEU PRO PRO HIS ILE ARG SER LEU GLY LEU
SEQRES 4 A 225 ILE SER ALA ASP SER ASP ASP VAL THR TYR ILE ALA ALA
SEQRES 5 A 225 ASP GLU ALA THR LYS GLN ALA MET VAL GLU VAL VAL TYR
SEQRES 6 A 225 GLY ARG SER LEU TYR ALA GLY ALA ALA HIS GLY PRO SER
SEQRES 7 A 225 PRO THR ALA GLY GLU VAL LEU ILE MET LEU GLY GLY PRO
SEQRES 8 A 225 ASN PRO ALA GLU VAL ARG ALA GLY LEU ASP ALA MET ILE
SEQRES 9 A 225 ALA HIS ILE GLU ASN GLY ALA ALA PHE GLN TRP ALA ASN
SEQRES 10 A 225 ASP ALA GLN ASP THR ALA PHE LEU ALA HIS VAL VAL SER
SEQRES 11 A 225 ARG THR GLY SER TYR LEU SER SER THR ALA GLY ILE THR
SEQRES 12 A 225 LEU GLY ASP PRO MET ALA TYR LEU VAL ALA PRO PRO LEU
SEQRES 13 A 225 GLU ALA THR TYR GLY ILE ASP ALA ALA LEU LYS SER ALA
SEQRES 14 A 225 ASP VAL GLN LEU ALA THR TYR VAL PRO PRO PRO SER GLU
SEQRES 15 A 225 THR ASN TYR SER ALA ALA PHE LEU THR GLY SER GLN ALA
SEQRES 16 A 225 ALA CYS LYS ALA ALA CYS ASN ALA PHE THR ASP ALA VAL
SEQRES 17 A 225 LEU GLU ILE ALA ARG ASN PRO ILE GLN ARG ALA HIS HIS
SEQRES 18 A 225 HIS HIS HIS HIS
SEQRES 1 B 225 MET PRO ALA LEU ASP LEU ILE ARG PRO SER VAL THR ALA
SEQRES 2 B 225 MET ARG VAL ILE ALA SER VAL ASN ALA ASP PHE ALA ARG
SEQRES 3 B 225 GLU LEU LYS LEU PRO PRO HIS ILE ARG SER LEU GLY LEU
SEQRES 4 B 225 ILE SER ALA ASP SER ASP ASP VAL THR TYR ILE ALA ALA
SEQRES 5 B 225 ASP GLU ALA THR LYS GLN ALA MET VAL GLU VAL VAL TYR
SEQRES 6 B 225 GLY ARG SER LEU TYR ALA GLY ALA ALA HIS GLY PRO SER
SEQRES 7 B 225 PRO THR ALA GLY GLU VAL LEU ILE MET LEU GLY GLY PRO
SEQRES 8 B 225 ASN PRO ALA GLU VAL ARG ALA GLY LEU ASP ALA MET ILE
SEQRES 9 B 225 ALA HIS ILE GLU ASN GLY ALA ALA PHE GLN TRP ALA ASN
SEQRES 10 B 225 ASP ALA GLN ASP THR ALA PHE LEU ALA HIS VAL VAL SER
SEQRES 11 B 225 ARG THR GLY SER TYR LEU SER SER THR ALA GLY ILE THR
SEQRES 12 B 225 LEU GLY ASP PRO MET ALA TYR LEU VAL ALA PRO PRO LEU
SEQRES 13 B 225 GLU ALA THR TYR GLY ILE ASP ALA ALA LEU LYS SER ALA
SEQRES 14 B 225 ASP VAL GLN LEU ALA THR TYR VAL PRO PRO PRO SER GLU
SEQRES 15 B 225 THR ASN TYR SER ALA ALA PHE LEU THR GLY SER GLN ALA
SEQRES 16 B 225 ALA CYS LYS ALA ALA CYS ASN ALA PHE THR ASP ALA VAL
SEQRES 17 B 225 LEU GLU ILE ALA ARG ASN PRO ILE GLN ARG ALA HIS HIS
SEQRES 18 B 225 HIS HIS HIS HIS
HET HG A 800 1
HET HG B 800 1
HETNAM HG MERCURY (II) ION
FORMUL 3 HG 2(HG 2+)
FORMUL 5 HOH *171(H2 O)
HELIX 1 1 ASN A 21 LEU A 28 1 8
HELIX 2 2 SER A 44 ALA A 59 1 16
HELIX 3 3 GLY A 72 GLY A 76 5 5
HELIX 4 4 ASN A 92 GLU A 108 1 17
HELIX 5 5 PRO A 154 ALA A 169 1 16
HELIX 6 6 LYS A 198 ASN A 214 1 17
HELIX 7 7 ASN B 21 LYS B 29 1 9
HELIX 8 8 SER B 44 ALA B 59 1 16
HELIX 9 9 GLY B 72 GLY B 76 5 5
HELIX 10 10 ASN B 92 ASN B 109 1 18
HELIX 11 11 PRO B 154 SER B 168 1 15
HELIX 12 12 LYS B 198 ASN B 214 1 17
SHEET 1 A 6 LEU A 6 ILE A 7 0
SHEET 2 A 6 PHE A 113 TRP A 115 -1 O PHE A 113 N ILE A 7
SHEET 3 A 6 ALA A 123 VAL A 129 -1 O PHE A 124 N GLN A 114
SHEET 4 A 6 MET A 148 ALA A 153 -1 O MET A 148 N VAL A 129
SHEET 5 A 6 SER A 186 THR A 191 -1 O ALA A 188 N LEU A 151
SHEET 6 A 6 GLN A 172 VAL A 177 -1 N ALA A 174 O PHE A 189
SHEET 1 B 4 VAL A 11 ILE A 17 0
SHEET 2 B 4 SER A 36 ALA A 42 -1 O LEU A 39 N ARG A 15
SHEET 3 B 4 VAL A 84 GLY A 90 -1 O LEU A 88 N GLY A 38
SHEET 4 B 4 GLU A 62 SER A 68 -1 N GLU A 62 O GLY A 89
SHEET 1 C 4 VAL B 11 ILE B 17 0
SHEET 2 C 4 SER B 36 ALA B 42 -1 O LEU B 37 N ILE B 17
SHEET 3 C 4 VAL B 84 GLY B 90 -1 O ILE B 86 N ILE B 40
SHEET 4 C 4 GLU B 62 SER B 68 -1 N GLU B 62 O GLY B 89
SHEET 1 D 5 GLN B 114 TRP B 115 0
SHEET 2 D 5 ALA B 123 VAL B 129 -1 O PHE B 124 N GLN B 114
SHEET 3 D 5 MET B 148 ALA B 153 -1 O MET B 148 N VAL B 129
SHEET 4 D 5 SER B 186 THR B 191 -1 O ALA B 188 N LEU B 151
SHEET 5 D 5 GLN B 172 VAL B 177 -1 N ALA B 174 O PHE B 189
SITE 1 AC1 4 VAL A 128 ALA A 149 CYS A 197 CYS A 201
SITE 1 AC2 5 HIS B 127 VAL B 128 ALA B 149 CYS B 197
SITE 2 AC2 5 CYS B 201
CRYST1 67.384 67.384 79.661 90.00 90.00 120.00 P 3 6
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 0.014840 0.008568 0.000000 0.00000
SCALE2 0.000000 0.017136 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012553 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
