HEADER STRUCTURAL PROTEIN 01-JUL-08 3DNC
TITLE CARBOXYSOME SHELL PROTEIN, CCMK2 C-TERMINAL DELETION MUTANT, WITH A
TITLE 2 CLOSER SPACING BETWEEN HEXAMERS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBON DIOXIDE-CONCENTRATING MECHANISM PROTEIN CCMK HOMOLOG
COMPND 3 2;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: C-TERMINAL (UNP RESIDUES 92-103) DELETION;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP.;
SOURCE 3 ORGANISM_TAXID: 1148;
SOURCE 4 STRAIN: PCC 6803;
SOURCE 5 GENE: CCMK2, SLL1028;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS HEXAMER, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.TANAKA,M.R.SAWAYA,T.O.YEATES
REVDAT 5 30-AUG-23 3DNC 1 REMARK SEQADV
REVDAT 4 25-OCT-17 3DNC 1 REMARK
REVDAT 3 13-JUL-11 3DNC 1 VERSN
REVDAT 2 05-JAN-10 3DNC 1 JRNL
REVDAT 1 20-JAN-09 3DNC 0
JRNL AUTH S.TANAKA,M.R.SAWAYA,M.PHILLIPS,T.O.YEATES
JRNL TITL INSIGHTS FROM MULTIPLE STRUCTURES OF THE SHELL PROTEINS FROM
JRNL TITL 2 THE BETA-CARBOXYSOME.
JRNL REF PROTEIN SCI. V. 18 108 2009
JRNL REFN ISSN 0961-8368
JRNL PMID 19177356
JRNL DOI 10.1002/PRO.14
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 3 NUMBER OF REFLECTIONS : 4369
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) : 0.224
REMARK 3 R VALUE (WORKING SET) : 0.222
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 204
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 339
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE SET COUNT : 19
REMARK 3 BIN FREE R VALUE : 0.4110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 661
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 40
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.08000
REMARK 3 B22 (A**2) : 0.08000
REMARK 3 B33 (A**2) : -0.12000
REMARK 3 B12 (A**2) : 0.04000
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): 0.365
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.251
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.148
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.831
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.912
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.884
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 694 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 457 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 944 ; 1.022 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): 1118 ; 0.891 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 93 ; 4.935 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 26 ;26.379 ;22.692
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 115 ;16.081 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;20.295 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 115 ; 0.059 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 766 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 133 ; 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): 449 ; 1.091 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 187 ; 0.211 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 727 ; 1.768 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 245 ; 1.200 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 215 ; 1.890 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 92
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2433 -9.4293 -9.3427
REMARK 3 T TENSOR
REMARK 3 T11: -0.2480 T22: -0.2054
REMARK 3 T33: -0.3014 T12: -0.0257
REMARK 3 T13: 0.0023 T23: -0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 1.3037 L22: 2.6661
REMARK 3 L33: 0.0367 L12: 0.2954
REMARK 3 L13: -0.2164 L23: -0.0049
REMARK 3 S TENSOR
REMARK 3 S11: -0.0673 S12: -0.0586 S13: -0.0049
REMARK 3 S21: 0.0865 S22: 0.0634 S23: 0.0697
REMARK 3 S31: 0.0240 S32: 0.0724 S33: 0.0039
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 3DNC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048251.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-OCT-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-D
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 4371
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 80.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.2
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.15200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.45600
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2A1B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 31.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CHES, 1.26M AMMONIUM SULFATE,
REMARK 280 0.15M NACL, PH 9.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6
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 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z
REMARK 290 6555 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 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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 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
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -182.0 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 350 BIOMT1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 5 0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 6 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 6 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 O4 SO4 A 100 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 1
REMARK 465 SER A 2
REMARK 465 GLU A 93
REMARK 465 HIS A 94
REMARK 465 HIS A 95
REMARK 465 HIS A 96
REMARK 465 HIS A 97
REMARK 465 HIS A 98
REMARK 465 HIS A 99
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 102
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BN4 RELATED DB: PDB
REMARK 900 CARBOXYSOME SUBUNIT, CCMK1
REMARK 900 RELATED ID: 3DN9 RELATED DB: PDB
REMARK 900 CARBOXYSOME SUBUNIT, CCMK1 C-TERMINAL DELETION MUTANT
REMARK 900 RELATED ID: 3CIM RELATED DB: PDB
REMARK 900 CARBOXYSOME SHELL PROTEIN, CCMK2 C-TERMINAL DELETION MUTANT
REMARK 900 RELATED ID: 2A1B RELATED DB: PDB
REMARK 900 CARBOXYSOME SHELL PROTEIN, CCMK2
REMARK 900 RELATED ID: 2A10 RELATED DB: PDB
REMARK 900 CARBOXYSOME SHELL PROTEIN, CCMK4
REMARK 900 RELATED ID: 2A18 RELATED DB: PDB
REMARK 900 CARBOXYSOME SHELL PROTEIN, CCMK4, CRYSTAL FORM 2
DBREF 3DNC A 1 91 UNP P72761 CCMK2_SYNY3 1 91
SEQADV 3DNC LEU A 92 UNP P72761 EXPRESSION TAG
SEQADV 3DNC GLU A 93 UNP P72761 EXPRESSION TAG
SEQADV 3DNC HIS A 94 UNP P72761 EXPRESSION TAG
SEQADV 3DNC HIS A 95 UNP P72761 EXPRESSION TAG
SEQADV 3DNC HIS A 96 UNP P72761 EXPRESSION TAG
SEQADV 3DNC HIS A 97 UNP P72761 EXPRESSION TAG
SEQADV 3DNC HIS A 98 UNP P72761 EXPRESSION TAG
SEQADV 3DNC HIS A 99 UNP P72761 EXPRESSION TAG
SEQRES 1 A 99 MET SER ILE ALA VAL GLY MET ILE GLU THR ARG GLY PHE
SEQRES 2 A 99 PRO ALA VAL VAL GLU ALA ALA ASP SER MET VAL LYS ALA
SEQRES 3 A 99 ALA ARG VAL THR LEU VAL GLY TYR GLU LYS ILE GLY SER
SEQRES 4 A 99 GLY ARG VAL THR VAL ILE VAL ARG GLY ASP VAL SER GLU
SEQRES 5 A 99 VAL GLN ALA SER VAL SER ALA GLY ILE GLU ALA ALA ASN
SEQRES 6 A 99 ARG VAL ASN GLY GLY GLU VAL LEU SER THR HIS ILE ILE
SEQRES 7 A 99 ALA ARG PRO HIS GLU ASN LEU GLU TYR VAL LEU PRO ILE
SEQRES 8 A 99 LEU GLU HIS HIS HIS HIS HIS HIS
HET SO4 A 100 5
HET SO4 A 101 5
HET GOL A 102 6
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 GOL C3 H8 O3
FORMUL 5 HOH *40(H2 O)
HELIX 1 1 GLY A 12 ALA A 27 1 16
HELIX 2 2 ASP A 49 ARG A 66 1 18
HELIX 3 3 HIS A 82 TYR A 87 1 6
SHEET 1 A 4 VAL A 29 LYS A 36 0
SHEET 2 A 4 ARG A 41 GLY A 48 -1 O THR A 43 N GLU A 35
SHEET 3 A 4 ALA A 4 ARG A 11 -1 N GLY A 6 O VAL A 46
SHEET 4 A 4 GLU A 71 ILE A 78 -1 O SER A 74 N GLU A 9
SITE 1 AC1 2 GLU A 62 ARG A 66
SITE 1 AC2 3 ARG A 11 SER A 39 ARG A 41
SITE 1 AC3 6 SER A 22 ALA A 59 GLU A 62 ALA A 63
SITE 2 AC3 6 ARG A 66 HOH A 103
CRYST1 67.362 67.362 29.034 90.00 90.00 120.00 P 6 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 0.014845 0.008571 0.000000 0.00000
SCALE2 0.000000 0.017142 0.000000 0.00000
SCALE3 0.000000 0.000000 0.034442 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
