HEADER STRUCTURAL PROTEIN 13-JUN-12 4AXI
TITLE STRUCTURE OF THE CLOSTRIDIUM DIFFICILE EUTS PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ETHANOLAMINE CARBOXYSOME STRUCTURAL PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: EUTS;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM DIFFICILE;
SOURCE 3 ORGANISM_TAXID: 272563;
SOURCE 4 STRAIN: 630;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI B;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 37762;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET28B
KEYWDS STRUCTURAL PROTEIN, ETHANOLAMINE, BACTERIAL MICROCOMPARTMENT, BMC
EXPDTA X-RAY DIFFRACTION
AUTHOR A.C.PITTS,L.R.TUCK,A.FAULDS-PAIN,R.J.LEWIS,J.MARLES-WRIGHT
REVDAT 4 20-DEC-23 4AXI 1 REMARK
REVDAT 3 08-MAY-19 4AXI 1 REMARK
REVDAT 2 17-APR-13 4AXI 1 JRNL
REVDAT 1 27-JUN-12 4AXI 0
JRNL AUTH A.C.PITTS,L.R.TUCK,A.FAULDS-PAIN,R.J.LEWIS,J.MARLES-WRIGHT
JRNL TITL STRUCTURAL INSIGHT INTO THE CLOSTRIDIUM DIFFICILE
JRNL TITL 2 ETHANOLAMINE UTILISATION MICROCOMPARTMENT.
JRNL REF PLOS ONE V. 7 48360 2012
JRNL REFN ESSN 1932-6203
JRNL PMID 23144756
JRNL DOI 10.1371/JOURNAL.PONE.0048360
REMARK 2
REMARK 2 RESOLUTION. 1.51 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.51
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.060
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 34282
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.142
REMARK 3 R VALUE (WORKING SET) : 0.140
REMARK 3 FREE R VALUE : 0.180
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1727
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 27.9348 - 3.2517 0.98 3150 206 0.1661 0.1849
REMARK 3 2 3.2517 - 2.5815 1.00 3269 152 0.1344 0.1805
REMARK 3 3 2.5815 - 2.2554 1.00 3279 171 0.1178 0.1397
REMARK 3 4 2.2554 - 2.0492 1.00 3233 179 0.1128 0.1750
REMARK 3 5 2.0492 - 1.9024 1.00 3281 176 0.1083 0.1588
REMARK 3 6 1.9024 - 1.7903 1.00 3295 152 0.1119 0.1718
REMARK 3 7 1.7903 - 1.7006 1.00 3252 184 0.1183 0.1940
REMARK 3 8 1.7006 - 1.6266 1.00 3255 179 0.1466 0.2043
REMARK 3 9 1.6266 - 1.5640 1.00 3297 161 0.1738 0.2350
REMARK 3 10 1.5640 - 1.5100 1.00 3244 167 0.2310 0.2972
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.39
REMARK 3 B_SOL : 53.97
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.64
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.90180
REMARK 3 B22 (A**2) : 3.90180
REMARK 3 B33 (A**2) : 6.54840
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.016 1804
REMARK 3 ANGLE : 1.679 2457
REMARK 3 CHIRALITY : 0.099 311
REMARK 3 PLANARITY : 0.007 313
REMARK 3 DIHEDRAL : 12.923 678
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUE GLU11 ADOPTS MULTIPLE
REMARK 3 CONFORMATIONS IN BOTH CHAINS AND IS MODELLED IN ALTERNATING
REMARK 3 CONFORMATIONS OWING TO STEREOCHEMICAL CONSTRAINTS.
REMARK 4
REMARK 4 4AXI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1290052886.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : SINGLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34286
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.510
REMARK 200 RESOLUTION RANGE LOW (A) : 61.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.50000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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 3CGI
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN IN 200 MM NACL, 50 MM TRIS HCL
REMARK 280 PH 8.0 HANGING DROP VAPOUR DIFFUSION WITH 100/100 NL PROTEIN:
REMARK 280 PRECIPITANT OVER 100 UL WELL SOLUTION OF 24% (W/V) PEG 1500, 20%
REMARK 280 (W/V) GLYCEROL, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 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 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 61.60000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 35.56478
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 12.90667
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 61.60000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 35.56478
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 12.90667
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 61.60000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 35.56478
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 12.90667
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 71.12955
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 25.81333
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 71.12955
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 25.81333
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 71.12955
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 25.81333
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: 20830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -99.6 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 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 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 0
REMARK 465 GLY A 1
REMARK 465 GLU A 118
REMARK 465 HIS A 119
REMARK 465 HIS A 120
REMARK 465 HIS A 121
REMARK 465 HIS A 122
REMARK 465 HIS A 123
REMARK 465 HIS A 124
REMARK 465 MET B 0
REMARK 465 GLY B 1
REMARK 465 LEU B 117
REMARK 465 GLU B 118
REMARK 465 HIS B 119
REMARK 465 HIS B 120
REMARK 465 HIS B 121
REMARK 465 HIS B 122
REMARK 465 HIS B 123
REMARK 465 HIS B 124
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 OD2 ASP B 87 HG SER B 89 1.52
REMARK 500 O THR B 116 O HOH B 2013 1.92
REMARK 500 O THR A 116 O HOH A 2035 1.96
REMARK 500 O HOH A 2034 O HOH A 2035 2.05
REMARK 500 O HOH A 2072 O HOH A 2073 2.13
REMARK 500 OD2 ASP B 87 OG SER B 89 2.16
REMARK 500 OD1 ASP A 97 O HOH A 2081 2.17
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 HE3 MET B 105 O HOH A 2088 3555 1.58
REMARK 500 O HOH A 2016 O HOH A 2017 2555 2.15
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 ARG B 8 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG B 8 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2006 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH A2007 DISTANCE = 6.82 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1118
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N-TERMINAL INSERTION OF GLYCINE AFTER INITIATING
REMARK 999 METHIONINE AND C-TERMINAL HIS-TAG
DBREF 4AXI A 2 116 UNP Q187M0 Q187M0_CLOD6 2 116
DBREF 4AXI B 2 116 UNP Q187M0 Q187M0_CLOD6 2 116
SEQADV 4AXI MET A 0 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI GLY A 1 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI LEU A 117 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI GLU A 118 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI HIS A 119 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI HIS A 120 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI HIS A 121 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI HIS A 122 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI HIS A 123 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI HIS A 124 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI MET B 0 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI GLY B 1 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI LEU B 117 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI GLU B 118 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI HIS B 119 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI HIS B 120 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI HIS B 121 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI HIS B 122 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI HIS B 123 UNP Q187M0 EXPRESSION TAG
SEQADV 4AXI HIS B 124 UNP Q187M0 EXPRESSION TAG
SEQRES 1 A 125 MET GLY THR GLU GLU SER LYS GLN ARG VAL ILE GLN GLU
SEQRES 2 A 125 TYR VAL PRO GLY LYS GLN VAL THR LEU ALA HIS ILE ILE
SEQRES 3 A 125 ALA ASN PRO ASN GLU ASP ILE TYR LYS LYS LEU GLY LEU
SEQRES 4 A 125 VAL LEU ASP LYS LYS ASP ALA ILE GLY ILE LEU THR ILE
SEQRES 5 A 125 THR PRO SER GLU ALA SER ILE ILE ALA ALA ASP VAL ALA
SEQRES 6 A 125 THR LYS ALA SER ASN VAL SER LEU GLY PHE ILE ASP ARG
SEQRES 7 A 125 PHE SER GLY SER VAL VAL ILE SER GLY ASP VAL SER SER
SEQRES 8 A 125 VAL GLU SER ALA LEU ASN ASP VAL LEU GLU VAL LEU GLY
SEQRES 9 A 125 ASN MET LEU ASN PHE SER SER THR LYS ILE THR ARG THR
SEQRES 10 A 125 LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 125 MET GLY THR GLU GLU SER LYS GLN ARG VAL ILE GLN GLU
SEQRES 2 B 125 TYR VAL PRO GLY LYS GLN VAL THR LEU ALA HIS ILE ILE
SEQRES 3 B 125 ALA ASN PRO ASN GLU ASP ILE TYR LYS LYS LEU GLY LEU
SEQRES 4 B 125 VAL LEU ASP LYS LYS ASP ALA ILE GLY ILE LEU THR ILE
SEQRES 5 B 125 THR PRO SER GLU ALA SER ILE ILE ALA ALA ASP VAL ALA
SEQRES 6 B 125 THR LYS ALA SER ASN VAL SER LEU GLY PHE ILE ASP ARG
SEQRES 7 B 125 PHE SER GLY SER VAL VAL ILE SER GLY ASP VAL SER SER
SEQRES 8 B 125 VAL GLU SER ALA LEU ASN ASP VAL LEU GLU VAL LEU GLY
SEQRES 9 B 125 ASN MET LEU ASN PHE SER SER THR LYS ILE THR ARG THR
SEQRES 10 B 125 LEU GLU HIS HIS HIS HIS HIS HIS
HET GOL A1118 14
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *150(H2 O)
HELIX 1 1 THR A 2 LYS A 6 5 5
HELIX 2 2 ASN A 29 LEU A 36 1 8
HELIX 3 3 GLU A 55 LYS A 66 1 12
HELIX 4 4 ASP A 87 ASN A 104 1 18
HELIX 5 5 THR B 2 LYS B 6 5 5
HELIX 6 6 ASN B 29 LEU B 36 1 8
HELIX 7 7 GLU B 55 SER B 68 1 14
HELIX 8 8 ASP B 87 ASN B 104 1 18
SHEET 1 AA 2 GLN A 7 TYR A 13 0
SHEET 2 AA 2 VAL B 9 PRO B 15 1 O ILE B 10 N VAL A 9
SHEET 1 AB 5 VAL A 70 ILE A 75 0
SHEET 2 AB 5 VAL A 82 GLY A 86 -1 O VAL A 83 N GLY A 73
SHEET 3 AB 5 ALA A 45 THR A 52 -1 O ALA A 45 N GLY A 86
SHEET 4 AB 5 GLN A 18 ILE A 25 -1 O GLN A 18 N THR A 52
SHEET 5 AB 5 THR A 114 THR A 116 1 O THR A 114 N ILE A 24
SHEET 1 BA 5 SER B 71 ILE B 75 0
SHEET 2 BA 5 VAL B 82 GLY B 86 -1 O VAL B 83 N GLY B 73
SHEET 3 BA 5 ALA B 45 THR B 52 -1 O ALA B 45 N GLY B 86
SHEET 4 BA 5 GLN B 18 ILE B 25 -1 O GLN B 18 N THR B 52
SHEET 5 BA 5 THR B 114 ARG B 115 1 O THR B 114 N ILE B 24
CISPEP 1 THR A 52 PRO A 53 0 -4.03
CISPEP 2 THR B 52 PRO B 53 0 -0.60
SITE 1 AC1 8 PRO A 53 SER A 54 GLU A 55 HOH A2053
SITE 2 AC1 8 HOH A2090 TYR B 13 SER B 79 HOH B2022
CRYST1 123.200 123.200 38.720 90.00 90.00 120.00 H 3 18
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 0.008117 0.004686 0.000000 0.00000
SCALE2 0.000000 0.009373 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025826 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
