HEADER HYDROLASE 15-APR-13 4BJ0
TITLE XYLOGLUCAN BINDING MODULE (CBM4-2 X2-L110F) IN COMPLEX WITH BRANCHED
TITLE 2 XYLOSES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: XYLANASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.2.1.8;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOTHERMUS MARINUS;
SOURCE 3 ORGANISM_TAXID: 29549;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: T7 EXPRESS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET22B
KEYWDS HYDROLASE, XYLOGLUCAN, CBM4-2, X2 L110F, CH-PI INTERACTION,
KEYWDS 2 ENGINEERED CONSTRUCT
EXPDTA X-RAY DIFFRACTION
AUTHOR L.SCHANTZ,M.HAKANSSON,D.T.LOGAN,E.NORDBERG-KARLSSON,M.OHLIN
REVDAT 6 20-DEC-23 4BJ0 1 HETSYN
REVDAT 5 29-JUL-20 4BJ0 1 COMPND REMARK HETNAM LINK
REVDAT 5 2 1 SITE ATOM
REVDAT 4 17-JAN-18 4BJ0 1 JRNL REMARK
REVDAT 3 03-DEC-14 4BJ0 1 JRNL
REVDAT 2 29-OCT-14 4BJ0 1 JRNL
REVDAT 1 23-APR-14 4BJ0 0
JRNL AUTH L.VON SCHANTZ,M.HAKANSSON,D.T.LOGAN,E.NORDBERG-KARLSSON,
JRNL AUTH 2 M.OHLIN
JRNL TITL CARBOHYDRATE BINDING MODULE RECOGNITION OF XYLOGLUCAN
JRNL TITL 2 DEFINED BY POLAR CONTACTS WITH BRANCHING XYLOSES AND CH-PI
JRNL TITL 3 INTERACTIONS.
JRNL REF PROTEINS V. 82 3466 2014
JRNL REFN ISSN 0887-3585
JRNL PMID 25302425
JRNL DOI 10.1002/PROT.24700
REMARK 2
REMARK 2 RESOLUTION. 1.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 76023
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) : 0.115
REMARK 3 R VALUE (WORKING SET) : 0.114
REMARK 3 FREE R VALUE : 0.129
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4040
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) : 1.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.03
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5228
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.29
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 280
REMARK 3 BIN FREE R VALUE : 0.2870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1261
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 85
REMARK 3 SOLVENT ATOMS : 316
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.21000
REMARK 3 B22 (A**2) : 0.46000
REMARK 3 B33 (A**2) : -0.25000
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): 0.020
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.020
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.012
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.502
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.981
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.981
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1481 ; 0.027 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2034 ; 0.017 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2055 ; 2.238 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3476 ; 1.747 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 198 ; 7.634 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 72 ;34.999 ;25.139
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 204 ;11.956 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;13.608 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 256 ; 0.298 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1711 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 341 ; 0.004 ; 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): 884 ; 2.375 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1000 ; 1.700 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1460 ; 3.543 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 597 ; 4.738 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 580 ; 6.709 ; 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): 3515 ; 1.913 ; 3.000
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 : 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 AND REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4BJ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1290056430.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.04
REMARK 200 MONOCHROMATOR : GERMANIUM CRYSTALS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80063
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.000
REMARK 200 RESOLUTION RANGE LOW (A) : 44.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 11.00
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 25.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.3
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.72000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
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 2Y6H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 % W/V PEG 1500, 0.1 M MMT BUFFER PH
REMARK 280 5.5, 20 MM SPERMINE, 8 MM XXXG
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 35.89000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 24.39500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.89000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 24.39500
REMARK 290 SMTRY3 4 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 A2183 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 ALA A 169
REMARK 465 LEU A 170
REMARK 465 GLU A 171
REMARK 465 HIS A 172
REMARK 465 HIS A 173
REMARK 465 HIS A 174
REMARK 465 HIS A 175
REMARK 465 HIS A 176
REMARK 465 HIS A 177
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 ALA A 168 CA C O CB
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 HOH A 2068 O HOH A 2123 2.08
REMARK 500 O HOH A 2301 O HOH A 2302 2.13
REMARK 500 O HOH A 2272 O HOH A 2274 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 O HOH A 2241 O HOH A 2272 3455 1.84
REMARK 500 OE1 GLN A 96 NE2 GLN A 96 2555 2.03
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 VAL A 3 CB VAL A 3 CG1 -0.158
REMARK 500 GLU A 52 CB GLU A 52 CG -0.185
REMARK 500 GLU A 52 CG GLU A 52 CD 0.133
REMARK 500 GLU A 95 CD GLU A 95 OE2 -0.068
REMARK 500 SER A 109 CA SER A 109 CB 0.093
REMARK 500 GLU A 112 CD GLU A 112 OE2 -0.077
REMARK 500 ARG A 142 CZ ARG A 142 NH1 0.114
REMARK 500 ARG A 142 CZ ARG A 142 NH2 -0.095
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 VAL A 3 CG1 - CB - CG2 ANGL. DEV. = -11.5 DEGREES
REMARK 500 ASP A 20 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 GLU A 23 OE1 - CD - OE2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 ASP A 29 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 91 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 91 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ARG A 91 NE - CZ - NH2 ANGL. DEV. = -8.9 DEGREES
REMARK 500 ASP A 97 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 97 O - C - N ANGL. DEV. = -11.1 DEGREES
REMARK 500 ARG A 142 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 142 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 142 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP A 166 CB - CG - OD2 ANGL. DEV. = -6.3 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 ASP A 136 -167.09 -119.33
REMARK 500 ILE A 141 -167.32 -121.51
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 A2022 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A2316 DISTANCE = 6.01 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1167 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 9 O
REMARK 620 2 GLU A 11 OE2 80.0
REMARK 620 3 GLU A 52 OE2 88.9 89.3
REMARK 620 4 GLU A 52 O 157.9 82.3 77.7
REMARK 620 5 LYS A 55 O 86.4 86.0 173.9 105.5
REMARK 620 6 ASP A 160 OD1 77.0 156.7 94.0 121.0 88.8
REMARK 620 7 ASP A 160 OD2 127.0 148.1 106.0 74.2 80.0 52.0
REMARK 620 N 1 2 3 4 5 6
DBREF 4BJ0 A 2 166 UNP Q6V8M0 Q6V8M0_RHOMR 1 165
SEQADV 4BJ0 LEU A 167 UNP Q6V8M0 EXPRESSION TAG
SEQADV 4BJ0 ALA A 168 UNP Q6V8M0 EXPRESSION TAG
SEQADV 4BJ0 ALA A 169 UNP Q6V8M0 EXPRESSION TAG
SEQADV 4BJ0 LEU A 170 UNP Q6V8M0 EXPRESSION TAG
SEQADV 4BJ0 GLU A 171 UNP Q6V8M0 EXPRESSION TAG
SEQADV 4BJ0 HIS A 172 UNP Q6V8M0 EXPRESSION TAG
SEQADV 4BJ0 HIS A 173 UNP Q6V8M0 EXPRESSION TAG
SEQADV 4BJ0 HIS A 174 UNP Q6V8M0 EXPRESSION TAG
SEQADV 4BJ0 HIS A 175 UNP Q6V8M0 EXPRESSION TAG
SEQADV 4BJ0 HIS A 176 UNP Q6V8M0 EXPRESSION TAG
SEQADV 4BJ0 HIS A 177 UNP Q6V8M0 EXPRESSION TAG
SEQADV 4BJ0 PHE A 69 UNP Q6V8M0 TRP 68 ENGINEERED MUTATION
SEQADV 4BJ0 ASN A 70 UNP Q6V8M0 ASP 69 ENGINEERED MUTATION
SEQADV 4BJ0 GLN A 72 UNP Q6V8M0 GLU 71 ENGINEERED MUTATION
SEQADV 4BJ0 LEU A 76 UNP Q6V8M0 PHE 75 ENGINEERED MUTATION
SEQADV 4BJ0 ARG A 91 UNP Q6V8M0 TRP 90 ENGINEERED MUTATION
SEQADV 4BJ0 ASP A 111 UNP Q6V8M0 GLN 110 ENGINEERED MUTATION
SEQADV 4BJ0 HIS A 118 UNP Q6V8M0 GLU 117 ENGINEERED MUTATION
SEQRES 1 A 176 LEU VAL ALA ASN ILE ASN GLY GLY PHE GLU SER THR PRO
SEQRES 2 A 176 ALA GLY VAL VAL THR ASP LEU ALA GLU GLY VAL GLU GLY
SEQRES 3 A 176 TRP ASP LEU ASN VAL GLY SER SER VAL THR ASN PRO PRO
SEQRES 4 A 176 VAL PHE GLU VAL LEU GLU THR SER ASP ALA PRO GLU GLY
SEQRES 5 A 176 ASN LYS VAL LEU ALA VAL THR VAL ASN GLY VAL GLY ASN
SEQRES 6 A 176 ASN PRO PHE ASN ILE GLN ALA THR ALA LEU PRO VAL ASN
SEQRES 7 A 176 VAL ARG PRO GLY VAL THR TYR THR TYR THR ILE ARG ALA
SEQRES 8 A 176 ARG ALA GLU GLN ASP GLY ALA VAL VAL SER PHE THR VAL
SEQRES 9 A 176 GLY ASN GLN SER PHE ASP GLU TYR GLY ARG LEU HIS HIS
SEQRES 10 A 176 GLN GLN ILE THR THR GLU TRP GLN PRO PHE THR PHE GLU
SEQRES 11 A 176 PHE THR VAL SER ASP GLN GLU THR VAL ILE ARG ALA PRO
SEQRES 12 A 176 ILE HIS PHE GLY TYR ALA ALA ASN VAL GLY ASN THR ILE
SEQRES 13 A 176 TYR ILE ASP GLY LEU ALA ILE VAL ASP LEU ALA ALA LEU
SEQRES 14 A 176 GLU HIS HIS HIS HIS HIS HIS
HET CA A1167 1
HET GLC A1169 12
HET BGC B 1 12
HET BGC B 2 11
HET BGC B 3 11
HET BGC B 4 11
HET XYS B 5 9
HET XYS B 6 9
HET XYS B 7 9
HETNAM CA CALCIUM ION
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM BGC BETA-D-GLUCOPYRANOSE
HETNAM XYS ALPHA-D-XYLOPYRANOSE
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN XYS ALPHA-D-XYLOSE; D-XYLOSE; XYLOSE; XYLOPYRANOSE
FORMUL 2 CA CA 2+
FORMUL 3 GLC C6 H12 O6
FORMUL 4 BGC 4(C6 H12 O6)
FORMUL 8 XYS 3(C5 H10 O5)
FORMUL 11 HOH *316(H2 O)
HELIX 1 1 ASN A 67 ASN A 70 5 4
HELIX 2 2 TYR A 149 VAL A 153 5 5
SHEET 1 AA 6 GLY A 16 VAL A 17 0
SHEET 2 AA 6 VAL A 41 GLU A 46 -1 O VAL A 44 N GLY A 16
SHEET 3 AA 6 LYS A 55 THR A 60 -1 O VAL A 56 N LEU A 45
SHEET 4 AA 6 THR A 156 ASP A 166 -1 O ILE A 157 N VAL A 59
SHEET 5 AA 6 THR A 85 ALA A 94 -1 O THR A 87 N VAL A 165
SHEET 6 AA 6 GLN A 126 THR A 133 -1 O GLN A 126 N ALA A 92
SHEET 1 AB 5 TRP A 28 ASP A 29 0
SHEET 2 AB 5 GLN A 72 ASN A 79 -1 O THR A 74 N ASP A 29
SHEET 3 AB 5 VAL A 140 HIS A 146 -1 O ILE A 141 N VAL A 78
SHEET 4 AB 5 ALA A 99 GLY A 106 -1 O SER A 102 N HIS A 146
SHEET 5 AB 5 GLU A 112 ILE A 121 -1 N TYR A 113 O VAL A 105
LINK O4 BGLC A1169 C1 BGC B 2 1555 1555 1.39
LINK O4 ABGC B 1 C1 BGC B 2 1555 1555 1.39
LINK O4 BGC B 2 C1 BGC B 3 1555 1555 1.41
LINK O6 BGC B 2 C1 XYS B 7 1555 1555 1.41
LINK O4 BGC B 3 C1 BGC B 4 1555 1555 1.39
LINK O6 BGC B 3 C1 XYS B 6 1555 1555 1.48
LINK O6 BGC B 4 C1 XYS B 5 1555 1555 1.41
LINK O GLY A 9 CA CA A1167 1555 1555 2.42
LINK OE2 GLU A 11 CA CA A1167 1555 1555 2.36
LINK OE2 GLU A 52 CA CA A1167 1555 1555 2.33
LINK O GLU A 52 CA CA A1167 1555 1555 2.40
LINK O LYS A 55 CA CA A1167 1555 1555 2.32
LINK OD1 ASP A 160 CA CA A1167 1555 1555 2.40
LINK OD2 ASP A 160 CA CA A1167 1555 1555 2.62
CISPEP 1 LEU A 76 PRO A 77 0 -13.32
CRYST1 71.780 48.790 44.220 90.00 90.00 90.00 P 21 21 2 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 0.013931 0.000000 0.000000 0.00000
SCALE2 0.000000 0.020496 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022614 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
