HEADER SUGAR BINDING PROTEIN 03-JUN-10 3NBD
TITLE CLITOCYBE NEBULARIS RICIN B-LIKE LECTIN (CNL) IN COMPLEX WITH LACTOSE,
TITLE 2 CRYSTALLIZED AT PH 7.1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RICIN B-LIKE LECTIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLITOCYBE NEBULARIS;
SOURCE 3 ORGANISM_TAXID: 117024;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS CLITOCYBE NEBULARIS RICIN B-LIKE LECTIN, LACTOSE, SUGAR BINDING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.RENKO,J.POHLEVEN,J.SABOTIC,J.KOS,D.TURK
REVDAT 6 01-NOV-23 3NBD 1 REMARK HETSYN
REVDAT 5 29-JUL-20 3NBD 1 COMPND REMARK HET HETNAM
REVDAT 5 2 1 FORMUL LINK SITE ATOM
REVDAT 4 08-NOV-17 3NBD 1 REMARK
REVDAT 3 19-MAR-14 3NBD 1 JRNL
REVDAT 2 07-MAR-12 3NBD 1 JRNL
REVDAT 1 21-SEP-11 3NBD 0
JRNL AUTH J.POHLEVEN,M.RENKO,S.MAGISTER,D.F.SMITH,M.KUNZLER,
JRNL AUTH 2 B.STRUKELJ,D.TURK,J.KOS,J.SABOTIC
JRNL TITL BIVALENT CARBOHYDRATE BINDING IS REQUIRED FOR BIOLOGICAL
JRNL TITL 2 ACTIVITY OF CLITOCYBE NEBULARIS LECTIN (CNL), THE
JRNL TITL 3 N,N'-DIACETYLLACTOSEDIAMINE (GALNAC BETA 1-4GLCNAC,
JRNL TITL 4 LACDINAC)-SPECIFIC LECTIN FROM BASIDIOMYCETE C. NEBULARIS
JRNL REF J.BIOL.CHEM. V. 287 10602 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22298779
JRNL DOI 10.1074/JBC.M111.317263
REMARK 2
REMARK 2 RESOLUTION. 1.15 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) : 1.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 128492
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) : 0.139
REMARK 3 R VALUE (WORKING SET) : 0.138
REMARK 3 FREE R VALUE : 0.160
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6458
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) : 1.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.18
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8401
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.3620
REMARK 3 BIN FREE R VALUE SET COUNT : 443
REMARK 3 BIN FREE R VALUE : 0.3740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2238
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 71
REMARK 3 SOLVENT ATOMS : 535
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.33000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : -0.32000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.029
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.013
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.608
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.977
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.970
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2441 ; 0.050 ; 0.041
REMARK 3 BOND LENGTHS OTHERS (A): 1532 ; 0.038 ; 0.039
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3391 ; 2.231 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3837 ; 1.689 ; 2.997
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 331 ; 8.566 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 104 ;35.059 ;26.154
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 374 ;10.972 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;19.342 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 417 ; 0.816 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2713 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 416 ; 0.002 ; 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): 1522 ; 2.361 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 606 ; 0.946 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2514 ; 3.427 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 919 ; 4.863 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 855 ; 6.829 ; 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): 3973 ; 2.226 ; 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 U VALUES: REFINED INDIVIDUALLY. THE STRUCTURE WAS
REMARK 3 REFINED ALSO WITH MAIN.
REMARK 4
REMARK 4 3NBD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059616.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ELETTRA
REMARK 200 BEAMLINE : 5.2R
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI111
REMARK 200 OPTICS : COLLIMATING AND FOCUSING, PT
REMARK 200 -COATED MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 128514
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.140
REMARK 200 RESOLUTION RANGE LOW (A) : 23.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 8.500
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.32600
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: AMORE
REMARK 200 STARTING MODEL: 3NBC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.085M HEPES SODIUM, 1.7%(V/V) PEG
REMARK 280 400, 2.0M AMMONIUM SULFATE, 19%(W/V) GLYCEROL, PH 7.1, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 21.55950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.81450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.54000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.81450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.55950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.54000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ALA A 147
REMARK 475 ALA B 147
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 VAL A 148 N CA C O CB CG1 CG2
REMARK 480 VAL B 148 N CA C O CB CG1 CG2
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 OD1 ASN A 137 O HOH A 208 2.07
REMARK 500 O HOH A 350 O HOH A 357 2.15
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 SER A 1 CA SER A 1 CB 0.116
REMARK 500 GLY A 112 N GLY A 112 CA 0.105
REMARK 500 SER A 119 CA SER A 119 CB 0.099
REMARK 500 TRP A 140 CE2 TRP A 140 CD2 0.072
REMARK 500 GLY B 102 C GLY B 102 O 0.142
REMARK 500 GLU B 130 CD GLU B 130 OE2 0.083
REMARK 500 VAL B 131 CB VAL B 131 CG1 0.139
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 ASN A 16 CB - CG - OD1 ANGL. DEV. = 13.0 DEGREES
REMARK 500 ARG A 17 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG A 17 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 LEU A 51 CB - CG - CD2 ANGL. DEV. = 17.4 DEGREES
REMARK 500 ARG A 74 NE - CZ - NH1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 GLU B 28 OE1 - CD - OE2 ANGL. DEV. = 13.4 DEGREES
REMARK 500 LEU B 51 CB - CG - CD2 ANGL. DEV. = 11.6 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 LYS A 39 141.82 -178.68
REMARK 500 LYS A 39 134.85 -173.80
REMARK 500 SER A 101 -2.47 -160.14
REMARK 500 ALA A 147 175.15 47.55
REMARK 500 ASN B 100 113.51 -160.66
REMARK 500 SER B 101 -132.78 151.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NBC RELATED DB: PDB
REMARK 900 IDENTICAL PROTEIN CRYSTALLIZED AT DIFFERENT PH
REMARK 900 RELATED ID: 3NBE RELATED DB: PDB
REMARK 900 IDENTICAL PROTEIN, CRYSTALLIZED WITH DIFFERENT LIGAND
DBREF 3NBD A 1 148 UNP B2ZRS9 B2ZRS9_CLINE 2 149
DBREF 3NBD B 1 148 UNP B2ZRS9 B2ZRS9_CLINE 2 149
SEQRES 1 A 148 SER ILE THR PRO GLY THR TYR ASN ILE THR ASN VAL ALA
SEQRES 2 A 148 TYR THR ASN ARG LEU ILE ASP LEU THR GLY SER ASN PRO
SEQRES 3 A 148 ALA GLU ASN THR LEU ILE ILE GLY HIS HIS LEU ASN LYS
SEQRES 4 A 148 THR PRO SER GLY TYR GLY ASN GLN GLN TRP THR LEU VAL
SEQRES 5 A 148 GLN LEU PRO HIS THR THR ILE TYR THR MET GLN ALA VAL
SEQRES 6 A 148 ASN PRO GLN SER TYR VAL ARG VAL ARG ASP ASP ASN LEU
SEQRES 7 A 148 VAL ASP GLY ALA ALA LEU VAL GLY SER GLN GLN PRO THR
SEQRES 8 A 148 PRO VAL SER ILE GLU SER ALA GLY ASN SER GLY GLN PHE
SEQRES 9 A 148 ARG ILE LYS ILE PRO ASN LEU GLY LEU ALA LEU THR LEU
SEQRES 10 A 148 PRO SER ASP ALA ASN SER THR PRO ILE VAL LEU GLY GLU
SEQRES 11 A 148 VAL ASP GLU THR SER THR ASN GLN LEU TRP ALA PHE GLU
SEQRES 12 A 148 SER VAL SER ALA VAL
SEQRES 1 B 148 SER ILE THR PRO GLY THR TYR ASN ILE THR ASN VAL ALA
SEQRES 2 B 148 TYR THR ASN ARG LEU ILE ASP LEU THR GLY SER ASN PRO
SEQRES 3 B 148 ALA GLU ASN THR LEU ILE ILE GLY HIS HIS LEU ASN LYS
SEQRES 4 B 148 THR PRO SER GLY TYR GLY ASN GLN GLN TRP THR LEU VAL
SEQRES 5 B 148 GLN LEU PRO HIS THR THR ILE TYR THR MET GLN ALA VAL
SEQRES 6 B 148 ASN PRO GLN SER TYR VAL ARG VAL ARG ASP ASP ASN LEU
SEQRES 7 B 148 VAL ASP GLY ALA ALA LEU VAL GLY SER GLN GLN PRO THR
SEQRES 8 B 148 PRO VAL SER ILE GLU SER ALA GLY ASN SER GLY GLN PHE
SEQRES 9 B 148 ARG ILE LYS ILE PRO ASN LEU GLY LEU ALA LEU THR LEU
SEQRES 10 B 148 PRO SER ASP ALA ASN SER THR PRO ILE VAL LEU GLY GLU
SEQRES 11 B 148 VAL ASP GLU THR SER THR ASN GLN LEU TRP ALA PHE GLU
SEQRES 12 B 148 SER VAL SER ALA VAL
HET GLC C 1 12
HET GAL C 2 11
HET GLC D 1 12
HET GAL D 2 11
HET SO4 A 672 5
HET SO4 A 677 5
HET SO4 A 679 5
HET SO4 B 671 5
HET SO4 B 678 5
HETNAM GLC ALPHA-D-GLUCOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM SO4 SULFATE ION
HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
FORMUL 3 GLC 2(C6 H12 O6)
FORMUL 3 GAL 2(C6 H12 O6)
FORMUL 5 SO4 5(O4 S 2-)
FORMUL 10 HOH *535(H2 O)
HELIX 1 1 GLY A 23 ASN A 25 5 3
HELIX 2 2 ASP A 75 ASN A 77 5 3
HELIX 3 3 SER A 135 GLN A 138 5 4
HELIX 4 4 GLY B 23 ASN B 25 5 3
HELIX 5 5 ASP B 75 ASN B 77 5 3
HELIX 6 6 SER B 135 GLN B 138 5 4
SHEET 1 A 9 VAL A 127 GLU A 130 0
SHEET 2 A 9 LEU A 113 THR A 116 -1 N THR A 116 O VAL A 127
SHEET 3 A 9 GLN A 103 ILE A 108 -1 N ILE A 108 O LEU A 113
SHEET 4 A 9 TRP A 140 SER A 144 -1 O TRP A 140 N PHE A 104
SHEET 5 A 9 GLY A 5 ASN A 11 -1 N THR A 10 O ALA A 141
SHEET 6 A 9 TRP A 49 GLN A 53 -1 O LEU A 51 N GLY A 5
SHEET 7 A 9 ILE A 59 ALA A 64 -1 O GLN A 63 N THR A 50
SHEET 8 A 9 VAL A 93 SER A 97 -1 O VAL A 93 N TYR A 60
SHEET 9 A 9 GLN A 103 ILE A 108 -1 O LYS A 107 N SER A 94
SHEET 1 B 4 LEU A 18 LEU A 21 0
SHEET 2 B 4 THR A 30 HIS A 35 -1 O HIS A 35 N LEU A 18
SHEET 3 B 4 LEU A 84 SER A 87 -1 O GLY A 86 N THR A 30
SHEET 4 B 4 TYR A 70 VAL A 73 -1 N TYR A 70 O SER A 87
SHEET 1 C 3 LEU A 18 LEU A 21 0
SHEET 2 C 3 THR A 30 HIS A 35 -1 O HIS A 35 N LEU A 18
SHEET 3 C 3 THR A 124 PRO A 125 -1 O THR A 124 N GLY A 34
SHEET 1 D 7 GLY B 5 ASN B 11 0
SHEET 2 D 7 TRP B 49 GLN B 53 -1 O LEU B 51 N GLY B 5
SHEET 3 D 7 ILE B 59 ALA B 64 -1 O GLN B 63 N THR B 50
SHEET 4 D 7 VAL B 93 SER B 97 -1 O VAL B 93 N TYR B 60
SHEET 5 D 7 GLN B 103 LYS B 107 -1 O LYS B 107 N SER B 94
SHEET 6 D 7 TRP B 140 SER B 144 -1 O TRP B 140 N PHE B 104
SHEET 7 D 7 GLY B 5 ASN B 11 -1 N THR B 10 O ALA B 141
SHEET 1 E 4 LEU B 18 LEU B 21 0
SHEET 2 E 4 THR B 30 HIS B 35 -1 O HIS B 35 N LEU B 18
SHEET 3 E 4 LEU B 84 SER B 87 -1 O GLY B 86 N THR B 30
SHEET 4 E 4 TYR B 70 VAL B 73 -1 N TYR B 70 O SER B 87
SHEET 1 F 3 LEU B 18 LEU B 21 0
SHEET 2 F 3 THR B 30 HIS B 35 -1 O HIS B 35 N LEU B 18
SHEET 3 F 3 THR B 124 PRO B 125 -1 O THR B 124 N GLY B 34
SHEET 1 G 2 LEU B 113 THR B 116 0
SHEET 2 G 2 VAL B 127 GLU B 130 -1 O VAL B 127 N THR B 116
LINK O4 GLC C 1 C1 GAL C 2 1555 1555 1.43
LINK O4 GLC D 1 C1 GAL D 2 1555 1555 1.40
CISPEP 1 THR A 40 PRO A 41 0 3.29
CISPEP 2 ASN A 66 PRO A 67 0 -10.21
CISPEP 3 THR B 40 PRO B 41 0 3.92
CISPEP 4 ASN B 66 PRO B 67 0 -10.88
CRYST1 43.119 85.080 97.629 90.00 90.00 90.00 P 21 21 21 8
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 0.023192 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011754 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010243 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
