HEADER IMMUNE SYSTEM 03-DEC-06 2JB5
TITLE FAB FRAGMENT IN COMPLEX WITH SMALL MOLECULE HAPTEN, CRYSTAL FORM-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FAB FRAGMENT MOR03268 HEAVY CHAIN;
COMPND 3 CHAIN: H;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: FAB FRAGMENT MOR03268 LIGHT CHAIN;
COMPND 7 CHAIN: L;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 OTHER_DETAILS: IN VITRO SELECTED FROM A LIBRARY AND OPTIMIZED IN
SOURCE 8 SEVERAL MATURATION STEPS;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 OTHER_DETAILS: IN VITRO SELECTED FROM A LIBRARY AND OPTIMIZED IN
SOURCE 16 SEVERAL MATURATION STEPS
KEYWDS CDR, TSC, FAB, HUCAL, FLUORESCENT DYE, IMMUNOGLOBULIN DOMAIN,
KEYWDS 2 ANTIBODY FRAGMENT, DIAGNOSTIC IMAGING, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR R.C.HILLIG,S.BAESLER,G.MALAWSKI,V.BADOCK,I.BAHR,M.SCHIRNER,K.LICHA
REVDAT 4 13-DEC-23 2JB5 1 REMARK
REVDAT 3 24-FEB-09 2JB5 1 VERSN
REVDAT 2 11-MAR-08 2JB5 1 JRNL
REVDAT 1 08-JAN-08 2JB5 0
JRNL AUTH R.C.HILLIG,S.URLINGER,J.FANGHANEL,B.BROCKS,C.HAENEL,Y.STARK,
JRNL AUTH 2 D.SULZLE,D.I.SVERGUN,S.BAESLER,G.MALAWSKI,D.MOOSMAYER,
JRNL AUTH 3 A.MENRAD,M.SCHIRNER,K.LICHA
JRNL TITL FAB MOR03268 TRIGGERS ABSORPTION SHIFT OF A DIAGNOSTIC DYE
JRNL TITL 2 VIA PACKAGING IN A SOLVENT-SHIELDED FAB DIMER INTERFACE
JRNL REF J.MOL.BIOL. V. 377 206 2008
JRNL REFN ISSN 0022-2836
JRNL PMID 18241888
JRNL DOI 10.1016/J.JMB.2007.12.071
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.C.HILLIG,S.BAESLER,S.URLINGER,Y.STARK,S.BAUER,V.BADOCK,
REMARK 1 AUTH 2 M.HUBER,I.BAHR,M.SCHIRNER,K.LICHA
REMARK 1 TITL CRYSTALLIZATION AND MOLECULAR-REPLACEMENT SOLUTION OF A
REMARK 1 TITL 2 DIAGNOSTIC FLUORESCENT DYE IN COMPLEX WITH A SPECIFIC FAB
REMARK 1 TITL 3 FRAGMENT.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 63 217 2007
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 17329818
REMARK 1 DOI 10.1107/S1744309107005957
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX 2005
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN,ACCELRYS
REMARK 3 : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,
REMARK 3 : YIP,DZAKULA)
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 13432
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) : 0.211
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 656
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.011
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.90
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3520
REMARK 3 BIN FREE R VALUE : 0.3960
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.056
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3191
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 47
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 61.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01200
REMARK 3 B22 (A**2) : -0.07700
REMARK 3 B33 (A**2) : 0.08900
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM SIGMAA (A) : 0.43
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.44
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.52
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.910
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.090 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.530 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.530 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.350 ; 6.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 41.99
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : LIG_FULL_LINKER.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE LIGAND TSC IS PARTIALLY DISORDERED.
REMARK 3 THEREFORE ONLY A FRAGMENT WAS MODELLED. H222-244 REPRESENTS A C-
REMARK 3 TERMINAL MYC- AND HIS-6 TAG
REMARK 4
REMARK 4 2JB5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-DEC-06.
REMARK 100 THE DEPOSITION ID IS D_1290030706.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13432
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 41.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : 0.55000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1VGE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.3M AMMONIUM SULPHATE, 5% PEG400,
REMARK 280 0.1M SODIUM CITRATE PH 4.0, FOR CRYO BUFFER ADITIONAL 15%
REMARK 280 GLYCEROL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 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 1.000000 0.000000 0.000000 35.97450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.24000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 76.89100
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.97450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.24000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 76.89100
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.97450
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.24000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 76.89100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.97450
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 49.24000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 76.89100
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L
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 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 GLN H 1
REMARK 465 VAL H 2
REMARK 465 THR H 138
REMARK 465 SER H 139
REMARK 465 GLY H 140
REMARK 465 GLU H 223
REMARK 465 PHE H 224
REMARK 465 GLU H 225
REMARK 465 GLN H 226
REMARK 465 LYS H 227
REMARK 465 LEU H 228
REMARK 465 ILE H 229
REMARK 465 SER H 230
REMARK 465 GLU H 231
REMARK 465 GLU H 232
REMARK 465 ASP H 233
REMARK 465 LEU H 234
REMARK 465 ASN H 235
REMARK 465 GLY H 236
REMARK 465 ALA H 237
REMARK 465 PRO H 238
REMARK 465 HIS H 239
REMARK 465 HIS H 240
REMARK 465 HIS H 241
REMARK 465 HIS H 242
REMARK 465 HIS H 243
REMARK 465 HIS H 244
REMARK 465 ASP L 1
REMARK 465 ILE L 2
REMARK 465 GLU L 215
REMARK 465 ALA L 216
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 SER H 222 CA C O CB OG
REMARK 470 THR L 214 CA C O CB OG1 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 NE ARG H 38 O HOH H 2007 2.11
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 PRO H 14 C - N - CA ANGL. DEV. = 10.2 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 PRO H 14 11.56 -45.06
REMARK 500 SER H 16 -164.08 -74.20
REMARK 500 PRO H 41 115.04 -37.78
REMARK 500 TYR H 54 -86.63 -51.01
REMARK 500 LEU H 86 115.68 -37.89
REMARK 500 SER H 102 -64.51 -99.55
REMARK 500 LYS H 104 10.36 57.93
REMARK 500 SER H 120 30.13 -99.31
REMARK 500 PRO H 133 -159.43 -85.24
REMARK 500 SER H 134 150.40 76.91
REMARK 500 SER H 135 -85.09 74.95
REMARK 500 ASP H 151 71.34 39.89
REMARK 500 PHE H 153 138.04 -177.29
REMARK 500 PRO H 154 -159.86 -91.94
REMARK 500 SER H 163 -0.09 50.15
REMARK 500 LEU H 166 89.33 -63.77
REMARK 500 LEU H 196 -82.43 -39.58
REMARK 500 GLU H 219 169.57 179.03
REMARK 500 PRO H 220 -167.32 -106.14
REMARK 500 PRO L 14 153.62 -45.13
REMARK 500 THR L 25 -163.74 -114.54
REMARK 500 ASP L 28 -92.42 -137.71
REMARK 500 ASN L 32 -172.04 175.79
REMARK 500 ASN L 62 10.83 -65.64
REMARK 500 LEU L 80 122.02 -33.43
REMARK 500 ALA L 86 176.64 175.31
REMARK 500 ASP L 143 77.99 17.09
REMARK 500 ALA L 148 62.37 -101.28
REMARK 500 ASP L 156 -32.25 66.83
REMARK 500 SER L 157 -0.41 161.92
REMARK 500 PRO L 159 94.49 -44.77
REMARK 500 VAL L 160 41.26 -79.85
REMARK 500 ALA L 162 121.45 73.41
REMARK 500 GLU L 165 108.88 -175.49
REMARK 500 LYS L 171 95.64 -50.48
REMARK 500 GLN L 172 -177.19 -62.63
REMARK 500 ASN L 174 44.93 -68.78
REMARK 500 ASN L 175 -16.13 49.98
REMARK 500 SER L 181 118.98 -172.85
REMARK 500 PRO L 187 3.46 -58.86
REMARK 500 HIS L 193 145.53 175.87
REMARK 500 ARG L 194 -81.54 -62.63
REMARK 500 HIS L 202 101.90 -162.12
REMARK 500 GLU L 203 -124.37 69.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 T5C H 1223
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T5C H1223
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C0V RELATED DB: PDB
REMARK 900 IGG RHEUMATOID FACTOR IN HOMO SAPIENS
REMARK 900 RELATED ID: 2JB6 RELATED DB: PDB
REMARK 900 FAB FRAGMENT IN COMPLEX WITH SMALL MOLECULE HAPTEN, CRYSTAL FORM-2
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 HEAVY CHAIN HAS A C-TERMINAL MYC-HIS6 TAG
REMARK 999 FAB FRAGMENT SELECTED IN VITRO FROM A LIBRARY, AND
REMARK 999 OPTIMIZED FURTHER BY MATURATION STEPS.
DBREF 2JB5 H 1 244 PDB 2JB5 2JB5 1 244
DBREF 2JB5 L 1 216 PDB 2JB5 2JB5 1 216
SEQRES 1 H 244 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS
SEQRES 2 H 244 PRO GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY
SEQRES 3 H 244 GLY THR PHE SER ASN TYR ALA ILE ASN TRP VAL ARG GLN
SEQRES 4 H 244 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY ASN ILE GLU
SEQRES 5 H 244 PRO TYR PHE GLY THR ALA ASN TYR ALA GLN LYS PHE GLN
SEQRES 6 H 244 GLY ARG VAL THR ILE THR ALA ASP GLU SER THR SER THR
SEQRES 7 H 244 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR
SEQRES 8 H 244 ALA VAL TYR TYR CYS ALA ARG TYR PHE MET SER TYR LYS
SEQRES 9 H 244 HIS LEU SER ASP TYR TRP GLY GLN GLY THR LEU VAL THR
SEQRES 10 H 244 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO
SEQRES 11 H 244 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA
SEQRES 12 H 244 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO
SEQRES 13 H 244 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY
SEQRES 14 H 244 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU
SEQRES 15 H 244 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER
SEQRES 16 H 244 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS
SEQRES 17 H 244 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS
SEQRES 18 H 244 SER GLU PHE GLU GLN LYS LEU ILE SER GLU GLU ASP LEU
SEQRES 19 H 244 ASN GLY ALA PRO HIS HIS HIS HIS HIS HIS
SEQRES 1 L 216 ASP ILE ALA LEU THR GLN PRO ALA SER VAL SER GLY SER
SEQRES 2 L 216 PRO GLY GLN SER ILE THR ILE SER CYS THR GLY THR SER
SEQRES 3 L 216 SER ASP VAL GLY SER ASN ASN TYR VAL SER TRP TYR GLN
SEQRES 4 L 216 GLN HIS PRO GLY LYS ALA PRO LYS LEU MET ILE TYR GLY
SEQRES 5 L 216 GLY SER ASN ARG PRO SER GLY VAL SER ASN ARG PHE SER
SEQRES 6 L 216 GLY SER LYS SER GLY ASN THR ALA SER LEU THR ILE SER
SEQRES 7 L 216 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS ARG
SEQRES 8 L 216 SER TRP ASP SER ASN LEU SER TYR SER VAL PHE GLY GLY
SEQRES 9 L 216 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA
SEQRES 10 L 216 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU
SEQRES 11 L 216 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP
SEQRES 12 L 216 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP
SEQRES 13 L 216 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO
SEQRES 14 L 216 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR
SEQRES 15 L 216 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER
SEQRES 16 L 216 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU
SEQRES 17 L 216 LYS THR VAL ALA PRO THR GLU ALA
HET T5C H1223 30
HETNAM T5C 2-{(1E,3Z,5E,7E)-7-[3,3-DIMETHYL-5-SULFO-1-(2-
HETNAM 2 T5C SULFOETHYL)-1,3-DIHYDRO-2H-INDOL-2-YLIDENE]-4-
HETNAM 3 T5C METHYLHEPTA-1,3,5-TRIEN-1-YL}-3,3-DIMETHYL-5-SULFO-1-
HETNAM 4 T5C (2-SULFOETHYL)-3H-INDOLIUM
HETSYN T5C TETRASULFOCYANINE
FORMUL 3 T5C C32 H39 N2 O12 S4 1+
FORMUL 4 HOH *47(H2 O)
HELIX 1 1 GLN H 62 GLN H 65 5 4
HELIX 2 2 GLU H 74 THR H 76 5 3
HELIX 3 3 ARG H 87 THR H 91 5 5
HELIX 4 4 SER H 163 ALA H 165 5 3
HELIX 5 5 SER H 195 GLN H 199 5 5
HELIX 6 6 LYS H 208 ASN H 211 5 4
HELIX 7 7 ASP L 28 ASN L 32 5 5
HELIX 8 8 GLN L 81 GLU L 85 5 5
HELIX 9 9 SER L 126 ALA L 132 1 7
SHEET 1 HA 4 LEU H 4 GLN H 6 0
SHEET 2 HA 4 VAL H 18 ALA H 24 -1 O LYS H 23 N VAL H 5
SHEET 3 HA 4 THR H 78 LEU H 83 -1 O ALA H 79 N CYS H 22
SHEET 4 HA 4 VAL H 68 ASP H 73 -1 O THR H 69 N GLU H 82
SHEET 1 HB 6 GLU H 10 LYS H 12 0
SHEET 2 HB 6 THR H 114 VAL H 118 1 O LEU H 115 N GLU H 10
SHEET 3 HB 6 ALA H 92 MET H 101 -1 O ALA H 92 N VAL H 116
SHEET 4 HB 6 ILE H 34 GLN H 39 -1 O ASN H 35 N ALA H 97
SHEET 5 HB 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38
SHEET 6 HB 6 ALA H 58 TYR H 60 -1 O ASN H 59 N ASN H 50
SHEET 1 HC 4 GLU H 10 LYS H 12 0
SHEET 2 HC 4 THR H 114 VAL H 118 1 O LEU H 115 N GLU H 10
SHEET 3 HC 4 ALA H 92 MET H 101 -1 O ALA H 92 N VAL H 116
SHEET 4 HC 4 LEU H 106 TRP H 110 -1 O SER H 107 N PHE H 100
SHEET 1 HD 4 SER H 127 LEU H 131 0
SHEET 2 HD 4 THR H 142 TYR H 152 -1 O GLY H 146 N LEU H 131
SHEET 3 HD 4 TYR H 183 PRO H 192 -1 O TYR H 183 N TYR H 152
SHEET 4 HD 4 VAL H 170 THR H 172 -1 O HIS H 171 N VAL H 188
SHEET 1 HE 4 SER H 127 LEU H 131 0
SHEET 2 HE 4 THR H 142 TYR H 152 -1 O GLY H 146 N LEU H 131
SHEET 3 HE 4 TYR H 183 PRO H 192 -1 O TYR H 183 N TYR H 152
SHEET 4 HE 4 VAL H 176 LEU H 177 -1 O VAL H 176 N SER H 184
SHEET 1 HF 3 THR H 158 TRP H 161 0
SHEET 2 HF 3 TYR H 201 HIS H 207 -1 O ASN H 204 N SER H 160
SHEET 3 HF 3 THR H 212 VAL H 218 -1 O THR H 212 N HIS H 207
SHEET 1 LA 5 SER L 9 GLY L 12 0
SHEET 2 LA 5 THR L 106 VAL L 110 1 O LYS L 107 N VAL L 10
SHEET 3 LA 5 ASP L 87 TRP L 93 -1 O TYR L 88 N THR L 106
SHEET 4 LA 5 VAL L 35 GLN L 40 -1 O SER L 36 N ARG L 91
SHEET 5 LA 5 LYS L 47 ILE L 50 -1 O LYS L 47 N GLN L 39
SHEET 1 LB 4 SER L 9 GLY L 12 0
SHEET 2 LB 4 THR L 106 VAL L 110 1 O LYS L 107 N VAL L 10
SHEET 3 LB 4 ASP L 87 TRP L 93 -1 O TYR L 88 N THR L 106
SHEET 4 LB 4 SER L 100 PHE L 102 -1 O VAL L 101 N SER L 92
SHEET 1 LC 3 ILE L 18 THR L 23 0
SHEET 2 LC 3 THR L 72 ILE L 77 -1 O ALA L 73 N CYS L 22
SHEET 3 LC 3 PHE L 64 SER L 69 -1 O SER L 65 N THR L 76
SHEET 1 LD 3 LEU L 122 PHE L 123 0
SHEET 2 LD 3 ALA L 135 CYS L 139 -1 O VAL L 138 N PHE L 123
SHEET 3 LD 3 TYR L 182 LEU L 185 -1 O LEU L 183 N LEU L 137
SHEET 1 LE 2 ILE L 141 PHE L 144 0
SHEET 2 LE 2 TYR L 177 ALA L 179 -1 O TYR L 177 N PHE L 144
SHEET 1 LF 4 SER L 158 PRO L 159 0
SHEET 2 LF 4 THR L 150 ALA L 155 -1 O ALA L 155 N SER L 158
SHEET 3 LF 4 TYR L 196 HIS L 202 -1 O SER L 197 N LYS L 154
SHEET 4 LF 4 SER L 205 VAL L 211 -1 O SER L 205 N HIS L 202
SSBOND 1 CYS H 22 CYS H 96 1555 1555 2.03
SSBOND 2 CYS H 147 CYS H 203 1555 1555 2.03
SSBOND 3 CYS L 22 CYS L 90 1555 1555 2.04
SSBOND 4 CYS L 139 CYS L 198 1555 1555 2.03
CISPEP 1 PHE H 153 PRO H 154 0 -0.29
CISPEP 2 GLU H 155 PRO H 156 0 -0.06
CISPEP 3 TYR L 145 PRO L 146 0 0.00
SITE 1 AC1 19 TYR H 32 ALA H 33 ASN H 35 ASN H 50
SITE 2 AC1 19 TYR H 99 MET H 101 LYS H 104 LEU H 106
SITE 3 AC1 19 HOH H2016 HOH H2017 HOH H2027 ASN L 33
SITE 4 AC1 19 TYR L 34 VAL L 35 TYR L 51 GLY L 52
SITE 5 AC1 19 TRP L 93 LEU L 97 HOH L2003
CRYST1 71.949 98.480 153.782 90.00 90.00 90.00 I 2 2 2 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 0.013899 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010154 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006503 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
