REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.C.HILLIG,S.BAESLER,S.URLINGER,Y.STARK,S.BAUER, REMARK 1 AUTH 2 V.BADOCK,M.HUBER,I.BAHR,M.SCHIRNER,K.LICHA REMARK 1 TITL CRYSTALLIZATION AND MOLECULAR-REPLACEMENT SOLUTION REMARK 1 TITL 2 OF A DIAGNOSTIC FLUORESCENT DYE IN COMPLEX WITH A REMARK 1 TITL 3 SPECIFIC FAB FRAGMENT. REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 63 217 2007 REMARK 1 REFN ISSN 1744-3091 REMARK 1 PMID 17329818 REMARK 1 DOI 10.1107/S1744309107005957 REMARK 2 REMARK 2 RESOLUTION. 2.8 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) : 2.8 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.7 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0 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) : NULL REMARK 3 R VALUE (WORKING SET) : 0.2112 REMARK 3 FREE R VALUE : 0.2715 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.7 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) (%) : 79.0 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.352 REMARK 3 BIN FREE R VALUE : 0.396 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.7 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) : 61.5 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.0 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.012 REMARK 3 B22 (A**2) : -0.077 REMARK 3 B33 (A**2) : 0.089 REMARK 3 B12 (A**2) : 0.000 REMARK 3 B13 (A**2) : 0.000 REMARK 3 B23 (A**2) : 0.000 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) : 1.4 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 26.9 REMARK 3 IMPROPER ANGLES (DEGREES) : 0.91 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) : 2.09 ; 2.00 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 3.53 ; 3.00 REMARK 3 SIDE-CHAIN BOND (A**2) : 5.53 ; 4.50 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.35 ; 6.00 REMARK 3 REMARK 3 BULK SOLVENT MODELING. REMARK 3 METHOD USED : FLAT MODEL REMARK 3 KSOL : 0.34733 REMARK 3 BSOL : 41.9918 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 TOPOLOGY FILE 1 : LIG_FULL_LINKER.TOP REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE LIGAND TSC IS PARTIALLY REMARK 3 DISORDERED. THEREFORE ONLY A FRAGMENT WAS MODELLED. H222-244 REMARK 3 REPRESENTS A C-TERMINAL MYC- AND HIS-6 TAG REMARK 4 REMARK 4 2JB5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-DEC-06. REMARK 100 THE PDBE ID CODE IS EBI-30706. 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 : HKL2000 REMARK 200 DATA SCALING SOFTWARE : HKL2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13432 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.80 REMARK 200 RESOLUTION RANGE LOW (A) : 41.70 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.0 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 200 DATA REDUNDANCY : 5.5 REMARK 200 R MERGE (I) : 0.10 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 17.10 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 : 3.4 REMARK 200 R MERGE FOR SHELL (I) : 0.55 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.20 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 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 2.3M AMMONIUM SULPHATE, 5% REMARK 280 PEG400, 0.1M SODIUM CITRATE PH 4.0, FOR CRYO BUFFER REMARK 280 ADITIONAL 15% 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 GENERATING THE BIOMOLECULE 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 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 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 SER H 16 -164.08 -74.20 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 134 150.41 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 LEU H 166 89.33 -63.77 REMARK 500 GLU H 219 169.57 179.03 REMARK 500 PRO H 220 -167.32 -106.14 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 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 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 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 REMARK 900 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.