REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.BACA,L.G.PRESTA,S.J.O'CONNOR,J.A.WELLS REMARK 1 TITL ANTIBODY HUMANIZATION USING MONOVALENT PHAGE REMARK 1 TITL 2 DISPLAY REMARK 1 REF J.BIOL.CHEM. V. 272 10678 1997 REMARK 1 REFN ISSN 0021-9258 REMARK 1 REFERENCE 2 REMARK 1 AUTH L.G.PRESTA,H.CHEN,S.J.O'CONNOR,V.CHISHOLM,Y.G.MENG, REMARK 1 AUTH 2 L.KRUMMEN,M.WINKLER,N.FERRARA REMARK 1 TITL HUMANIZATION OF AN ANTI-VASCULAR ENDOTHELIAL REMARK 1 TITL 2 GROWTH FACTOR MONOCLONAL ANTIBODY FOR THE THERAPY REMARK 1 TITL 3 OF SOLID TUMORS AND OTHER DISORDERS REMARK 1 REF CANCER RES. V. 57 4593 1997 REMARK 1 REFN ISSN 0008-5472 REMARK 2 REMARK 2 RESOLUTION. 2.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.8 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1000 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.8 REMARK 3 NUMBER OF REFLECTIONS : 60401 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : THIN RESOLUTION SHELLS REMARK 3 R VALUE (WORKING SET) : 0.196 REMARK 3 FREE R VALUE : 0.266 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.800 REMARK 3 FREE R VALUE TEST SET COUNT : 5908 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004 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) : 2.40 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.48 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.10 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4550 REMARK 3 BIN R VALUE (WORKING SET) : 0.3120 REMARK 3 BIN FREE R VALUE : 0.3410 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.90 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 389 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 8136 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 10 REMARK 3 SOLVENT ATOMS : 548 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.00 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 3.70000 REMARK 3 B22 (A**2) : -8.50000 REMARK 3 B33 (A**2) : 4.80000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.31000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM SIGMAA (A) : 0.35 REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK 3 ESD FROM C-V SIGMAA (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.012 REMARK 3 BOND ANGLES (DEGREES) : 1.66 REMARK 3 DIHEDRAL ANGLES (DEGREES) : 27.97 REMARK 3 IMPROPER ANGLES (DEGREES) : 1.47 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) : 2.600 ; 1.500 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.100 ; 2.000 REMARK 3 SIDE-CHAIN BOND (A**2) : 5.000 ; 2.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.300 ; 2.500 REMARK 3 REMARK 3 NCS MODEL : RESTRAINTS REMARK 3 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT REMARK 3 GROUP 1 POSITIONAL (A) : 0.231 ; 20 REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK 3 GROUP 2 POSITIONAL (A) : 0.220 ; 20 REMARK 3 GROUP 2 B-FACTOR (A**2) : NULL ; NULL REMARK 3 GROUP 3 POSITIONAL (A) : 0.227 ; 20 REMARK 3 GROUP 3 B-FACTOR (A**2) : NULL ; NULL REMARK 3 GROUP 4 POSITIONAL (A) : 0.423 ; 5 REMARK 3 GROUP 4 B-FACTOR (A**2) : NULL ; NULL REMARK 3 GROUP 5 POSITIONAL (A) : 0.398 ; 5 REMARK 3 GROUP 5 B-FACTOR (A**2) : NULL ; NULL REMARK 3 REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO REMARK 3 PARAMETER FILE 2 : NULL REMARK 3 PARAMETER FILE 3 : NULL REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO REMARK 3 TOPOLOGY FILE 2 : NULL REMARK 3 TOPOLOGY FILE 3 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE MODEL IS UNUSUAL IN REGARD TO REMARK 3 THE HIGH AVERAGE TEMPERATURE FACTOR OF 100 A2 OF THE CONSTANT REMARK 3 DOMAIN OF THE SECOND FAB MOLECULE. HOWEVER THE USE OF NON- REMARK 3 CRYSTALLOGRAPHIC SYMMETRY RESTRAINTS GREATLY RESTRICTS THE REMARK 3 CONFORMATIONAL FREEDOM OF THIS PORTION TO THE WELL-DEFINED REMARK 3 CONSTANT DOMAIN OF THE FIRST FAB FRAGMENT. MORE DETAILS CAN BE REMARK 3 FOUND IN THE PRIMARY PUBLICATION. REMARK 4 REMARK 4 1BJ1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : MAR-96 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : 2 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : CHESS REMARK 200 BEAMLINE : A1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.914 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63147 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 20.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0 REMARK 200 DATA REDUNDANCY : 3.800 REMARK 200 R MERGE (I) : 0.07100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48 REMARK 200 COMPLETENESS FOR SHELL (%) : 81.3 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.12800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 3.500 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: X-PLOR 3.8 REMARK 200 STARTING MODEL: PDB ENTRY 2VPF AND 1FVD REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 66.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 33.49000 REMARK 290 SMTRY3 2 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 13140 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 46130 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, V, W, J, K 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 CYS L 214 REMARK 465 SER H 138 REMARK 465 LYS H 139 REMARK 465 SER H 140 REMARK 465 THR H 141 REMARK 465 SER H 142 REMARK 465 GLY H 143 REMARK 465 SER H 225 REMARK 465 CYS H 226 REMARK 465 ASP H 227 REMARK 465 LYS H 228 REMARK 465 THR H 229 REMARK 465 HIS H 230 REMARK 465 THR H 231 REMARK 465 GLY V 8 REMARK 465 GLN V 9 REMARK 465 ASN V 10 REMARK 465 HIS V 11 REMARK 465 HIS V 12 REMARK 465 GLU V 13 REMARK 465 LYS V 108 REMARK 465 ASP V 109 REMARK 465 GLY W 8 REMARK 465 GLN W 9 REMARK 465 ASN W 10 REMARK 465 HIS W 11 REMARK 465 HIS W 12 REMARK 465 GLU W 13 REMARK 465 LYS W 108 REMARK 465 ASP W 109 REMARK 465 CYS J 214 REMARK 465 SER K 138 REMARK 465 LYS K 139 REMARK 465 SER K 140 REMARK 465 THR K 141 REMARK 465 SER K 142 REMARK 465 GLY K 143 REMARK 465 SER K 225 REMARK 465 CYS K 226 REMARK 465 ASP K 227 REMARK 465 LYS K 228 REMARK 465 THR K 229 REMARK 465 HIS K 230 REMARK 465 THR K 231 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 LEU H 188 CA - CB - CG ANGL. DEV. = 15.8 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 SER L 30 -114.66 59.89 REMARK 500 THR L 51 -46.85 68.05 REMARK 500 SER L 52 10.07 -143.49 REMARK 500 SER L 67 152.52 178.99 REMARK 500 ALA L 84 -173.12 176.85 REMARK 500 ASN L 138 72.80 50.40 REMARK 500 LYS H 43 -168.22 -116.60 REMARK 500 ASP H 154 70.69 52.33 REMARK 500 CYS V 26 107.82 -20.95 REMARK 500 GLU V 42 50.47 -95.31 REMARK 500 HIS V 86 -7.76 79.34 REMARK 500 CYS W 26 110.27 -10.68 REMARK 500 HIS W 86 -10.73 78.03 REMARK 500 HIS W 90 155.42 179.27 REMARK 500 SER J 30 -122.76 56.79 REMARK 500 THR J 51 -41.87 65.19 REMARK 500 SER J 67 147.16 173.60 REMARK 500 ALA J 84 -173.21 179.66 REMARK 500 ARG J 108 -156.36 -140.90 REMARK 500 THR J 129 -167.06 -127.05 REMARK 500 ALA J 130 125.51 -176.82 REMARK 500 ASN J 138 111.20 45.73 REMARK 500 TYR J 140 138.89 -178.72 REMARK 500 PRO J 141 -168.20 -66.51 REMARK 500 ASP J 151 50.08 73.68 REMARK 500 ASN J 152 -13.99 73.44 REMARK 500 LYS J 188 -8.17 -149.69 REMARK 500 LYS J 190 -60.06 -140.76 REMARK 500 LYS K 43 -166.70 -117.26 REMARK 500 ALA K 92 171.78 176.12 REMARK 500 LEU K 134 77.03 -118.25 REMARK 500 PRO K 136 -170.62 -63.03 REMARK 500 ASP K 154 88.94 66.47 REMARK 500 PRO K 157 -146.98 -92.14 REMARK 500 PRO K 159 -158.83 -109.78 REMARK 500 ASN K 209 94.91 -163.00 REMARK 500 LYS K 216 87.16 -151.67 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 TYR V 21 0.06 SIDE_CHAIN 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 H 239 DISTANCE = 6.07 ANGSTROMS REMARK 525 HOH W 135 DISTANCE = 5.11 ANGSTROMS REMARK 525 HOH W 139 DISTANCE = 5.05 ANGSTROMS REMARK 525 HOH H 287 DISTANCE = 6.52 ANGSTROMS REMARK 525 HOH H 300 DISTANCE = 6.53 ANGSTROMS REMARK 525 HOH H 304 DISTANCE = 5.15 ANGSTROMS REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 232 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 K 232 REMARK 999 REMARK 999 SEQUENCE REMARK 999 REMARK 999 THE NUMBERING OF THE LIGHT CHAINS L AND J AS WELL AS OF THE REMARK 999 HEAVY CHAINS H AND K IS SEQUENTIAL. CONVERSION TO THE REMARK 999 KABAT NUMBERING (E.A. KABAT, T.T. WU, M. REID-MILLER, REMARK 999 H.M. PERRY, K.S. GOTTESMAN (1991) SEQUENCES OF PROTEINS OF REMARK 999 IMMUNOLOGICAL INTEREST, 5TH ED, NATIONAL INSTITUTES OF REMARK 999 HEALTH, BETHESDA, MD) IS GIVEN BELOW: REMARK 999 REMARK 999 SEQUENTIAL NUMBERING KABAT NUMBERING REMARK 999 LIGHT CHAIN 1 - 213 1 - 213 REMARK 999 HEAVY CHAIN 1 - 52 1 - 52 REMARK 999 53 52A REMARK 999 54 - 83 53 - 82 REMARK 999 84 - 86 82A - 82C REMARK 999 87 - 104 83 - 100 REMARK 999 105 - 110 100A - 100F REMARK 999 111 - 226 101 - 216