REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.ALLEN,T.SIMON,F.SABLITZKY,K.RAJEWSKY,A.CUMANO REMARK 1 TITL ANTIBODY ENGINEERING FOR THE ANALYSIS OF AFFINITY REMARK 1 TITL 2 MATURATION OF AN ANTI-HAPTEN RESPONSE REMARK 1 REF EMBO J. V. 7 1995 1988 REMARK 1 REFN ISSN 0261-4189 REMARK 1 REFERENCE 2 REMARK 1 AUTH A.CUMANO,K.RAJEWSKY REMARK 1 TITL STRUCTURE OF PRIMARY REMARK 1 TITL 2 ANTI-(4-HYDROXY-3-NITROPHENYL)ACETYL (NP) REMARK 1 TITL 3 ANTIBODIES IN NORMAL AND IDIOTYPICALLY SUPPRESSED REMARK 1 TITL 4 C57BL/6 MICE REMARK 1 REF EUR.J.IMMUNOL. V. 15 512 1985 REMARK 1 REFN ISSN 0014-2980 REMARK 1 REFERENCE 3 REMARK 1 AUTH A.L.BOTHWELL,M.PASKIND,M.RETH,T.IMANISHI-KARI, REMARK 1 AUTH 2 K.RAJEWSKY,D.BALTIMORE REMARK 1 TITL SOMATIC VARIANTS OF MURINE IMMUNOGLOBULIN LAMBDA REMARK 1 TITL 2 LIGHT CHAINS REMARK 1 REF NATURE V. 298 380 1982 REMARK 1 REFN ISSN 0028-0836 REMARK 2 REMARK 2 RESOLUTION. 2.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROLSQ, X-PLOR 2.1 REMARK 3 AUTHORS : KONNERT,HENDRICKSON REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 89.3 REMARK 3 NUMBER OF REFLECTIONS : 21708 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.196 REMARK 3 FREE R VALUE : 0.250 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT : NULL 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) : 0.1960 REMARK 3 FREE R VALUE (NO CUTOFF) : 0.250 REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 10.000 REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 3230 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 19 REMARK 3 SOLVENT ATOMS : 134 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.70 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25 REMARK 3 ESD FROM SIGMAA (A) : NULL REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA REMARK 3 BOND LENGTH (A) : 0.015 ; 0.020 REMARK 3 ANGLE DISTANCE (A) : 0.039 ; 0.030 REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : 0.049 ; 0.050 REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL REMARK 3 REMARK 3 PLANE RESTRAINT (A) : 0.013 ; 0.020 REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : 0.170 ; 0.150 REMARK 3 REMARK 3 NON-BONDED CONTACT RESTRAINTS. REMARK 3 SINGLE TORSION (A) : 0.130 ; 0.500 REMARK 3 MULTIPLE TORSION (A) : 0.235 ; 0.500 REMARK 3 H-BOND (X...Y) (A) : 0.230 ; 0.500 REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL REMARK 3 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS. REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL REMARK 3 PLANAR (DEGREES) : 2.400 ; 3.000 REMARK 3 STAGGERED (DEGREES) : 22.000; 15.000 REMARK 3 TRANSVERSE (DEGREES) : 22.800; 20.000 REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : 0.891 ; 1.000 REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.620 ; 1.500 REMARK 3 SIDE-CHAIN BOND (A**2) : 3.464 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE (A**2) : 5.159 ; 4.000 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1NGP 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 : 22-FEB-94 REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.8931 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : DOUBLE CRYSTAL MONOCHROMATOR REMARK 200 / PT MIRROR REMARK 200 REMARK 200 DETECTOR TYPE : IMAGE PLATE REMARK 200 DETECTOR MANUFACTURER : SATOW REMARK 200 INTENSITY-INTEGRATION SOFTWARE : OSC REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21761 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 19.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 89.3 REMARK 200 DATA REDUNDANCY : 3.510 REMARK 200 R MERGE (I) : 0.06600 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : NULL REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: NULL REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: X-PLOR 2.1 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.50 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-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 49.12500 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 55.34550 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 55.34550 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 24.56250 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 55.34550 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 55.34550 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 73.68750 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 55.34550 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.34550 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 24.56250 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 55.34550 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.34550 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 73.68750 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 49.12500 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: 4250 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18550 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H 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 ALA L 212 REMARK 465 ASP L 213 REMARK 465 CYS L 214 REMARK 465 SER L 215 REMARK 465 ALA H 136 REMARK 465 ALA H 137 REMARK 465 GLN H 138 REMARK 465 THR H 139 REMARK 465 ASN H 140 REMARK 465 ASP H 221 REMARK 465 CYS H 222 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 GLN L 1 CD OE1 NE2 REMARK 470 ASP L 43 CG OD1 OD2 REMARK 470 ASN L 131 CG OD1 ND2 REMARK 470 ARG L 190 CG CD NE CZ NH1 NH2 REMARK 470 GLN L 197 CG CD OE1 NE2 REMARK 470 SER H 135 OG REMARK 470 PRO H 191 CG CD 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 GLU L 189 NH2 ARG L 211 2.06 REMARK 500 OG SER L 24 OH TYR L 94 2.06 REMARK 500 O GLN H 6 OE1 GLN H 112 2.14 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 NZ LYS H 19 NZ LYS H 19 8665 2.12 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 LEU L 20 CA - CB - CG ANGL. DEV. = 15.0 DEGREES REMARK 500 ARG L 23 NE - CZ - NH1 ANGL. DEV. = 4.9 DEGREES REMARK 500 ARG L 56 CD - NE - CZ ANGL. DEV. = -8.8 DEGREES REMARK 500 ARG L 56 NE - CZ - NH2 ANGL. DEV. = 5.0 DEGREES REMARK 500 ASP L 71 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES REMARK 500 GLU L 83 CG - CD - OE2 ANGL. DEV. = 12.0 DEGREES REMARK 500 ASP L 84 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES REMARK 500 CYS L 90 N - CA - CB ANGL. DEV. = 9.5 DEGREES REMARK 500 TRP L 98 N - CA - CB ANGL. DEV. = 11.4 DEGREES REMARK 500 TYR L 143 CB - CG - CD2 ANGL. DEV. = 4.1 DEGREES REMARK 500 TYR L 143 CB - CG - CD1 ANGL. DEV. = -5.1 DEGREES REMARK 500 ARG L 186 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 LEU L 209 CA - CB - CG ANGL. DEV. = 15.7 DEGREES REMARK 500 ARG H 40 CD - NE - CZ ANGL. DEV. = 10.2 DEGREES REMARK 500 ARG H 40 NE - CZ - NH1 ANGL. DEV. = 8.1 DEGREES REMARK 500 ARG H 40 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES REMARK 500 ASP H 52 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES REMARK 500 ASP H 52 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES REMARK 500 TYR H 80 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES REMARK 500 TYR H 94 CB - CG - CD2 ANGL. DEV. = 6.6 DEGREES REMARK 500 TYR H 94 CB - CG - CD1 ANGL. DEV. = -3.6 DEGREES REMARK 500 MET H 142 CA - CB - CG ANGL. DEV. = -18.8 DEGREES REMARK 500 MET H 142 CB - CG - SD ANGL. DEV. = -33.2 DEGREES REMARK 500 CYS H 147 CB - CA - C ANGL. DEV. = 15.0 DEGREES REMARK 500 CYS H 147 CA - CB - SG ANGL. DEV. = 9.2 DEGREES REMARK 500 LEU H 177 CA - CB - CG ANGL. DEV. = 15.0 DEGREES REMARK 500 ASP H 214 CA - CB - CG ANGL. DEV. = 13.9 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 TYR L 34 55.98 36.29 REMARK 500 ASP L 43 27.37 102.60 REMARK 500 LEU L 49 -64.27 -102.33 REMARK 500 THR L 53 -51.59 81.03 REMARK 500 ASN L 54 20.01 -140.58 REMARK 500 PRO L 61 154.56 -48.25 REMARK 500 SER L 67 -176.72 -171.99 REMARK 500 ALA L 86 -172.53 -172.19 REMARK 500 TYR L 94 63.56 -118.67 REMARK 500 SER L 95 -43.49 68.84 REMARK 500 ASN L 96 19.37 -153.78 REMARK 500 LEU L 109 106.27 -47.32 REMARK 500 GLN L 160 133.58 170.83 REMARK 500 ASN L 173 10.78 86.87 REMARK 500 ALA L 185 -29.47 -39.19 REMARK 500 GLU L 201 56.94 29.76 REMARK 500 ASN H 54 -74.00 -74.14 REMARK 500 ALA H 92 -176.97 175.70 REMARK 500 PRO H 133 -147.08 -60.76 REMARK 500 PRO H 154 -156.69 -83.00 REMARK 500 ASP H 180 -0.73 64.42 REMARK 500 SER H 197 -71.78 -51.51 REMARK 500 ALA H 208 -36.77 -39.54 REMARK 500 SER H 210 47.62 36.41 REMARK 500 REMARK 500 REMARK: NULL 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 301 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NPA H 302 REMARK 999 REMARK 999 SEQUENCE REMARK 999 REMARK 999 THE NUMBERING SYSTEM USED IN THIS ENTRY IS SEQUENTIAL, REMARK 999 FROM 1 TO 211 FOR THE LIGHT CHAIN AND FROM 1 TO 220 FOR REMARK 999 THE HEAVY CHAIN. THE CONVERSION TO KABAT NUMBERING REMARK 999 (E.A.KABAT,T.T.WU, M.REID-MILLER, H.M.PERRY, AND REMARK 999 K.S.GOTTESMAN (1991) SEQUENCES OF PROTEINS OF REMARK 999 IMMUNOLOGICAL INTEREST, 5TH ED., NATIONAL INSTITUTES OF REMARK 999 HEALTH BETHESDA, MD) FOR THE FAB REGIONS OF THE LIGHT AND REMARK 999 HEAVY CHAINS IS GIVEN BELOW. REMARK 999 REMARK 999 SEQUENTIAL NUMBERING KABAT NUMBERING REMARK 999 LIGHT CHAIN REMARK 999 1 - 9 1 - 9 REMARK 999 10 - 26 11 - 27 REMARK 999 27 27A REMARK 999 28 27B REMARK 999 29 27C REMARK 999 30 - 108 28 - 106 REMARK 999 109 106A REMARK 999 110 - 171 107 - 168 REMARK 999 172 - 202 170 - 200 REMARK 999 203 - 215 203 - 215 REMARK 999 HEAVY CHAIN REMARK 999 1 - 52 1 - 52 REMARK 999 53 52A REMARK 999 54 - 83 53 - 82 REMARK 999 84 82A REMARK 999 85 82B REMARK 999 86 82C REMARK 999 87 - 104 83 - 100 REMARK 999 105 100A REMARK 999 106 100J REMARK 999 107 100K REMARK 999 108 - 137 101 - 130 REMARK 999 138 - 159 133 - 154 REMARK 999 160 - 161 156 - 157 REMARK 999 162 - 169 162 - 169 REMARK 999 170 - 179 171 - 180 REMARK 999 180 - 193 183 - 196 REMARK 999 194 - 195 199 - 200 REMARK 999 196 - 217 202 - 223 REMARK 999 218 - 221 226 - 229 REMARK 999 222 235