REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH E.A.STURA,R.L.STANFIELD,G.G.FIESER,S.SILVER, REMARK 1 AUTH 2 M.ROGUSCA,L.M.HINCAPIE,H.K.B.SIMMERMAN,A.T.PROFY, REMARK 1 AUTH 3 I.A.WILSON REMARK 1 TITL CRYSTALLIZATION, SEQUENCE, AND PRELIMINARY REMARK 1 TITL 2 CRYSTALLOGRAPHIC DATA FOR AN ANTIPEPTIDE FAB 50.1 REMARK 1 TITL 3 AND PEPTIDE COMPLEXES WITH THE PRINCIPAL REMARK 1 TITL 4 NEUTRALIZING DETERMINANT OF HIV-1 GP120 REMARK 1 REF PROTEINS V. 14 499 1992 REMARK 1 REFN ISSN 0887-3585 REMARK 1 REFERENCE 2 REMARK 1 AUTH R.L.STANFIELD,M.TAKIMOTO-KAMIMURA,J.M.RINI, REMARK 1 AUTH 2 A.T.PROFY,I.A.WILSON REMARK 1 TITL MAJOR ANTIGEN-INDUCED DOMAIN REARRANGEMENTS IN AN REMARK 1 TITL 2 ANTIBODY REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL 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 : NULL 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 SET) : 0.188 REMARK 3 FREE R VALUE : NULL REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK 3 BIN R VALUE (WORKING SET) : NULL REMARK 3 BIN FREE R VALUE : NULL REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6718 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 0 REMARK 3 SOLVENT ATOMS : 0 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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) : NULL REMARK 3 ESD FROM SIGMAA (A) : NULL 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) : 0.018 REMARK 3 BOND ANGLES (DEGREES) : 3.79 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK 3 IMPROPER ANGLES (DEGREES) : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL MODEL : NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL 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 : NULL REMARK 3 TOPOLOGY FILE 1 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1GGI 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 : NULL REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : NULL REMARK 200 RADIATION SOURCE : NULL REMARK 200 BEAMLINE : NULL REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL REMARK 200 WAVELENGTH OR RANGE (A) : NULL REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : NULL REMARK 200 DETECTOR MANUFACTURER : NULL REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL REMARK 200 DATA SCALING SOFTWARE : NULL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL REMARK 200 RESOLUTION RANGE HIGH (A) : NULL REMARK 200 RESOLUTION RANGE LOW (A) : NULL REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : NULL REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : NULL 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 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.14 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL 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 26.28500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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 300 REMARK: REMARK 300 THERE ARE TWO FAB MOLECULES IN THE ASYMMETRIC UNIT. THE REMARK 300 TRANSFORMATIONS GIVEN ON *MTRIX* RECORDS BELOW YIELD REMARK 300 APPROXIMATE COORDINATES FOR CHAINS *L* AND *H* WHEN APPLIED REMARK 300 TO CHAINS *M* AND *J*. THESE TRANSFORMATIONS HAVE BEEN REMARK 300 PROVIDED SEPARATELY FOR THE VH AND CH DOMAINS OF THE HEAVY REMARK 300 CHAIN AND THE VL AND CL DOMAINS OF THE LIGHT CHAIN. REMARK 300 THE TRANSFORMATION PRESENTED ON *MTRIX 1* RECORDS BELOW REMARK 300 WILL YIELD APPROXIMATE COORDINATES FOR THE VL DOMAIN OF REMARK 300 CHAIN *L* WHEN APPLIED TO THE VL DOMAIN OF CHAIN *M*. REMARK 300 THE TRANSFORMATION PRESENTED ON *MTRIX 2* RECORDS BELOW REMARK 300 WILL YIELD APPROXIMATE COORDINATES FOR THE CL DOMAIN OF REMARK 300 CHAIN *L* WHEN APPLIED TO THE CL DOMAIN OF CHAIN *M*. REMARK 300 THE TRANSFORMATION PRESENTED ON *MTRIX 3* RECORDS BELOW REMARK 300 WILL YIELD APPROXIMATE COORDINATES FOR THE VH DOMAIN OF REMARK 300 CHAIN *H* WHEN APPLIED TO THE VH DOMAIN OF CHAIN *J*. REMARK 300 THE TRANSFORMATION PRESENTED ON *MTRIX 4* RECORDS BELOW REMARK 300 WILL YIELD APPROXIMATE COORDINATES FOR THE CH DOMAIN OF REMARK 300 CHAIN *H* WHEN APPLIED TO THE CH DOMAIN OF CHAIN *J*. 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4370 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19550 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, P 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 4410 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19680 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, J, Q 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 ASN L 212 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 GLY H 229 REMARK 465 PRO H 230 REMARK 465 THR H 231 REMARK 465 ILE H 232 REMARK 465 LYS H 233 REMARK 465 PRO H 234 REMARK 465 CYS H 235 REMARK 465 ARG P 322 REMARK 465 ALA P 323 REMARK 465 PHE P 324 REMARK 465 TYR P 325 REMARK 465 THR P 326 REMARK 465 THR P 327 REMARK 465 CYS P 328 REMARK 465 ASN M 212 REMARK 465 GLU M 213 REMARK 465 CYS M 214 REMARK 465 GLY J 229 REMARK 465 PRO J 230 REMARK 465 THR J 231 REMARK 465 ILE J 232 REMARK 465 LYS J 233 REMARK 465 PRO J 234 REMARK 465 CYS J 235 REMARK 465 ARG Q 322 REMARK 465 ALA Q 323 REMARK 465 PHE Q 324 REMARK 465 TYR Q 325 REMARK 465 THR Q 326 REMARK 465 THR Q 327 REMARK 465 CYS Q 328 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 HIS L 34 NE2 HIS L 34 CD2 -0.079 REMARK 500 HIS L 189 NE2 HIS L 189 CD2 -0.069 REMARK 500 HIS H 50 NE2 HIS H 50 CD2 -0.092 REMARK 500 HIS H 172 NE2 HIS H 172 CD2 -0.074 REMARK 500 HIS H 212 NE2 HIS H 212 CD2 -0.076 REMARK 500 HIS P 315 NE2 HIS P 315 CD2 -0.073 REMARK 500 HIS M 34 NE2 HIS M 34 CD2 -0.096 REMARK 500 HIS J 50 NE2 HIS J 50 CD2 -0.071 REMARK 500 HIS J 212 NE2 HIS J 212 CD2 -0.076 REMARK 500 HIS Q 315 NE2 HIS Q 315 CD2 -0.068 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 VAL L 3 CA - CB - CG2 ANGL. DEV. = -9.0 DEGREES REMARK 500 ARG L 24 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 SER L 26 CA - CB - OG ANGL. DEV. = 16.9 DEGREES REMARK 500 ASP L 28 CA - CB - CG ANGL. DEV. = -17.2 DEGREES REMARK 500 ASP L 27D CA - C - N ANGL. DEV. = -15.3 DEGREES REMARK 500 ASP L 28 CA - C - N ANGL. DEV. = -16.2 DEGREES REMARK 500 TRP L 35 CD1 - CG - CD2 ANGL. DEV. = 5.7 DEGREES REMARK 500 TRP L 35 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES REMARK 500 TYR L 49 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES REMARK 500 ARG L 50 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES REMARK 500 PRO L 77 O - C - N ANGL. DEV. = -9.7 DEGREES REMARK 500 TYR L 87 CB - CG - CD1 ANGL. DEV. = -4.1 DEGREES REMARK 500 LEU L 96 CB - CG - CD1 ANGL. DEV. = -10.5 DEGREES REMARK 500 TRP L 148 CE2 - CD2 - CG ANGL. DEV. = -5.5 DEGREES REMARK 500 TRP L 148 CG - CD2 - CE3 ANGL. DEV. = 6.2 DEGREES REMARK 500 LEU L 160 CA - CB - CG ANGL. DEV. = 17.7 DEGREES REMARK 500 TRP L 163 CB - CA - C ANGL. DEV. = -12.6 DEGREES REMARK 500 TRP L 163 CD1 - CG - CD2 ANGL. DEV. = 7.3 DEGREES REMARK 500 TRP L 163 CG - CD1 - NE1 ANGL. DEV. = -6.1 DEGREES REMARK 500 TRP L 163 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES REMARK 500 CYS L 194 CA - CB - SG ANGL. DEV. = 7.6 DEGREES REMARK 500 LEU H 4 CA - CB - CG ANGL. DEV. = 16.5 DEGREES REMARK 500 LEU H 12 CA - CB - CG ANGL. DEV. = 14.5 DEGREES REMARK 500 TYR H 32 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES REMARK 500 TRP H 36 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES REMARK 500 TRP H 36 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES REMARK 500 TRP H 47 CD1 - CG - CD2 ANGL. DEV. = 5.5 DEGREES REMARK 500 TRP H 47 CE2 - CD2 - CG ANGL. DEV. = -5.0 DEGREES REMARK 500 TRP H 53 CD1 - CG - CD2 ANGL. DEV. = 5.5 DEGREES REMARK 500 TRP H 53 CE2 - CD2 - CG ANGL. DEV. = -5.8 DEGREES REMARK 500 TRP H 53 CG - CD2 - CE3 ANGL. DEV. = 6.0 DEGREES REMARK 500 ASP H 56 CA - CB - CG ANGL. DEV. = 16.0 DEGREES REMARK 500 ARG H 58 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES REMARK 500 ARG H 66 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES REMARK 500 ARG H 66 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES REMARK 500 ILE H 69 CB - CA - C ANGL. DEV. = -12.2 DEGREES REMARK 500 TRP H 103 CE2 - CD2 - CG ANGL. DEV. = -4.9 DEGREES REMARK 500 TYR H 122 CB - CG - CD2 ANGL. DEV. = -6.2 DEGREES REMARK 500 VAL H 127 CA - CB - CG1 ANGL. DEV. = 9.3 DEGREES REMARK 500 VAL H 127 CA - CB - CG2 ANGL. DEV. = -10.1 DEGREES REMARK 500 CYS H 128 CA - C - N ANGL. DEV. = -12.1 DEGREES REMARK 500 TRP H 157 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES REMARK 500 TRP H 157 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES REMARK 500 GLN H 179 CA - CB - CG ANGL. DEV. = 14.0 DEGREES REMARK 500 TRP H 199 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES REMARK 500 TRP H 199 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES REMARK 500 TRP H 199 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES REMARK 500 ARG H 228 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES REMARK 500 CYS P 311 CA - CB - SG ANGL. DEV. = 7.8 DEGREES REMARK 500 HIS P 315 CB - CG - CD2 ANGL. DEV. = -11.3 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 95 ANGLE DEVIATIONS. 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 ASP L 28 97.49 123.37 REMARK 500 PHE L 32 53.87 -103.23 REMARK 500 SER L 51 -39.30 83.16 REMARK 500 ARG L 68 -99.11 50.15 REMARK 500 ALA L 80 -6.00 -49.78 REMARK 500 SER L 122 -43.12 -25.34 REMARK 500 GLN L 166 95.40 -28.22 REMARK 500 ASP L 167 90.56 -61.16 REMARK 500 ASP L 170 0.94 120.94 REMARK 500 GLU L 187 3.42 -69.09 REMARK 500 THR L 200 15.44 -67.46 REMARK 500 GLN H 16 -143.84 -84.71 REMARK 500 PRO H 40 -175.71 -55.02 REMARK 500 LEU H 48 -61.21 -106.10 REMARK 500 LYS H 68 116.24 -160.09 REMARK 500 VAL H 82C 108.80 -52.09 REMARK 500 ALA H 85 59.37 -90.54 REMARK 500 ASP H 86 -4.44 -153.56 REMARK 500 ALA H 88 -165.79 -171.27 REMARK 500 TYR H 97 14.05 57.59 REMARK 500 THR H 116 100.84 -55.25 REMARK 500 CYS H 128 101.46 115.61 REMARK 500 THR H 133 -166.02 -78.10 REMARK 500 THR H 134 -177.82 58.71 REMARK 500 ASN H 162 21.93 49.38 REMARK 500 SER H 167 -30.40 -135.73 REMARK 500 GLN H 179 -103.57 -94.79 REMARK 500 SER H 180 63.24 -64.72 REMARK 500 ASP H 183 2.18 51.44 REMARK 500 THR H 198 -98.47 -84.78 REMARK 500 SER H 202 -74.80 -65.88 REMARK 500 SER H 215 126.99 122.42 REMARK 500 LYS P 312 -168.98 -118.48 REMARK 500 LEU M 15 96.18 -60.02 REMARK 500 ASP M 28 90.37 81.18 REMARK 500 PHE M 32 49.07 -85.31 REMARK 500 PRO M 40 109.67 -53.22 REMARK 500 SER M 51 -46.78 92.27 REMARK 500 ILE M 58 109.03 -49.35 REMARK 500 ASP M 60 15.22 -67.35 REMARK 500 ARG M 68 -81.19 59.11 REMARK 500 VAL M 78 106.99 -54.14 REMARK 500 ALA M 80 -53.84 -25.83 REMARK 500 SER M 127 4.06 -69.27 REMARK 500 ASN M 138 75.86 51.21 REMARK 500 ASP M 165 -172.51 -67.45 REMARK 500 ASP M 167 90.68 -54.24 REMARK 500 ASP M 170 23.96 -145.25 REMARK 500 SER M 171 51.87 38.71 REMARK 500 LYS M 199 -68.13 -17.54 REMARK 500 THR M 200 -32.01 -36.42 REMARK 500 SER J 15 -17.17 72.34 REMARK 500 SER J 41 100.84 -37.31 REMARK 500 LYS J 43 -156.34 -118.74 REMARK 500 LEU J 48 -52.76 -120.50 REMARK 500 LYS J 64 -52.48 -14.43 REMARK 500 VAL J 82C 130.58 -27.39 REMARK 500 THR J 87 107.62 -58.89 REMARK 500 GLN J 105 -1.44 -53.81 REMARK 500 THR J 116 108.02 -35.53 REMARK 500 THR J 134 24.57 41.43 REMARK 500 SER J 163 -1.70 61.92 REMARK 500 SER J 180 92.36 32.82 REMARK 500 ASP J 183 -26.49 69.51 REMARK 500 ALA J 214 -5.75 -51.85 REMARK 500 SER J 215 48.29 -143.99 REMARK 500 SER J 216 69.37 -12.20 REMARK 500 ARG Q 313 120.10 -25.43 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 SER L 203 PRO L 204 149.54 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 L 192 0.08 SIDE_CHAIN REMARK 500 TYR M 186 0.06 SIDE_CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 REMARK 999 THE FAB FRAGMENT IS NUMBERED BY THE CONVENTION OF E. KABAT REMARK 999 (E.A. KABAT, T.T. WU, M. REID-MILLER, H.M. PERRY, K.S. REMARK 999 GOTTESMAN, SEQUENCES OF PROTEINS OF IMMUNOLOGICAL INTEREST, REMARK 999 4TH ED., (1987), NATIONAL INSTITUTE OF HEALTH, BETHESDA, REMARK 999 MD. REMARK 999 REMARK 999 THE PEPTIDE IS NUMBERED ACCORDING TO THE BH10 ISOLATE REMARK 999 SEQUENCE (L. RATNER, W. HASELTINE, R. PATARCA, K.J. LIVAK, REMARK 999 B. STARCICH, S.F. JOSEPHS, E.R. DORAN, J.A. RAFALSKI, E.A. REMARK 999 WHITEHORN, K. BAUMEISTER, L. IVANOFF, S.R. PETTEWAY JR., M. REMARK 999 L. PEARSON, J.A. LAUTENBERGER, T.S. PAPAS, J. GHRAYEB, N.T. REMARK 999 CHANG, R.C. GALLO, F. WONG-STAAL (1985) NATURE V. 313, REMARK 999 277-284.) (*CKRIHIGPG;311-316, 319-321) (*C IS AN REMARK 999 ACETAMIDOMETHYLATED CYSTEINE IN THE REAL PEPTIDE; HOWEVER REMARK 999 IN THE DEPOSITED MODEL THIS IS A CYS)