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HEADER IMMUNE SYSTEM 02-NOV-02 1N4X TITLE STRUCTURE OF SCFV 1696 AT ACIDIC PH COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMUNOGLOBULIN KAPPA CHAIN VARIABLE REGION; COMPND 3 CHAIN: L, M; COMPND 4 SYNONYM: SCFV 1696 MOLECULE 1, MONOCLONAL ANTIBODY 1696; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: IMMUNOGLOBULIN HEAVY CHAIN VARIABLE REGION; COMPND 8 CHAIN: H, I; COMPND 9 SYNONYM: SCFV 1696 MOLECULE 2, MONOCLONAL ANTIBODY 1696; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 8 ORGANISM_COMMON: MOUSE; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_COMMON: BACTERIA KEYWDS IMMUNOGLOBULIN EXPDTA X-RAY DIFFRACTION AUTHOR J.LESCAR,J.BRYNDA,M.FABRY,M.HOREJSI,P.REZACOVA,J.SEDLACEK, AUTHOR 2 G.A.BENTLEY REVDAT 1 10-JUN-03 1N4X 0 JRNL AUTH J.LESCAR,J.BRYNDA,M.FABRY,M.HOREJSI,P.REZACOVA, JRNL AUTH 2 J.SEDLACEK,G.A.BENTLEY JRNL TITL STRUCTURE OF A SINGLE-CHAIN FV FRAGMENT OF AN JRNL TITL 2 ANTIBODY THAT INHIBITS THE HIV-1 AND HIV-2 JRNL TITL 3 PROTEASES. JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 59 955 2003 JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK 3 : READ,RICE,SIMONSON,WARREN REMARK 3 REMARK 3 REFINEMENT TARGET : ENGH & HUBER REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00 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) (%) : 91.0 REMARK 3 NUMBER OF REFLECTIONS : 45422 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : NULL REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING SET) : 0.227 REMARK 3 FREE R VALUE : 0.256 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 2280 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 : 3656 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 2 REMARK 3 SOLVENT ATOMS : 530 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) : 0.005 REMARK 3 BOND ANGLES (DEGREES) : NULL 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 BULK SOLVENT MODELING. REMARK 3 METHOD USED : NULL REMARK 3 KSOL : NULL REMARK 3 BSOL : 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 1N4X COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006 REMARK 4 REMARK 4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY. REMARK 4 REMEDIATED DATA FILE REVISION 3.101 (2007-05-29) REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ . REMARK 100 THE RCSB ID CODE IS RCSB017523. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-JAN-1998 REMARK 200 TEMPERATURE (KELVIN) : NULL REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 3 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.99 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : AREA DETECTOR REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MARXDS REMARK 200 DATA SCALING SOFTWARE : XDS 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: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 34.69 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: NULL REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 1/2-X,-Y,1/2+Z REMARK 290 3555 -X,1/2+Y,1/2-Z REMARK 290 4555 1/2+X,1/2-Y,-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 63.46500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 28.65000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.60500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 28.65000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 63.46500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.60500 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). 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 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 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, I 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 I 420 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 MET L 0 CG SD CE REMARK 470 LEU M 3 CG CD1 CD2 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 REMARK 500 NH2 ARG M 24 O HOH 442 1.96 REMARK 500 O HOH 198 O HOH 319 2.00 REMARK 500 O HOH 20 O HOH 413 2.02 REMARK 500 O HOH 95 O HOH 319 2.02 REMARK 500 O SER L 48 O HOH 460 2.08 REMARK 500 O HOH 64 O HOH 308 2.08 REMARK 500 O HOH 45 O HOH 414 2.14 REMARK 500 O HOH 224 O HOH 382 2.14 REMARK 500 O HOH 245 O HOH 409 2.14 REMARK 500 O HOH 163 O HOH 373 2.15 REMARK 500 O HOH 238 O HOH 410 2.15 REMARK 500 O HOH 144 O HOH 436 2.16 REMARK 500 N MET M 0 O HOH 308 2.17 REMARK 500 O HOH 20 O HOH 290 2.17 REMARK 500 O HOH 44 O HOH 301 2.17 REMARK 500 O HOH 45 O HOH 316 2.17 REMARK 500 OG SER H 377 O HOH 521 2.18 REMARK 500 O HOH 45 O HOH 405 2.18 REMARK 500 O HOH 50 O HOH 309 2.18 REMARK 500 O HOH 117 O HOH 370 2.18 REMARK 500 O HOH 141 O HOH 426 2.18 REMARK 500 O HOH 177 O HOH 460 2.18 REMARK 500 O HOH 229 O HOH 437 2.18 REMARK 500 OD1 ASP L 1 O HOH 480 2.19 REMARK 500 OE1 GLN L 43 O HOH 491 2.19 REMARK 500 O GLY H 366 O HOH 329 2.19 REMARK 500 O HOH 152 O HOH 330 2.19 REMARK 500 O HOH 181 O HOH 355 2.19 REMARK 500 O HOH 222 O HOH 423 2.19 REMARK 500 O HOH 237 O HOH 386 2.19 REMARK 500 O HOH 409 O HOH 442 2.19 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 O HOH 406 O HOH 413 2565 2.17 REMARK 500 O HOH 63 O HOH 426 2564 2.18 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),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 PRO H 358 CB PRO H 358 CG 0.033 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: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 CYS L 93 N - CA - C ANGL. DEV. = -9.0 DEGREES REMARK 500 GLY L 104 N - CA - C ANGL. DEV. = -8.8 DEGREES REMARK 500 LEU H 311 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 ASN H 352 N - CA - C ANGL. DEV. = -8.7 DEGREES REMARK 500 ASP H 362 N - CA - C ANGL. DEV. = 8.3 DEGREES REMARK 500 ASP H 363 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 ASP H 373 N - CA - C ANGL. DEV. =-11.5 DEGREES REMARK 500 CYS H 396 N - CA - C ANGL. DEV. =-11.3 DEGREES REMARK 500 VAL M 56 N - CA - C ANGL. DEV. = 9.3 DEGREES REMARK 500 GLY M 104 N - CA - C ANGL. DEV. = -8.4 DEGREES REMARK 500 ASN I 326 N - CA - C ANGL. DEV. = 11.1 DEGREES REMARK 500 GLY I 343 N - CA - C ANGL. DEV. = 9.7 DEGREES REMARK 500 ASN I 352 N - CA - C ANGL. DEV. = -9.5 DEGREES REMARK 500 ALA I 361 N - CA - C ANGL. DEV. =-10.5 DEGREES REMARK 500 ASP I 362 N - CA - C ANGL. DEV. = 8.8 DEGREES REMARK 500 GLY I 366 N - CA - C ANGL. DEV. = 14.7 DEGREES REMARK 500 LEU I 381 N - CA - C ANGL. DEV. = -9.3 DEGREES REMARK 500 CYS I 396 N - CA - C ANGL. DEV. =-10.5 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 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 M RES CSSEQI PSI PHI REMARK 500 VAL L 56 -46.94 71.43 REMARK 500 VAL M 56 -53.93 69.75 REMARK 525 REMARK 525 SOLVENT REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH 95 DISTANCE = 5.62 ANGSTROMS REMARK 525 HOH 135 DISTANCE = 5.07 ANGSTROMS REMARK 525 HOH 150 DISTANCE = 5.96 ANGSTROMS REMARK 525 HOH 396 DISTANCE = 6.19 ANGSTROMS REMARK 525 HOH 450 DISTANCE = 6.39 ANGSTROMS REMARK 525 HOH 513 DISTANCE = 5.32 ANGSTROMS REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1CL7 RELATED DB: PDB REMARK 900 FREE FAB 1696 REMARK 900 RELATED ID: 1JP5 RELATED DB: PDB REMARK 900 COMPLEXED SCFV1696 DBREF 1N4X L 1 110 UNP Q99M37 Q99M37 23 130 DBREF 1N4X H 304 417 UNP Q921A6 Q921A6_MOUSE 2 117 DBREF 1N4X M 1 110 UNP Q99M37 Q99M37 23 130 DBREF 1N4X I 304 417 UNP Q921A6 Q921A6_MOUSE 2 117 SEQADV 1N4X MET L 0 UNP Q99M37 INITIATING MET SEQADV 1N4X ILE L 111 UNP Q99M37 CLONING ARTIFACT SEQADV 1N4X ALA L 112 UNP Q99M37 CLONING ARTIFACT SEQADV 1N4X MET M 0 UNP Q99M37 INITIATING MET SEQADV 1N4X ILE M 111 UNP Q99M37 CLONING ARTIFACT SEQADV 1N4X ALA M 112 UNP Q99M37 CLONING ARTIFACT SEQADV 1N4X GLU H 301 UNP Q921A6 CLONING ARTIFACT SEQADV 1N4X VAL H 302 UNP Q921A6 CLONING ARTIFACT SEQADV 1N4X GLN H 303 UNP Q921A6 CLONING ARTIFACT SEQADV 1N4X VAL H 418 UNP Q921A6 CLONING ARTIFACT SEQADV 1N4X SER H 419 UNP Q921A6 CLONING ARTIFACT SEQADV 1N4X ALA H 420 UNP Q921A6 CLONING ARTIFACT SEQADV 1N4X GLU I 301 UNP Q921A6 CLONING ARTIFACT SEQADV 1N4X VAL I 302 UNP Q921A6 CLONING ARTIFACT SEQADV 1N4X GLN I 303 UNP Q921A6 CLONING ARTIFACT SEQADV 1N4X VAL I 418 UNP Q921A6 CLONING ARTIFACT SEQADV 1N4X SER I 419 UNP Q921A6 CLONING ARTIFACT SEQADV 1N4X ALA I 420 UNP Q921A6 CLONING ARTIFACT SEQRES 1 L 113 MET ASP ILE LEU MET THR GLN THR PRO LEU TYR LEU PRO SEQRES 2 L 113 VAL SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SEQRES 3 L 113 SER GLN THR ILE VAL HIS ASN ASN GLY ASN THR TYR LEU SEQRES 4 L 113 GLU TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU SEQRES 5 L 113 LEU ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO SEQRES 6 L 113 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 L 113 LEU LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY ILE SEQRES 8 L 113 TYR TYR CYS PHE GLN GLY SER HIS PHE PRO PRO THR PHE SEQRES 9 L 113 GLY GLY GLY THR LYS LEU GLU ILE ALA SEQRES 1 H 120 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU LYS LYS SEQRES 2 H 120 PRO GLY GLU THR VAL LYS ILE SER CYS LYS ALA THR ASN SEQRES 3 H 120 TYR ALA PHE THR ASP TYR SER MET HIS TRP VAL LYS GLN SEQRES 4 H 120 ALA PRO GLY GLY ASP LEU LYS TYR VAL GLY TRP ILE ASN SEQRES 5 H 120 THR GLU THR ASP GLU PRO THR PHE ALA ASP ASP PHE LYS SEQRES 6 H 120 GLY ARG PHE ALA PHE SER LEU ASP THR SER THR SER THR SEQRES 7 H 120 ALA PHE LEU GLN ILE ASN ASN LEU LYS ASN GLU ASP THR SEQRES 8 H 120 ALA THR TYR PHE CYS VAL ARG ASP ARG HIS ASP TYR GLY SEQRES 9 H 120 GLU ILE PHE THR TYR TRP GLY GLN GLY THR THR VAL THR SEQRES 10 H 120 VAL SER ALA SEQRES 1 M 113 MET ASP ILE LEU MET THR GLN THR PRO LEU TYR LEU PRO SEQRES 2 M 113 VAL SER LEU GLY ASP GLN ALA SER ILE SER CYS ARG SER SEQRES 3 M 113 SER GLN THR ILE VAL HIS ASN ASN GLY ASN THR TYR LEU SEQRES 4 M 113 GLU TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU SEQRES 5 M 113 LEU ILE TYR LYS VAL SER ASN ARG PHE SER GLY VAL PRO SEQRES 6 M 113 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 M 113 LEU LYS ILE SER ARG VAL GLU ALA GLU ASP LEU GLY ILE SEQRES 8 M 113 TYR TYR CYS PHE GLN GLY SER HIS PHE PRO PRO THR PHE SEQRES 9 M 113 GLY GLY GLY THR LYS LEU GLU ILE ALA SEQRES 1 I 120 GLU VAL GLN LEU GLN GLN SER GLY PRO GLU LEU LYS LYS SEQRES 2 I 120 PRO GLY GLU THR VAL LYS ILE SER CYS LYS ALA THR ASN SEQRES 3 I 120 TYR ALA PHE THR ASP TYR SER MET HIS TRP VAL LYS GLN SEQRES 4 I 120 ALA PRO GLY GLY ASP LEU LYS TYR VAL GLY TRP ILE ASN SEQRES 5 I 120 THR GLU THR ASP GLU PRO THR PHE ALA ASP ASP PHE LYS SEQRES 6 I 120 GLY ARG PHE ALA PHE SER LEU ASP THR SER THR SER THR SEQRES 7 I 120 ALA PHE LEU GLN ILE ASN ASN LEU LYS ASN GLU ASP THR SEQRES 8 I 120 ALA THR TYR PHE CYS VAL ARG ASP ARG HIS ASP TYR GLY SEQRES 9 I 120 GLU ILE PHE THR TYR TRP GLY GLN GLY THR THR VAL THR SEQRES 10 I 120 VAL SER ALA HET CL 1001 1 HET CL 1002 1 HETNAM CL CHLORIDE ION FORMUL 5 CL 2(CL 1-) FORMUL 7 HOH *530(H2 O) HELIX 1 1 GLU L 84 LEU L 88 5 5 HELIX 2 2 ALA H 328 TYR H 332 5 5 HELIX 3 3 THR H 374 THR H 376 5 3 HELIX 4 4 LYS H 387 THR H 391 5 5 HELIX 5 5 GLU M 84 LEU M 88 5 5 HELIX 6 6 ALA I 328 TYR I 332 5 5 HELIX 7 7 ASP I 362 LYS I 365 5 4 HELIX 8 8 THR I 374 THR I 376 5 3 HELIX 9 9 LYS I 387 THR I 391 5 5 SHEET 1 A 4 MET L 4 THR L 7 0 SHEET 2 A 4 ALA L 19 SER L 25 -1 O SER L 22 N THR L 7 SHEET 3 A 4 ASP L 75 ILE L 80 -1 O ILE L 80 N ALA L 19 SHEET 4 A 4 PHE L 67 GLY L 71 -1 N SER L 70 O THR L 77 SHEET 1 B 5 ASN L 58 ARG L 59 0 SHEET 2 B 5 GLN L 50 TYR L 54 -1 N TYR L 54 O ASN L 58 SHEET 3 B 5 LEU L 38 GLN L 43 -1 N TRP L 40 O LEU L 52 SHEET 4 B 5 GLY L 89 GLN L 95 -1 O TYR L 92 N TYR L 41 SHEET 5 B 5 THR L 102 PHE L 103 -1 O THR L 102 N GLN L 95 SHEET 1 C 6 ASN L 58 ARG L 59 0 SHEET 2 C 6 GLN L 50 TYR L 54 -1 N TYR L 54 O ASN L 58 SHEET 3 C 6 LEU L 38 GLN L 43 -1 N TRP L 40 O LEU L 52 SHEET 4 C 6 GLY L 89 GLN L 95 -1 O TYR L 92 N TYR L 41 SHEET 5 C 6 THR L 107 ILE L 111 -1 O THR L 107 N TYR L 91 SHEET 6 C 6 TYR L 10 VAL L 13 1 N LEU L 11 O LYS L 108 SHEET 1 D 4 GLN H 303 GLN H 306 0 SHEET 2 D 4 VAL H 318 THR H 325 -1 O LYS H 323 N GLN H 305 SHEET 3 D 4 THR H 378 ILE H 383 -1 O LEU H 381 N ILE H 320 SHEET 4 D 4 PHE H 368 ASP H 373 -1 N ALA H 369 O GLN H 382 SHEET 1 E 5 GLU H 357 PHE H 360 0 SHEET 2 E 5 LEU H 345 ASN H 352 -1 N ASN H 352 O GLU H 357 SHEET 3 E 5 MET H 334 GLN H 339 -1 N LYS H 338 O LYS H 346 SHEET 4 E 5 ALA H 392 ASP H 399 -1 O VAL H 397 N HIS H 335 SHEET 5 E 5 PHE H 407 TRP H 410 -1 O TYR H 409 N ARG H 398 SHEET 1 F 6 GLU H 357 PHE H 360 0 SHEET 2 F 6 LEU H 345 ASN H 352 -1 N ASN H 352 O GLU H 357 SHEET 3 F 6 MET H 334 GLN H 339 -1 N LYS H 338 O LYS H 346 SHEET 4 F 6 ALA H 392 ASP H 399 -1 O VAL H 397 N HIS H 335 SHEET 5 F 6 THR H 414 VAL H 418 -1 O VAL H 416 N ALA H 392 SHEET 6 F 6 GLU H 310 LYS H 312 1 N GLU H 310 O THR H 417 SHEET 1 G 4 MET M 4 THR M 7 0 SHEET 2 G 4 ALA M 19 SER M 25 -1 O SER M 22 N THR M 7 SHEET 3 G 4 ASP M 75 ILE M 80 -1 O ILE M 80 N ALA M 19 SHEET 4 G 4 PHE M 67 SER M 72 -1 N SER M 68 O LYS M 79 SHEET 1 H 5 ASN M 58 ARG M 59 0 SHEET 2 H 5 GLN M 50 TYR M 54 -1 N TYR M 54 O ASN M 58 SHEET 3 H 5 LEU M 38 GLN M 43 -1 N TRP M 40 O LEU M 52 SHEET 4 H 5 GLY M 89 GLN M 95 -1 O ILE M 90 N GLN M 43 SHEET 5 H 5 THR M 102 PHE M 103 -1 O THR M 102 N GLN M 95 SHEET 1 I 6 ASN M 58 ARG M 59 0 SHEET 2 I 6 GLN M 50 TYR M 54 -1 N TYR M 54 O ASN M 58 SHEET 3 I 6 LEU M 38 GLN M 43 -1 N TRP M 40 O LEU M 52 SHEET 4 I 6 GLY M 89 GLN M 95 -1 O ILE M 90 N GLN M 43 SHEET 5 I 6 THR M 107 ILE M 111 -1 O THR M 107 N TYR M 91 SHEET 6 I 6 TYR M 10 VAL M 13 1 N LEU M 11 O LYS M 108 SHEET 1 J 4 GLN I 303 GLN I 306 0 SHEET 2 J 4 VAL I 318 THR I 325 -1 O LYS I 323 N GLN I 305 SHEET 3 J 4 THR I 378 ILE I 383 -1 O LEU I 381 N ILE I 320 SHEET 4 J 4 PHE I 368 ASP I 373 -1 N SER I 371 O PHE I 380 SHEET 1 K 5 PRO I 358 PHE I 360 0 SHEET 2 K 5 LEU I 345 ILE I 351 -1 N TRP I 350 O THR I 359 SHEET 3 K 5 MET I 334 GLN I 339 -1 N LYS I 338 O LYS I 346 SHEET 4 K 5 ALA I 392 ASP I 399 -1 O PHE I 395 N VAL I 337 SHEET 5 K 5 PHE I 407 TRP I 410 -1 O TYR I 409 N ARG I 398 SHEET 1 L 6 PRO I 358 PHE I 360 0 SHEET 2 L 6 LEU I 345 ILE I 351 -1 N TRP I 350 O THR I 359 SHEET 3 L 6 MET I 334 GLN I 339 -1 N LYS I 338 O LYS I 346 SHEET 4 L 6 ALA I 392 ASP I 399 -1 O PHE I 395 N VAL I 337 SHEET 5 L 6 THR I 414 VAL I 418 -1 O THR I 414 N TYR I 394 SHEET 6 L 6 GLU I 310 LYS I 312 1 N LYS I 312 O THR I 417 SSBOND 1 CYS L 23 CYS L 93 SSBOND 2 CYS H 322 CYS H 396 SSBOND 3 CYS M 23 CYS M 93 SSBOND 4 CYS I 322 CYS I 396 CISPEP 1 THR L 7 PRO L 8 0 -0.37 CISPEP 2 PHE L 99 PRO L 100 0 -0.29 CISPEP 3 THR M 7 PRO M 8 0 -0.22 CISPEP 4 PHE M 99 PRO M 100 0 0.17 CRYST1 126.930 61.210 57.300 90.00 90.00 90.00 P 21 21 21 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 0.007878 0.000000 0.000000 0.00000 SCALE2 0.000000 0.016337 0.000000 0.00000 SCALE3 0.000000 0.000000 0.017452 0.00000