HEADER IMMUNOGLOBULIN 25-OCT-93 1MFA TITLE STRUCTURE OF A SINGLE-CHAIN FV FRAGMENT COMPLEXED WITH A TITLE 2 CARBOHYDRATE ANTIGEN AT 1.7 ANGSTROMS RESOLUTION COMPND MOL_ID: 1; COMPND 2 MOLECULE: IGG1-LAMBDA SE155-4 FAB (LIGHT CHAIN); COMPND 3 CHAIN: L; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IGG1-LAMBDA SE155-4 FAB (HEAVY CHAIN); COMPND 7 CHAIN: H; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: MOUSE; SOURCE 4 MOL_ID: 2; SOURCE 5 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 6 ORGANISM_COMMON: MOUSE KEYWDS IMMUNOGLOBULIN EXPDTA X-RAY DIFFRACTION AUTHOR A.ZDANOV,M.CYGLER REVDAT 2 01-APR-03 1MFA 1 JRNL REVDAT 1 31-JAN-94 1MFA 0 JRNL AUTH A.ZDANOV,Y.LI,D.R.BUNDLE,S.J.DENG,C.R.MACKENZIE, JRNL AUTH 2 S.A.NARANG,N.M.YOUNG,M.CYGLER JRNL TITL STRUCTURE OF A SINGLE-CHAIN ANTIBODY VARIABLE JRNL TITL 2 DOMAIN (FV) FRAGMENT COMPLEXED WITH A CARBOHYDRATE JRNL TITL 3 ANTIGEN AT 1.7-A RESOLUTION. JRNL REF PROC.NATL.ACAD.SCI.USA V. 91 6423 1994 JRNL REFN ASTM PNASA6 US ISSN 0027-8424 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH D.R.BUNDLE,H.BAUMANN,J.-R.BRISSON,S.GAGNE,A.ZDANOV, REMARK 1 AUTH 2 M.CYGLER REMARK 1 TITL THE SOLUTION STRUCTURE OF A TRISACCHARIDE-ANTIBODY REMARK 1 TITL 2 COMPLEX: COMPARISON OF NMR MEASUREMENTS WITH A REMARK 1 TITL 3 CRYSTAL STRUCTURE REMARK 1 REF TO BE PUBLISHED REMARK 1 REFN REMARK 1 REFERENCE 2 REMARK 1 AUTH N.N.ANAND,S.MANDAL,C.R.MACKENZIE,J.SADOWSKA, REMARK 1 AUTH 2 B.SIJURSKJOLD,N.M.YOUNG,D.R.BUDLE,S.A.NARANG REMARK 1 TITL BACTERIAL EXPRESSION AND SECRETION OF VARIOUS REMARK 1 TITL 2 SINGLE-CHAIN FV GENES ENCODING PROTEINS SPECIFIC REMARK 1 TITL 3 FOR A SALMONELLA SEROTYPE B O-ANTIGEN REMARK 1 REF J.BIOL.CHEM. V. 266 21874 1991 REMARK 1 REFN ASTM JBCHA3 US ISSN 0021-9258 REMARK 1 REFERENCE 3 REMARK 1 AUTH M.CYGLER,D.R.ROSE,D.R.BUNDLE REMARK 1 TITL RECOGNITION OF A CELL-SURFACE OLIGO-SACCHARIDE OF REMARK 1 TITL 2 PATHOGENIC SALMONELLA BY AN ANTIBODY FAB FRAGMENT REMARK 1 REF SCIENCE V. 253 442 1991 REMARK 1 REFN ASTM SCIEAS US ISSN 0036-8075 REMARK 2 REMARK 2 RESOLUTION. 1.70 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) : 1.70 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) : 0.166 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 : 1711 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 33 REMARK 3 SOLVENT ATOMS : 174 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) : 0.013 REMARK 3 BOND ANGLES (DEGREES) : 2.80 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 1MFA 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 3.100 (2007-03-17) 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 (%): 46.14 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28 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 26.55000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.40000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.50000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.40000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.55000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.50000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 2 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 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 LYS L 113 REMARK 465 SER L 114 REMARK 465 SER L 115 REMARK 465 PRO L 116 REMARK 465 SER L 117 REMARK 465 VAL L 118 REMARK 465 THR L 119 REMARK 465 LEU L 120 REMARK 465 PHE L 121 REMARK 465 PRO L 122 REMARK 465 PRO L 123 REMARK 465 SER L 124 REMARK 465 SER L 125 REMARK 465 GLU L 126 REMARK 465 SER H 368 REMARK 465 ALA H 369 REMARK 465 LYS H 370 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 CB CG CD OE1 NE2 REMARK 470 ARG L 23 CG CD NE CZ NH1 NH2 REMARK 470 ASP L 43 CB CG OD1 OD2 REMARK 470 PRO L 112 CA C O CB CG CD REMARK 470 GLU H 251 CB CG CD OE1 OE2 REMARK 470 ARG H 315 CG CD NE CZ NH1 NH2 REMARK 470 SER H 367 OG 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 C GLY L 127 N GLU H 251 1.34 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 GLN L 111 C PRO L 112 N -0.113 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 THR L 53 -47.02 69.58 SEQRES 1 L 127 GLN ILE VAL VAL THR GLN GLU SER ALA LEU THR THR SER SEQRES 2 L 127 PRO GLY GLU THR VAL THR LEU THR CYS ARG SER SER THR SEQRES 3 L 127 GLY THR VAL THR SER GLY ASN HIS ALA ASN TRP VAL GLN SEQRES 4 L 127 GLU LYS PRO ASP HIS LEU PHE THR GLY LEU ILE GLY ASP SEQRES 5 L 127 THR ASN ASN ARG ALA PRO GLY VAL PRO ALA ARG PHE SER SEQRES 6 L 127 GLY SER LEU ILE GLY ASP LYS ALA ALA LEU THR ILE THR SEQRES 7 L 127 GLY ALA GLN PRO GLU ASP GLU ALA ILE TYR PHE CYS ALA SEQRES 8 L 127 LEU TRP SER ASN ASN HIS TRP ILE PHE GLY GLY GLY THR SEQRES 9 L 127 LYS LEU THR VAL LEU GLY GLN PRO LYS SER SER PRO SER SEQRES 10 L 127 VAL THR LEU PHE PRO PRO SER SER GLU GLY SEQRES 1 H 120 GLU VAL GLN VAL GLN GLN SER GLY THR VAL VAL ALA ARG SEQRES 2 H 120 PRO GLY ALA SER VAL LYS MET SER CYS LYS ALA SER GLY SEQRES 3 H 120 TYR THR PHE THR ASN TYR TRP MET HIS TRP ILE LYS GLN SEQRES 4 H 120 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY ALA ILE TYR SEQRES 5 H 120 PRO GLY ASN SER ALA THR PHE TYR ASN HIS LYS PHE ARG SEQRES 6 H 120 ALA LYS THR LYS LEU THR ALA VAL THR SER THR THR THR SEQRES 7 H 120 ALA TYR MET GLU LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 H 120 ALA VAL TYR TYR CYS THR ARG GLY GLY HIS GLY TYR TYR SEQRES 9 H 120 GLY ASP TYR TRP GLY GLN GLY ALA SER LEU THR VAL SER SEQRES 10 H 120 SER ALA LYS HET GLA 501 11 HET MMA 502 13 HET ABE 503 9 HETNAM GLA ALPHA D-GALACTOSE HETNAM MMA O1-METHYL-MANNOSE HETNAM ABE ABEQUOSE FORMUL 3 GLA C6 H12 O6 FORMUL 3 MMA C7 H14 O6 FORMUL 3 ABE C6 H12 O4 FORMUL 4 HOH *174(H2 O) HELIX 1 H1 SER L 24 GLY L 27 5 4 HELIX 2 H2 THR L 30 HIS L 34 5 5 HELIX 3 H3 THR H 278 TYR H 282 5 5 SHEET 1 B1 4 GLN L 1 GLU L 7 0 SHEET 2 B1 4 GLU L 16 THR L 26 -1 N SER L 25 O VAL L 3 SHEET 3 B1 4 ASP L 71 ALA L 80 1 N ALA L 80 O GLU L 16 SHEET 4 B1 4 SER L 65 GLY L 70 -1 O SER L 65 N THR L 76 SHEET 1 B2 6 SER L 8 THR L 12 0 SHEET 2 B2 6 HIS L 97 LEU L 109 1 N LYS L 105 O SER L 8 SHEET 3 B2 6 GLU L 85 TRP L 93 -1 O ALA L 86 N LEU L 106 SHEET 4 B2 6 ASN L 36 PRO L 42 1 O ASN L 36 N ALA L 91 SHEET 5 B2 6 HIS L 44 GLY L 51 -1 N LEU L 45 O LYS L 41 SHEET 6 B2 6 ASN L 55 PRO L 58 1 O ASN L 55 N GLY L 51 SHEET 1 B3 4 GLU H 251 SER H 257 0 SHEET 2 B3 4 GLY H 265 GLY H 276 -1 O SER H 271 N SER H 257 SHEET 3 B3 4 THR H 327 SER H 335 1 O THR H 327 N ALA H 274 SHEET 4 B3 4 LYS H 317 VAL H 323 -1 O LYS H 317 N SER H 334 SHEET 1 B4 6 GLY H 258 ALA H 262 0 SHEET 2 B4 6 TYR H 353 SER H 367 1 O SER H 363 N VAL H 260 SHEET 3 B4 6 SER H 341 GLY H 352 -1 N ALA H 342 O LEU H 364 SHEET 4 B4 6 TRP H 283 PRO H 291 1 O TRP H 283 N GLY H 349 SHEET 5 B4 6 GLY H 292 TYR H 302 -1 N GLN H 293 O ARG H 290 SHEET 6 B4 6 ALA H 307 ASN H 311 1 O ALA H 307 N TYR H 302 SSBOND 1 CYS L 22 CYS L 90 SSBOND 2 CYS H 272 CYS H 346 LINK C1 GLA 501 O2 MMA 502 LINK O3 MMA 502 C1 ABE 503 CRYST1 53.100 61.000 74.800 90.00 90.00 90.00 P 21 21 21 4 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 0.018832 0.000000 0.000000 0.00000 SCALE2 0.000000 0.016393 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013369 0.00000