HEADER IMMUNE SYSTEM 10-JUN-24 9C7F TITLE HUMAN MONOCLONAL ANTIBODY MAD24-01 BOUND TO THE N-TERMINUS OF CLEAVED TITLE 2 CIRCUMSPOROZOITE PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: MONOCLONAL ANTIBODY MAD24-01 FAB HEAVY CHAIN; COMPND 3 CHAIN: H, A, C, E; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MONOCLONAL ANTIBODY MAD24-01 FAB LIGHT CHAIN; COMPND 7 CHAIN: L, B, D, F; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: CIRCUMSPOROZOITE PROTEIN; COMPND 11 CHAIN: Q, G, I, J; COMPND 12 SYNONYM: CS,PFCSP; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7; SOURCE 18 ORGANISM_TAXID: 36329 KEYWDS ANTIBODY, MALARIA, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.MOSKOVITZ,I.A.WILSON REVDAT 1 25-DEC-24 9C7F 0 JRNL AUTH C.DACON,R.MOSKOVITZ,K.SWEARINGEN,L.DA SILVA PEREIRA, JRNL AUTH 2 Y.FLORES-GARCIA,M.ALESHNICK,S.KANATANI,B.FLYNN, JRNL AUTH 3 A.MOLINA-CRUZ,K.WOLLENBERG,M.TRAVER,P.KIRTLEY,L.PURSER, JRNL AUTH 4 M.DILLON,B.BONILLA,A.FRANCO,S.PETROS,J.KRITZBERG,C.TUCKER, JRNL AUTH 5 G.G.PAEZ,P.GUPTA,M.J.SHEARS,J.PAZZI,J.M.EDGAR,A.A.TENG, JRNL AUTH 6 A.BELMONTE,K.ODA,S.DOUMBO,L.KRYMSKAYA,J.SKINNER,S.LI, JRNL AUTH 7 S.GHOSAL,K.KAYENTAO,A.ONGOIBA,A.VAUGHAN,J.J.CAMPO,B.TRAORE, JRNL AUTH 8 C.BARILLAS-MURY,W.WIJAYALATH,A.IDRIS,P.D.CROMPTON,P.SINNIS, JRNL AUTH 9 B.K.WILDER,F.ZAVALA,R.A.SEDER,I.A.WILSON,J.TAN JRNL TITL PROTECTIVE ANTIBODIES TARGET CRYPTIC EPITOPE UNMASKED BY JRNL TITL 2 CLEAVAGE OF MALARIA SPOROZOITE PROTEIN JRNL REF SCIENCE 2024 JRNL REFN ESSN 1095-9203 JRNL DOI 10.1126/SCIENCE.ADR0510 REMARK 2 REMARK 2 RESOLUTION. 1.82 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21RC1_5127 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.00 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 3 NUMBER OF REFLECTIONS : 191764 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.212 REMARK 3 R VALUE (WORKING SET) : 0.211 REMARK 3 FREE R VALUE : 0.238 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970 REMARK 3 FREE R VALUE TEST SET COUNT : 9529 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 45.0000 - 5.6500 0.99 6360 307 0.2046 0.2320 REMARK 3 2 5.6500 - 4.4800 1.00 6307 320 0.1486 0.1818 REMARK 3 3 4.4800 - 3.9200 1.00 6252 333 0.1539 0.1770 REMARK 3 4 3.9200 - 3.5600 1.00 6236 341 0.1827 0.1850 REMARK 3 5 3.5600 - 3.3000 1.00 6206 345 0.1873 0.2221 REMARK 3 6 3.3000 - 3.1100 1.00 6223 338 0.2028 0.2225 REMARK 3 7 3.1100 - 2.9500 1.00 6222 338 0.1987 0.2057 REMARK 3 8 2.9500 - 2.8300 1.00 6248 304 0.1946 0.2355 REMARK 3 9 2.8300 - 2.7200 1.00 6242 284 0.1991 0.2370 REMARK 3 10 2.7200 - 2.6200 1.00 6164 335 0.2018 0.2290 REMARK 3 11 2.6200 - 2.5400 1.00 6203 355 0.1971 0.2363 REMARK 3 12 2.5400 - 2.4700 1.00 6194 313 0.2022 0.2412 REMARK 3 13 2.4700 - 2.4000 1.00 6159 309 0.2061 0.2409 REMARK 3 14 2.4000 - 2.3500 0.99 6196 327 0.2107 0.2532 REMARK 3 15 2.3500 - 2.2900 0.99 6205 327 0.2195 0.2719 REMARK 3 16 2.2900 - 2.2400 0.99 6139 337 0.2213 0.2793 REMARK 3 17 2.2400 - 2.2000 0.99 6133 339 0.2258 0.2659 REMARK 3 18 2.2000 - 2.1600 0.99 6168 335 0.2346 0.2680 REMARK 3 19 2.1600 - 2.1200 0.99 6237 269 0.2339 0.2918 REMARK 3 20 2.1200 - 2.0800 0.99 6125 329 0.2508 0.2602 REMARK 3 21 2.0800 - 2.0500 0.99 6161 327 0.2611 0.2804 REMARK 3 22 2.0500 - 2.0200 0.99 6075 363 0.2673 0.2810 REMARK 3 23 2.0200 - 1.9900 0.99 6200 295 0.2776 0.2996 REMARK 3 24 1.9900 - 1.9600 0.99 6108 322 0.2841 0.3197 REMARK 3 25 1.9600 - 1.9300 0.99 6213 296 0.2958 0.2941 REMARK 3 26 1.9300 - 1.9100 0.99 6108 315 0.3029 0.3408 REMARK 3 27 1.9100 - 1.8800 0.99 6116 342 0.3180 0.3353 REMARK 3 28 1.8800 - 1.8600 0.99 6051 327 0.3386 0.3388 REMARK 3 29 1.8600 - 1.8400 0.98 6054 318 0.3531 0.3599 REMARK 3 30 1.8400 - 1.8200 0.47 2930 139 0.3681 0.3868 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.239 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.447 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 20.30 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.58 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 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.004 14062 REMARK 3 ANGLE : 0.821 19150 REMARK 3 CHIRALITY : 0.047 2168 REMARK 3 PLANARITY : 0.005 2452 REMARK 3 DIHEDRAL : 13.502 5018 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 3 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "A" and (resid 1 through 6 or REMARK 3 resid 8 through 20 or resid 22 through 48 REMARK 3 or resid 50 through 178 or resid 180 REMARK 3 through 185 or resid 187 through 214)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "C" and (resid 1 through 6 or REMARK 3 resid 8 through 20 or resid 22 through 48 REMARK 3 or resid 50 through 178 or resid 180 REMARK 3 through 185 or resid 187 through 214)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "E" and (resid 1 through 6 or REMARK 3 resid 8 through 20 or resid 22 through 48 REMARK 3 or resid 50 through 178 or resid 180 REMARK 3 through 185 or resid 187 through 214)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "H" and (resid 1 through 6 or REMARK 3 resid 8 through 20 or resid 22 through 48 REMARK 3 or resid 50 through 178 or resid 180 REMARK 3 through 185 or resid 187 through 214)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_2 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "B" and (resid 1 through 11 or REMARK 3 resid 13 through 17 or resid 19 through REMARK 3 44 or resid 46 through 47 or resid 49 REMARK 3 through 71 or resid 73 through 113 or REMARK 3 resid 115 through 211 or resid 212)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "D" and (resid 1 through 11 or REMARK 3 resid 13 through 17 or resid 19 through REMARK 3 44 or resid 46 through 47 or resid 49 REMARK 3 through 71 or resid 73 through 113 or REMARK 3 resid 115 through 211 or resid 212)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "F" and (resid 1 through 11 or REMARK 3 resid 13 through 17 or resid 19 through REMARK 3 44 or resid 46 through 47 or resid 49 REMARK 3 through 71 or resid 73 through 113 or REMARK 3 resid 115 through 211 or resid 212)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : (chain "L" and (resid 1 through 11 or REMARK 3 resid 13 through 17 or resid 19 through REMARK 3 44 or resid 46 through 47 or resid 49 REMARK 3 through 71 or resid 73 through 113 or REMARK 3 resid 115 through 211 or resid 212)) REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS GROUP : ens_3 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "G" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "I" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 3 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "J" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 4 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "Q" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9C7F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1000284965. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 16-OCT-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS-II REMARK 200 BEAMLINE : 17-ID-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 192978 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820 REMARK 200 RESOLUTION RANGE LOW (A) : 45.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 200 DATA REDUNDANCY : 3.200 REMARK 200 R MERGE (I) : 0.18300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 3.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.82 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.02400 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: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 56.55 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350 AND 0.2 M POTASSIUM REMARK 280 FLUORIDE, PH 8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K 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 44.16000 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, 3, 4 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, G, M 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, I, N 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: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, Q, O 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 SER H 215 REMARK 465 CYS H 216 REMARK 465 CYS L 212 REMARK 465 SER A 215 REMARK 465 CYS A 216 REMARK 465 CYS B 212 REMARK 465 CYS D 212 REMARK 465 SER E 215 REMARK 465 CYS E 216 REMARK 465 CYS F 212 REMARK 465 PRO Q 11 REMARK 465 ASN Q 12 REMARK 465 ALA Q 13 REMARK 465 ASN Q 14 REMARK 465 PRO Q 15 REMARK 465 ASN Q 16 REMARK 465 VAL Q 17 REMARK 465 ASP Q 18 REMARK 465 PRO Q 19 REMARK 465 ASN Q 20 REMARK 465 PRO G 20 REMARK 465 ASN G 21 REMARK 465 ALA G 22 REMARK 465 ASN G 23 REMARK 465 PRO G 24 REMARK 465 ASN G 25 REMARK 465 VAL G 26 REMARK 465 ASP G 27 REMARK 465 PRO G 28 REMARK 465 ASN G 29 REMARK 465 PRO I 204 REMARK 465 ASN I 205 REMARK 465 ALA I 206 REMARK 465 ASN I 207 REMARK 465 PRO I 208 REMARK 465 ASN I 209 REMARK 465 VAL I 210 REMARK 465 ASP I 211 REMARK 465 PRO I 212 REMARK 465 ASN I 213 REMARK 465 PRO J 318 REMARK 465 ASN J 319 REMARK 465 ALA J 320 REMARK 465 ASN J 321 REMARK 465 PRO J 322 REMARK 465 ASN J 323 REMARK 465 VAL J 324 REMARK 465 ASP J 325 REMARK 465 PRO J 326 REMARK 465 ASN J 327 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 H 132 50.86 -141.20 REMARK 500 SER L 30 -128.41 58.35 REMARK 500 ALA L 51 -38.85 72.23 REMARK 500 ALA L 84 -176.13 -171.13 REMARK 500 ASN L 138 74.56 59.40 REMARK 500 SER A 132 49.96 -142.29 REMARK 500 SER B 30 -126.34 57.56 REMARK 500 ALA B 51 -39.55 73.61 REMARK 500 ALA B 84 -176.22 -171.70 REMARK 500 ASN B 138 73.42 58.68 REMARK 500 LEU C 189 88.24 -68.76 REMARK 500 SER D 30 -125.24 58.40 REMARK 500 ALA D 51 -39.43 72.42 REMARK 500 ALA D 84 -176.24 -172.17 REMARK 500 ASN D 138 70.70 62.71 REMARK 500 SER F 30 -127.52 57.92 REMARK 500 ALA F 51 -38.35 72.74 REMARK 500 ALA F 84 -176.32 -171.90 REMARK 500 ASN F 138 72.83 59.43 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 C 491 DISTANCE = 6.08 ANGSTROMS REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG K 1 REMARK 610 NAG M 1 REMARK 610 NAG N 1 REMARK 610 NAG O 1 DBREF 9C7F H 1 216 PDB 9C7F 9C7F 1 216 DBREF 9C7F L 1 212 PDB 9C7F 9C7F 1 212 DBREF 9C7F A 1 216 PDB 9C7F 9C7F 1 216 DBREF 9C7F B 1 212 PDB 9C7F 9C7F 1 212 DBREF 9C7F C 1 216 PDB 9C7F 9C7F 1 216 DBREF 9C7F D 1 212 PDB 9C7F 9C7F 1 212 DBREF 9C7F E 1 216 PDB 9C7F 9C7F 1 216 DBREF 9C7F F 1 212 PDB 9C7F 9C7F 1 212 DBREF 9C7F Q 3 20 UNP Q7K740 CSP_PLAF7 96 113 DBREF 9C7F G 12 29 UNP Q7K740 CSP_PLAF7 96 113 DBREF 9C7F I 196 213 UNP Q7K740 CSP_PLAF7 96 113 DBREF 9C7F J 310 327 UNP Q7K740 CSP_PLAF7 96 113 SEQRES 1 H 225 PCA VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 H 225 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 225 PHE THR PHE SER ASP TYR TYR MET SER TRP ILE ARG GLN SEQRES 4 H 225 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER TYR ILE GLY SEQRES 5 H 225 SER SER ASN THR TYR THR SER TYR ALA ALA SER VAL LYS SEQRES 6 H 225 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 H 225 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 H 225 ALA VAL TYR TYR CYS ALA ARG GLU ILE GLU ARG SER GLY SEQRES 9 H 225 TRP VAL ARG GLY ASN ASP TYR TRP GLY ARG GLY THR LEU SEQRES 10 H 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 H 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 H 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 H 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 H 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 H 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 H 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 H 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 H 225 PRO LYS SER CYS SEQRES 1 L 212 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 L 212 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 L 212 GLN ASN VAL SER THR TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 L 212 PRO GLY GLN ALA PRO ARG LEU LEU MET TYR ASP ALA SER SEQRES 5 L 212 LYS ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 L 212 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 212 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN ARG SEQRES 8 L 212 ARG ASN TRP PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 L 212 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 212 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 212 VAL THR GLN GLY THR THR SER VAL THR LYS SER PHE ASN SEQRES 17 L 212 ARG GLY GLU CYS SEQRES 1 A 225 PCA VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 A 225 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 225 PHE THR PHE SER ASP TYR TYR MET SER TRP ILE ARG GLN SEQRES 4 A 225 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER TYR ILE GLY SEQRES 5 A 225 SER SER ASN THR TYR THR SER TYR ALA ALA SER VAL LYS SEQRES 6 A 225 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 A 225 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 225 ALA VAL TYR TYR CYS ALA ARG GLU ILE GLU ARG SER GLY SEQRES 9 A 225 TRP VAL ARG GLY ASN ASP TYR TRP GLY ARG GLY THR LEU SEQRES 10 A 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 A 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 A 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 A 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 A 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 A 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 A 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 A 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 A 225 PRO LYS SER CYS SEQRES 1 B 212 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 B 212 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 B 212 GLN ASN VAL SER THR TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 B 212 PRO GLY GLN ALA PRO ARG LEU LEU MET TYR ASP ALA SER SEQRES 5 B 212 LYS ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 B 212 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 B 212 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN ARG SEQRES 8 B 212 ARG ASN TRP PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 B 212 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 B 212 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 B 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 B 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 B 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 B 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 B 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 B 212 VAL THR GLN GLY THR THR SER VAL THR LYS SER PHE ASN SEQRES 17 B 212 ARG GLY GLU CYS SEQRES 1 C 225 PCA VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 C 225 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 225 PHE THR PHE SER ASP TYR TYR MET SER TRP ILE ARG GLN SEQRES 4 C 225 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER TYR ILE GLY SEQRES 5 C 225 SER SER ASN THR TYR THR SER TYR ALA ALA SER VAL LYS SEQRES 6 C 225 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 C 225 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 C 225 ALA VAL TYR TYR CYS ALA ARG GLU ILE GLU ARG SER GLY SEQRES 9 C 225 TRP VAL ARG GLY ASN ASP TYR TRP GLY ARG GLY THR LEU SEQRES 10 C 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 C 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 C 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 C 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 C 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 C 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 C 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 C 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 C 225 PRO LYS SER CYS SEQRES 1 D 212 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 D 212 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 D 212 GLN ASN VAL SER THR TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 D 212 PRO GLY GLN ALA PRO ARG LEU LEU MET TYR ASP ALA SER SEQRES 5 D 212 LYS ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 D 212 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 D 212 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN ARG SEQRES 8 D 212 ARG ASN TRP PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 D 212 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 D 212 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 D 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 D 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 D 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 D 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 D 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 D 212 VAL THR GLN GLY THR THR SER VAL THR LYS SER PHE ASN SEQRES 17 D 212 ARG GLY GLU CYS SEQRES 1 E 225 PCA VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL LYS SEQRES 2 E 225 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 225 PHE THR PHE SER ASP TYR TYR MET SER TRP ILE ARG GLN SEQRES 4 E 225 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER TYR ILE GLY SEQRES 5 E 225 SER SER ASN THR TYR THR SER TYR ALA ALA SER VAL LYS SEQRES 6 E 225 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN SER SEQRES 7 E 225 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 E 225 ALA VAL TYR TYR CYS ALA ARG GLU ILE GLU ARG SER GLY SEQRES 9 E 225 TRP VAL ARG GLY ASN ASP TYR TRP GLY ARG GLY THR LEU SEQRES 10 E 225 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL SEQRES 11 E 225 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY SEQRES 12 E 225 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO SEQRES 13 E 225 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SEQRES 14 E 225 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER SEQRES 15 E 225 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER SEQRES 16 E 225 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN SEQRES 17 E 225 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU SEQRES 18 E 225 PRO LYS SER CYS SEQRES 1 F 212 GLU ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 2 F 212 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 3 F 212 GLN ASN VAL SER THR TYR LEU ALA TRP TYR GLN GLN LYS SEQRES 4 F 212 PRO GLY GLN ALA PRO ARG LEU LEU MET TYR ASP ALA SER SEQRES 5 F 212 LYS ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER SEQRES 6 F 212 GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU SEQRES 7 F 212 GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN ARG SEQRES 8 F 212 ARG ASN TRP PRO LEU THR PHE GLY GLY GLY THR LYS VAL SEQRES 9 F 212 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 F 212 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 F 212 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 F 212 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 F 212 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 F 212 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 F 212 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 F 212 VAL THR GLN GLY THR THR SER VAL THR LYS SER PHE ASN SEQRES 17 F 212 ARG GLY GLU CYS SEQRES 1 Q 18 PCA PRO ALA ASP GLY ASN PRO ASP PRO ASN ALA ASN PRO SEQRES 2 Q 18 ASN VAL ASP PRO ASN SEQRES 1 G 18 PCA PRO ALA ASP GLY ASN PRO ASP PRO ASN ALA ASN PRO SEQRES 2 G 18 ASN VAL ASP PRO ASN SEQRES 1 I 18 PCA PRO ALA ASP GLY ASN PRO ASP PRO ASN ALA ASN PRO SEQRES 2 I 18 ASN VAL ASP PRO ASN SEQRES 1 J 18 PCA PRO ALA ASP GLY ASN PRO ASP PRO ASN ALA ASN PRO SEQRES 2 J 18 ASN VAL ASP PRO ASN MODRES 9C7F PCA Q 3 GLN MODIFIED RESIDUE MODRES 9C7F PCA G 12 GLN MODIFIED RESIDUE MODRES 9C7F PCA I 196 GLN MODIFIED RESIDUE MODRES 9C7F PCA J 310 GLN MODIFIED RESIDUE HET PCA H 1 14 HET PCA A 1 14 HET PCA C 1 14 HET PCA E 1 14 HET PCA Q 3 13 HET PCA G 12 13 HET PCA I 196 13 HET PCA J 310 13 HET NAG K 1 25 HET NAG K 2 27 HET FUC K 3 20 HET NAG M 1 25 HET NAG M 2 27 HET FUC M 3 20 HET NAG N 1 24 HET NAG N 2 27 HET FUC N 3 20 HET NAG O 1 24 HET NAG O 2 27 HET FUC O 3 20 HETNAM PCA PYROGLUTAMIC ACID HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE FORMUL 1 PCA 8(C5 H7 N O3) FORMUL 13 NAG 8(C8 H15 N O6) FORMUL 13 FUC 4(C6 H12 O5) FORMUL 17 HOH *1414(H2 O) HELIX 1 AA1 THR H 28 TYR H 32 5 5 HELIX 2 AA2 ALA H 61 LYS H 64 5 4 HELIX 3 AA3 ASN H 73 LYS H 75 5 3 HELIX 4 AA4 ARG H 83 THR H 87 5 5 HELIX 5 AA5 SER H 156 ALA H 158 5 3 HELIX 6 AA6 SER H 187 LEU H 189 5 3 HELIX 7 AA7 LYS H 201 ASN H 204 5 4 HELIX 8 AA8 GLU L 79 PHE L 83 5 5 HELIX 9 AA9 SER L 121 LYS L 126 1 6 HELIX 10 AB1 LYS L 183 LYS L 188 1 6 HELIX 11 AB2 THR A 28 TYR A 32 5 5 HELIX 12 AB3 ALA A 61 LYS A 64 5 4 HELIX 13 AB4 ASN A 73 LYS A 75 5 3 HELIX 14 AB5 ARG A 83 THR A 87 5 5 HELIX 15 AB6 SER A 156 ALA A 158 5 3 HELIX 16 AB7 SER A 187 LEU A 189 5 3 HELIX 17 AB8 LYS A 201 ASN A 204 5 4 HELIX 18 AB9 GLU B 79 PHE B 83 5 5 HELIX 19 AC1 SER B 121 SER B 127 1 7 HELIX 20 AC2 LYS B 183 LYS B 188 1 6 HELIX 21 AC3 THR C 28 TYR C 32 5 5 HELIX 22 AC4 ASN C 73 LYS C 75 5 3 HELIX 23 AC5 ARG C 83 THR C 87 5 5 HELIX 24 AC6 SER C 127 LYS C 129 5 3 HELIX 25 AC7 SER C 156 ALA C 158 5 3 HELIX 26 AC8 SER C 187 LEU C 189 5 3 HELIX 27 AC9 LYS C 201 ASN C 204 5 4 HELIX 28 AD1 GLU D 79 PHE D 83 5 5 HELIX 29 AD2 SER D 121 SER D 127 1 7 HELIX 30 AD3 LYS D 183 GLU D 187 1 5 HELIX 31 AD4 THR E 28 TYR E 32 5 5 HELIX 32 AD5 ASN E 73 LYS E 75 5 3 HELIX 33 AD6 ARG E 83 THR E 87 5 5 HELIX 34 AD7 SER E 127 LYS E 129 5 3 HELIX 35 AD8 SER E 156 ALA E 158 5 3 HELIX 36 AD9 SER E 187 LEU E 189 5 3 HELIX 37 AE1 LYS E 201 ASN E 204 5 4 HELIX 38 AE2 GLU F 79 PHE F 83 5 5 HELIX 39 AE3 SER F 121 LYS F 126 1 6 HELIX 40 AE4 LYS F 183 GLU F 187 1 5 SHEET 1 AA1 4 GLN H 3 SER H 7 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7 SHEET 3 AA1 4 SER H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AA1 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81 SHEET 1 AA2 6 LEU H 11 VAL H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 ARG H 98 -1 N ALA H 88 O VAL H 109 SHEET 4 AA2 6 MET H 34 GLN H 39 -1 N ILE H 37 O TYR H 91 SHEET 5 AA2 6 LEU H 45 ILE H 51 -1 O ILE H 51 N MET H 34 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O SER H 58 N TYR H 50 SHEET 1 AA3 4 LEU H 11 VAL H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 ARG H 98 -1 N ALA H 88 O VAL H 109 SHEET 4 AA3 4 TRP H 100A TRP H 103 -1 O ARG H 100C N ILE H 96 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 SER H 120 LEU H 124 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O LYS H 143 N SER H 120 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O LEU H 178 N VAL H 142 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 LYS H 210 -1 O THR H 205 N HIS H 200 SHEET 1 AA7 4 LEU L 4 THR L 5 0 SHEET 2 AA7 4 ALA L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AA7 4 GLU L 70 ILE L 75 -1 O LEU L 73 N LEU L 21 SHEET 4 AA7 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AA8 6 THR L 10 LEU L 13 0 SHEET 2 AA8 6 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA8 6 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N TYR L 36 O TYR L 87 SHEET 5 AA8 6 ARG L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 LYS L 53 ARG L 54 -1 O LYS L 53 N TYR L 49 SHEET 1 AA9 4 THR L 10 LEU L 13 0 SHEET 2 AA9 4 THR L 102 ILE L 106 1 O LYS L 103 N LEU L 11 SHEET 3 AA9 4 VAL L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AA9 4 THR L 97 PHE L 98 -1 O THR L 97 N GLN L 90 SHEET 1 AB1 4 SER L 114 PHE L 118 0 SHEET 2 AB1 4 THR L 129 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AB1 4 TYR L 173 SER L 182 -1 O SER L 177 N CYS L 134 SHEET 4 AB1 4 SER L 159 VAL L 163 -1 N SER L 162 O SER L 176 SHEET 1 AB2 4 ALA L 153 LEU L 154 0 SHEET 2 AB2 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB2 4 VAL L 191 GLN L 198 -1 O GLU L 195 N GLN L 147 SHEET 4 AB2 4 THR L 201 ASN L 208 -1 O VAL L 203 N VAL L 196 SHEET 1 AB3 4 GLN A 3 SER A 7 0 SHEET 2 AB3 4 LEU A 18 SER A 25 -1 O SER A 25 N GLN A 3 SHEET 3 AB3 4 SER A 77 MET A 82 -1 O MET A 82 N LEU A 18 SHEET 4 AB3 4 PHE A 67 ASP A 72 -1 N THR A 68 O GLN A 81 SHEET 1 AB4 6 LEU A 11 VAL A 12 0 SHEET 2 AB4 6 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AB4 6 ALA A 88 ARG A 98 -1 N TYR A 90 O THR A 107 SHEET 4 AB4 6 MET A 34 GLN A 39 -1 N ILE A 37 O TYR A 91 SHEET 5 AB4 6 LEU A 45 ILE A 51 -1 O ILE A 51 N MET A 34 SHEET 6 AB4 6 THR A 57 TYR A 59 -1 O SER A 58 N TYR A 50 SHEET 1 AB5 4 LEU A 11 VAL A 12 0 SHEET 2 AB5 4 THR A 107 VAL A 111 1 O THR A 110 N VAL A 12 SHEET 3 AB5 4 ALA A 88 ARG A 98 -1 N TYR A 90 O THR A 107 SHEET 4 AB5 4 TRP A 100A TRP A 103 -1 O GLY A 100D N ILE A 96 SHEET 1 AB6 4 SER A 120 LEU A 124 0 SHEET 2 AB6 4 THR A 135 TYR A 145 -1 O LYS A 143 N SER A 120 SHEET 3 AB6 4 TYR A 176 PRO A 185 -1 O LEU A 178 N VAL A 142 SHEET 4 AB6 4 VAL A 163 THR A 165 -1 N HIS A 164 O VAL A 181 SHEET 1 AB7 4 SER A 120 LEU A 124 0 SHEET 2 AB7 4 THR A 135 TYR A 145 -1 O LYS A 143 N SER A 120 SHEET 3 AB7 4 TYR A 176 PRO A 185 -1 O LEU A 178 N VAL A 142 SHEET 4 AB7 4 VAL A 169 LEU A 170 -1 N VAL A 169 O SER A 177 SHEET 1 AB8 3 THR A 151 TRP A 154 0 SHEET 2 AB8 3 ILE A 195 HIS A 200 -1 O ASN A 197 N SER A 153 SHEET 3 AB8 3 THR A 205 LYS A 210 -1 O VAL A 207 N VAL A 198 SHEET 1 AB9 4 LEU B 4 THR B 5 0 SHEET 2 AB9 4 ALA B 19 ALA B 25 -1 O ARG B 24 N THR B 5 SHEET 3 AB9 4 GLU B 70 ILE B 75 -1 O LEU B 73 N LEU B 21 SHEET 4 AB9 4 PHE B 62 GLY B 66 -1 N SER B 63 O THR B 74 SHEET 1 AC1 6 THR B 10 LEU B 13 0 SHEET 2 AC1 6 THR B 102 ILE B 106 1 O GLU B 105 N LEU B 11 SHEET 3 AC1 6 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AC1 6 LEU B 33 GLN B 38 -1 N TYR B 36 O TYR B 87 SHEET 5 AC1 6 ARG B 45 TYR B 49 -1 O LEU B 47 N TRP B 35 SHEET 6 AC1 6 LYS B 53 ARG B 54 -1 O LYS B 53 N TYR B 49 SHEET 1 AC2 4 THR B 10 LEU B 13 0 SHEET 2 AC2 4 THR B 102 ILE B 106 1 O GLU B 105 N LEU B 11 SHEET 3 AC2 4 VAL B 85 GLN B 90 -1 N TYR B 86 O THR B 102 SHEET 4 AC2 4 THR B 97 PHE B 98 -1 O THR B 97 N GLN B 90 SHEET 1 AC3 4 SER B 114 PHE B 118 0 SHEET 2 AC3 4 THR B 129 PHE B 139 -1 O VAL B 133 N PHE B 118 SHEET 3 AC3 4 TYR B 173 SER B 182 -1 O LEU B 175 N LEU B 136 SHEET 4 AC3 4 SER B 159 VAL B 163 -1 N SER B 162 O SER B 176 SHEET 1 AC4 4 ALA B 153 LEU B 154 0 SHEET 2 AC4 4 LYS B 145 VAL B 150 -1 N VAL B 150 O ALA B 153 SHEET 3 AC4 4 VAL B 191 GLN B 198 -1 O GLU B 195 N GLN B 147 SHEET 4 AC4 4 THR B 201 ASN B 208 -1 O VAL B 203 N VAL B 196 SHEET 1 AC5 4 GLN C 3 SER C 7 0 SHEET 2 AC5 4 LEU C 18 SER C 25 -1 O SER C 25 N GLN C 3 SHEET 3 AC5 4 SER C 77 MET C 82 -1 O MET C 82 N LEU C 18 SHEET 4 AC5 4 PHE C 67 ASP C 72 -1 N THR C 68 O GLN C 81 SHEET 1 AC6 6 LEU C 11 VAL C 12 0 SHEET 2 AC6 6 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12 SHEET 3 AC6 6 ALA C 88 ARG C 98 -1 N ALA C 88 O VAL C 109 SHEET 4 AC6 6 MET C 34 GLN C 39 -1 N ILE C 37 O TYR C 91 SHEET 5 AC6 6 LEU C 45 ILE C 51 -1 O ILE C 51 N MET C 34 SHEET 6 AC6 6 THR C 57 TYR C 59 -1 O SER C 58 N TYR C 50 SHEET 1 AC7 4 LEU C 11 VAL C 12 0 SHEET 2 AC7 4 THR C 107 VAL C 111 1 O THR C 110 N VAL C 12 SHEET 3 AC7 4 ALA C 88 ARG C 98 -1 N ALA C 88 O VAL C 109 SHEET 4 AC7 4 TRP C 100A TRP C 103 -1 O GLY C 100D N ILE C 96 SHEET 1 AC8 4 SER C 120 LEU C 124 0 SHEET 2 AC8 4 THR C 135 TYR C 145 -1 O LYS C 143 N SER C 120 SHEET 3 AC8 4 TYR C 176 PRO C 185 -1 O VAL C 184 N ALA C 136 SHEET 4 AC8 4 VAL C 163 THR C 165 -1 N HIS C 164 O VAL C 181 SHEET 1 AC9 4 THR C 131 SER C 132 0 SHEET 2 AC9 4 THR C 135 TYR C 145 -1 O THR C 135 N SER C 132 SHEET 3 AC9 4 TYR C 176 PRO C 185 -1 O VAL C 184 N ALA C 136 SHEET 4 AC9 4 VAL C 169 LEU C 170 -1 N VAL C 169 O SER C 177 SHEET 1 AD1 3 THR C 151 TRP C 154 0 SHEET 2 AD1 3 ILE C 195 HIS C 200 -1 O ASN C 197 N SER C 153 SHEET 3 AD1 3 THR C 205 LYS C 210 -1 O VAL C 207 N VAL C 198 SHEET 1 AD2 4 LEU D 4 THR D 5 0 SHEET 2 AD2 4 ALA D 19 ALA D 25 -1 O ARG D 24 N THR D 5 SHEET 3 AD2 4 GLU D 70 ILE D 75 -1 O LEU D 73 N LEU D 21 SHEET 4 AD2 4 PHE D 62 SER D 67 -1 N SER D 63 O THR D 74 SHEET 1 AD3 6 THR D 10 LEU D 13 0 SHEET 2 AD3 6 THR D 102 ILE D 106 1 O LYS D 103 N LEU D 11 SHEET 3 AD3 6 VAL D 85 GLN D 90 -1 N TYR D 86 O THR D 102 SHEET 4 AD3 6 LEU D 33 GLN D 38 -1 N ALA D 34 O GLN D 89 SHEET 5 AD3 6 ARG D 45 TYR D 49 -1 O LEU D 47 N TRP D 35 SHEET 6 AD3 6 LYS D 53 ARG D 54 -1 O LYS D 53 N TYR D 49 SHEET 1 AD4 4 THR D 10 LEU D 13 0 SHEET 2 AD4 4 THR D 102 ILE D 106 1 O LYS D 103 N LEU D 11 SHEET 3 AD4 4 VAL D 85 GLN D 90 -1 N TYR D 86 O THR D 102 SHEET 4 AD4 4 THR D 97 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 1 AD5 4 SER D 114 PHE D 118 0 SHEET 2 AD5 4 THR D 129 PHE D 139 -1 O VAL D 133 N PHE D 118 SHEET 3 AD5 4 TYR D 173 SER D 182 -1 O LEU D 181 N ALA D 130 SHEET 4 AD5 4 SER D 159 VAL D 163 -1 N SER D 162 O SER D 176 SHEET 1 AD6 4 ALA D 153 LEU D 154 0 SHEET 2 AD6 4 LYS D 145 VAL D 150 -1 N VAL D 150 O ALA D 153 SHEET 3 AD6 4 VAL D 191 GLN D 198 -1 O GLU D 195 N GLN D 147 SHEET 4 AD6 4 THR D 201 ASN D 208 -1 O VAL D 203 N VAL D 196 SHEET 1 AD7 4 GLN E 3 SER E 7 0 SHEET 2 AD7 4 LEU E 18 SER E 25 -1 O SER E 25 N GLN E 3 SHEET 3 AD7 4 SER E 77 MET E 82 -1 O MET E 82 N LEU E 18 SHEET 4 AD7 4 PHE E 67 ASP E 72 -1 N THR E 68 O GLN E 81 SHEET 1 AD8 6 LEU E 11 VAL E 12 0 SHEET 2 AD8 6 THR E 107 VAL E 111 1 O THR E 110 N VAL E 12 SHEET 3 AD8 6 ALA E 88 ARG E 98 -1 N ALA E 88 O VAL E 109 SHEET 4 AD8 6 MET E 34 GLN E 39 -1 N ILE E 37 O TYR E 91 SHEET 5 AD8 6 LEU E 45 ILE E 51 -1 O GLU E 46 N ARG E 38 SHEET 6 AD8 6 THR E 57 TYR E 59 -1 O SER E 58 N TYR E 50 SHEET 1 AD9 4 LEU E 11 VAL E 12 0 SHEET 2 AD9 4 THR E 107 VAL E 111 1 O THR E 110 N VAL E 12 SHEET 3 AD9 4 ALA E 88 ARG E 98 -1 N ALA E 88 O VAL E 109 SHEET 4 AD9 4 TRP E 100A TRP E 103 -1 O GLY E 100D N ILE E 96 SHEET 1 AE1 4 SER E 120 LEU E 124 0 SHEET 2 AE1 4 THR E 135 TYR E 145 -1 O LYS E 143 N SER E 120 SHEET 3 AE1 4 TYR E 176 PRO E 185 -1 O VAL E 184 N ALA E 136 SHEET 4 AE1 4 VAL E 163 THR E 165 -1 N HIS E 164 O VAL E 181 SHEET 1 AE2 4 THR E 131 SER E 132 0 SHEET 2 AE2 4 THR E 135 TYR E 145 -1 O THR E 135 N SER E 132 SHEET 3 AE2 4 TYR E 176 PRO E 185 -1 O VAL E 184 N ALA E 136 SHEET 4 AE2 4 VAL E 169 LEU E 170 -1 N VAL E 169 O SER E 177 SHEET 1 AE3 3 THR E 151 TRP E 154 0 SHEET 2 AE3 3 ILE E 195 HIS E 200 -1 O ASN E 197 N SER E 153 SHEET 3 AE3 3 THR E 205 LYS E 210 -1 O VAL E 207 N VAL E 198 SHEET 1 AE4 4 LEU F 4 SER F 7 0 SHEET 2 AE4 4 ALA F 19 ALA F 25 -1 O ARG F 24 N THR F 5 SHEET 3 AE4 4 GLU F 70 ILE F 75 -1 O LEU F 73 N LEU F 21 SHEET 4 AE4 4 PHE F 62 SER F 67 -1 N SER F 63 O THR F 74 SHEET 1 AE5 6 THR F 10 LEU F 13 0 SHEET 2 AE5 6 THR F 102 ILE F 106 1 O LYS F 103 N LEU F 11 SHEET 3 AE5 6 VAL F 85 GLN F 90 -1 N TYR F 86 O THR F 102 SHEET 4 AE5 6 LEU F 33 GLN F 38 -1 N TYR F 36 O TYR F 87 SHEET 5 AE5 6 ARG F 45 TYR F 49 -1 O LEU F 47 N TRP F 35 SHEET 6 AE5 6 LYS F 53 ARG F 54 -1 O LYS F 53 N TYR F 49 SHEET 1 AE6 4 THR F 10 LEU F 13 0 SHEET 2 AE6 4 THR F 102 ILE F 106 1 O LYS F 103 N LEU F 11 SHEET 3 AE6 4 VAL F 85 GLN F 90 -1 N TYR F 86 O THR F 102 SHEET 4 AE6 4 THR F 97 PHE F 98 -1 O THR F 97 N GLN F 90 SHEET 1 AE7 4 SER F 114 PHE F 118 0 SHEET 2 AE7 4 THR F 129 PHE F 139 -1 O LEU F 135 N PHE F 116 SHEET 3 AE7 4 TYR F 173 SER F 182 -1 O LEU F 179 N VAL F 132 SHEET 4 AE7 4 SER F 159 VAL F 163 -1 N SER F 162 O SER F 176 SHEET 1 AE8 4 ALA F 153 LEU F 154 0 SHEET 2 AE8 4 LYS F 145 VAL F 150 -1 N VAL F 150 O ALA F 153 SHEET 3 AE8 4 VAL F 191 GLN F 198 -1 O GLU F 195 N GLN F 147 SHEET 4 AE8 4 THR F 201 ASN F 208 -1 O VAL F 203 N VAL F 196 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 3 CYS L 23 CYS L 88 1555 1555 2.05 SSBOND 4 CYS L 134 CYS L 194 1555 1555 2.02 SSBOND 5 CYS A 22 CYS A 92 1555 1555 2.04 SSBOND 6 CYS A 140 CYS A 196 1555 1555 2.04 SSBOND 7 CYS B 23 CYS B 88 1555 1555 2.04 SSBOND 8 CYS B 134 CYS B 194 1555 1555 2.02 SSBOND 9 CYS C 22 CYS C 92 1555 1555 2.04 SSBOND 10 CYS C 140 CYS C 196 1555 1555 2.03 SSBOND 11 CYS D 23 CYS D 88 1555 1555 2.05 SSBOND 12 CYS D 134 CYS D 194 1555 1555 2.03 SSBOND 13 CYS E 22 CYS E 92 1555 1555 2.04 SSBOND 14 CYS E 140 CYS E 196 1555 1555 2.03 SSBOND 15 CYS F 23 CYS F 88 1555 1555 2.04 SSBOND 16 CYS F 134 CYS F 194 1555 1555 2.02 LINK C PCA H 1 N VAL H 2 1555 1555 1.33 LINK C PCA A 1 N VAL A 2 1555 1555 1.33 LINK C PCA C 1 N VAL C 2 1555 1555 1.33 LINK C PCA E 1 N VAL E 2 1555 1555 1.33 LINK C PCA Q 3 N PRO Q 4 1555 1555 1.34 LINK C PCA G 12 N PRO G 13 1555 1555 1.35 LINK C PCA I 196 N PRO I 197 1555 1555 1.35 LINK C PCA J 310 N PRO J 311 1555 1555 1.35 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.43 LINK O6 NAG K 1 C1 FUC K 3 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.43 LINK O6 NAG M 1 C1 FUC M 3 1555 1555 1.44 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.43 LINK O6 NAG N 1 C1 FUC N 3 1555 1555 1.45 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.43 LINK O6 NAG O 1 C1 FUC O 3 1555 1555 1.45 CISPEP 1 PHE H 146 PRO H 147 0 -6.91 CISPEP 2 GLU H 148 PRO H 149 0 -1.49 CISPEP 3 SER L 7 PRO L 8 0 3.10 CISPEP 4 TRP L 94 PRO L 95 0 -1.60 CISPEP 5 TYR L 140 PRO L 141 0 0.31 CISPEP 6 PHE A 146 PRO A 147 0 -6.98 CISPEP 7 GLU A 148 PRO A 149 0 -0.44 CISPEP 8 SER B 7 PRO B 8 0 2.44 CISPEP 9 TRP B 94 PRO B 95 0 -0.76 CISPEP 10 TYR B 140 PRO B 141 0 0.43 CISPEP 11 PHE C 146 PRO C 147 0 -7.22 CISPEP 12 GLU C 148 PRO C 149 0 -1.16 CISPEP 13 SER D 7 PRO D 8 0 2.96 CISPEP 14 TRP D 94 PRO D 95 0 -1.29 CISPEP 15 TYR D 140 PRO D 141 0 0.30 CISPEP 16 PHE E 146 PRO E 147 0 -7.55 CISPEP 17 GLU E 148 PRO E 149 0 -0.75 CISPEP 18 SER F 7 PRO F 8 0 -0.22 CISPEP 19 TRP F 94 PRO F 95 0 -1.25 CISPEP 20 TYR F 140 PRO F 141 0 1.21 CRYST1 74.541 88.320 168.952 90.00 89.75 90.00 P 1 21 1 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 0.013415 0.000000 -0.000060 0.00000 SCALE2 0.000000 0.011322 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005919 0.00000 MTRIX1 1 -0.999266 -0.027805 0.026359 110.91091 1 MTRIX2 1 0.029381 -0.997679 0.061424 -78.33866 1 MTRIX3 1 0.024590 0.062153 0.997764 42.95783 1 MTRIX1 2 0.999466 0.021238 -0.024832 -36.15592 1 MTRIX2 2 0.023069 -0.996846 0.075939 -120.53074 1 MTRIX3 2 -0.023141 -0.076471 -0.996803 40.96933 1 MTRIX1 3 -0.999723 -0.015849 0.017407 74.17121 1 MTRIX2 3 -0.016354 0.999439 -0.029240 43.77847 1 MTRIX3 3 -0.016934 -0.029517 -0.999421 84.44821 1 MTRIX1 4 -0.999496 -0.030905 0.007280 111.43355 1 MTRIX2 4 0.031263 -0.997959 0.055689 -78.02667 1 MTRIX3 4 0.005544 0.055888 0.998422 43.58613 1 MTRIX1 5 0.999765 0.021689 -0.000178 -36.94151 1 MTRIX2 5 0.021638 -0.996778 0.077234 -120.18166 1 MTRIX3 5 0.001498 -0.077220 -0.997013 39.84316 1 MTRIX1 6 -0.999816 -0.018864 0.003599 74.47074 1 MTRIX2 6 -0.018948 0.999511 -0.024859 43.55185 1 MTRIX3 6 -0.003128 -0.024923 -0.999684 83.91201 1 MTRIX1 7 -0.999906 -0.011528 0.007445 112.95427 1 MTRIX2 7 0.011898 -0.998589 0.051763 -77.07951 1 MTRIX3 7 0.006837 0.051847 0.998632 43.05902 1 MTRIX1 8 -0.999772 0.018547 0.010623 76.67671 1 MTRIX2 8 0.018408 0.999746 -0.013001 41.24226 1 MTRIX3 8 -0.010862 -0.012803 -0.999859 85.26221 1 MTRIX1 9 0.995783 -0.053388 -0.074599 -39.74258 1 MTRIX2 9 -0.041531 -0.987459 0.152318 -117.85560 1 MTRIX3 9 -0.081795 -0.148577 -0.985512 40.15995 1