HEADER IMMUNE SYSTEM 13-JAN-25 9HZJ TITLE SDAB1 IN COMPLEX WITH PFCSP A-TSR DOMAIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: CIRCUMSPOROZOITE PROTEIN; COMPND 3 CHAIN: B; COMPND 4 SYNONYM: CS,PFCSP; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: SDAB1; COMPND 8 CHAIN: A; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM NF54; SOURCE 3 ORGANISM_TAXID: 5843; SOURCE 4 GENE: CSP; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 9 ORGANISM_TAXID: 9844; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS MALARIA, CIRCUMSPOROZOITE PROTEIN, CAMELID SINGLE-DOMAIN ANTIBODY, KEYWDS 2 IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR Y.G.-J.STERCKX,R.GEENS REVDAT 1 23-APR-25 9HZJ 0 JRNL AUTH R.GEENS,L.DE VOCHT,M.C.AGUIRRE-BOTERO,C.VINCKE,R.ROMAO, JRNL AUTH 2 S.MAGEZ,S.MUYLDERMANS,R.AMINO,Y.G.-J.STERCKX JRNL TITL EVIDENCE FOR A MODEL OF CONFORMATIONAL CHANGE BY THE JRNL TITL 2 PLASMODIUM FALCIPARUM CIRCUMSPOROZOITE PROTEIN DURING JRNL TITL 3 SPOROZOITE DEVELOPMENT IN THE MOSQUITO HOST THROUGH THE USE JRNL TITL 4 OF CAMELID SINGLE-DOMAIN ANTIBODIES JRNL REF TO BE PUBLISHED 2025 JRNL REFN JRNL DOI 10.1128/IAI.00081-25 REMARK 2 REMARK 2 RESOLUTION. 2.06 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21.2_5419: ???) 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.06 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.82 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 3 NUMBER OF REFLECTIONS : 11689 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.197 REMARK 3 R VALUE (WORKING SET) : 0.195 REMARK 3 FREE R VALUE : 0.242 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 586 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 34.8200 - 3.2800 1.00 2948 156 0.1626 0.1991 REMARK 3 2 3.2800 - 2.6000 0.96 2699 142 0.1858 0.2379 REMARK 3 3 2.6000 - 2.2700 0.99 2771 146 0.2318 0.3101 REMARK 3 4 2.2700 - 2.0600 0.98 2685 142 0.3948 0.4373 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) : 0.380 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.010 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 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 : 0.006 1521 REMARK 3 ANGLE : 0.813 2037 REMARK 3 CHIRALITY : 0.049 213 REMARK 3 PLANARITY : 0.008 262 REMARK 3 DIHEDRAL : 16.197 566 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 : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9HZJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1292144609. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 07-JUL-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ESRF REMARK 200 BEAMLINE : ID30B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.967697 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21593 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.060 REMARK 200 RESOLUTION RANGE LOW (A) : 34.820 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3 REMARK 200 DATA REDUNDANCY : 3.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.9200 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.06 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27 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 : 0.800 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 (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 8000, 100 MM IMIDAZOLE PH 8.0, REMARK 280 200 MM NACL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K 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 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-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 18.59500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.89000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.58500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.89000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.59500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.58500 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 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2230 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 9820 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A 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 MET B 309 REMARK 465 GLU B 310 REMARK 465 SER B 376 REMARK 465 VAL B 377 REMARK 465 PHE B 378 REMARK 465 ASN B 379 REMARK 465 VAL B 380 REMARK 465 VAL B 381 REMARK 465 ASN B 382 REMARK 465 SER B 383 REMARK 465 SER B 384 REMARK 465 GLU B 385 REMARK 465 ASN B 386 REMARK 465 LEU B 387 REMARK 465 TYR B 388 REMARK 465 PHE B 389 REMARK 465 GLN B 390 REMARK 465 SER B 391 REMARK 465 GLY B 392 REMARK 465 GLY B 393 REMARK 465 HIS B 394 REMARK 465 HIS B 395 REMARK 465 HIS B 396 REMARK 465 HIS B 397 REMARK 465 HIS B 398 REMARK 465 HIS B 399 REMARK 465 ALA A 126 REMARK 465 ALA A 127 REMARK 465 ALA A 128 REMARK 465 TYR A 129 REMARK 465 PRO A 130 REMARK 465 TYR A 131 REMARK 465 ASP A 132 REMARK 465 VAL A 133 REMARK 465 PRO A 134 REMARK 465 ASP A 135 REMARK 465 TYR A 136 REMARK 465 GLY A 137 REMARK 465 SER A 138 REMARK 465 HIS A 139 REMARK 465 HIS A 140 REMARK 465 HIS A 141 REMARK 465 HIS A 142 REMARK 465 HIS A 143 REMARK 465 HIS A 144 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 LYS B 373 CG CD CE NZ 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 ASN B 352 -0.96 78.05 REMARK 500 ARG A 67 -35.25 -133.97 REMARK 500 SER A 106 114.34 -163.36 REMARK 500 REMARK 500 REMARK: NULL DBREF 9HZJ B 310 384 UNP P19597 CSP_PLAFO 310 384 DBREF 9HZJ A 1 144 PDB 9HZJ 9HZJ 1 144 SEQADV 9HZJ MET B 309 UNP P19597 INITIATING METHIONINE SEQADV 9HZJ GLU B 385 UNP P19597 EXPRESSION TAG SEQADV 9HZJ ASN B 386 UNP P19597 EXPRESSION TAG SEQADV 9HZJ LEU B 387 UNP P19597 EXPRESSION TAG SEQADV 9HZJ TYR B 388 UNP P19597 EXPRESSION TAG SEQADV 9HZJ PHE B 389 UNP P19597 EXPRESSION TAG SEQADV 9HZJ GLN B 390 UNP P19597 EXPRESSION TAG SEQADV 9HZJ SER B 391 UNP P19597 EXPRESSION TAG SEQADV 9HZJ GLY B 392 UNP P19597 EXPRESSION TAG SEQADV 9HZJ GLY B 393 UNP P19597 EXPRESSION TAG SEQADV 9HZJ HIS B 394 UNP P19597 EXPRESSION TAG SEQADV 9HZJ HIS B 395 UNP P19597 EXPRESSION TAG SEQADV 9HZJ HIS B 396 UNP P19597 EXPRESSION TAG SEQADV 9HZJ HIS B 397 UNP P19597 EXPRESSION TAG SEQADV 9HZJ HIS B 398 UNP P19597 EXPRESSION TAG SEQADV 9HZJ HIS B 399 UNP P19597 EXPRESSION TAG SEQRES 1 B 91 MET GLU PRO SER ASP LYS HIS ILE LYS GLU TYR LEU ASN SEQRES 2 B 91 LYS ILE GLN ASN SER LEU SER THR GLU TRP SER PRO CYS SEQRES 3 B 91 SER VAL THR CYS GLY ASN GLY ILE GLN VAL ARG ILE LYS SEQRES 4 B 91 PRO GLY SER ALA ASN LYS PRO LYS ASP GLU LEU ASP TYR SEQRES 5 B 91 ALA ASN ASP ILE GLU LYS LYS ILE CYS LYS MET GLU LYS SEQRES 6 B 91 CYS SER SER VAL PHE ASN VAL VAL ASN SER SER GLU ASN SEQRES 7 B 91 LEU TYR PHE GLN SER GLY GLY HIS HIS HIS HIS HIS HIS SEQRES 1 A 144 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 144 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 A 144 ARG THR PHE SER SER TYR SER MET GLY TRP PHE ARG LEU SEQRES 4 A 144 VAL PRO GLY LYS GLU ARG GLU PHE VAL ALA ARG ILE SER SEQRES 5 A 144 SER SER GLY GLY ASN THR TYR TYR ALA ASP SER VAL ARG SEQRES 6 A 144 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 A 144 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 A 144 ALA VAL TYR TYR CYS ALA ALA ASP LEU LEU GLN PHE GLY SEQRES 9 A 144 ARG SER SER ARG ALA ALA ASP TYR ASP TYR TRP GLY GLN SEQRES 10 A 144 GLY THR GLN VAL THR VAL SER SER ALA ALA ALA TYR PRO SEQRES 11 A 144 TYR ASP VAL PRO ASP TYR GLY SER HIS HIS HIS HIS HIS SEQRES 12 A 144 HIS HET GOL B 401 6 HET GOL B 402 6 HET GOL B 403 6 HET PEG B 404 7 HET GOL A 201 6 HET GOL A 202 6 HETNAM GOL GLYCEROL HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 3 GOL 5(C3 H8 O3) FORMUL 6 PEG C4 H10 O3 FORMUL 9 HOH *122(H2 O) HELIX 1 AA1 SER B 312 ILE B 323 1 12 HELIX 2 AA2 GLN B 324 LEU B 327 5 4 HELIX 3 AA3 PRO B 348 ALA B 351 5 4 HELIX 4 AA4 PRO B 354 LEU B 358 5 5 HELIX 5 AA5 THR A 28 TYR A 32 5 5 HELIX 6 AA6 ASN A 74 LYS A 76 5 3 HELIX 7 AA7 LYS A 87 THR A 91 5 5 HELIX 8 AA8 ARG A 108 TYR A 112 5 5 SHEET 1 AA1 2 ASN B 340 ILE B 346 0 SHEET 2 AA1 2 ILE B 364 LYS B 370 -1 O CYS B 369 N GLY B 341 SHEET 1 AA2 4 LEU A 4 SER A 7 0 SHEET 2 AA2 4 LEU A 18 ALA A 24 -1 O SER A 21 N SER A 7 SHEET 3 AA2 4 THR A 78 MET A 83 -1 O MET A 83 N LEU A 18 SHEET 4 AA2 4 PHE A 68 ASP A 73 -1 N SER A 71 O TYR A 80 SHEET 1 AA3 6 GLY A 10 GLN A 13 0 SHEET 2 AA3 6 THR A 119 SER A 124 1 O THR A 122 N GLY A 10 SHEET 3 AA3 6 ALA A 92 ASP A 99 -1 N TYR A 94 O THR A 119 SHEET 4 AA3 6 SER A 33 LEU A 39 -1 N SER A 33 O ASP A 99 SHEET 5 AA3 6 GLU A 46 ILE A 51 -1 O GLU A 46 N ARG A 38 SHEET 6 AA3 6 THR A 58 TYR A 60 -1 O TYR A 59 N ARG A 50 SHEET 1 AA4 4 GLY A 10 GLN A 13 0 SHEET 2 AA4 4 THR A 119 SER A 124 1 O THR A 122 N GLY A 10 SHEET 3 AA4 4 ALA A 92 ASP A 99 -1 N TYR A 94 O THR A 119 SHEET 4 AA4 4 TYR A 114 TRP A 115 -1 O TYR A 114 N ALA A 98 SSBOND 1 CYS B 334 CYS B 369 1555 1555 2.05 SSBOND 2 CYS B 338 CYS B 374 1555 1555 2.04 SSBOND 3 CYS A 22 CYS A 96 1555 1555 2.04 CRYST1 37.190 55.170 89.780 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 0.026889 0.000000 0.000000 0.00000 SCALE2 0.000000 0.018126 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011138 0.00000