HEADER IMMUNE SYSTEM 05-MAR-25 9M5D TITLE CRYSTAL STRUCTURE OF S. AUREUS PROTEIN A BOUND TO A HUMAN SINGLE- TITLE 2 DOMAIN ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: N501; COMPND 3 CHAIN: D, A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: IMMUNOGLOBULIN G-BINDING PROTEIN A; COMPND 7 CHAIN: H, B; COMPND 8 SYNONYM: IGG-BINDING PROTEIN A,STAPHYLOCOCCAL PROTEIN A,SPA; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS (STRAIN NCTC 8325 / PS SOURCE 8 47); SOURCE 9 ORGANISM_TAXID: 93061; SOURCE 10 GENE: SPA, SAOUHSC_00069; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS COMPLEX, ANTIBODY, S. AUREUS, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR Y.KONG,J.L.SHI,T.L.YING,Z.L.YANG,Q.Y.XU REVDAT 1 12-NOV-25 9M5D 0 JRNL AUTH Y.KONG,J.SHI,F.WU,T.ZHAO,R.WANG,X.ZHU,Q.XU,Y.SONG,Q.LI, JRNL AUTH 2 Y.WANG,X.GAO,Y.YANG,Y.FENG,Z.WANG,W.GE,Y.WU,Z.YANG,J.YAO, JRNL AUTH 3 T.YING JRNL TITL A SYNERGISTIC GENERATIVE-RANKING FRAMEWORK FOR TAILORED JRNL TITL 2 DESIGN OF THERAPEUTIC SINGLE-DOMAIN ANTIBODIES. JRNL REF CELL DISCOV V. 11 85 2025 JRNL REFN ESSN 2056-5968 JRNL PMID 41162386 JRNL DOI 10.1038/S41421-025-00843-8 REMARK 2 REMARK 2 RESOLUTION. 3.57 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.18.2_3874 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) : 3.57 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.02 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 7511 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.235 REMARK 3 R VALUE (WORKING SET) : 0.233 REMARK 3 FREE R VALUE : 0.271 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 376 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 55.0200 - 5.1500 1.00 2459 140 0.2133 0.2329 REMARK 3 2 5.1500 - 4.0900 1.00 2368 111 0.2162 0.2544 REMARK 3 3 4.0900 - 3.5700 1.00 2308 125 0.2986 0.3771 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 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) : 0.553 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.352 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 81.91 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.08 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 2766 REMARK 3 ANGLE : 0.773 3732 REMARK 3 CHIRALITY : 0.048 388 REMARK 3 PLANARITY : 0.006 498 REMARK 3 DIHEDRAL : 10.871 382 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'D' AND RESID 1 THROUGH 120) REMARK 3 ORIGIN FOR THE GROUP (A): 25.2366 -43.4463 23.6107 REMARK 3 T TENSOR REMARK 3 T11: 0.6097 T22: 0.6443 REMARK 3 T33: 0.6667 T12: -0.0723 REMARK 3 T13: -0.0389 T23: 0.0407 REMARK 3 L TENSOR REMARK 3 L11: 0.9841 L22: 1.0068 REMARK 3 L33: 1.1720 L12: 0.2081 REMARK 3 L13: -0.1497 L23: 0.5716 REMARK 3 S TENSOR REMARK 3 S11: 0.0616 S12: -0.0400 S13: -0.0073 REMARK 3 S21: 0.0297 S22: -0.0772 S23: 0.0698 REMARK 3 S31: -0.1580 S32: -0.0720 S33: 0.0464 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 1 THROUGH 120) REMARK 3 ORIGIN FOR THE GROUP (A): 0.4269 -43.2725 18.8285 REMARK 3 T TENSOR REMARK 3 T11: 0.5845 T22: 0.7658 REMARK 3 T33: 0.7339 T12: -0.0326 REMARK 3 T13: -0.0636 T23: -0.0331 REMARK 3 L TENSOR REMARK 3 L11: 1.3009 L22: 1.1488 REMARK 3 L33: 1.1821 L12: 0.1421 REMARK 3 L13: -0.0630 L23: 0.2495 REMARK 3 S TENSOR REMARK 3 S11: 0.0680 S12: 0.2387 S13: 0.1137 REMARK 3 S21: -0.1333 S22: -0.1088 S23: -0.0982 REMARK 3 S31: 0.0522 S32: -0.2915 S33: 0.0547 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'H' AND RESID 2803 THROUGH 2856) REMARK 3 ORIGIN FOR THE GROUP (A): 37.9833 -27.1031 15.7513 REMARK 3 T TENSOR REMARK 3 T11: 0.7716 T22: 0.6116 REMARK 3 T33: 0.7589 T12: 0.0011 REMARK 3 T13: 0.0584 T23: -0.0804 REMARK 3 L TENSOR REMARK 3 L11: 3.8569 L22: 3.9415 REMARK 3 L33: 1.8639 L12: 0.0237 REMARK 3 L13: -0.5901 L23: 0.5878 REMARK 3 S TENSOR REMARK 3 S11: 0.0319 S12: 0.0361 S13: 0.2064 REMARK 3 S21: -0.5113 S22: 0.1982 S23: -0.2131 REMARK 3 S31: -0.1798 S32: 0.2361 S33: -0.1391 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 2803 THROUGH 2856) REMARK 3 ORIGIN FOR THE GROUP (A): 41.4525 -17.4507 31.4382 REMARK 3 T TENSOR REMARK 3 T11: 0.7298 T22: 0.6105 REMARK 3 T33: 0.7223 T12: -0.0471 REMARK 3 T13: -0.0225 T23: -0.0714 REMARK 3 L TENSOR REMARK 3 L11: 0.5646 L22: 2.5597 REMARK 3 L33: 1.7570 L12: 0.2632 REMARK 3 L13: 0.9438 L23: -0.2082 REMARK 3 S TENSOR REMARK 3 S11: 0.3004 S12: -0.2052 S13: 0.1230 REMARK 3 S21: 0.2368 S22: -0.2431 S23: -0.0853 REMARK 3 S31: 0.3087 S32: -0.1096 S33: -0.0638 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : 2 REMARK 3 NCS GROUP : ens_1 REMARK 3 NCS OPERATOR : 1 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "A" 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" 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" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 NCS OPERATOR : 2 REMARK 3 REFERENCE SELECTION: NULL REMARK 3 SELECTION : chain "H" REMARK 3 ATOM PAIRS NUMBER : NULL REMARK 3 RMSD : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9M5D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 07-MAR-25. REMARK 100 THE DEPOSITION ID IS D_1300057196. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-OCT-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL10U2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97903 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS REMARK 200 DATA SCALING SOFTWARE : DIALS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7538 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.570 REMARK 200 RESOLUTION RANGE LOW (A) : 123.200 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 23.70 REMARK 200 R MERGE (I) : 0.67100 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.4000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.57 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.66 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 3.01800 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: PHENIX 1.18.2_3874 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 67.29 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.76 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 25% W/V POLYETHYLENE GLYCOL 3350, 0.2M REMARK 280 MAGNESIUM CHLORIDE AND 0.1M BIS-TRIS 5.5, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -Y,X,Z REMARK 290 4555 Y,-X,Z REMARK 290 5555 -X,Y,-Z REMARK 290 6555 X,-Y,-Z REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z REMARK 290 9555 X+1/2,Y+1/2,Z+1/2 REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2 REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2 REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2 REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2 REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2 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 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 86.98650 REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 86.98650 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 39.80550 REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 86.98650 REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 86.98650 REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 39.80550 REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 86.98650 REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 86.98650 REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 39.80550 REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 86.98650 REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 86.98650 REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 39.80550 REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 86.98650 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 86.98650 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 39.80550 REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 86.98650 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 86.98650 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 39.80550 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 86.98650 REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 86.98650 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 39.80550 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 86.98650 REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 86.98650 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 39.80550 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, A, H, B 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 H 2796 REMARK 465 ASP H 2797 REMARK 465 ALA H 2798 REMARK 465 GLN H 2799 REMARK 465 GLN H 2800 REMARK 465 ASN H 2801 REMARK 465 ASN H 2802 REMARK 465 ALA B 2796 REMARK 465 ASP B 2797 REMARK 465 ALA B 2798 REMARK 465 GLN B 2799 REMARK 465 GLN B 2800 REMARK 465 ASN B 2801 REMARK 465 ASN B 2802 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 PHE D 29 -21.11 73.67 REMARK 500 REMARK 500 REMARK: NULL DBREF 9M5D D 1 120 PDB 9M5D 9M5D 1 120 DBREF 9M5D A 1 120 PDB 9M5D 9M5D 1 120 DBREF 9M5D H 2796 2856 UNP P02976 SPA_STAA8 93 153 DBREF 9M5D B 2796 2856 UNP P02976 SPA_STAA8 93 153 SEQRES 1 D 120 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 120 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER ASP SEQRES 3 D 120 PHE THR PHE ARG ASN TYR GLU MET SER TRP VAL ARG GLN SEQRES 4 D 120 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE SER SEQRES 5 D 120 GLY SER GLY GLY SER THR TYR TYR ALA HIS SER LEU LYS SEQRES 6 D 120 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 D 120 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 D 120 ALA ILE TYR TYR CYS ALA ARG LEU ARG ASP GLY PHE ASN SEQRES 9 D 120 ASN GLY PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 D 120 VAL SER SER SEQRES 1 A 120 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 A 120 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER ASP SEQRES 3 A 120 PHE THR PHE ARG ASN TYR GLU MET SER TRP VAL ARG GLN SEQRES 4 A 120 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE SER SEQRES 5 A 120 GLY SER GLY GLY SER THR TYR TYR ALA HIS SER LEU LYS SEQRES 6 A 120 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 A 120 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR SEQRES 8 A 120 ALA ILE TYR TYR CYS ALA ARG LEU ARG ASP GLY PHE ASN SEQRES 9 A 120 ASN GLY PHE ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 A 120 VAL SER SER SEQRES 1 H 61 ALA ASP ALA GLN GLN ASN ASN PHE ASN LYS ASP GLN GLN SEQRES 2 H 61 SER ALA PHE TYR GLU ILE LEU ASN MET PRO ASN LEU ASN SEQRES 3 H 61 GLU ALA GLN ARG ASN GLY PHE ILE GLN SER LEU LYS ASP SEQRES 4 H 61 ASP PRO SER GLN SER THR ASN VAL LEU GLY GLU ALA LYS SEQRES 5 H 61 LYS LEU ASN GLU SER GLN ALA PRO LYS SEQRES 1 B 61 ALA ASP ALA GLN GLN ASN ASN PHE ASN LYS ASP GLN GLN SEQRES 2 B 61 SER ALA PHE TYR GLU ILE LEU ASN MET PRO ASN LEU ASN SEQRES 3 B 61 GLU ALA GLN ARG ASN GLY PHE ILE GLN SER LEU LYS ASP SEQRES 4 B 61 ASP PRO SER GLN SER THR ASN VAL LEU GLY GLU ALA LYS SEQRES 5 B 61 LYS LEU ASN GLU SER GLN ALA PRO LYS HELIX 1 AA1 ARG D 87 THR D 91 5 5 HELIX 2 AA2 ASP D 101 ASN D 105 5 5 HELIX 3 AA3 ARG A 87 THR A 91 5 5 HELIX 4 AA4 ASN H 2804 ASN H 2816 1 13 HELIX 5 AA5 ASN H 2821 ASP H 2835 1 15 HELIX 6 AA6 GLN H 2838 GLN H 2853 1 16 HELIX 7 AA7 ASN B 2804 ASN B 2816 1 13 HELIX 8 AA8 ASN B 2821 ASP B 2835 1 15 HELIX 9 AA9 GLN B 2838 GLN B 2853 1 16 SHEET 1 AA1 4 GLN D 3 SER D 7 0 SHEET 2 AA1 4 LEU D 18 SER D 25 -1 O ALA D 23 N VAL D 5 SHEET 3 AA1 4 THR D 78 MET D 83 -1 O LEU D 81 N LEU D 20 SHEET 4 AA1 4 PHE D 68 ASP D 73 -1 N THR D 69 O GLN D 82 SHEET 1 AA2 6 LEU D 11 VAL D 12 0 SHEET 2 AA2 6 THR D 114 VAL D 118 1 O THR D 117 N VAL D 12 SHEET 3 AA2 6 ALA D 92 LEU D 99 -1 N TYR D 94 O THR D 114 SHEET 4 AA2 6 GLU D 33 GLN D 39 -1 N VAL D 37 O TYR D 95 SHEET 5 AA2 6 LEU D 45 ILE D 51 -1 O SER D 49 N TRP D 36 SHEET 6 AA2 6 THR D 58 TYR D 60 -1 O TYR D 59 N SER D 50 SHEET 1 AA3 4 LEU D 11 VAL D 12 0 SHEET 2 AA3 4 THR D 114 VAL D 118 1 O THR D 117 N VAL D 12 SHEET 3 AA3 4 ALA D 92 LEU D 99 -1 N TYR D 94 O THR D 114 SHEET 4 AA3 4 PHE D 107 TYR D 109 -1 O TYR D 109 N ARG D 98 SHEET 1 AA4 4 GLN A 3 SER A 7 0 SHEET 2 AA4 4 LEU A 18 SER A 25 -1 O SER A 21 N SER A 7 SHEET 3 AA4 4 THR A 78 MET A 83 -1 O LEU A 81 N LEU A 20 SHEET 4 AA4 4 PHE A 68 ASP A 73 -1 N ASP A 73 O THR A 78 SHEET 1 AA5 6 LEU A 11 VAL A 12 0 SHEET 2 AA5 6 THR A 114 VAL A 118 1 O THR A 117 N VAL A 12 SHEET 3 AA5 6 ALA A 92 LEU A 99 -1 N TYR A 94 O THR A 114 SHEET 4 AA5 6 GLU A 33 GLN A 39 -1 N VAL A 37 O TYR A 95 SHEET 5 AA5 6 LEU A 45 ILE A 51 -1 O ILE A 51 N MET A 34 SHEET 6 AA5 6 THR A 58 TYR A 60 -1 O TYR A 59 N SER A 50 SHEET 1 AA6 4 LEU A 11 VAL A 12 0 SHEET 2 AA6 4 THR A 114 VAL A 118 1 O THR A 117 N VAL A 12 SHEET 3 AA6 4 ALA A 92 LEU A 99 -1 N TYR A 94 O THR A 114 SHEET 4 AA6 4 PHE A 107 TRP A 110 -1 O TYR A 109 N ARG A 98 SSBOND 1 CYS D 22 CYS D 96 1555 1555 2.04 SSBOND 2 CYS A 22 CYS A 96 1555 1555 2.04 CRYST1 173.973 173.973 79.611 90.00 90.00 90.00 I 4 2 2 32 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 0.005748 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005748 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012561 0.00000 MTRIX1 1 -0.458966 -0.760670 0.459056 -16.12856 1 MTRIX2 1 -0.854975 0.518649 0.004610 -20.72601 1 MTRIX3 1 -0.241596 -0.390366 -0.888395 23.54726 1 MTRIX1 2 0.754170 -0.486020 0.441602 -15.64257 1 MTRIX2 2 -0.535879 -0.844180 -0.013914 -19.17723 1 MTRIX3 2 0.379554 -0.226152 -0.897103 24.27818 1