HEADER IMMUNE SYSTEM/CHAPERONE 04-MAR-24 9AVO TITLE THE CRYSTAL STRUCTURE OF AN ENGINEERED PROTEIN GD WITH HUMAN KAPPA FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: FAB HEAVY CHAIN; COMPND 3 CHAIN: B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: FAB LIGHT CHAIN; COMPND 7 CHAIN: D; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HISTONE CHAPERONE ASF1; COMPND 11 CHAIN: A; COMPND 12 SYNONYM: ANTI-SILENCING FUNCTION PROTEIN 1,YASF1; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 4; COMPND 15 MOLECULE: PROTEIN GD; COMPND 16 CHAIN: C; COMPND 17 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: ASF1, CIA1, YJL115W, J0755; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 18 MOL_ID: 4; SOURCE 19 ORGANISM_SCIENTIFIC: STREPTOCOCCUS SP. 'GROUP G'; SOURCE 20 ORGANISM_TAXID: 1320; SOURCE 21 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 22 EXPRESSION_SYSTEM_TAXID: 469008 KEYWDS FAB, ANTIBODY, PROTEIN G, IMMUNOGLOBULIN BINDING PROTEIN, ASF1, KEYWDS 2 IMMUNE SYSTEM-CHAPERONE COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR T.SLEZAK,A.A.KOSSIAKOFF REVDAT 1 05-FEB-25 9AVO 0 JRNL AUTH T.SLEZAK,K.M.O'LEARY,J.LI,A.ROHAIM,E.K.DAVYDOVA, JRNL AUTH 2 A.A.KOSSIAKOFF JRNL TITL ENGINEERED PROTEIN G VARIANTS FOR MULTIFUNCTIONAL JRNL TITL 2 ANTIBODY-BASED ASSEMBLIES. JRNL REF PROTEIN SCI. V. 34 70019 2025 JRNL REFN ESSN 1469-896X JRNL PMID 39865354 JRNL DOI 10.1002/PRO.70019 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.20.1_4487: ???) 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) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.73 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 31735 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.216 REMARK 3 R VALUE (WORKING SET) : 0.215 REMARK 3 FREE R VALUE : 0.241 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1619 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 86.7300 - 6.8700 0.99 2663 176 0.2019 0.2151 REMARK 3 2 6.8700 - 5.4500 0.99 2556 132 0.1984 0.2465 REMARK 3 3 5.4500 - 4.7600 1.00 2540 138 0.1544 0.1811 REMARK 3 4 4.7600 - 4.3300 0.99 2513 113 0.1436 0.1793 REMARK 3 5 4.3300 - 4.0200 1.00 2516 138 0.1840 0.1691 REMARK 3 6 4.0200 - 3.7800 1.00 2495 151 0.2292 0.3009 REMARK 3 7 3.7800 - 3.5900 1.00 2505 121 0.2399 0.2375 REMARK 3 8 3.5900 - 3.4300 1.00 2479 133 0.2554 0.2898 REMARK 3 9 3.4300 - 3.3000 0.99 2467 123 0.2937 0.3314 REMARK 3 10 3.3000 - 3.1900 0.99 2465 143 0.3439 0.3663 REMARK 3 11 3.1900 - 3.0900 1.00 2452 138 0.3517 0.4128 REMARK 3 12 3.0900 - 3.0000 0.99 2465 113 0.3892 0.4363 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) : 0.430 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.650 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 80.87 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 : 0.010 730 REMARK 3 ANGLE : 1.280 690 REMARK 3 CHIRALITY : 0.067 791 REMARK 3 PLANARITY : 0.012 873 REMARK 3 DIHEDRAL : 6.469 691 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A): 23.2028 -8.1480 25.4010 REMARK 3 T TENSOR REMARK 3 T11: 0.8735 T22: 0.5093 REMARK 3 T33: 0.8233 T12: -0.0042 REMARK 3 T13: -0.1767 T23: -0.0022 REMARK 3 L TENSOR REMARK 3 L11: 1.5043 L22: 0.7522 REMARK 3 L33: 3.0029 L12: -0.0279 REMARK 3 L13: -0.3516 L23: 0.0459 REMARK 3 S TENSOR REMARK 3 S11: -0.0306 S12: -0.0721 S13: 0.0090 REMARK 3 S21: 0.4250 S22: 0.1165 S23: -0.1194 REMARK 3 S31: 0.2593 S32: 0.7983 S33: -0.0826 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 9AVO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-24. REMARK 100 THE DEPOSITION ID IS D_1000281871. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-DEC-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-E REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31838 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000 REMARK 200 RESOLUTION RANGE LOW (A) : 86.730 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 12.50 REMARK 200 R MERGE (I) : 0.16700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.16 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 13.00 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 77.44 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.45 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CACODYLATE PH 6.8 AND 0.8M REMARK 280 SODIUM CITRATE TRIBASIC, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 3555 -Y,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X,Z+3/4 REMARK 290 5555 -X+1/2,Y,-Z+3/4 REMARK 290 6555 X,-Y+1/2,-Z+1/4 REMARK 290 7555 Y+1/2,X+1/2,-Z+1/2 REMARK 290 8555 -Y,-X,-Z REMARK 290 9555 X+1/2,Y+1/2,Z+1/2 REMARK 290 10555 -X,-Y,Z REMARK 290 11555 -Y+1/2,X,Z+3/4 REMARK 290 12555 Y,-X+1/2,Z+1/4 REMARK 290 13555 -X,Y+1/2,-Z+1/4 REMARK 290 14555 X+1/2,-Y,-Z+3/4 REMARK 290 15555 Y,X,-Z 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 67.48550 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 67.48550 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 169.78400 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 67.48550 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 84.89200 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 67.48550 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 254.67600 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 67.48550 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 254.67600 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 67.48550 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 84.89200 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 67.48550 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 67.48550 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 169.78400 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 67.48550 REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 67.48550 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 169.78400 REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 67.48550 REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 254.67600 REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 67.48550 REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 84.89200 REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 67.48550 REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 84.89200 REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 67.48550 REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 254.67600 REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 67.48550 REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 67.48550 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 169.78400 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7790 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 27330 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, A, C 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 GLU B -1 REMARK 465 ILE B 0 REMARK 465 SER B 1 REMARK 465 PRO B 207 REMARK 465 SER B 220 REMARK 465 CYS B 221 REMARK 465 ASP B 222 REMARK 465 LYS B 223 REMARK 465 THR B 224 REMARK 465 HIS B 225 REMARK 465 THR B 226 REMARK 465 SER D 0 REMARK 465 ASP D 1 REMARK 465 GLU D 213 REMARK 465 CYS D 214 REMARK 465 GLU A 35 REMARK 465 ASN A 158 REMARK 465 GLU A 159 REMARK 465 ASN A 160 REMARK 465 GLU A 161 REMARK 465 GLY A 162 REMARK 465 LEU A 163 REMARK 465 GLU A 164 REMARK 465 THR C 2 REMARK 465 PRO C 3 REMARK 465 ALA C 4 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 219 CG CD CE NZ REMARK 470 ARG D 18 CG CD NE CZ NH1 NH2 REMARK 470 ARG D 211 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 13 CG CD CE NZ REMARK 470 LEU A 34 CG CD1 CD2 REMARK 470 ARG A 52 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 74 CG CD CE NZ REMARK 470 ARG C 15 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 64 CG CD OE1 OE2 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 29 130.34 67.63 REMARK 500 TYR B 55 -42.01 64.80 REMARK 500 SER B 58 120.80 66.24 REMARK 500 SER B 86 53.18 28.88 REMARK 500 ALA B 104 -165.29 -121.85 REMARK 500 PHE B 151 136.13 -172.38 REMARK 500 ASN B 209 67.26 31.62 REMARK 500 GLN D 3 111.04 63.45 REMARK 500 LEU D 47 -62.51 -107.77 REMARK 500 ALA D 51 -43.25 59.89 REMARK 500 SER D 67 88.47 -158.14 REMARK 500 ALA D 84 -168.42 -175.33 REMARK 500 ASP D 91 90.23 -68.41 REMARK 500 SER D 121 134.25 79.61 REMARK 500 ASN D 138 72.51 52.68 REMARK 500 ARG D 211 115.11 149.28 REMARK 500 SER A 3 54.08 -93.81 REMARK 500 SER A 5 103.81 59.83 REMARK 500 ASP A 40 142.70 64.25 REMARK 500 SER A 51 -168.92 -104.13 REMARK 500 VAL A 93 51.28 -114.09 REMARK 500 SER C 42 16.39 -66.98 REMARK 500 SER C 43 100.43 -58.25 REMARK 500 GLU C 47 -83.41 -64.93 REMARK 500 TRP C 48 119.18 98.64 REMARK 500 GLU C 61 -86.94 -75.77 REMARK 500 LYS C 62 128.78 62.58 REMARK 500 GLU C 64 7.58 51.33 REMARK 500 REMARK 500 REMARK: NULL DBREF 9AVO B -1 226 PDB 9AVO 9AVO -1 226 DBREF 9AVO D 0 214 PDB 9AVO 9AVO 0 214 DBREF 9AVO A 5 162 UNP P32447 ASF1_YEAST 2 159 DBREF 9AVO C 2 66 PDB 9AVO 9AVO 2 66 SEQADV 9AVO GLN A 1 UNP P32447 EXPRESSION TAG SEQADV 9AVO GLY A 2 UNP P32447 EXPRESSION TAG SEQADV 9AVO SER A 3 UNP P32447 EXPRESSION TAG SEQADV 9AVO SER A 4 UNP P32447 EXPRESSION TAG SEQADV 9AVO LEU A 163 UNP P32447 EXPRESSION TAG SEQADV 9AVO GLU A 164 UNP P32447 EXPRESSION TAG SEQRES 1 B 228 GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY SEQRES 2 B 228 LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA SEQRES 3 B 228 ALA SER GLY PHE ASN VAL SER TYR TYR SER ILE HIS TRP SEQRES 4 B 228 VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA SEQRES 5 B 228 SER ILE TYR PRO TYR TYR GLY SER THR SER TYR ALA ASP SEQRES 6 B 228 SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER SEQRES 7 B 228 LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA SEQRES 8 B 228 GLU ASP THR ALA VAL TYR TYR CYS ALA ARG GLY TYR GLY SEQRES 9 B 228 TRP ALA LEU ASP TYR TRP GLY GLN GLY THR LEU VAL THR SEQRES 10 B 228 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 B 228 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 B 228 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 B 228 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 B 228 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 B 228 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 B 228 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 B 228 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 18 B 228 SER CYS ASP LYS THR HIS THR SEQRES 1 D 215 SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER SEQRES 2 D 215 ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SEQRES 3 D 215 SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN SEQRES 4 D 215 LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SEQRES 5 D 215 SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY SEQRES 6 D 215 SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 D 215 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 D 215 ASP GLY TRP SER LEU ILE THR PHE GLY GLN GLY THR LYS SEQRES 9 D 215 VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 D 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 D 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 D 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 D 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 D 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 D 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 D 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 D 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 A 164 GLN GLY SER SER SER ILE VAL SER LEU LEU GLY ILE LYS SEQRES 2 A 164 VAL LEU ASN ASN PRO ALA LYS PHE THR ASP PRO TYR GLU SEQRES 3 A 164 PHE GLU ILE THR PHE GLU CYS LEU GLU SER LEU LYS HIS SEQRES 4 A 164 ASP LEU GLU TRP LYS LEU THR TYR VAL GLY SER SER ARG SEQRES 5 A 164 SER LEU ASP HIS ASP GLN GLU LEU ASP SER ILE LEU VAL SEQRES 6 A 164 GLY PRO VAL PRO VAL GLY VAL ASN LYS PHE VAL PHE SER SEQRES 7 A 164 ALA ASP PRO PRO SER ALA GLU LEU ILE PRO ALA SER GLU SEQRES 8 A 164 LEU VAL SER VAL THR VAL ILE LEU LEU SER CYS SER TYR SEQRES 9 A 164 ASP GLY ARG GLU PHE VAL ARG VAL GLY TYR TYR VAL ASN SEQRES 10 A 164 ASN GLU TYR ASP GLU GLU GLU LEU ARG GLU ASN PRO PRO SEQRES 11 A 164 ALA LYS VAL GLN VAL ASP HIS ILE VAL ARG ASN ILE LEU SEQRES 12 A 164 ALA GLU LYS PRO ARG VAL THR ARG PHE ASN ILE VAL TRP SEQRES 13 A 164 ASP ASN GLU ASN GLU GLY LEU GLU SEQRES 1 C 65 THR PRO ALA VAL THR THR TYR LYS LEU VAL ILE ASN GLY SEQRES 2 C 65 ARG THR LEU SER GLY TYR THR THR THR THR ALA VAL ASP SEQRES 3 C 65 ALA ALA THR ALA GLU LYS VAL PHE LYS GLN ILE ASP MET SEQRES 4 C 65 VAL SER SER VAL ASP GLY GLU TRP THR TYR ASP ASP ALA SEQRES 5 C 65 THR LYS THR PHE THR VAL THR GLU LYS PRO GLU LYS LEU HELIX 1 AA1 ASN B 29 TYR B 33 5 5 HELIX 2 AA2 ASP B 63 LYS B 66 5 4 HELIX 3 AA3 ARG B 88 THR B 92 5 5 HELIX 4 AA4 SER B 161 ALA B 163 5 3 HELIX 5 AA5 SER B 192 GLN B 197 1 6 HELIX 6 AA6 VAL D 29 SER D 31 5 3 HELIX 7 AA7 GLN D 79 PHE D 83 5 5 HELIX 8 AA8 SER D 121 SER D 127 1 7 HELIX 9 AA9 LYS D 183 GLU D 187 1 5 HELIX 10 AB1 PRO A 88 VAL A 93 5 6 HELIX 11 AB2 GLU A 122 ASN A 128 1 7 HELIX 12 AB3 GLN A 134 ASP A 136 5 3 HELIX 13 AB4 ASP C 27 GLN C 37 1 11 SHEET 1 AA1 4 GLN B 4 SER B 8 0 SHEET 2 AA1 4 LEU B 19 SER B 26 -1 O ALA B 24 N VAL B 6 SHEET 3 AA1 4 THR B 79 MET B 84 -1 O MET B 84 N LEU B 19 SHEET 4 AA1 4 PHE B 69 ASP B 74 -1 N ASP B 74 O THR B 79 SHEET 1 AA2 6 LEU B 12 VAL B 13 0 SHEET 2 AA2 6 THR B 112 VAL B 116 1 O THR B 115 N VAL B 13 SHEET 3 AA2 6 ALA B 93 TYR B 101 -1 N TYR B 95 O THR B 112 SHEET 4 AA2 6 ILE B 35 GLN B 40 -1 N VAL B 38 O TYR B 96 SHEET 5 AA2 6 LEU B 46 TYR B 53 -1 O VAL B 49 N TRP B 37 SHEET 6 AA2 6 GLY B 57 TYR B 61 -1 O SER B 60 N SER B 51 SHEET 1 AA3 4 LEU B 12 VAL B 13 0 SHEET 2 AA3 4 THR B 112 VAL B 116 1 O THR B 115 N VAL B 13 SHEET 3 AA3 4 ALA B 93 TYR B 101 -1 N TYR B 95 O THR B 112 SHEET 4 AA3 4 ALA B 104 TRP B 108 -1 O ALA B 104 N TYR B 101 SHEET 1 AA4 4 SER B 125 LEU B 129 0 SHEET 2 AA4 4 THR B 140 TYR B 150 -1 O GLY B 144 N LEU B 129 SHEET 3 AA4 4 TYR B 181 PRO B 190 -1 O LEU B 183 N VAL B 147 SHEET 4 AA4 4 VAL B 168 THR B 170 -1 N HIS B 169 O VAL B 186 SHEET 1 AA5 4 SER B 125 LEU B 129 0 SHEET 2 AA5 4 THR B 140 TYR B 150 -1 O GLY B 144 N LEU B 129 SHEET 3 AA5 4 TYR B 181 PRO B 190 -1 O LEU B 183 N VAL B 147 SHEET 4 AA5 4 VAL B 174 LEU B 175 -1 N VAL B 174 O SER B 182 SHEET 1 AA6 7 THR B 156 TRP B 159 0 SHEET 2 AA6 7 ILE B 200 HIS B 205 -1 O ASN B 202 N SER B 158 SHEET 3 AA6 7 THR B 210 LYS B 215 -1 O VAL B 212 N VAL B 203 SHEET 4 AA6 7 SER C 18 ALA C 25 -1 O SER C 18 N ASP B 213 SHEET 5 AA6 7 THR C 6 ASN C 13 -1 N LEU C 10 O THR C 21 SHEET 6 AA6 7 THR C 56 THR C 60 1 O PHE C 57 N LYS C 9 SHEET 7 AA6 7 THR C 49 ASP C 51 -1 N THR C 49 O THR C 58 SHEET 1 AA7 4 THR D 5 SER D 7 0 SHEET 2 AA7 4 VAL D 19 ARG D 24 -1 O THR D 22 N SER D 7 SHEET 3 AA7 4 ASP D 70 ILE D 75 -1 O PHE D 71 N CYS D 23 SHEET 4 AA7 4 PHE D 62 SER D 67 -1 N SER D 65 O THR D 72 SHEET 1 AA8 6 SER D 10 ALA D 13 0 SHEET 2 AA8 6 THR D 102 ILE D 106 1 O LYS D 103 N LEU D 11 SHEET 3 AA8 6 THR D 85 ASP D 91 -1 N TYR D 86 O THR D 102 SHEET 4 AA8 6 VAL D 33 GLN D 38 -1 N TYR D 36 O TYR D 87 SHEET 5 AA8 6 LYS D 45 TYR D 49 -1 O LYS D 45 N GLN D 37 SHEET 6 AA8 6 SER D 53 LEU D 54 -1 O SER D 53 N TYR D 49 SHEET 1 AA9 4 SER D 10 ALA D 13 0 SHEET 2 AA9 4 THR D 102 ILE D 106 1 O LYS D 103 N LEU D 11 SHEET 3 AA9 4 THR D 85 ASP D 91 -1 N TYR D 86 O THR D 102 SHEET 4 AA9 4 ILE D 96 PHE D 98 -1 O THR D 97 N GLN D 90 SHEET 1 AB1 4 SER D 114 PHE D 118 0 SHEET 2 AB1 4 THR D 129 PHE D 139 -1 O LEU D 135 N PHE D 116 SHEET 3 AB1 4 TYR D 173 SER D 182 -1 O LEU D 179 N VAL D 132 SHEET 4 AB1 4 SER D 159 GLN D 160 -1 N GLN D 160 O THR D 178 SHEET 1 AB2 4 ALA D 153 GLN D 155 0 SHEET 2 AB2 4 LYS D 145 VAL D 150 -1 N TRP D 148 O GLN D 155 SHEET 3 AB2 4 VAL D 191 THR D 197 -1 O GLU D 195 N GLN D 147 SHEET 4 AB2 4 VAL D 205 ASN D 210 -1 O LYS D 207 N CYS D 194 SHEET 1 AB3 3 VAL A 7 VAL A 14 0 SHEET 2 AB3 3 TYR A 25 CYS A 33 -1 O GLU A 28 N LYS A 13 SHEET 3 AB3 3 GLY A 71 ALA A 79 -1 O PHE A 77 N PHE A 27 SHEET 1 AB4 6 ALA A 19 LYS A 20 0 SHEET 2 AB4 6 ILE A 138 ARG A 151 -1 O ARG A 140 N ALA A 19 SHEET 3 AB4 6 ARG A 107 TYR A 120 -1 N GLU A 119 O VAL A 139 SHEET 4 AB4 6 VAL A 95 TYR A 104 -1 N THR A 96 O VAL A 116 SHEET 5 AB4 6 LEU A 41 SER A 50 -1 N LYS A 44 O SER A 101 SHEET 6 AB4 6 ASP A 55 VAL A 65 -1 O ILE A 63 N TRP A 43 SSBOND 1 CYS B 23 CYS B 97 1555 1555 2.04 SSBOND 2 CYS B 145 CYS B 201 1555 1555 2.04 SSBOND 3 CYS D 23 CYS D 88 1555 1555 2.05 SSBOND 4 CYS D 134 CYS D 194 1555 1555 2.03 CISPEP 1 PHE B 151 PRO B 152 0 -4.93 CISPEP 2 GLU B 153 PRO B 154 0 2.73 CISPEP 3 SER D 7 PRO D 8 0 1.30 CISPEP 4 TYR D 140 PRO D 141 0 -5.97 CISPEP 5 ASN A 17 PRO A 18 0 -4.64 CRYST1 134.971 134.971 339.568 90.00 90.00 90.00 I 41 2 2 16 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 0.007409 0.000000 0.000000 0.00000 SCALE2 0.000000 0.007409 0.000000 0.00000 SCALE3 0.000000 0.000000 0.002945 0.00000