HEADER IMMUNE SYSTEM 29-APR-24 8ZCA TITLE CRYSTAL STRUCTURE OF HUMAN CD47 ECD BOUND TO FAB OF HU1C8 COMPND MOL_ID: 1; COMPND 2 MOLECULE: 1C8 FAB LIGHT CHAIN; COMPND 3 CHAIN: A, B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: 1C8 FAB HEAVY CHAIN; COMPND 7 CHAIN: D, C; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: LEUKOCYTE SURFACE ANTIGEN CD47; COMPND 11 CHAIN: E, F; COMPND 12 SYNONYM: ANTIGENIC SURFACE DETERMINANT PROTEIN OA3,INTEGRIN- COMPND 13 ASSOCIATED PROTEIN,IAP,PROTEIN MER6; COMPND 14 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_TAXID: 10029; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_COMMON: HUMAN; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 GENE: CD47, MER6; SOURCE 18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS CD47, ANTIBODY, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR Z.CHEN,J.DING REVDAT 1 07-MAY-25 8ZCA 0 JRNL AUTH X.LU,B.SUN JRNL TITL THE HUMANIZED ANTIBODY HU1C8 BINDS TO A DISTINCT EPITOPE OF JRNL TITL 2 CD47 IN A NOVEL METAL ION-DEPENDENT MANNER TO INDUCE LOW RBC JRNL TITL 3 TOXICITY AND EFFECTIVE ANTITUMOUR ACTIVITY JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.50 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) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.52 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980 REMARK 3 COMPLETENESS FOR RANGE (%) : 91.1 REMARK 3 NUMBER OF REFLECTIONS : 36287 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.217 REMARK 3 R VALUE (WORKING SET) : 0.215 REMARK 3 FREE R VALUE : 0.266 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.240 REMARK 3 FREE R VALUE TEST SET COUNT : 1902 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 38.5200 - 6.0000 0.97 2613 144 0.1712 0.1894 REMARK 3 2 6.0000 - 4.7600 0.98 2645 148 0.1737 0.2110 REMARK 3 3 4.7600 - 4.1600 0.99 2648 140 0.1640 0.2178 REMARK 3 4 4.1600 - 3.7800 0.98 2635 146 0.1921 0.2681 REMARK 3 5 3.7800 - 3.5100 0.98 2643 145 0.2131 0.2923 REMARK 3 6 3.5100 - 3.3000 0.97 2639 150 0.2432 0.3072 REMARK 3 7 3.3000 - 3.1400 0.96 2584 140 0.2500 0.2761 REMARK 3 8 3.1400 - 3.0000 0.95 2522 143 0.2715 0.3721 REMARK 3 9 3.0000 - 2.8900 0.92 2513 132 0.2739 0.2794 REMARK 3 10 2.8900 - 2.7900 0.92 2484 138 0.2778 0.3324 REMARK 3 11 2.7900 - 2.7000 0.88 2382 125 0.2774 0.3775 REMARK 3 12 2.7000 - 2.6200 0.85 2295 135 0.2795 0.3157 REMARK 3 13 2.6200 - 2.5500 0.84 2264 125 0.2933 0.3296 REMARK 3 14 2.5500 - 2.5000 0.57 1518 91 0.3094 0.4217 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) : 33.400 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 : 0.009 8572 REMARK 3 ANGLE : 1.045 11631 REMARK 3 CHIRALITY : 0.056 1326 REMARK 3 PLANARITY : 0.009 1470 REMARK 3 DIHEDRAL : 7.067 1202 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 8ZCA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC ON 06-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1300047429. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-NOV-22 REMARK 200 TEMPERATURE (KELVIN) : 193 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NFPSS REMARK 200 BEAMLINE : BL18U REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.979 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38158 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7 REMARK 200 DATA REDUNDANCY : 2.800 REMARK 200 R MERGE (I) : 0.16300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.8000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54 REMARK 200 COMPLETENESS FOR SHELL (%) : 86.9 REMARK 200 DATA REDUNDANCY IN SHELL : 2.20 REMARK 200 R MERGE FOR SHELL (I) : 0.35700 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: HKL-3000 REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.70 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES (PH 7.0) AND 20% (W/V) REMARK 280 POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 289K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 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: A, D, F 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: B, C, E 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 ASP A 1 REMARK 465 CYS A 218 REMARK 465 VAL D 62 REMARK 465 LYS D 134 REMARK 465 SER D 135 REMARK 465 THR D 136 REMARK 465 SER D 137 REMARK 465 SER D 220 REMARK 465 CYS D 221 REMARK 465 ASP D 222 REMARK 465 LYS D 223 REMARK 465 THR D 224 REMARK 465 HIS D 225 REMARK 465 ASP B 1 REMARK 465 GLU B 217 REMARK 465 CYS B 218 REMARK 465 VAL C 62 REMARK 465 LYS C 63 REMARK 465 LYS C 134 REMARK 465 SER C 135 REMARK 465 THR C 136 REMARK 465 SER C 137 REMARK 465 SER C 220 REMARK 465 CYS C 221 REMARK 465 ASP C 222 REMARK 465 LYS C 223 REMARK 465 THR C 224 REMARK 465 HIS C 225 REMARK 465 PHE E 119 REMARK 465 SER E 120 REMARK 465 PRO E 121 REMARK 465 GLY E 122 REMARK 465 SER E 123 REMARK 465 HIS E 124 REMARK 465 HIS E 125 REMARK 465 HIS E 126 REMARK 465 HIS E 127 REMARK 465 HIS E 128 REMARK 465 HIS E 129 REMARK 465 HIS E 130 REMARK 465 HIS E 131 REMARK 465 VAL F 116 REMARK 465 SER F 117 REMARK 465 TRP F 118 REMARK 465 PHE F 119 REMARK 465 SER F 120 REMARK 465 PRO F 121 REMARK 465 GLY F 122 REMARK 465 SER F 123 REMARK 465 HIS F 124 REMARK 465 HIS F 125 REMARK 465 HIS F 126 REMARK 465 HIS F 127 REMARK 465 HIS F 128 REMARK 465 HIS F 129 REMARK 465 HIS F 130 REMARK 465 HIS F 131 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O GLU E 11 C8 NAG E 202 1.39 REMARK 500 OD1 ASP D 71 OG1 THR D 74 2.11 REMARK 500 O HOH C 416 O HOH C 437 2.19 REMARK 500 REMARK 500 REMARK: NULL 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 A 10 51.57 -162.65 REMARK 500 ASN A 32 -2.25 64.87 REMARK 500 ALA A 53 -34.11 81.72 REMARK 500 SER A 54 -10.44 -141.68 REMARK 500 SER A 79 58.42 38.31 REMARK 500 ASP A 174 11.82 -143.09 REMARK 500 LYS A 194 -51.14 -120.35 REMARK 500 LYS D 42 -164.95 -111.74 REMARK 500 ALA D 59 -165.83 -74.52 REMARK 500 ASP D 60 76.97 -100.45 REMARK 500 ASP D 71 -160.43 -116.99 REMARK 500 SER D 73 10.80 -147.30 REMARK 500 SER D 81 74.10 44.75 REMARK 500 PRO D 97 107.05 -53.52 REMARK 500 SER D 132 -40.46 -131.00 REMARK 500 ASP D 149 73.26 62.37 REMARK 500 ARG B 31 14.83 59.29 REMARK 500 LYS B 33 -1.71 -140.01 REMARK 500 ALA B 53 -35.59 72.62 REMARK 500 SER B 79 56.52 31.50 REMARK 500 ASN B 142 70.34 60.84 REMARK 500 HIS B 202 143.49 -171.80 REMARK 500 SER C 24 141.28 -172.47 REMARK 500 ASP C 71 -155.29 -142.66 REMARK 500 SER C 81 55.84 39.90 REMARK 500 ASP C 149 66.61 70.28 REMARK 500 THR C 165 -36.18 -131.55 REMARK 500 GLU E 29 47.51 -149.11 REMARK 500 HIS E 90 42.62 -151.14 REMARK 500 LEU E 101 -129.49 56.74 REMARK 500 THR F 13 -160.69 -125.59 REMARK 500 LEU F 101 -122.82 61.62 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 PRO B 8 SER B 9 -145.23 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 A 431 DISTANCE = 6.70 ANGSTROMS REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 301 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 93 OD1 REMARK 620 2 ASP A 93 OD2 51.4 REMARK 620 3 TYR A 94 O 90.2 94.6 REMARK 620 4 ASP A 97 OD1 77.1 128.1 91.1 REMARK 620 5 ASP D 101 OD1 94.5 88.8 175.3 89.3 REMARK 620 6 HOH F 305 O 147.9 160.6 88.3 70.9 87.4 REMARK 620 7 HOH F 311 O 129.6 78.2 96.8 151.9 80.7 82.4 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA B 301 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP B 93 OD1 REMARK 620 2 ASP B 93 OD2 48.9 REMARK 620 3 TYR B 94 O 95.6 90.4 REMARK 620 4 ASP B 97 OD1 84.3 133.1 94.8 REMARK 620 5 ASP C 101 OD1 90.3 90.5 172.9 89.8 REMARK 620 6 HOH E 310 O 162.5 148.5 88.0 78.4 87.6 REMARK 620 7 HOH E 311 O 114.0 65.4 89.8 160.7 84.1 83.1 REMARK 620 N 1 2 3 4 5 6 DBREF 8ZCA A 1 218 PDB 8ZCA 8ZCA 1 218 DBREF 8ZCA D 1 225 PDB 8ZCA 8ZCA 1 225 DBREF 8ZCA B 1 218 PDB 8ZCA 8ZCA 1 218 DBREF 8ZCA C 1 225 PDB 8ZCA 8ZCA 1 225 DBREF 8ZCA E 1 121 UNP Q08722 CD47_HUMAN 19 139 DBREF 8ZCA F 1 121 UNP Q08722 CD47_HUMAN 19 139 SEQADV 8ZCA GLY E 15 UNP Q08722 CYS 33 CONFLICT SEQADV 8ZCA GLY E 122 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA SER E 123 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS E 124 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS E 125 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS E 126 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS E 127 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS E 128 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS E 129 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS E 130 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS E 131 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA GLY F 15 UNP Q08722 CYS 33 CONFLICT SEQADV 8ZCA GLY F 122 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA SER F 123 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS F 124 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS F 125 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS F 126 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS F 127 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS F 128 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS F 129 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS F 130 UNP Q08722 EXPRESSION TAG SEQADV 8ZCA HIS F 131 UNP Q08722 EXPRESSION TAG SEQRES 1 A 218 ASP PRO MET LEU THR GLN SER PRO SER PHE LEU SER ALA SEQRES 2 A 218 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN SER SER SEQRES 3 A 218 GLN SER VAL TYR ARG ASN LYS TYR LEU SER TRP TYR GLN SEQRES 4 A 218 GLN LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR TYR SEQRES 5 A 218 ALA SER THR LEU ALA SER GLY VAL PRO SER ARG PHE SER SEQRES 6 A 218 GLY SER GLY SER GLY THR GLU PHE THR LEU THR ILE SER SEQRES 7 A 218 SER LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS ALA SEQRES 8 A 218 GLY ASP TYR SER ASP ASP ILE GLU ASN ALA PHE GLY GLY SEQRES 9 A 218 GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SEQRES 10 A 218 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SEQRES 11 A 218 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE SEQRES 12 A 218 TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN SEQRES 13 A 218 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU SEQRES 14 A 218 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR SEQRES 15 A 218 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL SEQRES 16 A 218 TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO SEQRES 17 A 218 VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 D 225 GLN SER VAL LYS GLU SER GLY GLY GLY LEU PHE GLN PRO SEQRES 2 D 225 GLY GLY SER LEU ARG LEU SER CYS SER VAL SER GLY PHE SEQRES 3 D 225 SER LEU SER SER TYR ALA ILE SER TRP VAL ARG GLN ALA SEQRES 4 D 225 PRO GLY LYS GLY LEU GLU TYR ILE GLY TYR ILE SER SER SEQRES 5 D 225 ILE GLY ASP PRO TYR TYR ALA ASP TRP VAL LYS GLY ARG SEQRES 6 D 225 PHE THR ILE SER ARG ASP SER SER THR VAL TYR LEU GLN SEQRES 7 D 225 MET THR SER LEU ARG ALA GLU ASP THR ALA VAL TYR PHE SEQRES 8 D 225 CYS ALA ARG SER TYR PRO GLY ASN GLY ASP LEU GLY ARG SEQRES 9 D 225 LEU ASP ILE TRP GLY GLN GLY THR THR VAL THR VAL SER SEQRES 10 D 225 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 D 225 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 D 225 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 D 225 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 D 225 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 D 225 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 D 225 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 D 225 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 18 D 225 ASP LYS THR HIS SEQRES 1 B 218 ASP PRO MET LEU THR GLN SER PRO SER PHE LEU SER ALA SEQRES 2 B 218 SER VAL GLY ASP ARG VAL THR ILE THR CYS GLN SER SER SEQRES 3 B 218 GLN SER VAL TYR ARG ASN LYS TYR LEU SER TRP TYR GLN SEQRES 4 B 218 GLN LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR TYR SEQRES 5 B 218 ALA SER THR LEU ALA SER GLY VAL PRO SER ARG PHE SER SEQRES 6 B 218 GLY SER GLY SER GLY THR GLU PHE THR LEU THR ILE SER SEQRES 7 B 218 SER LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS ALA SEQRES 8 B 218 GLY ASP TYR SER ASP ASP ILE GLU ASN ALA PHE GLY GLY SEQRES 9 B 218 GLY THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SEQRES 10 B 218 SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SEQRES 11 B 218 SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE SEQRES 12 B 218 TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN SEQRES 13 B 218 ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU SEQRES 14 B 218 GLN ASP SER LYS ASP SER THR TYR SER LEU SER SER THR SEQRES 15 B 218 LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL SEQRES 16 B 218 TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO SEQRES 17 B 218 VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 C 225 GLN SER VAL LYS GLU SER GLY GLY GLY LEU PHE GLN PRO SEQRES 2 C 225 GLY GLY SER LEU ARG LEU SER CYS SER VAL SER GLY PHE SEQRES 3 C 225 SER LEU SER SER TYR ALA ILE SER TRP VAL ARG GLN ALA SEQRES 4 C 225 PRO GLY LYS GLY LEU GLU TYR ILE GLY TYR ILE SER SER SEQRES 5 C 225 ILE GLY ASP PRO TYR TYR ALA ASP TRP VAL LYS GLY ARG SEQRES 6 C 225 PHE THR ILE SER ARG ASP SER SER THR VAL TYR LEU GLN SEQRES 7 C 225 MET THR SER LEU ARG ALA GLU ASP THR ALA VAL TYR PHE SEQRES 8 C 225 CYS ALA ARG SER TYR PRO GLY ASN GLY ASP LEU GLY ARG SEQRES 9 C 225 LEU ASP ILE TRP GLY GLN GLY THR THR VAL THR VAL SER SEQRES 10 C 225 SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA SEQRES 11 C 225 PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU SEQRES 12 C 225 GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR SEQRES 13 C 225 VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS SEQRES 14 C 225 THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER SEQRES 15 C 225 LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY SEQRES 16 C 225 THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER SEQRES 17 C 225 ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS SEQRES 18 C 225 ASP LYS THR HIS SEQRES 1 E 131 PCA LEU LEU PHE ASN LYS THR LYS SER VAL GLU PHE THR SEQRES 2 E 131 PHE GLY ASN ASP THR VAL VAL ILE PRO CYS PHE VAL THR SEQRES 3 E 131 ASN MET GLU ALA GLN ASN THR THR GLU VAL TYR VAL LYS SEQRES 4 E 131 TRP LYS PHE LYS GLY ARG ASP ILE TYR THR PHE ASP GLY SEQRES 5 E 131 ALA LEU ASN LYS SER THR VAL PRO THR ASP PHE SER SER SEQRES 6 E 131 ALA LYS ILE GLU VAL SER GLN LEU LEU LYS GLY ASP ALA SEQRES 7 E 131 SER LEU LYS MET ASP LYS SER ASP ALA VAL SER HIS THR SEQRES 8 E 131 GLY ASN TYR THR CYS GLU VAL THR GLU LEU THR ARG GLU SEQRES 9 E 131 GLY GLU THR ILE ILE GLU LEU LYS TYR ARG VAL VAL SER SEQRES 10 E 131 TRP PHE SER PRO GLY SER HIS HIS HIS HIS HIS HIS HIS SEQRES 11 E 131 HIS SEQRES 1 F 131 PCA LEU LEU PHE ASN LYS THR LYS SER VAL GLU PHE THR SEQRES 2 F 131 PHE GLY ASN ASP THR VAL VAL ILE PRO CYS PHE VAL THR SEQRES 3 F 131 ASN MET GLU ALA GLN ASN THR THR GLU VAL TYR VAL LYS SEQRES 4 F 131 TRP LYS PHE LYS GLY ARG ASP ILE TYR THR PHE ASP GLY SEQRES 5 F 131 ALA LEU ASN LYS SER THR VAL PRO THR ASP PHE SER SER SEQRES 6 F 131 ALA LYS ILE GLU VAL SER GLN LEU LEU LYS GLY ASP ALA SEQRES 7 F 131 SER LEU LYS MET ASP LYS SER ASP ALA VAL SER HIS THR SEQRES 8 F 131 GLY ASN TYR THR CYS GLU VAL THR GLU LEU THR ARG GLU SEQRES 9 F 131 GLY GLU THR ILE ILE GLU LEU LYS TYR ARG VAL VAL SER SEQRES 10 F 131 TRP PHE SER PRO GLY SER HIS HIS HIS HIS HIS HIS HIS SEQRES 11 F 131 HIS MODRES 8ZCA PCA E 1 GLN MODIFIED RESIDUE MODRES 8ZCA PCA F 1 GLN MODIFIED RESIDUE HET PCA E 1 8 HET PCA F 1 8 HET CA A 301 1 HET GOL D 301 6 HET CA B 301 1 HET GOL C 301 6 HET NAG E 201 14 HET NAG E 202 14 HET NAG F 201 14 HET NAG F 202 14 HETNAM PCA PYROGLUTAMIC ACID HETNAM CA CALCIUM ION HETNAM GOL GLYCEROL HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL 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 FORMUL 5 PCA 2(C5 H7 N O3) FORMUL 7 CA 2(CA 2+) FORMUL 8 GOL 2(C3 H8 O3) FORMUL 11 NAG 4(C8 H15 N O6) FORMUL 15 HOH *170(H2 O) HELIX 1 AA1 VAL A 29 LYS A 33 5 5 HELIX 2 AA2 GLN A 81 PHE A 85 5 5 HELIX 3 AA3 ASP A 96 ASN A 100 5 5 HELIX 4 AA4 SER A 125 LYS A 130 1 6 HELIX 5 AA5 LYS A 187 GLU A 191 1 5 HELIX 6 AA6 ARG D 83 THR D 87 5 5 HELIX 7 AA7 SER D 161 ALA D 163 5 3 HELIX 8 AA8 SER D 192 LEU D 194 5 3 HELIX 9 AA9 VAL B 29 LYS B 33 5 5 HELIX 10 AB1 GLN B 81 PHE B 85 5 5 HELIX 11 AB2 ASP B 96 ASN B 100 5 5 HELIX 12 AB3 SER B 125 LYS B 130 1 6 HELIX 13 AB4 LYS B 187 GLU B 191 1 5 HELIX 14 AB5 SER C 27 TYR C 31 5 5 HELIX 15 AB6 ARG C 83 THR C 87 5 5 HELIX 16 AB7 SER C 161 ALA C 163 5 3 HELIX 17 AB8 SER C 192 LEU C 194 5 3 HELIX 18 AB9 LYS C 206 ASN C 209 5 4 HELIX 19 AC1 ASN E 32 THR E 34 5 3 HELIX 20 AC2 ALA E 53 ASN E 55 5 3 HELIX 21 AC3 PRO E 60 SER E 64 5 5 HELIX 22 AC4 VAL E 70 GLY E 76 5 7 HELIX 23 AC5 LYS E 84 SER E 89 1 6 HELIX 24 AC6 ASN F 32 THR F 34 5 3 HELIX 25 AC7 PRO F 60 SER F 64 5 5 HELIX 26 AC8 GLU F 69 LEU F 73 5 5 HELIX 27 AC9 LYS F 84 SER F 89 1 6 SHEET 1 AA1 4 LEU A 4 GLN A 6 0 SHEET 2 AA1 4 VAL A 19 SER A 25 -1 O GLN A 24 N THR A 5 SHEET 3 AA1 4 GLU A 72 ILE A 77 -1 O LEU A 75 N ILE A 21 SHEET 4 AA1 4 PHE A 64 SER A 69 -1 N SER A 65 O THR A 76 SHEET 1 AA2 6 LEU A 11 SER A 14 0 SHEET 2 AA2 6 THR A 106 LYS A 111 1 O LYS A 111 N ALA A 13 SHEET 3 AA2 6 ALA A 86 GLY A 92 -1 N ALA A 86 O VAL A 108 SHEET 4 AA2 6 LEU A 35 GLN A 40 -1 N GLN A 40 O THR A 87 SHEET 5 AA2 6 LYS A 47 TYR A 51 -1 O ILE A 50 N TRP A 37 SHEET 6 AA2 6 THR A 55 LEU A 56 -1 O THR A 55 N TYR A 51 SHEET 1 AA3 4 LEU A 11 SER A 14 0 SHEET 2 AA3 4 THR A 106 LYS A 111 1 O LYS A 111 N ALA A 13 SHEET 3 AA3 4 ALA A 86 GLY A 92 -1 N ALA A 86 O VAL A 108 SHEET 4 AA3 4 ALA A 101 PHE A 102 -1 O ALA A 101 N GLY A 92 SHEET 1 AA4 4 SER A 118 PHE A 122 0 SHEET 2 AA4 4 THR A 133 PHE A 143 -1 O VAL A 137 N PHE A 122 SHEET 3 AA4 4 TYR A 177 SER A 186 -1 O LEU A 179 N LEU A 140 SHEET 4 AA4 4 SER A 163 VAL A 167 -1 N GLN A 164 O THR A 182 SHEET 1 AA5 3 LYS A 149 VAL A 154 0 SHEET 2 AA5 3 VAL A 195 THR A 201 -1 O GLU A 199 N GLN A 151 SHEET 3 AA5 3 VAL A 209 ASN A 214 -1 O VAL A 209 N VAL A 200 SHEET 1 AA6 4 SER D 2 GLU D 5 0 SHEET 2 AA6 4 LEU D 17 SER D 24 -1 O SER D 22 N LYS D 4 SHEET 3 AA6 4 THR D 74 MET D 79 -1 O LEU D 77 N LEU D 19 SHEET 4 AA6 4 PHE D 66 ARG D 70 -1 N THR D 67 O GLN D 78 SHEET 1 AA7 6 GLY D 9 PHE D 11 0 SHEET 2 AA7 6 THR D 112 VAL D 116 1 O THR D 115 N PHE D 11 SHEET 3 AA7 6 ALA D 88 SER D 95 -1 N TYR D 90 O THR D 112 SHEET 4 AA7 6 ALA D 32 GLN D 38 -1 N VAL D 36 O PHE D 91 SHEET 5 AA7 6 LEU D 44 ILE D 50 -1 O GLU D 45 N ARG D 37 SHEET 6 AA7 6 PRO D 56 TYR D 58 -1 O TYR D 57 N TYR D 49 SHEET 1 AA8 4 GLY D 9 PHE D 11 0 SHEET 2 AA8 4 THR D 112 VAL D 116 1 O THR D 115 N PHE D 11 SHEET 3 AA8 4 ALA D 88 SER D 95 -1 N TYR D 90 O THR D 112 SHEET 4 AA8 4 LEU D 105 TRP D 108 -1 O ASP D 106 N ARG D 94 SHEET 1 AA9 4 SER D 125 LEU D 129 0 SHEET 2 AA9 4 THR D 140 TYR D 150 -1 O LEU D 146 N PHE D 127 SHEET 3 AA9 4 TYR D 181 PRO D 190 -1 O LEU D 183 N VAL D 147 SHEET 4 AA9 4 HIS D 169 THR D 170 -1 N HIS D 169 O VAL D 186 SHEET 1 AB1 4 SER D 125 LEU D 129 0 SHEET 2 AB1 4 THR D 140 TYR D 150 -1 O LEU D 146 N PHE D 127 SHEET 3 AB1 4 TYR D 181 PRO D 190 -1 O LEU D 183 N VAL D 147 SHEET 4 AB1 4 VAL D 174 LEU D 175 -1 N VAL D 174 O SER D 182 SHEET 1 AB2 3 THR D 156 TRP D 159 0 SHEET 2 AB2 3 ILE D 200 HIS D 205 -1 O ASN D 202 N SER D 158 SHEET 3 AB2 3 THR D 210 LYS D 215 -1 O VAL D 212 N VAL D 203 SHEET 1 AB3 4 LEU B 4 GLN B 6 0 SHEET 2 AB3 4 VAL B 19 SER B 25 -1 O GLN B 24 N THR B 5 SHEET 3 AB3 4 GLU B 72 ILE B 77 -1 O PHE B 73 N CYS B 23 SHEET 4 AB3 4 PHE B 64 SER B 69 -1 N SER B 67 O THR B 74 SHEET 1 AB4 6 PHE B 10 SER B 14 0 SHEET 2 AB4 6 THR B 106 LYS B 111 1 O GLU B 109 N LEU B 11 SHEET 3 AB4 6 THR B 87 GLY B 92 -1 N TYR B 88 O THR B 106 SHEET 4 AB4 6 LEU B 35 GLN B 40 -1 N TYR B 38 O TYR B 89 SHEET 5 AB4 6 LYS B 47 TYR B 51 -1 O LEU B 49 N TRP B 37 SHEET 6 AB4 6 THR B 55 LEU B 56 -1 O THR B 55 N TYR B 51 SHEET 1 AB5 4 PHE B 10 SER B 14 0 SHEET 2 AB5 4 THR B 106 LYS B 111 1 O GLU B 109 N LEU B 11 SHEET 3 AB5 4 THR B 87 GLY B 92 -1 N TYR B 88 O THR B 106 SHEET 4 AB5 4 ALA B 101 PHE B 102 -1 O ALA B 101 N GLY B 92 SHEET 1 AB6 4 SER B 118 PHE B 122 0 SHEET 2 AB6 4 THR B 133 PHE B 143 -1 O VAL B 137 N PHE B 122 SHEET 3 AB6 4 TYR B 177 SER B 186 -1 O LEU B 179 N LEU B 140 SHEET 4 AB6 4 SER B 163 GLN B 164 -1 N GLN B 164 O THR B 182 SHEET 1 AB7 4 ALA B 157 LEU B 158 0 SHEET 2 AB7 4 LYS B 149 VAL B 154 -1 N VAL B 154 O ALA B 157 SHEET 3 AB7 4 VAL B 195 THR B 201 -1 O ALA B 197 N LYS B 153 SHEET 4 AB7 4 VAL B 209 ASN B 214 -1 O VAL B 209 N VAL B 200 SHEET 1 AB8 4 SER C 2 GLU C 5 0 SHEET 2 AB8 4 LEU C 17 SER C 24 -1 O SER C 22 N LYS C 4 SHEET 3 AB8 4 THR C 74 MET C 79 -1 O VAL C 75 N CYS C 21 SHEET 4 AB8 4 PHE C 66 ARG C 70 -1 N SER C 69 O TYR C 76 SHEET 1 AB9 6 GLY C 9 PHE C 11 0 SHEET 2 AB9 6 THR C 112 VAL C 116 1 O THR C 115 N PHE C 11 SHEET 3 AB9 6 ALA C 88 SER C 95 -1 N ALA C 88 O VAL C 114 SHEET 4 AB9 6 ALA C 32 GLN C 38 -1 N VAL C 36 O PHE C 91 SHEET 5 AB9 6 LEU C 44 ILE C 50 -1 O GLU C 45 N ARG C 37 SHEET 6 AB9 6 PRO C 56 TYR C 58 -1 O TYR C 57 N TYR C 49 SHEET 1 AC1 4 GLY C 9 PHE C 11 0 SHEET 2 AC1 4 THR C 112 VAL C 116 1 O THR C 115 N PHE C 11 SHEET 3 AC1 4 ALA C 88 SER C 95 -1 N ALA C 88 O VAL C 114 SHEET 4 AC1 4 LEU C 105 TRP C 108 -1 O ILE C 107 N ARG C 94 SHEET 1 AC2 4 SER C 125 LEU C 129 0 SHEET 2 AC2 4 THR C 140 TYR C 150 -1 O LEU C 146 N PHE C 127 SHEET 3 AC2 4 TYR C 181 PRO C 190 -1 O LEU C 183 N VAL C 147 SHEET 4 AC2 4 VAL C 168 THR C 170 -1 N HIS C 169 O VAL C 186 SHEET 1 AC3 4 SER C 125 LEU C 129 0 SHEET 2 AC3 4 THR C 140 TYR C 150 -1 O LEU C 146 N PHE C 127 SHEET 3 AC3 4 TYR C 181 PRO C 190 -1 O LEU C 183 N VAL C 147 SHEET 4 AC3 4 VAL C 174 LEU C 175 -1 N VAL C 174 O SER C 182 SHEET 1 AC4 3 THR C 156 TRP C 159 0 SHEET 2 AC4 3 ILE C 200 HIS C 205 -1 O ASN C 204 N THR C 156 SHEET 3 AC4 3 THR C 210 LYS C 215 -1 O THR C 210 N HIS C 205 SHEET 1 AC5 6 SER E 9 PHE E 12 0 SHEET 2 AC5 6 ARG E 103 TYR E 113 1 O LYS E 112 N VAL E 10 SHEET 3 AC5 6 GLY E 92 GLU E 100 -1 N TYR E 94 O ILE E 109 SHEET 4 AC5 6 VAL E 36 PHE E 42 -1 N LYS E 39 O GLU E 97 SHEET 5 AC5 6 ARG E 45 ASP E 51 -1 O TYR E 48 N TRP E 40 SHEET 6 AC5 6 SER E 57 THR E 58 -1 O THR E 58 N THR E 49 SHEET 1 AC6 3 THR E 18 ILE E 21 0 SHEET 2 AC6 3 LEU E 80 ASP E 83 -1 O MET E 82 N VAL E 19 SHEET 3 AC6 3 LYS E 67 ILE E 68 -1 N LYS E 67 O LYS E 81 SHEET 1 AC7 6 SER F 9 PHE F 12 0 SHEET 2 AC7 6 ARG F 103 TYR F 113 1 O LYS F 112 N VAL F 10 SHEET 3 AC7 6 GLY F 92 GLU F 100 -1 N GLY F 92 O LEU F 111 SHEET 4 AC7 6 VAL F 36 PHE F 42 -1 N TYR F 37 O THR F 99 SHEET 5 AC7 6 ARG F 45 ASP F 51 -1 O TYR F 48 N TRP F 40 SHEET 6 AC7 6 LYS F 56 THR F 58 -1 O LYS F 56 N ASP F 51 SHEET 1 AC8 2 THR F 18 ILE F 21 0 SHEET 2 AC8 2 LEU F 80 ASP F 83 -1 O MET F 82 N VAL F 19 SSBOND 1 CYS A 23 CYS A 90 1555 1555 2.05 SSBOND 2 CYS A 138 CYS A 198 1555 1555 2.04 SSBOND 3 CYS D 21 CYS D 92 1555 1555 2.06 SSBOND 4 CYS D 145 CYS D 201 1555 1555 2.02 SSBOND 5 CYS B 23 CYS B 90 1555 1555 2.06 SSBOND 6 CYS B 138 CYS B 198 1555 1555 2.07 SSBOND 7 CYS C 21 CYS C 92 1555 1555 2.04 SSBOND 8 CYS C 145 CYS C 201 1555 1555 2.06 SSBOND 9 CYS E 23 CYS E 96 1555 1555 2.08 SSBOND 10 CYS F 23 CYS F 96 1555 1555 2.02 LINK C PCA E 1 N LEU E 2 1555 1555 1.33 LINK ND2 ASN E 16 C1 NAG E 202 1555 1555 1.42 LINK ND2 ASN E 93 C1 NAG E 201 1555 1555 1.42 LINK C PCA F 1 N LEU F 2 1555 1555 1.34 LINK ND2 ASN F 16 C1 NAG F 202 1555 1555 1.42 LINK ND2 ASN F 93 C1 NAG F 201 1555 1555 1.44 LINK OD1 ASP A 93 CA CA A 301 1555 1555 2.54 LINK OD2 ASP A 93 CA CA A 301 1555 1555 2.54 LINK O TYR A 94 CA CA A 301 1555 1555 2.36 LINK OD1 ASP A 97 CA CA A 301 1555 1555 2.55 LINK CA CA A 301 OD1 ASP D 101 1555 1555 2.12 LINK CA CA A 301 O HOH F 305 1555 1555 2.61 LINK CA CA A 301 O HOH F 311 1555 1555 2.42 LINK OD1 ASP B 93 CA CA B 301 1555 1555 2.46 LINK OD2 ASP B 93 CA CA B 301 1555 1555 2.76 LINK O TYR B 94 CA CA B 301 1555 1555 2.40 LINK OD1 ASP B 97 CA CA B 301 1555 1555 2.33 LINK CA CA B 301 OD1 ASP C 101 1555 1555 2.29 LINK CA CA B 301 O HOH E 310 1555 1555 2.62 LINK CA CA B 301 O HOH E 311 1555 1555 2.48 CISPEP 1 TYR A 144 PRO A 145 0 3.30 CISPEP 2 PHE D 151 PRO D 152 0 -8.88 CISPEP 3 GLU D 153 PRO D 154 0 6.34 CISPEP 4 TYR B 144 PRO B 145 0 3.87 CISPEP 5 PHE C 151 PRO C 152 0 -1.45 CISPEP 6 GLU C 153 PRO C 154 0 1.73 CRYST1 45.224 79.931 92.751 112.50 96.61 103.16 P 1 2 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 0.022112 0.005170 0.005239 0.00000 SCALE2 0.000000 0.012848 0.005993 0.00000 SCALE3 0.000000 0.000000 0.011976 0.00000