HEADER IMMUNE SYSTEM 29-AUG-24 9GMU TITLE STRUCTURE OFHUMAN AM LIGAND BINDING DOMAIN IN COMPLEX WITH THE ACR3 TITLE 2 NANOBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTEGRIN ALPHA-M; COMPND 3 CHAIN: A, B; COMPND 4 FRAGMENT: UNP RESIDUES 145-337; COMPND 5 SYNONYM: CD11 ANTIGEN-LIKE FAMILY MEMBER B,CR-3 ALPHA CHAIN,CELL COMPND 6 SURFACE GLYCOPROTEIN MAC-1 SUBUNIT ALPHA,LEUKOCYTE ADHESION RECEPTOR COMPND 7 MO1,NEUTROPHIL ADHERENCE RECEPTOR; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: ACR VHH; COMPND 11 CHAIN: C, D; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ITGAM, CD11B, CR3A; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_TAXID: 9844; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS INTEGRIN RECEPTOR, LIGAND BINDING DOMAIN, ANTIBODY, VHH, IMMUNE KEYWDS 2 SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.LORENTZEN,G.R.ANDERSEN REVDAT 1 10-SEP-25 9GMU 0 JRNL AUTH J.LORENTZEN,G.R.ANDERSEN JRNL TITL STRUCTURE OF LIGAND BOUND AMB2 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.80 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.25 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.460 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 11989 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.245 REMARK 3 R VALUE (WORKING SET) : 0.242 REMARK 3 FREE R VALUE : 0.298 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.520 REMARK 3 FREE R VALUE TEST SET COUNT : 780 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 49.2500 - 6.9000 0.99 1925 131 0.2423 0.2960 REMARK 3 2 6.9000 - 5.4800 1.00 1878 127 0.2860 0.3134 REMARK 3 3 5.4800 - 4.7900 1.00 1859 131 0.2235 0.2999 REMARK 3 4 4.7900 - 4.3500 1.00 1840 131 0.1974 0.2416 REMARK 3 5 4.3500 - 4.0400 1.00 1833 135 0.2364 0.3314 REMARK 3 6 4.0400 - 3.8000 1.00 1855 125 0.2663 0.3263 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) : 0.470 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.555 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 131.3 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 186.2 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 4968 REMARK 3 ANGLE : 0.832 6696 REMARK 3 CHIRALITY : 0.051 718 REMARK 3 PLANARITY : 0.007 876 REMARK 3 DIHEDRAL : 11.928 1844 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 4 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN A REMARK 3 ORIGIN FOR THE GROUP (A): 18.0342 30.3133 54.3226 REMARK 3 T TENSOR REMARK 3 T11: 3.3618 T22: 1.1850 REMARK 3 T33: 1.3772 T12: -0.0221 REMARK 3 T13: 0.4985 T23: 0.0862 REMARK 3 L TENSOR REMARK 3 L11: 9.5419 L22: 4.7546 REMARK 3 L33: 4.3129 L12: -0.1124 REMARK 3 L13: -2.6719 L23: -0.2481 REMARK 3 S TENSOR REMARK 3 S11: 0.0856 S12: 0.1513 S13: -0.1498 REMARK 3 S21: -2.3336 S22: -0.4787 S23: -1.2446 REMARK 3 S31: -0.2381 S32: 1.0313 S33: 0.4704 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN B REMARK 3 ORIGIN FOR THE GROUP (A): -32.9229 9.2879 118.2789 REMARK 3 T TENSOR REMARK 3 T11: 1.5613 T22: 1.0305 REMARK 3 T33: 2.5763 T12: -0.0140 REMARK 3 T13: 0.6890 T23: 0.0649 REMARK 3 L TENSOR REMARK 3 L11: 6.1603 L22: 4.4556 REMARK 3 L33: 9.5706 L12: 0.4388 REMARK 3 L13: -0.0677 L23: -0.2571 REMARK 3 S TENSOR REMARK 3 S11: 0.2728 S12: -1.0618 S13: -0.5978 REMARK 3 S21: 1.2846 S22: -0.5795 S23: 2.0521 REMARK 3 S31: -0.0521 S32: -0.1585 S33: 0.1261 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN C REMARK 3 ORIGIN FOR THE GROUP (A): -4.7444 11.6482 104.1104 REMARK 3 T TENSOR REMARK 3 T11: 1.1370 T22: 1.4735 REMARK 3 T33: 1.0092 T12: -0.1296 REMARK 3 T13: -0.4108 T23: 0.1649 REMARK 3 L TENSOR REMARK 3 L11: 6.8349 L22: 9.3285 REMARK 3 L33: 3.3968 L12: 2.0765 REMARK 3 L13: -1.7800 L23: 0.4022 REMARK 3 S TENSOR REMARK 3 S11: -0.1411 S12: -0.5082 S13: -0.2661 REMARK 3 S21: 0.4899 S22: -0.3379 S23: 0.0293 REMARK 3 S31: -0.3590 S32: 1.0446 S33: 0.5849 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN D REMARK 3 ORIGIN FOR THE GROUP (A): 10.6693 27.9453 84.9822 REMARK 3 T TENSOR REMARK 3 T11: 1.1917 T22: 1.4168 REMARK 3 T33: 0.9295 T12: -0.0917 REMARK 3 T13: -0.3027 T23: 0.1662 REMARK 3 L TENSOR REMARK 3 L11: 5.5683 L22: 9.9361 REMARK 3 L33: 6.7174 L12: -0.7313 REMARK 3 L13: -0.6549 L23: -2.9685 REMARK 3 S TENSOR REMARK 3 S11: 0.4329 S12: -1.2312 S13: -0.2443 REMARK 3 S21: -0.5783 S22: -0.6131 S23: -0.8227 REMARK 3 S31: -0.6083 S32: 0.6951 S33: 0.1862 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 "B" 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 "C" 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 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9GMU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-AUG-24. REMARK 100 THE DEPOSITION ID IS D_1292141262. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 02-APR-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : MAX IV REMARK 200 BEAMLINE : BIOMAX REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97626 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 : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11989 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.800 REMARK 200 RESOLUTION RANGE LOW (A) : 49.250 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 200 DATA REDUNDANCY : 6.800 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.16890 REMARK 200 FOR THE DATA SET : 7.4800 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.94 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 7.00 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 1.35200 REMARK 200 FOR SHELL : 1.900 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 (%): 69.64 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.05 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, PH 7.0, 1.5 M LI2S04., REMARK 280 PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 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 X+1/2,Y+1/2,Z 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 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 1.000000 0.000000 0.000000 99.28200 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.07100 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 99.28200 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 28.07100 REMARK 290 SMTRY3 4 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 GLY A 124 REMARK 465 ALA A 125 REMARK 465 MET A 126 REMARK 465 GLY A 127 REMARK 465 SER A 128 REMARK 465 PRO A 129 REMARK 465 GLN A 130 REMARK 465 GLU A 131 REMARK 465 GLY A 316 REMARK 465 PHE A 317 REMARK 465 ALA A 318 REMARK 465 ILE A 319 REMARK 465 GLU A 320 REMARK 465 GLY A 321 REMARK 465 GLY B 124 REMARK 465 ALA B 125 REMARK 465 MET B 126 REMARK 465 GLY B 127 REMARK 465 SER B 128 REMARK 465 PRO B 129 REMARK 465 GLN B 130 REMARK 465 GLU B 131 REMARK 465 GLY B 316 REMARK 465 PHE B 317 REMARK 465 ALA B 318 REMARK 465 ILE B 319 REMARK 465 GLU B 320 REMARK 465 GLY B 321 REMARK 465 LEU C 124 REMARK 465 GLU C 125 REMARK 465 HIS C 126 REMARK 465 HIS C 127 REMARK 465 HIS C 128 REMARK 465 HIS C 129 REMARK 465 HIS C 130 REMARK 465 HIS C 131 REMARK 465 LEU D 124 REMARK 465 GLU D 125 REMARK 465 HIS D 126 REMARK 465 HIS D 127 REMARK 465 HIS D 128 REMARK 465 HIS D 129 REMARK 465 HIS D 130 REMARK 465 HIS D 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 OG SER A 144 O HOH A 501 1.88 REMARK 500 OG SER B 144 O HOH B 501 1.99 REMARK 500 OG SER B 142 O HOH B 501 2.10 REMARK 500 OE1 GLU A 278 OH TYR D 59 2.11 REMARK 500 OE1 GLU B 278 OH TYR C 59 2.12 REMARK 500 OE2 GLU B 162 NZ LYS B 165 2.15 REMARK 500 OE2 GLU A 162 NZ LYS A 165 2.16 REMARK 500 OD1 ASN A 285 OH TYR D 109 2.16 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 LYS A 168 32.04 -89.47 REMARK 500 SER A 177 -97.77 -144.37 REMARK 500 LEU A 206 175.83 65.98 REMARK 500 HIS A 210 68.01 -100.67 REMARK 500 PHE A 223 30.64 -87.33 REMARK 500 ASN A 232 73.43 -101.46 REMARK 500 LYS B 168 32.16 -89.64 REMARK 500 SER B 177 -97.92 -142.97 REMARK 500 LEU B 206 175.97 66.59 REMARK 500 HIS B 210 68.60 -100.56 REMARK 500 ILE B 225 -26.54 85.77 REMARK 500 ASN B 232 75.23 -104.66 REMARK 500 REMARK 500 REMARK: NULL 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 MG A 401 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER A 142 OG REMARK 620 2 SER A 144 OG 71.2 REMARK 620 3 THR A 209 OG1 64.5 113.1 REMARK 620 4 HOH A 501 O 48.4 52.9 60.3 REMARK 620 5 HOH A 502 O 123.3 118.9 60.6 90.9 REMARK 620 N 1 2 3 4 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG B 401 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 SER B 142 OG REMARK 620 2 SER B 144 OG 68.0 REMARK 620 3 THR B 209 OG1 67.5 110.2 REMARK 620 4 HOH B 501 O 46.0 56.3 54.0 REMARK 620 5 HOH B 502 O 132.0 109.1 69.7 90.8 REMARK 620 N 1 2 3 4 DBREF 9GMU A 129 321 UNP P11215 ITAM_HUMAN 145 337 DBREF 9GMU B 129 321 UNP P11215 ITAM_HUMAN 145 337 DBREF 9GMU C 2 131 PDB 9GMU 9GMU 2 131 DBREF 9GMU D 2 131 PDB 9GMU 9GMU 2 131 SEQADV 9GMU GLY A 124 UNP P11215 EXPRESSION TAG SEQADV 9GMU ALA A 125 UNP P11215 EXPRESSION TAG SEQADV 9GMU MET A 126 UNP P11215 EXPRESSION TAG SEQADV 9GMU GLY A 127 UNP P11215 EXPRESSION TAG SEQADV 9GMU SER A 128 UNP P11215 EXPRESSION TAG SEQADV 9GMU GLY A 316 UNP P11215 ILE 332 CONFLICT SEQADV 9GMU GLY B 124 UNP P11215 EXPRESSION TAG SEQADV 9GMU ALA B 125 UNP P11215 EXPRESSION TAG SEQADV 9GMU MET B 126 UNP P11215 EXPRESSION TAG SEQADV 9GMU GLY B 127 UNP P11215 EXPRESSION TAG SEQADV 9GMU SER B 128 UNP P11215 EXPRESSION TAG SEQADV 9GMU GLY B 316 UNP P11215 ILE 332 CONFLICT SEQRES 1 A 198 GLY ALA MET GLY SER PRO GLN GLU ASP SER ASP ILE ALA SEQRES 2 A 198 PHE LEU ILE ASP GLY SER GLY SER ILE ILE PRO HIS ASP SEQRES 3 A 198 PHE ARG ARG MET LYS GLU PHE VAL SER THR VAL MET GLU SEQRES 4 A 198 GLN LEU LYS LYS SER LYS THR LEU PHE SER LEU MET GLN SEQRES 5 A 198 TYR SER GLU GLU PHE ARG ILE HIS PHE THR PHE LYS GLU SEQRES 6 A 198 PHE GLN ASN ASN PRO ASN PRO ARG SER LEU VAL LYS PRO SEQRES 7 A 198 ILE THR GLN LEU LEU GLY ARG THR HIS THR ALA THR GLY SEQRES 8 A 198 ILE ARG LYS VAL VAL ARG GLU LEU PHE ASN ILE THR ASN SEQRES 9 A 198 GLY ALA ARG LYS ASN ALA PHE LYS ILE LEU VAL VAL ILE SEQRES 10 A 198 THR ASP GLY GLU LYS PHE GLY ASP PRO LEU GLY TYR GLU SEQRES 11 A 198 ASP VAL ILE PRO GLU ALA ASP ARG GLU GLY VAL ILE ARG SEQRES 12 A 198 TYR VAL ILE GLY VAL GLY ASP ALA PHE ARG SER GLU LYS SEQRES 13 A 198 SER ARG GLN GLU LEU ASN THR ILE ALA SER LYS PRO PRO SEQRES 14 A 198 ARG ASP HIS VAL PHE GLN VAL ASN ASN PHE GLU ALA LEU SEQRES 15 A 198 LYS THR ILE GLN ASN GLN LEU ARG GLU LYS GLY PHE ALA SEQRES 16 A 198 ILE GLU GLY SEQRES 1 B 198 GLY ALA MET GLY SER PRO GLN GLU ASP SER ASP ILE ALA SEQRES 2 B 198 PHE LEU ILE ASP GLY SER GLY SER ILE ILE PRO HIS ASP SEQRES 3 B 198 PHE ARG ARG MET LYS GLU PHE VAL SER THR VAL MET GLU SEQRES 4 B 198 GLN LEU LYS LYS SER LYS THR LEU PHE SER LEU MET GLN SEQRES 5 B 198 TYR SER GLU GLU PHE ARG ILE HIS PHE THR PHE LYS GLU SEQRES 6 B 198 PHE GLN ASN ASN PRO ASN PRO ARG SER LEU VAL LYS PRO SEQRES 7 B 198 ILE THR GLN LEU LEU GLY ARG THR HIS THR ALA THR GLY SEQRES 8 B 198 ILE ARG LYS VAL VAL ARG GLU LEU PHE ASN ILE THR ASN SEQRES 9 B 198 GLY ALA ARG LYS ASN ALA PHE LYS ILE LEU VAL VAL ILE SEQRES 10 B 198 THR ASP GLY GLU LYS PHE GLY ASP PRO LEU GLY TYR GLU SEQRES 11 B 198 ASP VAL ILE PRO GLU ALA ASP ARG GLU GLY VAL ILE ARG SEQRES 12 B 198 TYR VAL ILE GLY VAL GLY ASP ALA PHE ARG SER GLU LYS SEQRES 13 B 198 SER ARG GLN GLU LEU ASN THR ILE ALA SER LYS PRO PRO SEQRES 14 B 198 ARG ASP HIS VAL PHE GLN VAL ASN ASN PHE GLU ALA LEU SEQRES 15 B 198 LYS THR ILE GLN ASN GLN LEU ARG GLU LYS GLY PHE ALA SEQRES 16 B 198 ILE GLU GLY SEQRES 1 C 130 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 130 ALA GLY GLY SER LEU ARG LEU SER CYS THR THR SER GLY SEQRES 3 C 130 PHE THR PHE ASP ASP TYR ALA ILE GLY TRP PHE ARG GLN SEQRES 4 C 130 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 C 130 SER SER GLU GLY LYS TYR TYR SER ASP SER ALA LYS GLY SEQRES 6 C 130 ARG PHE THR ILE SER SER ASP ASN ALA LYS ASN THR VAL SEQRES 7 C 130 TYR LEU GLN MET ASN ASN LEU LYS PRO GLU ASP THR ALA SEQRES 8 C 130 VAL TYR TYR CYS ALA ALA GLU TRP ASN ASN PHE GLY ARG SEQRES 9 C 130 LEU CYS MET TYR PRO ASP TYR TRP GLY GLN GLY THR GLN SEQRES 10 C 130 VAL THR VAL SER SER LEU GLU HIS HIS HIS HIS HIS HIS SEQRES 1 D 130 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 130 ALA GLY GLY SER LEU ARG LEU SER CYS THR THR SER GLY SEQRES 3 D 130 PHE THR PHE ASP ASP TYR ALA ILE GLY TRP PHE ARG GLN SEQRES 4 D 130 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 D 130 SER SER GLU GLY LYS TYR TYR SER ASP SER ALA LYS GLY SEQRES 6 D 130 ARG PHE THR ILE SER SER ASP ASN ALA LYS ASN THR VAL SEQRES 7 D 130 TYR LEU GLN MET ASN ASN LEU LYS PRO GLU ASP THR ALA SEQRES 8 D 130 VAL TYR TYR CYS ALA ALA GLU TRP ASN ASN PHE GLY ARG SEQRES 9 D 130 LEU CYS MET TYR PRO ASP TYR TRP GLY GLN GLY THR GLN SEQRES 10 D 130 VAL THR VAL SER SER LEU GLU HIS HIS HIS HIS HIS HIS HET MG A 401 1 HET MG B 401 1 HET SO4 C 201 5 HET SO4 D 201 5 HETNAM MG MAGNESIUM ION HETNAM SO4 SULFATE ION FORMUL 5 MG 2(MG 2+) FORMUL 7 SO4 2(O4 S 2-) FORMUL 9 HOH *4(H2 O) HELIX 1 AA1 ILE A 146 LYS A 165 1 20 HELIX 2 AA2 THR A 185 ASN A 192 1 8 HELIX 3 AA3 ASN A 194 LYS A 200 1 7 HELIX 4 AA4 HIS A 210 LEU A 222 1 13 HELIX 5 AA5 ASN A 224 GLY A 228 5 5 HELIX 6 AA6 GLY A 251 ASP A 254 5 4 HELIX 7 AA7 VAL A 255 GLU A 262 1 8 HELIX 8 AA8 ASP A 273 ARG A 276 5 4 HELIX 9 AA9 SER A 277 ALA A 288 1 12 HELIX 10 AB1 PRO A 291 ASP A 294 5 4 HELIX 11 AB2 PHE A 302 LYS A 315 1 14 HELIX 12 AB3 ILE B 146 LYS B 165 1 20 HELIX 13 AB4 THR B 185 ASN B 192 1 8 HELIX 14 AB5 ASN B 194 LYS B 200 1 7 HELIX 15 AB6 HIS B 210 PHE B 223 1 14 HELIX 16 AB7 GLY B 251 ASP B 254 5 4 HELIX 17 AB8 VAL B 255 GLU B 262 1 8 HELIX 18 AB9 SER B 277 ALA B 288 1 12 HELIX 19 AC1 PRO B 291 ASP B 294 5 4 HELIX 20 AC2 PHE B 302 LYS B 315 1 14 HELIX 21 AC3 THR C 29 ASP C 31 5 3 HELIX 22 AC4 LYS C 87 THR C 91 5 5 HELIX 23 AC5 ASN C 102 GLY C 104 5 3 HELIX 24 AC6 THR D 29 ASP D 31 5 3 HELIX 25 AC7 LYS D 87 THR D 91 5 5 HELIX 26 AC8 ASN D 102 GLY D 104 5 3 SHEET 1 AA1 6 PHE A 180 PHE A 184 0 SHEET 2 AA1 6 THR A 169 TYR A 176 -1 N GLN A 175 O ARG A 181 SHEET 3 AA1 6 SER A 133 ASP A 140 1 N PHE A 137 O SER A 172 SHEET 4 AA1 6 PHE A 234 THR A 241 1 O ILE A 236 N ALA A 136 SHEET 5 AA1 6 ILE A 265 GLY A 270 1 O ILE A 265 N LEU A 237 SHEET 6 AA1 6 VAL A 296 GLN A 298 1 O PHE A 297 N GLY A 270 SHEET 1 AA2 6 PHE B 180 PHE B 184 0 SHEET 2 AA2 6 THR B 169 TYR B 176 -1 N GLN B 175 O ARG B 181 SHEET 3 AA2 6 SER B 133 ASP B 140 1 N PHE B 137 O SER B 172 SHEET 4 AA2 6 PHE B 234 THR B 241 1 O ILE B 236 N ALA B 136 SHEET 5 AA2 6 ILE B 265 GLY B 270 1 O ILE B 265 N LEU B 237 SHEET 6 AA2 6 VAL B 296 GLN B 298 1 O PHE B 297 N GLY B 270 SHEET 1 AA3 4 GLN C 4 SER C 8 0 SHEET 2 AA3 4 LEU C 19 SER C 26 -1 O SER C 22 N SER C 8 SHEET 3 AA3 4 THR C 78 MET C 83 -1 O MET C 83 N LEU C 19 SHEET 4 AA3 4 PHE C 68 ASP C 73 -1 N ASP C 73 O THR C 78 SHEET 1 AA412 GLY C 57 TYR C 60 0 SHEET 2 AA412 ARG C 46 SER C 53 -1 N SER C 53 O GLY C 57 SHEET 3 AA412 TYR C 33 GLN C 40 -1 N TRP C 37 O SER C 50 SHEET 4 AA412 ALA C 92 TRP C 100 -1 O TYR C 95 N PHE C 38 SHEET 5 AA412 THR C 117 SER C 122 -1 O THR C 117 N TYR C 94 SHEET 6 AA412 GLY C 11 GLN C 14 1 N GLY C 11 O THR C 120 SHEET 7 AA412 GLY D 11 GLN D 14 -1 O LEU D 12 N LEU C 12 SHEET 8 AA412 THR D 117 SER D 122 1 O THR D 120 N GLY D 11 SHEET 9 AA412 ALA D 92 TRP D 100 -1 N TYR D 94 O THR D 117 SHEET 10 AA412 TYR D 33 GLN D 40 -1 N PHE D 38 O TYR D 95 SHEET 11 AA412 ARG D 46 SER D 53 -1 O SER D 50 N TRP D 37 SHEET 12 AA412 GLY D 57 TYR D 60 -1 O GLY D 57 N SER D 53 SHEET 1 AA5 8 TYR C 112 TRP C 113 0 SHEET 2 AA5 8 ALA C 92 TRP C 100 -1 N ALA C 98 O TYR C 112 SHEET 3 AA5 8 THR C 117 SER C 122 -1 O THR C 117 N TYR C 94 SHEET 4 AA5 8 GLY C 11 GLN C 14 1 N GLY C 11 O THR C 120 SHEET 5 AA5 8 GLY D 11 GLN D 14 -1 O LEU D 12 N LEU C 12 SHEET 6 AA5 8 THR D 117 SER D 122 1 O THR D 120 N GLY D 11 SHEET 7 AA5 8 ALA D 92 TRP D 100 -1 N TYR D 94 O THR D 117 SHEET 8 AA5 8 TYR D 112 TRP D 113 -1 O TYR D 112 N ALA D 98 SHEET 1 AA6 4 GLN D 4 SER D 8 0 SHEET 2 AA6 4 LEU D 19 SER D 26 -1 O SER D 22 N SER D 8 SHEET 3 AA6 4 THR D 78 MET D 83 -1 O MET D 83 N LEU D 19 SHEET 4 AA6 4 PHE D 68 ASP D 73 -1 N THR D 69 O GLN D 82 SSBOND 1 CYS C 23 CYS C 96 1555 1555 2.04 SSBOND 2 CYS C 51 CYS C 107 1555 1555 2.04 SSBOND 3 CYS D 23 CYS D 96 1555 1555 2.03 SSBOND 4 CYS D 51 CYS D 107 1555 1555 2.04 LINK OG SER A 142 MG MG A 401 1555 1555 2.96 LINK OG SER A 144 MG MG A 401 1555 1555 2.03 LINK OG1 THR A 209 MG MG A 401 1555 1555 2.68 LINK MG MG A 401 O HOH A 501 1555 1555 2.18 LINK MG MG A 401 O HOH A 502 1555 1555 2.18 LINK OG SER B 142 MG MG B 401 1555 1555 2.91 LINK OG SER B 144 MG MG B 401 1555 1555 2.04 LINK OG1 THR B 209 MG MG B 401 1555 1555 2.65 LINK MG MG B 401 O HOH B 501 1555 1555 2.18 LINK MG MG B 401 O HOH B 502 1555 1555 2.18 CRYST1 198.564 56.142 137.444 90.00 128.61 90.00 C 1 2 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 0.005036 0.000000 0.004022 0.00000 SCALE2 0.000000 0.017812 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009311 0.00000 MTRIX1 1 0.227454 0.003348 0.973783 -90.02542 1 MTRIX2 1 -0.001497 -0.999992 0.003787 39.42290 1 MTRIX3 1 0.973788 -0.002319 -0.227447 113.14852 1 MTRIX1 2 0.217612 0.001784 0.976034 -89.93358 1 MTRIX2 2 0.005988 -0.999982 0.000492 39.57114 1 MTRIX3 2 0.976017 0.005738 -0.217619 112.20140 1