HEADER SIGNALING PROTEIN/IMMUNE SYSTEM 27-JUN-21 7R8U TITLE LOX-1 - STRUCTURAL AND FUNCTIONAL STUDIES OF A RECEPTOR IMPLICATED IN TITLE 2 ATHEROSCLEROSIS COMPND MOL_ID: 1; COMPND 2 MOLECULE: OXIDIZED LOW-DENSITY LIPOPROTEIN RECEPTOR 1; COMPND 3 CHAIN: AAA, BBB; COMPND 4 FRAGMENT: EXTRACELLULAR FRAGMENT (UNP RESIDUES 140-271); COMPND 5 SYNONYM: OX-LDL RECEPTOR 1,C-TYPE LECTIN DOMAIN FAMILY 8 MEMBER A, COMPND 6 LECTIN-LIKE OXIDIZED LDL RECEPTOR 1,LOX-1,LECTIN-LIKE OXLDL RECEPTOR COMPND 7 1,HLOX-1,LECTIN-TYPE OXIDIZED LDL RECEPTOR 1; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: ANTIGEN BINDING FRAGMENT, VH AND CH1; COMPND 11 CHAIN: HHH; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: ANTIBODY LIGHT CHAIN, KAPPA; COMPND 15 CHAIN: LLL; COMPND 16 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: OLR1, CLEC8A, LOX1; SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 14 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 16 MOL_ID: 3; SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 18 ORGANISM_COMMON: HUMAN; SOURCE 19 ORGANISM_TAXID: 9606; SOURCE 20 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 21 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 22 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS LOW DENSITY LIPOPROTEIN RECEPTOR ANTIBODY COMPLEX LOX-1 SCAVENGER KEYWDS 2 RECEPTOR ATHEROGENESIS-ATHEROSCLEROSIS MACROPHAGE CARDIOVASCULAR KEYWDS 3 DISEASE, SIGNALING PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR V.OGANESYAN,N.VAN DYK JRNL AUTH E.L.ONGSTAD,R.GADDIPATI,M.BELKHODJA,N.VAN DYK,S.LEVY, JRNL AUTH 2 D.SAGAR,P.CARIUK,M.WOLNY,R.N.HANNA,M.J.BORROK,A.BUCHANAN, JRNL AUTH 3 V.OGANESYAN,R.GUPTA JRNL TITL A MONOCLONAL ANTIBODY BLOCKS LOX-1 ACTIVATION - STRUCTURAL JRNL TITL 2 AND FUNCTIONAL STUDIES OF A RECEPTOR IMPLICATED IN JRNL TITL 3 ATHEROSCLEROSIS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0258 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.49 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 56992 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.186 REMARK 3 FREE R VALUE : 0.218 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.062 REMARK 3 FREE R VALUE TEST SET COUNT : 1175 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95 REMARK 3 REFLECTION IN BIN (WORKING SET) : 3994 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.62 REMARK 3 BIN R VALUE (WORKING SET) : 0.3510 REMARK 3 BIN FREE R VALUE SET COUNT : 71 REMARK 3 BIN FREE R VALUE : 0.3220 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 5407 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 30 REMARK 3 SOLVENT ATOMS : 436 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.91 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.08300 REMARK 3 B22 (A**2) : -2.62800 REMARK 3 B33 (A**2) : 2.71100 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.155 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.137 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.120 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.399 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5754 ; 0.009 ; 0.013 REMARK 3 BOND LENGTHS OTHERS (A): 5078 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7869 ; 1.611 ; 1.640 REMARK 3 BOND ANGLES OTHERS (DEGREES): 11897 ; 1.341 ; 1.570 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 742 ; 7.372 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 250 ;34.568 ;23.160 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 901 ;15.624 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;17.460 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 744 ; 0.073 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6480 ; 0.008 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1192 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 943 ; 0.202 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 59 ; 0.227 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2684 ; 0.169 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 401 ; 0.161 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2885 ; 3.187 ; 3.738 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2884 ; 3.186 ; 3.736 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3620 ; 4.395 ; 5.582 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3621 ; 4.394 ; 5.584 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2869 ; 3.914 ; 4.091 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2870 ; 3.913 ; 4.092 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4237 ; 5.713 ; 5.970 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4238 ; 5.713 ; 5.970 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL PLUS MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 7R8U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000257789. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-JAN-19 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 : SSRL REMARK 200 BEAMLINE : BL14-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.19499 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57364 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 39.492 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9 REMARK 200 DATA REDUNDANCY : 6.500 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 1.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 1YPU REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 47.10 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M 1,6-HEXANEDIOL, 0.2 M 1-BUTANOL, REMARK 280 0.2 M 1,2-PROPANEDIOL, 0.2 M 2-PROPANOL, 0.2 M 1,4-BUTANEDIOL, REMARK 280 0.2 M 1,3-PROPANEDIOL, 1 M TRIS BASE, BICINE, PH 8.5, 50% V/V REMARK 280 PRECIPITANT MIX (25% V/V MPD, 25% PEG1000, 25% W/V PEG3350), REMARK 280 VAPOR DIFFUSION, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 35.95400 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.46250 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.95050 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.46250 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.95400 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.95050 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 9180 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 30200 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: AAA, BBB, HHH, LLL 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 ARG B 271 REMARK 465 UNK H 145 REMARK 465 UNK H 146 REMARK 465 UNK H 147 REMARK 465 UNK H 148 REMARK 465 UNK H 149 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 HOHLL 500 O HOHLL 505 2.13 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 ASPAA 146 -2.68 82.21 REMARK 500 ARGAA 230 -168.15 -102.13 REMARK 500 ASPBB 147 -0.68 80.69 REMARK 500 LEUBB 227 -62.03 -101.64 REMARK 500 ARGBB 248 -128.76 43.14 REMARK 500 GLNHH 65 137.48 -31.17 REMARK 500 THRHH 132 125.54 -36.81 REMARK 500 ASPHH 160 64.09 66.81 REMARK 500 SERLL 2 40.64 -95.09 REMARK 500 ASNLL 28 -85.07 -136.86 REMARK 500 ASNLL 53 -36.32 78.67 REMARK 500 SERLL 54 -3.19 -143.21 REMARK 500 ASPLL 156 -114.96 54.20 REMARK 500 ASNLL 175 -1.12 78.02 REMARK 500 REMARK 500 REMARK: NULL DBREF 7R8UAA 139 270 UNP P78380 OLR1_HUMAN 140 271 DBREF 7R8UBB 140 271 UNP P78380 OLR1_HUMAN 140 271 DBREF 7R8UHH 1 230 PDB 7R8U 7R8U 1 230 DBREF 7R8ULL 1 216 PDB 7R8U 7R8U 1 216 SEQRES 1AA 132 CYS SER ALA PRO CYS PRO GLN ASP TRP ILE TRP HIS GLY SEQRES 2AA 132 GLU ASN CYS TYR LEU PHE SER SER GLY SER PHE ASN TRP SEQRES 3AA 132 GLU LYS SER GLN GLU LYS CYS LEU SER LEU ASP ALA LYS SEQRES 4AA 132 LEU LEU LYS ILE ASN SER THR ALA ASP LEU ASP PHE ILE SEQRES 5AA 132 GLN GLN ALA ILE SER TYR SER SER PHE PRO PHE TRP MET SEQRES 6AA 132 GLY LEU SER ARG ARG ASN PRO SER TYR PRO TRP LEU TRP SEQRES 7AA 132 GLU ASP GLY SER PRO LEU MET PRO HIS LEU PHE ARG VAL SEQRES 8AA 132 ARG GLY ALA VAL SER GLN THR TYR PRO SER GLY THR CYS SEQRES 9AA 132 ALA TYR ILE GLN ARG GLY ALA VAL TYR ALA GLU ASN CYS SEQRES 10AA 132 ILE LEU ALA ALA PHE SER ILE CYS GLN LYS LYS ALA ASN SEQRES 11AA 132 LEU ARG SEQRES 1BB 132 CYS SER ALA PRO CYS PRO GLN ASP TRP ILE TRP HIS GLY SEQRES 2BB 132 GLU ASN CYS TYR LEU PHE SER SER GLY SER PHE ASN TRP SEQRES 3BB 132 GLU LYS SER GLN GLU LYS CYS LEU SER LEU ASP ALA LYS SEQRES 4BB 132 LEU LEU LYS ILE ASN SER THR ALA ASP LEU ASP PHE ILE SEQRES 5BB 132 GLN GLN ALA ILE SER TYR SER SER PHE PRO PHE TRP MET SEQRES 6BB 132 GLY LEU SER ARG ARG ASN PRO SER TYR PRO TRP LEU TRP SEQRES 7BB 132 GLU ASP GLY SER PRO LEU MET PRO HIS LEU PHE ARG VAL SEQRES 8BB 132 ARG GLY ALA VAL SER GLN THR TYR PRO SER GLY THR CYS SEQRES 9BB 132 ALA TYR ILE GLN ARG GLY ALA VAL TYR ALA GLU ASN CYS SEQRES 10BB 132 ILE LEU ALA ALA PHE SER ILE CYS GLN LYS LYS ALA ASN SEQRES 11BB 132 LEU ARG SEQRES 1HH 230 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS SEQRES 2HH 230 PRO GLY ALA SER VAL LYS VAL SER CYS LYS VAL SER GLY SEQRES 3HH 230 TYR THR LEU THR GLU LEU SER MET HIS TRP VAL ARG GLN SEQRES 4HH 230 ALA PRO GLY LYS GLY LEU GLU TRP MET GLY GLY PHE ASP SEQRES 5HH 230 PRO GLU ASP PHE LYS TYR HIS THR HIS GLN LYS PHE GLN SEQRES 6HH 230 GLY ARG VAL THR MET THR GLU ASP THR SER THR ASP THR SEQRES 7HH 230 ALA TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8HH 230 ALA VAL TYR TYR CYS ALA LEU VAL TRP GLY THR GLN GLY SEQRES 9HH 230 LYS GLY VAL ARG GLY TRP ASP TYR TYR TYR GLY MET ASP SEQRES 10HH 230 VAL TRP GLY GLN GLY THR THR VAL THR VAL SER SER ALA SEQRES 11HH 230 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 12HH 230 SER UNK UNK UNK UNK UNK GLY THR ALA ALA LEU GLY CYS SEQRES 13HH 230 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 14HH 230 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 15HH 230 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 16HH 230 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 17HH 230 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 18HH 230 LYS VAL ASP LYS ARG VAL GLU PRO LYS SEQRES 1LL 216 GLN SER VAL VAL THR GLN PRO PRO SER VAL SER GLY ALA SEQRES 2LL 216 PRO GLY GLN ARG VAL THR ILE SER CYS THR GLY SER SER SEQRES 3LL 216 SER ASN ILE GLY ALA GLY TYR ASP VAL HIS TRP TYR GLN SEQRES 4LL 216 GLN LEU PRO GLY THR ALA PRO LYS LEU LEU ILE TYR GLY SEQRES 5LL 216 ASN SER ASN ARG PRO SER GLY VAL PRO ASP ARG PHE SER SEQRES 6LL 216 GLY SER LYS SER GLY THR SER ALA SER LEU ALA ILE THR SEQRES 7LL 216 GLY LEU GLN ALA GLU ASP GLU ALA ASP TYR TYR CYS GLN SEQRES 8LL 216 SER TYR ASP SER SER LEU SER GLY TRP VAL PHE GLY GLY SEQRES 9LL 216 GLY THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA SEQRES 10LL 216 PRO SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU SEQRES 11LL 216 GLN ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP SEQRES 12LL 216 PHE TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SEQRES 13LL 216 SER SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SEQRES 14LL 216 SER LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR SEQRES 15LL 216 LEU SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER SEQRES 16LL 216 TYR SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU SEQRES 17LL 216 LYS THR VAL ALA PRO THR GLU CYS HET GOL AA 301 6 HET GOL BB 301 6 HET GOL BB 302 6 HET GOL LL 301 6 HET GOL LL 302 6 HETNAM GOL GLYCEROL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 5 GOL 5(C3 H8 O3) FORMUL 10 HOH *436(H2 O) HELIX 1 AA1 ASNAA 163 LEUAA 174 1 12 HELIX 2 AA2 SERAA 183 ILEAA 194 1 12 HELIX 3 AA3 ASNBB 164 LEUBB 175 1 12 HELIX 4 AA4 SERBB 184 SERBB 196 1 13 HELIX 5 AA5 THRHH 28 LEUHH 32 5 5 HELIX 6 AA6 ARGHH 87 THRHH 91 5 5 HELIX 7 AA7 VALHH 107 GLYHH 109 5 3 HELIX 8 AA8 TRPHH 110 GLYHH 115 1 6 HELIX 9 AA9 SERHH 172 ALAHH 174 5 3 HELIX 10 AB1 SERHH 203 LEUHH 205 5 3 HELIX 11 AB2 LYSHH 217 ASNHH 220 5 4 HELIX 12 AB3 ASNLL 28 GLYLL 32 5 5 HELIX 13 AB4 GLNLL 81 GLULL 85 5 5 HELIX 14 AB5 SERLL 126 ALALL 132 1 7 HELIX 15 AB6 THRLL 186 HISLL 193 1 8 SHEET 1 AA1 4 ILEAA 148 HISAA 150 0 SHEET 2 AA1 4 ASNAA 153 PHEAA 157 -1 O TYRAA 155 N ILEAA 148 SHEET 3 AA1 4 PHEAA 260 LYSAA 266 -1 O CYSAA 263 N LEUAA 156 SHEET 4 AA1 4 LYSAA 177 LEUAA 178 -1 N LYSAA 177 O GLNAA 264 SHEET 1 AA2 7 ILEAA 148 HISAA 150 0 SHEET 2 AA2 7 ASNAA 153 PHEAA 157 -1 O TYRAA 155 N ILEAA 148 SHEET 3 AA2 7 PHEAA 260 LYSAA 266 -1 O CYSAA 263 N LEUAA 156 SHEET 4 AA2 7 PHEAA 201 ARGAA 207 1 N TRPAA 202 O PHEAA 260 SHEET 5 AA2 7 THRAA 241 GLNAA 246 -1 O ILEAA 245 N PHEAA 201 SHEET 6 AA2 7 ALAAA 249 ASNAA 254 -1 O GLUAA 253 N CYSAA 242 SHEET 7 AA2 7 VALAA 229 GLYAA 231 1 N ARGAA 230 O VALAA 250 SHEET 1 AA3 5 ILEBB 149 HISBB 151 0 SHEET 2 AA3 5 ASNBB 154 PHEBB 158 -1 O ASNBB 154 N HISBB 151 SHEET 3 AA3 5 PHEBB 261 LYSBB 267 -1 O LYSBB 266 N CYSBB 155 SHEET 4 AA3 5 PHEBB 202 ARGBB 208 1 N TRPBB 203 O PHEBB 261 SHEET 5 AA3 5 LEUBB 216 TRPBB 217 -1 O LEUBB 216 N SERBB 207 SHEET 1 AA4 6 LYSBB 178 LEUBB 179 0 SHEET 2 AA4 6 PHEBB 261 LYSBB 267 -1 O GLNBB 265 N LYSBB 178 SHEET 3 AA4 6 PHEBB 202 ARGBB 208 1 N TRPBB 203 O PHEBB 261 SHEET 4 AA4 6 THRBB 242 GLNBB 247 -1 O THRBB 242 N ARGBB 208 SHEET 5 AA4 6 ALABB 250 ASNBB 255 -1 O ALABB 250 N GLNBB 247 SHEET 6 AA4 6 VALBB 230 GLYBB 232 1 N ARGBB 231 O VALBB 251 SHEET 1 AA5 4 GLNHH 3 GLNHH 6 0 SHEET 2 AA5 4 VALHH 18 SERHH 25 -1 O LYSHH 23 N VALHH 5 SHEET 3 AA5 4 THRHH 78 LEUHH 83 -1 O ALAHH 79 N CYSHH 22 SHEET 4 AA5 4 VALHH 68 ASPHH 73 -1 N THRHH 69 O GLUHH 82 SHEET 1 AA6 6 GLUHH 10 LYSHH 12 0 SHEET 2 AA6 6 THRHH 123 VALHH 127 1 O THRHH 126 N LYSHH 12 SHEET 3 AA6 6 ALAHH 92 VALHH 99 -1 N TYRHH 94 O THRHH 123 SHEET 4 AA6 6 SERHH 33 GLNHH 39 -1 N VALHH 37 O TYRHH 95 SHEET 5 AA6 6 GLUHH 46 PHEHH 51 -1 O METHH 48 N TRPHH 36 SHEET 6 AA6 6 TYRHH 58 THRHH 60 -1 O HISHH 59 N GLYHH 50 SHEET 1 AA7 4 GLUHH 10 LYSHH 12 0 SHEET 2 AA7 4 THRHH 123 VALHH 127 1 O THRHH 126 N LYSHH 12 SHEET 3 AA7 4 ALAHH 92 VALHH 99 -1 N TYRHH 94 O THRHH 123 SHEET 4 AA7 4 VALHH 118 TRPHH 119 -1 O VALHH 118 N LEUHH 98 SHEET 1 AA8 4 SERHH 136 LEUHH 140 0 SHEET 2 AA8 4 THRHH 151 TYRHH 161 -1 O GLYHH 155 N LEUHH 140 SHEET 3 AA8 4 TYRHH 192 PROHH 201 -1 O LEUHH 194 N VALHH 158 SHEET 4 AA8 4 VALHH 179 THRHH 181 -1 N HISHH 180 O VALHH 197 SHEET 1 AA9 4 SERHH 136 LEUHH 140 0 SHEET 2 AA9 4 THRHH 151 TYRHH 161 -1 O GLYHH 155 N LEUHH 140 SHEET 3 AA9 4 TYRHH 192 PROHH 201 -1 O LEUHH 194 N VALHH 158 SHEET 4 AA9 4 VALHH 185 LEUHH 186 -1 N VALHH 185 O SERHH 193 SHEET 1 AB1 3 THRHH 167 TRPHH 170 0 SHEET 2 AB1 3 ILEHH 211 HISHH 216 -1 O ASNHH 213 N SERHH 169 SHEET 3 AB1 3 THRHH 221 ARGHH 226 -1 O VALHH 223 N VALHH 214 SHEET 1 AB2 5 SERLL 9 GLYLL 12 0 SHEET 2 AB2 5 THRLL 106 VALLL 110 1 O LYSLL 107 N VALLL 10 SHEET 3 AB2 5 ALALL 86 ASPLL 94 -1 N ALALL 86 O LEULL 108 SHEET 4 AB2 5 HISLL 36 GLNLL 40 -1 N GLNLL 40 O ASPLL 87 SHEET 5 AB2 5 LYSLL 47 ILELL 50 -1 O LEULL 49 N TRPLL 37 SHEET 1 AB3 4 SERLL 9 GLYLL 12 0 SHEET 2 AB3 4 THRLL 106 VALLL 110 1 O LYSLL 107 N VALLL 10 SHEET 3 AB3 4 ALALL 86 ASPLL 94 -1 N ALALL 86 O LEULL 108 SHEET 4 AB3 4 GLYLL 99 PHELL 102 -1 O GLYLL 99 N ASPLL 94 SHEET 1 AB4 3 VALLL 18 THRLL 23 0 SHEET 2 AB4 3 SERLL 72 ILELL 77 -1 O ALALL 73 N CYSLL 22 SHEET 3 AB4 3 PHELL 64 SERLL 69 -1 N SERLL 69 O SERLL 72 SHEET 1 AB5 4 SERLL 119 PHELL 123 0 SHEET 2 AB5 4 ALALL 135 PHELL 144 -1 O LEULL 140 N THRLL 121 SHEET 3 AB5 4 TYRLL 177 LEULL 185 -1 O ALALL 179 N ILELL 141 SHEET 4 AB5 4 VALLL 164 THRLL 166 -1 N GLULL 165 O TYRLL 182 SHEET 1 AB6 4 SERLL 119 PHELL 123 0 SHEET 2 AB6 4 ALALL 135 PHELL 144 -1 O LEULL 140 N THRLL 121 SHEET 3 AB6 4 TYRLL 177 LEULL 185 -1 O ALALL 179 N ILELL 141 SHEET 4 AB6 4 SERLL 170 LYSLL 171 -1 N SERLL 170 O ALALL 178 SHEET 1 AB7 4 SERLL 158 VALLL 160 0 SHEET 2 AB7 4 THRLL 150 ALALL 155 -1 N ALALL 155 O SERLL 158 SHEET 3 AB7 4 TYRLL 196 HISLL 202 -1 O THRLL 201 N THRLL 150 SHEET 4 AB7 4 SERLL 205 VALLL 211 -1 O VALLL 207 N VALLL 200 SSBOND 1 CYSAA 139 CYSBB 140 1555 1555 2.04 SSBOND 2 CYSAA 143 CYSAA 154 1555 1555 2.06 SSBOND 3 CYSAA 171 CYSAA 263 1555 1555 2.05 SSBOND 4 CYSAA 242 CYSAA 255 1555 1555 2.04 SSBOND 5 CYSBB 144 CYSBB 155 1555 1555 2.04 SSBOND 6 CYSBB 172 CYSBB 264 1555 1555 2.06 SSBOND 7 CYSBB 243 CYSBB 256 1555 1555 2.05 SSBOND 8 CYSHH 22 CYSHH 96 1555 1555 2.08 SSBOND 9 CYSHH 156 CYSHH 212 1555 1555 2.03 SSBOND 10 CYSLL 22 CYSLL 90 1555 1555 2.10 SSBOND 11 CYSLL 139 CYSLL 198 1555 1555 2.03 CISPEP 1 PHEHH 162 PROHH 163 0 -10.39 CISPEP 2 GLUHH 164 PROHH 165 0 -14.07 CISPEP 3 TYRLL 145 PROLL 146 0 -0.57 CRYST1 71.908 89.901 110.925 90.00 90.00 90.00 P 21 21 21 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 0.013907 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011123 0.000000 0.00000 SCALE3 0.000000 0.000000 0.009015 0.00000