HEADER HYDROLASE 11-SEP-18 6HLD
TITLE X-RAY STRUCTURE OF FURIN IN COMPLEX WITH THE CYCLIC PEPTIDE
TITLE 2 C[SUCCINYL-PHE-2-NAL-(ARG)3-LYS]-LYS-4-AMBA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FURIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DIBASIC-PROCESSING ENZYME,PAIRED BASIC AMINO ACID RESIDUE-
COMPND 5 CLEAVING ENZYME,PACE;
COMPND 6 EC: 3.4.21.75;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ALN-ARG-ARG-ARG-SLL-LYS-00S;
COMPND 10 CHAIN: B;
COMPND 11 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: FURIN, FUR, PACE, PCSK3;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 12 ORGANISM_TAXID: 32630
KEYWDS PROTEASE PROPROTEIN CONVERTASE INHIBITOR COMPLEX CYCLIC PEPTIDE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.O.DAHMS
REVDAT 4 24-JAN-24 6HLD 1 REMARK LINK
REVDAT 3 03-APR-19 6HLD 1 JRNL
REVDAT 2 27-FEB-19 6HLD 1 JRNL
REVDAT 1 06-FEB-19 6HLD 0
JRNL AUTH T.VAN LAM VAN,T.IVANOVA,K.HARDES,M.R.HEINDL,R.E.MORTY,
JRNL AUTH 2 E.BOTTCHER-FRIEBERTSHAUSER,I.LINDBERG,M.E.THAN,S.O.DAHMS,
JRNL AUTH 3 T.STEINMETZER
JRNL TITL DESIGN, SYNTHESIS, AND CHARACTERIZATION OF MACROCYCLIC
JRNL TITL 2 INHIBITORS OF THE PROPROTEIN CONVERTASE FURIN.
JRNL REF CHEMMEDCHEM V. 14 673 2019
JRNL REFN ESSN 1860-7187
JRNL PMID 30680958
JRNL DOI 10.1002/CMDC.201800807
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.56
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 48412
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 2376
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 46.5745 - 5.3971 0.99 2964 160 0.1834 0.1874
REMARK 3 2 5.3971 - 4.2848 1.00 2791 147 0.1352 0.1456
REMARK 3 3 4.2848 - 3.7434 0.99 2748 147 0.1304 0.1530
REMARK 3 4 3.7434 - 3.4013 1.00 2729 152 0.1447 0.1850
REMARK 3 5 3.4013 - 3.1575 1.00 2716 153 0.1665 0.1918
REMARK 3 6 3.1575 - 2.9714 1.00 2709 133 0.1748 0.1899
REMARK 3 7 2.9714 - 2.8226 1.00 2704 144 0.1879 0.2407
REMARK 3 8 2.8226 - 2.6998 1.00 2697 149 0.1858 0.2272
REMARK 3 9 2.6998 - 2.5958 0.99 2668 126 0.1849 0.2341
REMARK 3 10 2.5958 - 2.5063 1.00 2693 129 0.1878 0.2086
REMARK 3 11 2.5063 - 2.4279 0.99 2662 132 0.1912 0.2050
REMARK 3 12 2.4279 - 2.3585 0.99 2696 127 0.1838 0.2181
REMARK 3 13 2.3585 - 2.2964 0.99 2668 120 0.2034 0.2451
REMARK 3 14 2.2964 - 2.2404 0.99 2646 132 0.2004 0.2388
REMARK 3 15 2.2404 - 2.1895 0.99 2658 140 0.2140 0.2733
REMARK 3 16 2.1895 - 2.1429 0.99 2669 137 0.2348 0.2626
REMARK 3 17 2.1429 - 2.1000 0.99 2618 148 0.2570 0.3226
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.080
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 : 0.008 3806
REMARK 3 ANGLE : 0.871 5189
REMARK 3 CHIRALITY : 0.057 559
REMARK 3 PLANARITY : 0.006 686
REMARK 3 DIHEDRAL : 22.369 2276
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 6HLD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1200011801.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-18
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 : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.994211
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48535
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 46.570
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.3300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 6EQV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALLIZATION SOLUTION: 100MM MES,
REMARK 280 200MM K/NAH2PO4, PH 5.5-6.0, 2 M NACL, 3% DMSO; RESERVOIR
REMARK 280 SOLUTION: 3-4M NACL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 104.91667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 52.45833
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 78.68750
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 26.22917
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 131.14583
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 104.91667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 52.45833
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 26.22917
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 78.68750
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 131.14583
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 NA NA A 606 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1036 LIES ON A SPECIAL POSITION.
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 108
REMARK 465 ARG A 581
REMARK 465 GLY A 582
REMARK 465 SER A 583
REMARK 465 HIS A 584
REMARK 465 HIS A 585
REMARK 465 HIS A 586
REMARK 465 HIS A 587
REMARK 465 HIS A 588
REMARK 465 HIS A 589
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 SLL B 5 CK CL CP CX OX OP1 OP2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 VAL A 109 CG1 CG2
REMARK 480 GLN A 111 OE1 NE2
REMARK 480 VAL A 127 CG1 CG2
REMARK 480 GLN A 129 CG CD OE1 NE2
REMARK 480 GLN A 178 OE1 NE2
REMARK 480 LYS A 261 NZ
REMARK 480 ARG A 298 CZ NH1 NH2
REMARK 480 LYS A 386 NZ
REMARK 480 LYS A 419 CE NZ
REMARK 480 LYS A 463 CD CE NZ
REMARK 480 ARG A 468 CZ NH1 NH2
REMARK 480 GLU A 556 CD OE1 OE2
REMARK 480 LEU A 578 CD1 CD2
REMARK 480 PRO A 580 C O
REMARK 480 ALN B 1 CG1 CD1 CE1 CD2 CE2 CZ1 CG2
REMARK 480 ALN B 1 CD3 CE3 CZ2
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 GLN A 129 -0.63 85.06
REMARK 500 ASP A 153 -141.39 -161.68
REMARK 500 ASN A 192 43.35 -92.96
REMARK 500 ALA A 203 32.96 -146.49
REMARK 500 CYS A 211 -132.06 49.19
REMARK 500 ALA A 216 73.22 -115.98
REMARK 500 MET A 226 -9.11 -140.69
REMARK 500 SER A 253 52.65 -109.63
REMARK 500 ASP A 258 46.91 -93.85
REMARK 500 SER A 342 -154.67 -152.50
REMARK 500 GLN A 350 -162.60 -124.31
REMARK 500 GLU A 485 -103.61 -113.04
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 CA A 602 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 115 OD2
REMARK 620 2 ASP A 162 OD1 149.0
REMARK 620 3 ASP A 162 OD2 158.5 51.8
REMARK 620 4 VAL A 205 O 89.8 86.4 99.7
REMARK 620 5 ASN A 208 OD1 73.2 76.0 125.5 90.0
REMARK 620 6 VAL A 210 O 93.0 90.3 78.3 176.6 88.9
REMARK 620 7 GLY A 212 O 81.7 128.8 79.5 87.8 154.8 94.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 174 OD2
REMARK 620 2 ASP A 179 OD1 101.4
REMARK 620 3 ASP A 179 OD2 87.9 49.4
REMARK 620 4 ASP A 181 O 92.6 72.1 120.2
REMARK 620 5 HOH A 755 O 94.2 150.3 157.5 82.2
REMARK 620 6 HOH A 871 O 84.8 125.2 76.9 162.6 80.9
REMARK 620 7 HOH A 959 O 171.4 86.2 94.2 93.5 80.7 87.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 603 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 258 OD1
REMARK 620 2 ASP A 301 OD2 94.6
REMARK 620 3 GLU A 331 OE1 74.6 91.9
REMARK 620 4 GLU A 331 OE2 126.2 84.3 51.8
REMARK 620 5 HOH A 750 O 146.0 81.5 138.9 87.2
REMARK 620 6 HOH A 770 O 101.8 163.4 89.7 83.8 86.4
REMARK 620 7 HOH A 866 O 72.8 94.8 147.2 161.0 73.9 92.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 605 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 279 O
REMARK 620 2 GLY A 284 O 87.9
REMARK 620 3 HOH A 763 O 89.4 166.2
REMARK 620 4 HOH A 769 O 91.8 75.5 118.1
REMARK 620 5 HOH A 996 O 95.2 83.0 83.8 157.1
REMARK 620 6 HOH A1011 O 176.6 89.8 93.4 85.2 86.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 604 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 309 O
REMARK 620 2 SER A 311 O 101.7
REMARK 620 3 THR A 314 O 160.7 94.7
REMARK 620 4 THR A 314 OG1 95.9 91.7 73.5
REMARK 620 5 HOH A 809 O 101.7 123.5 76.9 135.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 606 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 544 O
REMARK 620 2 SER A 544 O 0.0
REMARK 620 3 HOH A 787 O 86.7 86.7
REMARK 620 4 HOH A 787 O 92.2 92.2 152.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 610
DBREF 6HLD A 108 574 UNP P09958 FURIN_HUMAN 108 574
DBREF 6HLD B 1 7 PDB 6HLD 6HLD 1 7
SEQADV 6HLD SER A 575 UNP P09958 EXPRESSION TAG
SEQADV 6HLD GLY A 576 UNP P09958 EXPRESSION TAG
SEQADV 6HLD SER A 577 UNP P09958 EXPRESSION TAG
SEQADV 6HLD LEU A 578 UNP P09958 EXPRESSION TAG
SEQADV 6HLD VAL A 579 UNP P09958 EXPRESSION TAG
SEQADV 6HLD PRO A 580 UNP P09958 EXPRESSION TAG
SEQADV 6HLD ARG A 581 UNP P09958 EXPRESSION TAG
SEQADV 6HLD GLY A 582 UNP P09958 EXPRESSION TAG
SEQADV 6HLD SER A 583 UNP P09958 EXPRESSION TAG
SEQADV 6HLD HIS A 584 UNP P09958 EXPRESSION TAG
SEQADV 6HLD HIS A 585 UNP P09958 EXPRESSION TAG
SEQADV 6HLD HIS A 586 UNP P09958 EXPRESSION TAG
SEQADV 6HLD HIS A 587 UNP P09958 EXPRESSION TAG
SEQADV 6HLD HIS A 588 UNP P09958 EXPRESSION TAG
SEQADV 6HLD HIS A 589 UNP P09958 EXPRESSION TAG
SEQRES 1 A 482 ASP VAL TYR GLN GLU PRO THR ASP PRO LYS PHE PRO GLN
SEQRES 2 A 482 GLN TRP TYR LEU SER GLY VAL THR GLN ARG ASP LEU ASN
SEQRES 3 A 482 VAL LYS ALA ALA TRP ALA GLN GLY TYR THR GLY HIS GLY
SEQRES 4 A 482 ILE VAL VAL SER ILE LEU ASP ASP GLY ILE GLU LYS ASN
SEQRES 5 A 482 HIS PRO ASP LEU ALA GLY ASN TYR ASP PRO GLY ALA SER
SEQRES 6 A 482 PHE ASP VAL ASN ASP GLN ASP PRO ASP PRO GLN PRO ARG
SEQRES 7 A 482 TYR THR GLN MET ASN ASP ASN ARG HIS GLY THR ARG CYS
SEQRES 8 A 482 ALA GLY GLU VAL ALA ALA VAL ALA ASN ASN GLY VAL CYS
SEQRES 9 A 482 GLY VAL GLY VAL ALA TYR ASN ALA ARG ILE GLY GLY VAL
SEQRES 10 A 482 ARG MET LEU ASP GLY GLU VAL THR ASP ALA VAL GLU ALA
SEQRES 11 A 482 ARG SER LEU GLY LEU ASN PRO ASN HIS ILE HIS ILE TYR
SEQRES 12 A 482 SER ALA SER TRP GLY PRO GLU ASP ASP GLY LYS THR VAL
SEQRES 13 A 482 ASP GLY PRO ALA ARG LEU ALA GLU GLU ALA PHE PHE ARG
SEQRES 14 A 482 GLY VAL SER GLN GLY ARG GLY GLY LEU GLY SER ILE PHE
SEQRES 15 A 482 VAL TRP ALA SER GLY ASN GLY GLY ARG GLU HIS ASP SER
SEQRES 16 A 482 CYS ASN CYS ASP GLY TYR THR ASN SER ILE TYR THR LEU
SEQRES 17 A 482 SER ILE SER SER ALA THR GLN PHE GLY ASN VAL PRO TRP
SEQRES 18 A 482 TYR SER GLU ALA CYS SER SER THR LEU ALA THR THR TYR
SEQRES 19 A 482 SER SER GLY ASN GLN ASN GLU LYS GLN ILE VAL THR THR
SEQRES 20 A 482 ASP LEU ARG GLN LYS CYS THR GLU SER HIS THR GLY THR
SEQRES 21 A 482 SER ALA SER ALA PRO LEU ALA ALA GLY ILE ILE ALA LEU
SEQRES 22 A 482 THR LEU GLU ALA ASN LYS ASN LEU THR TRP ARG ASP MET
SEQRES 23 A 482 GLN HIS LEU VAL VAL GLN THR SER LYS PRO ALA HIS LEU
SEQRES 24 A 482 ASN ALA ASN ASP TRP ALA THR ASN GLY VAL GLY ARG LYS
SEQRES 25 A 482 VAL SER HIS SER TYR GLY TYR GLY LEU LEU ASP ALA GLY
SEQRES 26 A 482 ALA MET VAL ALA LEU ALA GLN ASN TRP THR THR VAL ALA
SEQRES 27 A 482 PRO GLN ARG LYS CYS ILE ILE ASP ILE LEU THR GLU PRO
SEQRES 28 A 482 LYS ASP ILE GLY LYS ARG LEU GLU VAL ARG LYS THR VAL
SEQRES 29 A 482 THR ALA CYS LEU GLY GLU PRO ASN HIS ILE THR ARG LEU
SEQRES 30 A 482 GLU HIS ALA GLN ALA ARG LEU THR LEU SER TYR ASN ARG
SEQRES 31 A 482 ARG GLY ASP LEU ALA ILE HIS LEU VAL SER PRO MET GLY
SEQRES 32 A 482 THR ARG SER THR LEU LEU ALA ALA ARG PRO HIS ASP TYR
SEQRES 33 A 482 SER ALA ASP GLY PHE ASN ASP TRP ALA PHE MET THR THR
SEQRES 34 A 482 HIS SER TRP ASP GLU ASP PRO SER GLY GLU TRP VAL LEU
SEQRES 35 A 482 GLU ILE GLU ASN THR SER GLU ALA ASN ASN TYR GLY THR
SEQRES 36 A 482 LEU THR LYS PHE THR LEU VAL LEU TYR GLY THR ALA SER
SEQRES 37 A 482 GLY SER LEU VAL PRO ARG GLY SER HIS HIS HIS HIS HIS
SEQRES 38 A 482 HIS
SEQRES 1 B 7 ALN ARG ARG ARG SLL LYS 00S
HET ALN B 1 15
HET SLL B 5 9
HET 00S B 7 11
HET CA A 601 1
HET CA A 602 1
HET CA A 603 1
HET NA A 604 1
HET NA A 605 1
HET NA A 606 1
HET CL A 607 1
HET PO4 A 608 5
HET PO4 A 609 5
HET DMS A 610 4
HETNAM ALN NAPHTHALEN-2-YL-3-ALANINE
HETNAM SLL (2S)-2-AZANYL-6-[(4-HYDROXY-4-OXO-BUTANOYL)
HETNAM 2 SLL AMINO]HEXANOIC ACID
HETNAM 00S 4-(AMINOMETHYL)BENZENECARBOXIMIDAMIDE
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM CL CHLORIDE ION
HETNAM PO4 PHOSPHATE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN SLL 6-N-SUCCINYL-L-LYSINE
FORMUL 2 ALN C13 H13 N O2
FORMUL 2 SLL C10 H18 N2 O5
FORMUL 2 00S C8 H11 N3
FORMUL 3 CA 3(CA 2+)
FORMUL 6 NA 3(NA 1+)
FORMUL 9 CL CL 1-
FORMUL 10 PO4 2(O4 P 3-)
FORMUL 12 DMS C2 H6 O S
FORMUL 13 HOH *343(H2 O)
HELIX 1 AA1 LYS A 117 GLN A 121 5 5
HELIX 2 AA2 ASN A 133 GLN A 140 1 8
HELIX 3 AA3 LEU A 163 TYR A 167 5 5
HELIX 4 AA4 ASP A 168 SER A 172 5 5
HELIX 5 AA5 ASN A 190 ASN A 192 5 3
HELIX 6 AA6 ARG A 193 ALA A 204 1 12
HELIX 7 AA7 THR A 232 GLY A 241 1 10
HELIX 8 AA8 ALA A 267 GLY A 281 1 15
HELIX 9 AA9 ARG A 282 LEU A 285 5 4
HELIX 10 AB1 GLY A 296 HIS A 300 5 5
HELIX 11 AB2 SER A 302 ASP A 306 5 5
HELIX 12 AB3 GLY A 366 ASN A 385 1 20
HELIX 13 AB4 THR A 389 SER A 401 1 13
HELIX 14 AB5 ASP A 430 GLN A 439 1 10
HELIX 15 AB6 ARG A 497 GLY A 499 5 3
SHEET 1 AA1 7 PHE A 173 ASP A 174 0
SHEET 2 AA1 7 ARG A 220 ARG A 225 1 O ARG A 225 N PHE A 173
SHEET 3 AA1 7 VAL A 148 ASP A 153 1 N ILE A 151 O VAL A 224
SHEET 4 AA1 7 ILE A 249 ALA A 252 1 O ILE A 249 N SER A 150
SHEET 5 AA1 7 ILE A 288 ALA A 292 1 O ILE A 288 N TYR A 250
SHEET 6 AA1 7 THR A 314 ALA A 320 1 O LEU A 315 N PHE A 289
SHEET 7 AA1 7 ALA A 338 TYR A 341 1 O ALA A 338 N SER A 318
SHEET 1 AA2 2 ILE A 351 ASP A 355 0
SHEET 2 AA2 2 LYS A 359 HIS A 364 -1 O LYS A 359 N ASP A 355
SHEET 1 AA3 2 ALA A 412 THR A 413 0
SHEET 2 AA3 2 LYS A 419 VAL A 420 -1 O VAL A 420 N ALA A 412
SHEET 1 AA4 3 ARG A 448 ASP A 453 0
SHEET 2 AA4 3 GLY A 561 THR A 573 -1 O GLY A 572 N ARG A 448
SHEET 3 AA4 3 LYS A 459 ASP A 460 -1 N LYS A 459 O LEU A 563
SHEET 1 AA5 4 ARG A 448 ASP A 453 0
SHEET 2 AA5 4 GLY A 561 THR A 573 -1 O GLY A 572 N ARG A 448
SHEET 3 AA5 4 ARG A 483 TYR A 495 -1 N GLU A 485 O TYR A 571
SHEET 4 AA5 4 PHE A 528 THR A 535 -1 O THR A 535 N ALA A 487
SHEET 1 AA6 4 ARG A 464 VAL A 471 0
SHEET 2 AA6 4 GLY A 545 ASN A 553 -1 O TRP A 547 N LYS A 469
SHEET 3 AA6 4 LEU A 501 VAL A 506 -1 N HIS A 504 O GLU A 550
SHEET 4 AA6 4 ARG A 512 LEU A 516 -1 O SER A 513 N LEU A 505
SSBOND 1 CYS A 211 CYS A 360 1555 1555 2.05
SSBOND 2 CYS A 303 CYS A 333 1555 1555 2.06
SSBOND 3 CYS A 450 CYS A 474 1555 1555 2.07
LINK C ALN B 1 N ARG B 2 1555 1555 1.35
LINK C ARG B 4 N SLL B 5 1555 1555 1.35
LINK C SLL B 5 N LYS B 6 1555 1555 1.35
LINK C LYS B 6 N23 00S B 7 1555 1555 1.35
LINK OD2 ASP A 115 CA CA A 602 1555 1555 2.38
LINK OD1 ASP A 162 CA CA A 602 1555 1555 2.43
LINK OD2 ASP A 162 CA CA A 602 1555 1555 2.58
LINK OD2 ASP A 174 CA CA A 601 1555 1555 2.47
LINK OD1 ASP A 179 CA CA A 601 1555 1555 2.67
LINK OD2 ASP A 179 CA CA A 601 1555 1555 2.56
LINK O ASP A 181 CA CA A 601 1555 1555 2.50
LINK O VAL A 205 CA CA A 602 1555 1555 2.34
LINK OD1 ASN A 208 CA CA A 602 1555 1555 2.66
LINK O VAL A 210 CA CA A 602 1555 1555 2.31
LINK O GLY A 212 CA CA A 602 1555 1555 2.41
LINK OD1 ASP A 258 CA CA A 603 1555 1555 2.40
LINK O SER A 279 NA NA A 605 1555 1555 2.42
LINK O GLY A 284 NA NA A 605 1555 1555 2.77
LINK OD2 ASP A 301 CA CA A 603 1555 1555 2.41
LINK O THR A 309 NA NA A 604 1555 1555 2.43
LINK O SER A 311 NA NA A 604 1555 1555 2.32
LINK O THR A 314 NA NA A 604 1555 1555 2.46
LINK OG1 THR A 314 NA NA A 604 1555 1555 2.56
LINK OE1 GLU A 331 CA CA A 603 1555 1555 2.55
LINK OE2 GLU A 331 CA CA A 603 1555 1555 2.50
LINK O SER A 544 NA NA A 606 1555 1555 2.21
LINK O SER A 544 NA NA A 606 1555 9555 2.21
LINK CA CA A 601 O HOH A 755 1555 1555 2.36
LINK CA CA A 601 O HOH A 871 1555 1555 2.36
LINK CA CA A 601 O HOH A 959 1555 1555 2.51
LINK CA CA A 603 O HOH A 750 1555 1555 2.49
LINK CA CA A 603 O HOH A 770 1555 1555 2.41
LINK CA CA A 603 O HOH A 866 1555 1555 2.54
LINK NA NA A 604 O HOH A 809 1555 1555 2.53
LINK NA NA A 605 O HOH A 763 1555 10555 2.45
LINK NA NA A 605 O HOH A 769 1555 1555 2.49
LINK NA NA A 605 O HOH A 996 1555 1555 2.62
LINK NA NA A 605 O HOH A1011 1555 1555 2.63
LINK NA NA A 606 O HOH A 787 1555 1555 2.42
LINK NA NA A 606 O HOH A 787 1555 9555 2.43
SITE 1 AC1 6 ASP A 174 ASP A 179 ASP A 181 HOH A 755
SITE 2 AC1 6 HOH A 871 HOH A 959
SITE 1 AC2 6 ASP A 115 ASP A 162 VAL A 205 ASN A 208
SITE 2 AC2 6 VAL A 210 GLY A 212
SITE 1 AC3 6 ASP A 258 ASP A 301 GLU A 331 HOH A 750
SITE 2 AC3 6 HOH A 770 HOH A 866
SITE 1 AC4 4 THR A 309 SER A 311 THR A 314 HOH A 809
SITE 1 AC5 6 SER A 279 GLY A 284 HOH A 763 HOH A 769
SITE 2 AC5 6 HOH A 996 HOH A1011
SITE 1 AC6 2 SER A 544 HOH A 787
SITE 1 AC7 3 ARG A 276 LYS A 449 TYR A 571
SITE 1 AC8 3 PHE A 118 GLN A 121 SER A 125
SITE 1 AC9 6 VAL A 326 GLN A 346 ASN A 347 ALA A 408
SITE 2 AC9 6 ASN A 409 HOH A 848
SITE 1 AD1 5 VAL A 263 GLY A 527 PHE A 528 ASN A 529
SITE 2 AD1 5 HOH A 749
CRYST1 133.395 133.395 157.375 90.00 90.00 120.00 P 65 2 2 12
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 0.007497 0.004328 0.000000 0.00000
SCALE2 0.000000 0.008656 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006354 0.00000
(ATOM LINES ARE NOT SHOWN.)
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