HEADER HYDROLASE 29-MAR-15 4Z2A
TITLE CRYSTAL STRUCTURE OF UNGLYCOSYLATED APO HUMAN FURIN @1.89A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FURIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 110-74;
COMPND 5 SYNONYM: DIBASIC-PROCESSING ENZYME,PAIRED BASIC AMINO ACID RESIDUE-
COMPND 6 CLEAVING ENZYME,PACE;
COMPND 7 EC: 3.4.21.75;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: 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: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS UNGLYCOSYLATED, APO, SERINE PROTEINASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.T.GAMPE,K.PEARCE,R.REID
REVDAT 3 27-SEP-23 4Z2A 1 LINK
REVDAT 2 17-APR-19 4Z2A 1 JRNL REMARK
REVDAT 1 04-MAY-16 4Z2A 0
JRNL AUTH K.H.PEARCE,L.K.OVERTON,R.T.GRAMPE,G.B.BARRET,J.D.TAYLOR,
JRNL AUTH 2 D.D.MCKEE,N.CAMPOBASSOM,R.T.NOLTE,R.A.REID
JRNL TITL BACMAM PRODUCTION AND CRYSTAL STRUCTURE OF NONGLYCOSYLATED
JRNL TITL 2 APO HUMAN FURIN AT 1.89A RESOLUTION
JRNL REF ACTA CRYSTALLOGR.,SECT.F 2019
JRNL REFN ESSN 2053-230X
JRNL DOI S2053230X1900178X
REMARK 2
REMARK 2 RESOLUTION. 1.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 37664
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.110
REMARK 3 FREE R VALUE TEST SET COUNT : 1173
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 29.5845 - 3.7778 1.00 4663 176 0.1380 0.1360
REMARK 3 2 3.7778 - 2.9995 1.00 4568 156 0.1434 0.1921
REMARK 3 3 2.9995 - 2.6206 1.00 4567 154 0.1480 0.1871
REMARK 3 4 2.6206 - 2.3811 1.00 4561 154 0.1475 0.1848
REMARK 3 5 2.3811 - 2.2105 0.99 4528 138 0.1670 0.2110
REMARK 3 6 2.2105 - 2.0802 1.00 4557 131 0.1389 0.2146
REMARK 3 7 2.0802 - 1.9761 1.00 4561 135 0.1498 0.2265
REMARK 3 8 1.9761 - 1.8900 0.99 4486 129 0.1736 0.2097
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.380
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.83
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.00
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 4Z2A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000208481.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37707
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.890
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.14800
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: NULL
REMARK 200 STARTING MODEL: 1P8J
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: WELL 13% PEG 8K, 0.110M K-DIHYDROGEN
REMARK 280 PHOSPHATE, 0.1M HEPES PH 7.5, 350 UL PROTEIN WITH 350UL WELL
REMARK 280 DROPS, MRC SITTING DROP, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
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 47.99150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.29850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 47.99150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.29850
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 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 GLN A 111 CG CD OE1 NE2
REMARK 470 VAL A 127 CG1 CG2
REMARK 470 GLN A 129 CG CD OE1 NE2
REMARK 470 ARG A 130 CZ NH1 NH2
REMARK 470 LYS A 349 CE NZ
REMARK 470 LYS A 386 CD CE NZ
REMARK 470 HIS A 405 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 483 CD NE CZ NH1 NH2
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 NH2 ARG A 193 O2 PO4 A 606 1.95
REMARK 500 O HOH A 1045 O HOH A 1073 2.05
REMARK 500 O HOH A 757 O HOH A 808 2.17
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 VAL A 127 54.69 -140.72
REMARK 500 GLN A 129 -20.11 78.07
REMARK 500 ASP A 153 -137.46 -160.98
REMARK 500 ALA A 203 23.26 -148.36
REMARK 500 CYS A 211 -130.37 45.13
REMARK 500 CYS A 211 -132.37 48.36
REMARK 500 ALA A 216 70.90 -112.40
REMARK 500 MET A 226 -10.21 -143.34
REMARK 500 ASN A 243 58.70 33.95
REMARK 500 SER A 253 24.35 -141.30
REMARK 500 SER A 342 -153.58 -148.93
REMARK 500 GLN A 350 -161.50 -121.85
REMARK 500 GLU A 485 -104.23 -109.16
REMARK 500 ASP A 540 -5.11 74.69
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 601 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 115 OD2
REMARK 620 2 ASP A 162 OD1 153.9
REMARK 620 3 ASP A 162 OD2 153.6 52.2
REMARK 620 4 VAL A 205 O 92.5 84.6 95.9
REMARK 620 5 ASN A 208 OD1 77.0 77.0 127.8 89.9
REMARK 620 6 VAL A 210 O 93.4 90.6 78.1 173.9 92.7
REMARK 620 7 GLY A 212 O 83.4 122.3 71.9 88.3 160.3 91.1
REMARK 620 N 1 2 3 4 5 6
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 174 OD2
REMARK 620 2 ASP A 179 OD1 81.7
REMARK 620 3 ASP A 179 OD2 110.0 48.6
REMARK 620 4 ASP A 181 O 89.8 118.4 79.4
REMARK 620 5 HOH A 745 O 86.4 154.4 156.4 84.0
REMARK 620 6 HOH A 864 O 91.1 66.9 105.1 174.8 90.9
REMARK 620 7 HOH A1047 O 164.4 106.3 84.9 97.7 80.8 80.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 604 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 258 OD1
REMARK 620 2 ASP A 301 OD2 99.5
REMARK 620 3 GLU A 331 OE1 130.8 82.7
REMARK 620 4 GLU A 331 OE2 77.3 89.4 53.5
REMARK 620 5 HOH A 777 O 94.2 165.8 85.7 90.2
REMARK 620 6 HOH A 925 O 74.9 94.8 154.2 152.3 92.1
REMARK 620 7 HOH A1001 O 148.8 77.6 80.1 133.2 92.4 74.4
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 THR A 309 O
REMARK 620 2 SER A 311 O 99.1
REMARK 620 3 THR A 314 O 163.1 87.7
REMARK 620 4 THR A 314 OG1 86.6 81.9 78.9
REMARK 620 5 SER A 316 OG 67.8 163.5 102.4 87.1
REMARK 620 6 HOH A 788 O 112.8 115.6 77.4 149.7 79.7
REMARK 620 N 1 2 3 4 5
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 CA A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 607
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P8J RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GLYCOSYLATED MOUSE FURIN
REMARK 900 RELATED ID: 4OMC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF GLYCOSYLATED HUMAN FURIN
DBREF 4Z2A A 110 574 UNP P09958 FURIN_HUMAN 110 574
SEQADV 4Z2A ASP A 387 UNP P09958 ASN 387 ENGINEERED MUTATION
SEQADV 4Z2A ASP A 440 UNP P09958 ASN 440 ENGINEERED MUTATION
SEQRES 1 A 465 TYR GLN GLU PRO THR ASP PRO LYS PHE PRO GLN GLN TRP
SEQRES 2 A 465 TYR LEU SER GLY VAL THR GLN ARG ASP LEU ASN VAL LYS
SEQRES 3 A 465 ALA ALA TRP ALA GLN GLY TYR THR GLY HIS GLY ILE VAL
SEQRES 4 A 465 VAL SER ILE LEU ASP ASP GLY ILE GLU LYS ASN HIS PRO
SEQRES 5 A 465 ASP LEU ALA GLY ASN TYR ASP PRO GLY ALA SER PHE ASP
SEQRES 6 A 465 VAL ASN ASP GLN ASP PRO ASP PRO GLN PRO ARG TYR THR
SEQRES 7 A 465 GLN MET ASN ASP ASN ARG HIS GLY THR ARG CYS ALA GLY
SEQRES 8 A 465 GLU VAL ALA ALA VAL ALA ASN ASN GLY VAL CYS GLY VAL
SEQRES 9 A 465 GLY VAL ALA TYR ASN ALA ARG ILE GLY GLY VAL ARG MET
SEQRES 10 A 465 LEU ASP GLY GLU VAL THR ASP ALA VAL GLU ALA ARG SER
SEQRES 11 A 465 LEU GLY LEU ASN PRO ASN HIS ILE HIS ILE TYR SER ALA
SEQRES 12 A 465 SER TRP GLY PRO GLU ASP ASP GLY LYS THR VAL ASP GLY
SEQRES 13 A 465 PRO ALA ARG LEU ALA GLU GLU ALA PHE PHE ARG GLY VAL
SEQRES 14 A 465 SER GLN GLY ARG GLY GLY LEU GLY SER ILE PHE VAL TRP
SEQRES 15 A 465 ALA SER GLY ASN GLY GLY ARG GLU HIS ASP SER CYS ASN
SEQRES 16 A 465 CYS ASP GLY TYR THR ASN SER ILE TYR THR LEU SER ILE
SEQRES 17 A 465 SER SER ALA THR GLN PHE GLY ASN VAL PRO TRP TYR SER
SEQRES 18 A 465 GLU ALA CYS SER SER THR LEU ALA THR THR TYR SER SER
SEQRES 19 A 465 GLY ASN GLN ASN GLU LYS GLN ILE VAL THR THR ASP LEU
SEQRES 20 A 465 ARG GLN LYS CYS THR GLU SER HIS THR GLY THR SER ALA
SEQRES 21 A 465 SER ALA PRO LEU ALA ALA GLY ILE ILE ALA LEU THR LEU
SEQRES 22 A 465 GLU ALA ASN LYS ASP LEU THR TRP ARG ASP MET GLN HIS
SEQRES 23 A 465 LEU VAL VAL GLN THR SER LYS PRO ALA HIS LEU ASN ALA
SEQRES 24 A 465 ASN ASP TRP ALA THR ASN GLY VAL GLY ARG LYS VAL SER
SEQRES 25 A 465 HIS SER TYR GLY TYR GLY LEU LEU ASP ALA GLY ALA MET
SEQRES 26 A 465 VAL ALA LEU ALA GLN ASP TRP THR THR VAL ALA PRO GLN
SEQRES 27 A 465 ARG LYS CYS ILE ILE ASP ILE LEU THR GLU PRO LYS ASP
SEQRES 28 A 465 ILE GLY LYS ARG LEU GLU VAL ARG LYS THR VAL THR ALA
SEQRES 29 A 465 CYS LEU GLY GLU PRO ASN HIS ILE THR ARG LEU GLU HIS
SEQRES 30 A 465 ALA GLN ALA ARG LEU THR LEU SER TYR ASN ARG ARG GLY
SEQRES 31 A 465 ASP LEU ALA ILE HIS LEU VAL SER PRO MET GLY THR ARG
SEQRES 32 A 465 SER THR LEU LEU ALA ALA ARG PRO HIS ASP TYR SER ALA
SEQRES 33 A 465 ASP GLY PHE ASN ASP TRP ALA PHE MET THR THR HIS SER
SEQRES 34 A 465 TRP ASP GLU ASP PRO SER GLY GLU TRP VAL LEU GLU ILE
SEQRES 35 A 465 GLU ASN THR SER GLU ALA ASN ASN TYR GLY THR LEU THR
SEQRES 36 A 465 LYS PHE THR LEU VAL LEU TYR GLY THR ALA
HET CA A 601 1
HET CA A 602 1
HET CA A 603 1
HET CA A 604 1
HET PO4 A 605 5
HET PO4 A 606 5
HET EDO A 607 4
HETNAM CA CALCIUM ION
HETNAM PO4 PHOSPHATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 CA 4(CA 2+)
FORMUL 6 PO4 2(O4 P 3-)
FORMUL 8 EDO C2 H6 O2
FORMUL 9 HOH *408(H2 O)
HELIX 1 AA1 GLN A 121 GLY A 126 1 6
HELIX 2 AA2 VAL A 134 GLN A 140 1 7
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 ARG A 193 ALA A 204 1 12
HELIX 6 AA6 THR A 232 GLY A 241 1 10
HELIX 7 AA7 ALA A 267 GLY A 281 1 15
HELIX 8 AA8 ARG A 282 LEU A 285 5 4
HELIX 9 AA9 GLY A 296 HIS A 300 5 5
HELIX 10 AB1 SER A 302 ASP A 306 5 5
HELIX 11 AB2 GLY A 366 SER A 368 5 3
HELIX 12 AB3 ALA A 369 ASN A 385 1 17
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 SER A 251 N LEU A 152
SHEET 5 AA1 7 ILE A 288 ALA A 292 1 O VAL A 290 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 LEU A 568 N ILE A 452
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 LEU A 568 N ILE A 452
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 LEU A 549 N VAL A 467
SHEET 3 AA6 4 LEU A 501 VAL A 506 -1 N VAL A 506 O VAL A 548
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 2.04
SSBOND 3 CYS A 450 CYS A 474 1555 1555 2.06
LINK OD2 ASP A 115 CA CA A 601 1555 1555 2.23
LINK OD1 ASP A 162 CA CA A 601 1555 1555 2.31
LINK OD2 ASP A 162 CA CA A 601 1555 1555 2.64
LINK OD2 ASP A 174 CA CA A 602 1555 1555 2.38
LINK OD1 ASP A 179 CA CA A 602 1555 1555 2.68
LINK OD2 ASP A 179 CA CA A 602 1555 1555 2.64
LINK O ASP A 181 CA CA A 602 1555 1555 2.30
LINK O VAL A 205 CA CA A 601 1555 1555 2.31
LINK OD1 ASN A 208 CA CA A 601 1555 1555 2.49
LINK O VAL A 210 CA CA A 601 1555 1555 2.31
LINK O GLY A 212 CA CA A 601 1555 1555 2.38
LINK OD1 ASP A 258 CA CA A 604 1555 1555 2.28
LINK OD2 ASP A 301 CA CA A 604 1555 1555 2.29
LINK O THR A 309 CA CA A 603 1555 1555 2.40
LINK O SER A 311 CA CA A 603 1555 1555 2.48
LINK O THR A 314 CA CA A 603 1555 1555 2.38
LINK OG1 THR A 314 CA CA A 603 1555 1555 2.48
LINK OG SER A 316 CA CA A 603 1555 1555 2.63
LINK OE1 GLU A 331 CA CA A 604 1555 1555 2.52
LINK OE2 GLU A 331 CA CA A 604 1555 1555 2.41
LINK CA CA A 602 O HOH A 745 1555 1555 2.40
LINK CA CA A 602 O HOH A 864 1555 1555 2.29
LINK CA CA A 602 O HOH A1047 1555 1555 2.32
LINK CA CA A 603 O HOH A 788 1555 1555 2.58
LINK CA CA A 604 O HOH A 777 1555 1555 2.39
LINK CA CA A 604 O HOH A 925 1555 1555 2.40
LINK CA CA A 604 O HOH A1001 1555 1555 2.46
SITE 1 AC1 6 ASP A 115 ASP A 162 VAL A 205 ASN A 208
SITE 2 AC1 6 VAL A 210 GLY A 212
SITE 1 AC2 6 ASP A 174 ASP A 179 ASP A 181 HOH A 745
SITE 2 AC2 6 HOH A 864 HOH A1047
SITE 1 AC3 5 THR A 309 SER A 311 THR A 314 SER A 316
SITE 2 AC3 5 HOH A 788
SITE 1 AC4 6 ASP A 258 ASP A 301 GLU A 331 HOH A 777
SITE 2 AC4 6 HOH A 925 HOH A1001
SITE 1 AC5 7 ARG A 193 HIS A 194 ARG A 197 SER A 363
SITE 2 AC5 7 HIS A 364 THR A 365 PO4 A 606
SITE 1 AC6 6 ARG A 193 ARG A 197 HIS A 300 SER A 363
SITE 2 AC6 6 HIS A 521 PO4 A 605
SITE 1 AC7 5 ARG A 298 TRP A 328 THR A 365 GLY A 366
SITE 2 AC7 5 HOH A 950
CRYST1 95.983 66.597 88.443 90.00 122.41 90.00 C 1 2 1 4
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 0.010419 0.000000 0.006614 0.00000
SCALE2 0.000000 0.015016 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013393 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
