HEADER HYDROLASE 01-OCT-15 5E2Q
TITLE STRUCTURE OF HUMAN DPP3 IN COMPLEX WITH ANGIOTENSIN-II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIPEPTIDYL PEPTIDASE 3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DIPEPTIDYL AMINOPEPTIDASE III,DIPEPTIDYL ARYLAMIDASE III,
COMPND 5 DIPEPTIDYL PEPTIDASE III,DPP III,ENKEPHALINASE B;
COMPND 6 EC: 3.4.14.4;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: ANGIOTENSIN-II;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: UNP RESIDUES 34-41;
COMPND 13 SYNONYM: SERPIN A8;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DPP3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28MHL;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606
KEYWDS COMPLEX, PEPTIDASE, ZINC-HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.KUMAR,M.REISINGER,V.REITHOFER,K.GRUBER
REVDAT 3 10-JAN-24 5E2Q 1 ATOM
REVDAT 2 06-SEP-17 5E2Q 1 REMARK
REVDAT 1 13-APR-16 5E2Q 0
JRNL AUTH P.KUMAR,V.REITHOFER,M.REISINGER,S.WALLNER,T.PAVKOV-KELLER,
JRNL AUTH 2 P.MACHEROUX,K.GRUBER
JRNL TITL SUBSTRATE COMPLEXES OF HUMAN DIPEPTIDYL PEPTIDASE III REVEAL
JRNL TITL 2 THE MECHANISM OF ENZYME INHIBITION.
JRNL REF SCI REP V. 6 23787 2016
JRNL REFN ESSN 2045-2322
JRNL PMID 27025154
JRNL DOI 10.1038/SREP23787
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.33
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 30446
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.208
REMARK 3 R VALUE (WORKING SET) : 0.206
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1524
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 45.3300 - 5.3441 0.99 2736 145 0.1517 0.1825
REMARK 3 2 5.3441 - 4.2428 1.00 2713 143 0.1487 0.2039
REMARK 3 3 4.2428 - 3.7067 0.98 2671 140 0.1816 0.1873
REMARK 3 4 3.7067 - 3.3679 0.98 2652 140 0.2378 0.2965
REMARK 3 5 3.3679 - 3.1266 1.00 2679 141 0.2257 0.2531
REMARK 3 6 3.1266 - 2.9423 1.00 2690 142 0.2343 0.2600
REMARK 3 7 2.9423 - 2.7950 1.00 2713 142 0.2341 0.2720
REMARK 3 8 2.7950 - 2.6733 1.00 2687 142 0.2432 0.2960
REMARK 3 9 2.6733 - 2.5704 0.99 2619 138 0.2658 0.3563
REMARK 3 10 2.5704 - 2.4817 0.94 2533 133 0.2814 0.3460
REMARK 3 11 2.4817 - 2.4041 0.83 2229 118 0.3169 0.4100
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) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.650
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.50
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 : 0.002 5969
REMARK 3 ANGLE : 0.577 8090
REMARK 3 CHIRALITY : 0.023 871
REMARK 3 PLANARITY : 0.003 1062
REMARK 3 DIHEDRAL : 12.533 2204
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 5E2Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214257.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.2
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.953730
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : BENT COLLIMATING MIRROR AND
REMARK 200 TOROID
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30464
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 45.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10470
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.57710
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.560
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.9_1692
REMARK 200 STARTING MODEL: 3T6B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.056 M SODIUM PHOSPHATE MONOBASIC
REMARK 280 MONOHYDRATE, 1.344 M POTASSIUM PHOSPHATE DIBASIC MONOHYDRATE, PH
REMARK 280 8.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 59.56550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.96100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.56550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 52.96100
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 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 HOH A1010 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 MET A 1
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 SER A 19 13.45 -144.39
REMARK 500 THR A 52 -70.22 -107.81
REMARK 500 GLU A 166 40.81 -100.37
REMARK 500 SER A 317 56.25 -116.43
REMARK 500 PRO A 358 33.45 -71.70
REMARK 500 THR A 370 73.24 49.27
REMARK 500 THR A 401 -43.46 -130.70
REMARK 500 ASP A 464 -178.71 -69.02
REMARK 500 SER A 500 -107.39 45.12
REMARK 500 THR A 592 -158.73 -130.98
REMARK 500 ASP A 633 80.23 -69.70
REMARK 500 GLU A 680 55.67 -94.70
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 801 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 164 O
REMARK 620 2 GLY A 167 O 81.6
REMARK 620 3 HOH A 958 O 154.7 95.1
REMARK 620 4 HOH A1028 O 71.5 76.7 83.4
REMARK 620 5 HOH A1037 O 105.8 172.0 76.9 102.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 802 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 317 O
REMARK 620 2 SER A 317 OG 60.7
REMARK 620 3 GLY A 323 O 89.4 73.3
REMARK 620 4 ASP A 496 OD1 141.7 81.1 76.5
REMARK 620 5 SER A 504 OG 77.7 110.7 161.3 121.9
REMARK 620 6 HOH A1018 O 96.7 156.6 102.4 120.9 66.3
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 MG A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 802
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FVY RELATED DB: PDB
REMARK 900 3FVY CONTAINS THE SAME PROTEIN IN ITS UNBOUND FORM
REMARK 900 RELATED ID: 3T6B RELATED DB: PDB
REMARK 900 3T6B CONTAINS THE SAME PROTEIN IN COMPLEX WITH VVYPW
DBREF 5E2Q A 1 726 UNP Q9NY33 DPP3_HUMAN 1 726
DBREF 5E2Q B 1 8 UNP P01019 ANGT_HUMAN 34 41
SEQADV 5E2Q SER A 19 UNP Q9NY33 CYS 19 ENGINEERED MUTATION
SEQADV 5E2Q CYS A 207 UNP Q9NY33 GLU 207 ENGINEERED MUTATION
SEQADV 5E2Q ALA A 451 UNP Q9NY33 GLU 451 ENGINEERED MUTATION
SEQADV 5E2Q CYS A 491 UNP Q9NY33 SER 491 ENGINEERED MUTATION
SEQADV 5E2Q SER A 519 UNP Q9NY33 CYS 519 ENGINEERED MUTATION
SEQADV 5E2Q SER A 654 UNP Q9NY33 CYS 654 ENGINEERED MUTATION
SEQRES 1 A 726 MET ALA ASP THR GLN TYR ILE LEU PRO ASN ASP ILE GLY
SEQRES 2 A 726 VAL SER SER LEU ASP SER ARG GLU ALA PHE ARG LEU LEU
SEQRES 3 A 726 SER PRO THR GLU ARG LEU TYR ALA TYR HIS LEU SER ARG
SEQRES 4 A 726 ALA ALA TRP TYR GLY GLY LEU ALA VAL LEU LEU GLN THR
SEQRES 5 A 726 SER PRO GLU ALA PRO TYR ILE TYR ALA LEU LEU SER ARG
SEQRES 6 A 726 LEU PHE ARG ALA GLN ASP PRO ASP GLN LEU ARG GLN HIS
SEQRES 7 A 726 ALA LEU ALA GLU GLY LEU THR GLU GLU GLU TYR GLN ALA
SEQRES 8 A 726 PHE LEU VAL TYR ALA ALA GLY VAL TYR SER ASN MET GLY
SEQRES 9 A 726 ASN TYR LYS SER PHE GLY ASP THR LYS PHE VAL PRO ASN
SEQRES 10 A 726 LEU PRO LYS GLU LYS LEU GLU ARG VAL ILE LEU GLY SER
SEQRES 11 A 726 GLU ALA ALA GLN GLN HIS PRO GLU GLU VAL ARG GLY LEU
SEQRES 12 A 726 TRP GLN THR CYS GLY GLU LEU MET PHE SER LEU GLU PRO
SEQRES 13 A 726 ARG LEU ARG HIS LEU GLY LEU GLY LYS GLU GLY ILE THR
SEQRES 14 A 726 THR TYR PHE SER GLY ASN CYS THR MET GLU ASP ALA LYS
SEQRES 15 A 726 LEU ALA GLN ASP PHE LEU ASP SER GLN ASN LEU SER ALA
SEQRES 16 A 726 TYR ASN THR ARG LEU PHE LYS GLU VAL ASP GLY CYS GLY
SEQRES 17 A 726 LYS PRO TYR TYR GLU VAL ARG LEU ALA SER VAL LEU GLY
SEQRES 18 A 726 SER GLU PRO SER LEU ASP SER GLU VAL THR SER LYS LEU
SEQRES 19 A 726 LYS SER TYR GLU PHE ARG GLY SER PRO PHE GLN VAL THR
SEQRES 20 A 726 ARG GLY ASP TYR ALA PRO ILE LEU GLN LYS VAL VAL GLU
SEQRES 21 A 726 GLN LEU GLU LYS ALA LYS ALA TYR ALA ALA ASN SER HIS
SEQRES 22 A 726 GLN GLY GLN MET LEU ALA GLN TYR ILE GLU SER PHE THR
SEQRES 23 A 726 GLN GLY SER ILE GLU ALA HIS LYS ARG GLY SER ARG PHE
SEQRES 24 A 726 TRP ILE GLN ASP LYS GLY PRO ILE VAL GLU SER TYR ILE
SEQRES 25 A 726 GLY PHE ILE GLU SER TYR ARG ASP PRO PHE GLY SER ARG
SEQRES 26 A 726 GLY GLU PHE GLU GLY PHE VAL ALA VAL VAL ASN LYS ALA
SEQRES 27 A 726 MET SER ALA LYS PHE GLU ARG LEU VAL ALA SER ALA GLU
SEQRES 28 A 726 GLN LEU LEU LYS GLU LEU PRO TRP PRO PRO THR PHE GLU
SEQRES 29 A 726 LYS ASP LYS PHE LEU THR PRO ASP PHE THR SER LEU ASP
SEQRES 30 A 726 VAL LEU THR PHE ALA GLY SER GLY ILE PRO ALA GLY ILE
SEQRES 31 A 726 ASN ILE PRO ASN TYR ASP ASP LEU ARG GLN THR GLU GLY
SEQRES 32 A 726 PHE LYS ASN VAL SER LEU GLY ASN VAL LEU ALA VAL ALA
SEQRES 33 A 726 TYR ALA THR GLN ARG GLU LYS LEU THR PHE LEU GLU GLU
SEQRES 34 A 726 ASP ASP LYS ASP LEU TYR ILE LEU TRP LYS GLY PRO SER
SEQRES 35 A 726 PHE ASP VAL GLN VAL GLY LEU HIS ALA LEU LEU GLY HIS
SEQRES 36 A 726 GLY SER GLY LYS LEU PHE VAL GLN ASP GLU LYS GLY ALA
SEQRES 37 A 726 PHE ASN PHE ASP GLN GLU THR VAL ILE ASN PRO GLU THR
SEQRES 38 A 726 GLY GLU GLN ILE GLN SER TRP TYR ARG CYS GLY GLU THR
SEQRES 39 A 726 TRP ASP SER LYS PHE SER THR ILE ALA SER SER TYR GLU
SEQRES 40 A 726 GLU CYS ARG ALA GLU SER VAL GLY LEU TYR LEU SER LEU
SEQRES 41 A 726 HIS PRO GLN VAL LEU GLU ILE PHE GLY PHE GLU GLY ALA
SEQRES 42 A 726 ASP ALA GLU ASP VAL ILE TYR VAL ASN TRP LEU ASN MET
SEQRES 43 A 726 VAL ARG ALA GLY LEU LEU ALA LEU GLU PHE TYR THR PRO
SEQRES 44 A 726 GLU ALA PHE ASN TRP ARG GLN ALA HIS MET GLN ALA ARG
SEQRES 45 A 726 PHE VAL ILE LEU ARG VAL LEU LEU GLU ALA GLY GLU GLY
SEQRES 46 A 726 LEU VAL THR ILE THR PRO THR THR GLY SER ASP GLY ARG
SEQRES 47 A 726 PRO ASP ALA ARG VAL ARG LEU ASP ARG SER LYS ILE ARG
SEQRES 48 A 726 SER VAL GLY LYS PRO ALA LEU GLU ARG PHE LEU ARG ARG
SEQRES 49 A 726 LEU GLN VAL LEU LYS SER THR GLY ASP VAL ALA GLY GLY
SEQRES 50 A 726 ARG ALA LEU TYR GLU GLY TYR ALA THR VAL THR ASP ALA
SEQRES 51 A 726 PRO PRO GLU SER PHE LEU THR LEU ARG ASP THR VAL LEU
SEQRES 52 A 726 LEU ARG LYS GLU SER ARG LYS LEU ILE VAL GLN PRO ASN
SEQRES 53 A 726 THR ARG LEU GLU GLY SER ASP VAL GLN LEU LEU GLU TYR
SEQRES 54 A 726 GLU ALA SER ALA ALA GLY LEU ILE ARG SER PHE SER GLU
SEQRES 55 A 726 ARG PHE PRO GLU ASP GLY PRO GLU LEU GLU GLU ILE LEU
SEQRES 56 A 726 THR GLN LEU ALA THR ALA ASP ALA ARG PHE TRP
SEQRES 1 B 8 ASP ARG VAL TYR ILE HIS PRO PHE
HET MG A 801 1
HET K A 802 1
HETNAM MG MAGNESIUM ION
HETNAM K POTASSIUM ION
FORMUL 3 MG MG 2+
FORMUL 4 K K 1+
FORMUL 5 HOH *165(H2 O)
HELIX 1 AA1 SER A 19 LEU A 25 1 7
HELIX 2 AA2 SER A 27 GLY A 45 1 19
HELIX 3 AA3 LEU A 46 GLN A 51 1 6
HELIX 4 AA4 GLU A 55 GLN A 70 1 16
HELIX 5 AA5 ASP A 71 GLU A 82 1 12
HELIX 6 AA6 THR A 85 MET A 103 1 19
HELIX 7 AA7 PRO A 119 GLY A 129 1 11
HELIX 8 AA8 SER A 130 HIS A 136 1 7
HELIX 9 AA9 HIS A 136 SER A 153 1 18
HELIX 10 AB1 GLU A 155 ARG A 159 5 5
HELIX 11 AB2 THR A 177 GLN A 191 1 15
HELIX 12 AB3 TYR A 251 ALA A 267 1 17
HELIX 13 AB4 ASN A 271 GLY A 288 1 18
HELIX 14 AB5 SER A 289 ASP A 303 1 15
HELIX 15 AB6 SER A 340 SER A 349 1 10
HELIX 16 AB7 SER A 349 LEU A 354 1 6
HELIX 17 AB8 LYS A 355 LEU A 357 5 3
HELIX 18 AB9 PRO A 360 GLU A 364 5 5
HELIX 19 AC1 TYR A 395 GLN A 400 1 6
HELIX 20 AC2 GLY A 410 ALA A 414 1 5
HELIX 21 AC3 GLN A 420 LEU A 424 5 5
HELIX 22 AC4 GLU A 428 LEU A 452 1 25
HELIX 23 AC5 THR A 494 SER A 500 1 7
HELIX 24 AC6 ILE A 502 SER A 519 1 18
HELIX 25 AC7 HIS A 521 PHE A 528 1 8
HELIX 26 AC8 GLY A 532 ALA A 553 1 22
HELIX 27 AC9 GLN A 566 ALA A 582 1 17
HELIX 28 AD1 ARG A 607 ILE A 610 5 4
HELIX 29 AD2 VAL A 613 THR A 631 1 19
HELIX 30 AD3 ASP A 633 ALA A 645 1 13
HELIX 31 AD4 SER A 654 ARG A 665 1 12
HELIX 32 AD5 SER A 692 GLU A 702 1 11
HELIX 33 AD6 ASP A 707 ASP A 722 1 16
HELIX 34 AD7 ALA A 723 TRP A 726 5 4
SHEET 1 AA1 2 VAL A 14 SER A 16 0
SHEET 2 AA1 2 LEU A 671 VAL A 673 1 O LEU A 671 N SER A 15
SHEET 1 AA2 4 THR A 198 VAL A 204 0
SHEET 2 AA2 4 PRO A 210 ALA A 217 -1 O TYR A 211 N GLU A 203
SHEET 3 AA2 4 SER A 242 ASP A 250 1 O GLN A 245 N VAL A 214
SHEET 4 AA2 4 SER A 236 PHE A 239 -1 N TYR A 237 O PHE A 244
SHEET 1 AA3 6 VAL A 308 GLU A 316 0
SHEET 2 AA3 6 GLU A 327 VAL A 335 -1 O GLU A 329 N GLY A 313
SHEET 3 AA3 6 ASP A 372 ALA A 382 -1 O LEU A 379 N VAL A 332
SHEET 4 AA3 6 LYS A 405 LEU A 409 1 O ASN A 406 N ASP A 372
SHEET 5 AA3 6 GLY A 389 ILE A 392 -1 N ILE A 392 O LYS A 405
SHEET 6 AA3 6 ARG B 2 VAL B 3 -1 O VAL B 3 N GLY A 389
SHEET 1 AA4 2 TYR A 557 THR A 558 0
SHEET 2 AA4 2 ASN A 563 TRP A 564 -1 O ASN A 563 N THR A 558
SHEET 1 AA5 2 VAL A 587 THR A 593 0
SHEET 2 AA5 2 PRO A 599 LEU A 605 -1 O ARG A 602 N THR A 590
SHEET 1 AA6 2 ASN A 676 GLU A 680 0
SHEET 2 AA6 2 ASP A 683 LEU A 687 -1 O LEU A 687 N ASN A 676
LINK O GLY A 164 MG MG A 801 1555 1555 2.64
LINK O GLY A 167 MG MG A 801 1555 1555 2.79
LINK O SER A 317 K K A 802 1555 1555 2.85
LINK OG SER A 317 K K A 802 1555 1555 2.91
LINK O GLY A 323 K K A 802 1555 1555 2.74
LINK OD1 ASP A 496 K K A 802 1555 1555 3.02
LINK OG SER A 504 K K A 802 1555 1555 2.76
LINK MG MG A 801 O HOH A 958 1555 1555 2.91
LINK MG MG A 801 O HOH A1028 1555 1555 2.82
LINK MG MG A 801 O HOH A1037 1555 1555 2.54
LINK K K A 802 O HOH A1018 1555 1555 3.16
CISPEP 1 ILE A 392 PRO A 393 0 2.13
CISPEP 2 PRO A 651 PRO A 652 0 -0.88
CISPEP 3 HIS B 6 PRO B 7 0 0.96
SITE 1 AC1 6 GLY A 162 GLY A 164 GLY A 167 HOH A 958
SITE 2 AC1 6 HOH A1028 HOH A1037
SITE 1 AC2 4 SER A 317 GLY A 323 ASP A 496 SER A 504
CRYST1 119.131 105.922 64.846 90.00 93.91 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 0.008394 0.000000 0.000574 0.00000
SCALE2 0.000000 0.009441 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015457 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
