HEADER MEMBRANE PROTEIN 09-JUL-17 5OEO TITLE SOLUTION STRUCTURE OF THE COMPLEX OF TRPV5(655-725) WITH A CALMODULIN TITLE 2 E32Q/E68Q DOUBLE MUTANT COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALMODULIN-1; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MUTATION: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY V COMPND 8 MEMBER 5; COMPND 9 CHAIN: C; COMPND 10 SYNONYM: TRPV5,CALCIUM TRANSPORT PROTEIN 2,CAT2,EPITHELIAL CALCIUM COMPND 11 CHANNEL 1,ECAC1,OSM-9-LIKE TRP CHANNEL 3,OTRPC3; 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: CALM1, CALM, CAM, CAM1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: TRPV5, ECAC1; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 511693 KEYWDS TRPV5, CALCIUM CHANNEL, DYNAMICS, CALMODULIN, REGULATION, MEMBRANE KEYWDS 2 PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR G.W.VUISTER,F.M.BOKHOVCHUK,N.BATE,N.KOVALEVSKAYA,B.T.GOULT, AUTHOR 2 C.A.E.M.SPRONK REVDAT 3 08-MAY-19 5OEO 1 REMARK REVDAT 2 16-MAY-18 5OEO 1 JRNL REVDAT 1 25-APR-18 5OEO 0 JRNL AUTH F.M.BOKHOVCHUK,N.BATE,N.V.KOVALEVSKAYA,B.T.GOULT, JRNL AUTH 2 C.A.E.M.SPRONK,G.W.VUISTER JRNL TITL THE STRUCTURAL BASIS OF CALCIUM-DEPENDENT INACTIVATION OF JRNL TITL 2 THE TRANSIENT RECEPTOR POTENTIAL VANILLOID 5 CHANNEL. JRNL REF BIOCHEMISTRY V. 57 2623 2018 JRNL REFN ISSN 1520-4995 JRNL PMID 29584409 JRNL DOI 10.1021/ACS.BIOCHEM.7B01287 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA 3.97, YASARA 15.6 REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH (CYANA), YASARA REMARK 3 BIOSCIENCES; KRIEGER ET AL. (YASARA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT USING LOG-NORMAL POTENTIALS REMARK 3 AS DESCRIBED BY BORDEAUX ET AL, 2011 REMARK 4 REMARK 4 5OEO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JUL-17. REMARK 100 THE DEPOSITION ID IS D_1200005661. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 7.4 REMARK 210 IONIC STRENGTH : 84 REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 220 UM 13C/15N CALMODULIN, 220 REMARK 210 UM HTRPV5(655-725), 95% H2O/5% REMARK 210 D2O; 380 UM [U-99% 15N] REMARK 210 CALMODULIN, 380 UM [U-99% 13C; U- REMARK 210 99% 15N] HTRPV5(655-725), 95% REMARK 210 H2O/5% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 1H-15N NOESY; 3D 1H-13C NOESY REMARK 210 ALIPHATIC; 3D 1H-13C NOESY REMARK 210 AROMATIC REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : AVI; AVIII REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CCPNMR ANALYSIS 2.4, REMARK 210 ANALYSISASSIGN 3.0, NMRPIPE 7.9 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 120 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST REMARK 210 ENERGY REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: NULL REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 1680 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 17450 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS 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 ARG A 106 HG1 THR A 110 1.60 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 1 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 2 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 3 ASP A 129 CB - CG - OD1 ANGL. DEV. = -6.5 DEGREES REMARK 500 3 ARG C 690 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 3 ARG C 690 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 3 ARG C 705 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES REMARK 500 3 ARG C 705 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES REMARK 500 4 ARG A 37 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 4 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 4 ARG A 90 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 5 ARG A 37 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 5 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 5 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES REMARK 500 5 ARG C 699 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 5 ARG C 705 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 6 ARG A 74 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 6 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 6 ASP A 129 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES REMARK 500 7 ARG A 37 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 7 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 7 ARG A 90 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 7 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 7 ASP A 131 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES REMARK 500 7 ARG C 678 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 7 ARG C 705 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 8 ARG A 74 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 8 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES REMARK 500 8 ARG C 705 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 9 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES REMARK 500 9 ARG C 678 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 10 ARG A 37 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 10 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 10 ARG A 126 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 10 ARG C 699 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 10 ARG C 705 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 11 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 12 ARG C 690 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 12 ARG C 699 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 13 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 14 ARG A 86 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES REMARK 500 15 ARG A 74 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES REMARK 500 15 ARG A 90 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES REMARK 500 16 ARG A 74 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 16 ARG A 90 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES REMARK 500 16 ARG C 690 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 17 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES REMARK 500 17 ARG C 678 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES REMARK 500 17 ARG C 705 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES REMARK 500 18 ARG C 705 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES REMARK 500 19 PRO A 66 C - N - CA ANGL. DEV. = -9.4 DEGREES REMARK 500 REMARK 500 THIS ENTRY HAS 57 ANGLE DEVIATIONS. 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 1 ASN A 42 72.32 51.02 REMARK 500 1 ASP A 56 40.28 -93.78 REMARK 500 1 GLN C 660 86.91 -158.77 REMARK 500 1 HIS C 662 50.37 -149.59 REMARK 500 1 GLN C 694 18.61 59.95 REMARK 500 2 ASP A 20 50.31 -93.34 REMARK 500 2 ASP A 78 176.89 168.70 REMARK 500 2 SER C 697 -84.45 -90.67 REMARK 500 2 LEU C 714 -62.39 -168.13 REMARK 500 3 SER C 669 83.75 63.16 REMARK 500 4 ASP A 20 53.03 -93.03 REMARK 500 4 ASP A 78 7.01 57.68 REMARK 500 4 GLU C 661 10.89 58.29 REMARK 500 4 GLN C 667 75.27 -152.95 REMARK 500 4 SER C 669 14.28 55.78 REMARK 500 5 ASP A 78 -157.29 58.93 REMARK 500 5 SER C 696 32.36 -142.62 REMARK 500 5 HIS C 711 -121.50 -72.51 REMARK 500 5 GLU C 720 51.18 -102.97 REMARK 500 6 ASN A 42 -65.86 -149.89 REMARK 500 6 ASP A 64 -113.76 -76.47 REMARK 500 6 PHE A 65 -48.25 -147.44 REMARK 500 6 LYS C 656 -50.38 -140.80 REMARK 500 6 GLU C 665 87.88 -150.66 REMARK 500 7 ASP A 56 46.18 -140.28 REMARK 500 8 ASP A 20 50.35 -98.44 REMARK 500 8 THR C 691 11.73 47.05 REMARK 500 9 ASP A 78 90.18 11.82 REMARK 500 9 SER C 695 44.01 -152.89 REMARK 500 9 HIS C 711 95.95 -68.86 REMARK 500 9 LEU C 712 149.23 67.38 REMARK 500 10 ASP A 20 49.75 -97.15 REMARK 500 10 LYS A 77 -67.41 -100.32 REMARK 500 10 GLU C 657 8.22 57.75 REMARK 500 10 GLN C 694 43.55 -84.52 REMARK 500 10 ARG C 699 -9.00 -55.62 REMARK 500 10 HIS C 711 -79.73 -82.36 REMARK 500 11 ASP A 20 51.12 -99.74 REMARK 500 11 ASP A 56 43.97 -89.99 REMARK 500 11 THR A 79 -33.69 -132.42 REMARK 500 11 THR C 691 -5.91 62.24 REMARK 500 12 LYS C 666 -58.20 -120.22 REMARK 500 12 SER C 680 50.06 38.13 REMARK 500 12 SER C 719 26.68 -142.78 REMARK 500 13 ASP A 2 -70.21 -96.83 REMARK 500 13 GLN A 3 -57.08 -130.74 REMARK 500 13 LEU A 4 93.24 47.67 REMARK 500 13 LYS A 77 -65.24 -99.41 REMARK 500 13 GLU A 114 81.69 61.33 REMARK 500 13 SER C 697 -75.77 -140.73 REMARK 500 REMARK 500 THIS ENTRY HAS 80 RAMACHANDRAN OUTLIERS. 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 201 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 93 OD1 REMARK 620 2 ASP A 95 OD1 70.2 REMARK 620 3 ASN A 97 OD1 88.2 76.0 REMARK 620 4 TYR A 99 O 94.2 144.1 71.2 REMARK 620 5 GLU A 104 OE1 87.2 128.9 150.5 80.1 REMARK 620 6 GLU A 104 OE2 136.1 140.5 123.7 72.6 49.9 REMARK 620 N 1 2 3 4 5 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 202 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 129 OD1 REMARK 620 2 ASP A 129 OD2 43.6 REMARK 620 3 ASP A 131 OD1 84.1 97.2 REMARK 620 4 ASP A 131 OD2 96.9 77.7 44.7 REMARK 620 5 ASP A 133 OD1 102.3 61.2 126.9 82.3 REMARK 620 6 ASP A 133 OD2 143.8 103.2 87.6 54.7 56.5 REMARK 620 7 GLN A 135 O 93.7 89.2 167.9 147.3 65.2 100.9 REMARK 620 8 GLU A 140 OE1 95.2 137.0 87.9 128.9 142.1 119.7 80.5 REMARK 620 9 GLU A 140 OE2 53.4 95.2 88.6 129.8 137.3 161.6 80.7 42.1 REMARK 620 N 1 2 3 4 5 6 7 8 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 201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 202 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 34161 RELATED DB: BMRB REMARK 900 SOLUTION STRUCTURE OF THE COMPLEX OF TRPV5(655-725) WITH A REMARK 900 CALMODULIN E32Q/E68Q DOUBLE MUTANT DBREF 5OEO A 0 148 UNP P0DP23 CALM1_HUMAN 1 149 DBREF 5OEO C 655 725 UNP Q9NQA5 TRPV5_HUMAN 655 725 SEQADV 5OEO SER A -1 UNP P0DP23 EXPRESSION TAG SEQADV 5OEO GLN A 31 UNP P0DP23 GLU 32 ENGINEERED MUTATION SEQADV 5OEO GLN A 67 UNP P0DP23 GLU 68 ENGINEERED MUTATION SEQADV 5OEO GLY C 653 UNP Q9NQA5 EXPRESSION TAG SEQADV 5OEO ALA C 654 UNP Q9NQA5 EXPRESSION TAG SEQRES 1 A 150 SER MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU SEQRES 2 A 150 PHE LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP SEQRES 3 A 150 GLY THR ILE THR THR LYS GLN LEU GLY THR VAL MET ARG SEQRES 4 A 150 SER LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP SEQRES 5 A 150 MET ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE SEQRES 6 A 150 ASP PHE PRO GLN PHE LEU THR MET MET ALA ARG LYS MET SEQRES 7 A 150 LYS ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE SEQRES 8 A 150 ARG VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA SEQRES 9 A 150 ALA GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS SEQRES 10 A 150 LEU THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA SEQRES 11 A 150 ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE SEQRES 12 A 150 VAL GLN MET MET THR ALA LYS SEQRES 1 C 73 GLY ALA ASP LYS GLU ASP ASP GLN GLU HIS PRO SER GLU SEQRES 2 C 73 LYS GLN PRO SER GLY ALA GLU SER GLY THR LEU ALA ARG SEQRES 3 C 73 ALA SER LEU ALA LEU PRO THR SER SER LEU SER ARG THR SEQRES 4 C 73 ALA SER GLN SER SER SER HIS ARG GLY TRP GLU ILE LEU SEQRES 5 C 73 ARG GLN ASN THR LEU GLY HIS LEU ASN LEU GLY LEU ASN SEQRES 6 C 73 LEU SER GLU GLY ASP GLY GLU GLU HET CA A 201 1 HET CA A 202 1 HETNAM CA CALCIUM ION FORMUL 3 CA 2(CA 2+) HELIX 1 AA1 MET A 0 LEU A 4 5 5 HELIX 2 AA2 THR A 5 ASP A 20 1 16 HELIX 3 AA3 THR A 29 GLY A 40 1 12 HELIX 4 AA4 THR A 44 ASP A 56 1 13 HELIX 5 AA5 PHE A 65 ASP A 78 1 14 HELIX 6 AA6 GLU A 82 ASP A 93 1 12 HELIX 7 AA7 SER A 101 LEU A 112 1 12 HELIX 8 AA8 THR A 117 ASP A 129 1 13 HELIX 9 AA9 ASN A 137 ALA A 147 1 11 HELIX 10 AB1 HIS C 698 GLY C 710 1 13 SHEET 1 AA1 2 THR A 26 THR A 28 0 SHEET 2 AA1 2 THR A 62 ASP A 64 -1 O ILE A 63 N ILE A 27 LINK OD1 ASP A 93 CA CA A 201 1555 1555 2.46 LINK OD1 ASP A 95 CA CA A 201 1555 1555 2.54 LINK OD1 ASN A 97 CA CA A 201 1555 1555 2.43 LINK O TYR A 99 CA CA A 201 1555 1555 2.78 LINK OE1 GLU A 104 CA CA A 201 1555 1555 2.53 LINK OE2 GLU A 104 CA CA A 201 1555 1555 2.58 LINK OD1 ASP A 129 CA CA A 202 1555 1555 1.91 LINK OD2 ASP A 129 CA CA A 202 1555 1555 3.07 LINK OD1 ASP A 131 CA CA A 202 1555 1555 2.82 LINK OD2 ASP A 131 CA CA A 202 1555 1555 2.95 LINK OD1 ASP A 133 CA CA A 202 1555 1555 2.37 LINK OD2 ASP A 133 CA CA A 202 1555 1555 2.09 LINK O GLN A 135 CA CA A 202 1555 1555 2.57 LINK OE1 GLU A 140 CA CA A 202 1555 1555 3.02 LINK OE2 GLU A 140 CA CA A 202 1555 1555 3.02 SITE 1 AC1 5 ASP A 93 ASP A 95 ASN A 97 TYR A 99 SITE 2 AC1 5 GLU A 104 SITE 1 AC2 5 ASP A 129 ASP A 131 ASP A 133 GLN A 135 SITE 2 AC2 5 GLU A 140 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000 MODEL 1