HEADER HYDROLASE REGULATOR 20-DEC-12 2M2F
TITLE THE MEMBRAN-PROXIMAL DOMAIN OF ADAM17
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DISINTEGRIN AND METALLOPROTEINASE DOMAIN-CONTAINING PROTEIN
COMPND 3 17;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 581-642;
COMPND 6 SYNONYM: ADAM 17, SNAKE VENOM-LIKE PROTEASE, TNF-ALPHA CONVERTASE,
COMPND 7 TNF-ALPHA-CONVERTING ENZYME;
COMPND 8 EC: 3.4.24.86;
COMPND 9 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: ADAM17, CSVP, TACE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS ADAM17, MEMBRANE-PROXIMAL DOMAIN, HYDROLASE REGULATOR, CLOSED
KEYWDS 2 CONFORMER
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.DUESTERHOEFT,S.JUNG,C.HUNG,A.THOLEY,F.D.SOENNICHSEN,J.GROETZINGER,
AUTHOR 2 I.LORENZEN
REVDAT 3 14-JUN-23 2M2F 1 REMARK SEQADV
REVDAT 2 19-JUN-13 2M2F 1 JRNL
REVDAT 1 10-APR-13 2M2F 0
JRNL AUTH S.DUSTERHOFT,S.JUNG,C.W.HUNG,A.THOLEY,F.D.SONNICHSEN,
JRNL AUTH 2 J.GROTZINGER,I.LORENZEN
JRNL TITL MEMBRANE-PROXIMAL DOMAIN OF A DISINTEGRIN AND
JRNL TITL 2 METALLOPROTEASE-17 REPRESENTS THE PUTATIVE MOLECULAR SWITCH
JRNL TITL 3 OF ITS SHEDDING ACTIVITY OPERATED BY PROTEIN-DISULFIDE
JRNL TITL 4 ISOMERASE.
JRNL REF J.AM.CHEM.SOC. V. 135 5776 2013
JRNL REFN ISSN 0002-7863
JRNL PMID 23521534
JRNL DOI 10.1021/JA400340U
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, CYANA
REMARK 3 AUTHORS : DELAGLIO, GRZESIEK, VUISTER, ZHU, PFEIFER AND BAX
REMARK 3 (NMRPIPE)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2M2F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1000103123.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 0.15
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0 MM [U-100% 13C; U-100% 15N]
REMARK 210 PROTEIN, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D HNCA; 3D
REMARK 210 HNCO; 3D HN(CO)CA; 3D H(CCO)NH;
REMARK 210 3D HN(CA)CO; 3D CBCA(CO)NH; 3D
REMARK 210 HNCACB; 3D 1H-15N NOESY; 3D 1H-
REMARK 210 15N TOCSY; 3D 1H-13C NOESY; 3D
REMARK 210 1H-13C NOESY ALIPHATIC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 MET A -25
REMARK 465 GLY A -24
REMARK 465 SER A -23
REMARK 465 SER A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 SER A -15
REMARK 465 SER A -14
REMARK 465 GLY A -13
REMARK 465 LEU A -12
REMARK 465 VAL A -11
REMARK 465 PRO A -10
REMARK 465 ARG A -9
REMARK 465 GLY A -8
REMARK 465 SER A -7
REMARK 465 HIS A -6
REMARK 465 MET A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 ASP A -1
REMARK 465 LYS A 0
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 OD2 ASP A 17 HZ2 LYS A 21 1.55
REMARK 500 OE1 GLU A 38 HZ3 LYS A 40 1.56
REMARK 500 OD2 ASP A 36 HZ2 LYS A 40 1.59
REMARK 500 HZ1 LYS A 46 OD2 ASP A 56 1.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 7 ASP A 36 CA ASP A 36 C -0.157
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 GLU A 3 -70.95 -58.18
REMARK 500 1 GLN A 6 16.77 -145.79
REMARK 500 1 GLN A 39 34.06 71.53
REMARK 500 1 ASP A 56 -169.18 -104.34
REMARK 500 1 MET A 57 0.45 -65.90
REMARK 500 2 CYS A 50 -154.18 -129.55
REMARK 500 3 CYS A 2 -29.97 55.16
REMARK 500 3 CYS A 11 -174.91 -170.41
REMARK 500 3 ASP A 36 -164.28 -101.73
REMARK 500 3 CYS A 50 -154.26 -135.18
REMARK 500 5 GLN A 39 35.74 75.78
REMARK 500 6 CYS A 2 -6.63 65.91
REMARK 500 6 GLU A 3 -71.39 -56.04
REMARK 500 6 GLN A 6 17.72 -152.21
REMARK 500 6 CYS A 50 -162.59 -123.85
REMARK 500 7 GLU A 3 -70.96 -49.84
REMARK 500 7 ALA A 37 -31.87 -30.09
REMARK 500 8 ASP A 36 -165.26 -108.03
REMARK 500 8 CYS A 50 -156.96 -127.35
REMARK 500 9 ALA A 37 -33.79 -30.87
REMARK 500 9 GLN A 39 32.30 74.35
REMARK 500 9 CYS A 50 -159.10 -112.65
REMARK 500 10 CYS A 13 40.72 -77.21
REMARK 500 10 ASN A 14 -13.81 7.61
REMARK 500 10 ASP A 36 -166.14 -100.10
REMARK 500 10 CYS A 50 -156.54 -124.73
REMARK 500 10 ASP A 56 -154.04 -125.78
REMARK 500 10 MET A 57 -56.85 -27.21
REMARK 500 11 GLN A 39 38.48 74.06
REMARK 500 11 LEU A 42 97.78 -171.54
REMARK 500 11 LEU A 44 -179.38 -66.45
REMARK 500 11 CYS A 50 -162.89 -124.80
REMARK 500 12 ASP A 36 -164.83 -106.43
REMARK 500 12 GLN A 39 41.92 77.68
REMARK 500 12 LEU A 44 -174.64 -67.69
REMARK 500 12 CYS A 50 -161.02 -123.15
REMARK 500 13 CYS A 2 -34.98 -133.32
REMARK 500 13 LEU A 44 -175.24 -68.79
REMARK 500 13 CYS A 50 -156.93 -115.03
REMARK 500 13 ASP A 56 -166.62 -129.63
REMARK 500 14 GLU A 3 -70.19 -57.18
REMARK 500 14 ASP A 36 -169.09 -109.24
REMARK 500 14 CYS A 50 -161.34 -124.52
REMARK 500 15 ASP A 36 -167.32 -104.30
REMARK 500 15 CYS A 50 -156.26 -118.73
REMARK 500 16 GLU A 3 -70.49 -53.09
REMARK 500 16 LEU A 44 -175.98 -61.19
REMARK 500 17 GLU A 3 -70.62 -53.99
REMARK 500 18 GLN A 39 34.39 77.97
REMARK 500 18 LEU A 44 -175.98 -68.97
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 11 ARG A 25 0.07 SIDE CHAIN
REMARK 500 14 ARG A 4 0.09 SIDE CHAIN
REMARK 500 20 ARG A 4 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 10 CYS A 13 -10.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 18912 RELATED DB: BMRB
DBREF 2M2F A 1 62 UNP P78536 ADA17_HUMAN 581 642
SEQADV 2M2F MET A -25 UNP P78536 EXPRESSION TAG
SEQADV 2M2F GLY A -24 UNP P78536 EXPRESSION TAG
SEQADV 2M2F SER A -23 UNP P78536 EXPRESSION TAG
SEQADV 2M2F SER A -22 UNP P78536 EXPRESSION TAG
SEQADV 2M2F HIS A -21 UNP P78536 EXPRESSION TAG
SEQADV 2M2F HIS A -20 UNP P78536 EXPRESSION TAG
SEQADV 2M2F HIS A -19 UNP P78536 EXPRESSION TAG
SEQADV 2M2F HIS A -18 UNP P78536 EXPRESSION TAG
SEQADV 2M2F HIS A -17 UNP P78536 EXPRESSION TAG
SEQADV 2M2F HIS A -16 UNP P78536 EXPRESSION TAG
SEQADV 2M2F SER A -15 UNP P78536 EXPRESSION TAG
SEQADV 2M2F SER A -14 UNP P78536 EXPRESSION TAG
SEQADV 2M2F GLY A -13 UNP P78536 EXPRESSION TAG
SEQADV 2M2F LEU A -12 UNP P78536 EXPRESSION TAG
SEQADV 2M2F VAL A -11 UNP P78536 EXPRESSION TAG
SEQADV 2M2F PRO A -10 UNP P78536 EXPRESSION TAG
SEQADV 2M2F ARG A -9 UNP P78536 EXPRESSION TAG
SEQADV 2M2F GLY A -8 UNP P78536 EXPRESSION TAG
SEQADV 2M2F SER A -7 UNP P78536 EXPRESSION TAG
SEQADV 2M2F HIS A -6 UNP P78536 EXPRESSION TAG
SEQADV 2M2F MET A -5 UNP P78536 EXPRESSION TAG
SEQADV 2M2F ASP A -4 UNP P78536 EXPRESSION TAG
SEQADV 2M2F ASP A -3 UNP P78536 EXPRESSION TAG
SEQADV 2M2F ASP A -2 UNP P78536 EXPRESSION TAG
SEQADV 2M2F ASP A -1 UNP P78536 EXPRESSION TAG
SEQADV 2M2F LYS A 0 UNP P78536 EXPRESSION TAG
SEQRES 1 A 88 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 88 LEU VAL PRO ARG GLY SER HIS MET ASP ASP ASP ASP LYS
SEQRES 3 A 88 PHE CYS GLU ARG GLU GLN GLN LEU GLU SER CYS ALA CYS
SEQRES 4 A 88 ASN GLU THR ASP ASN SER CYS LYS VAL CYS CYS ARG ASP
SEQRES 5 A 88 LEU SER GLY ARG CYS VAL PRO TYR VAL ASP ALA GLU GLN
SEQRES 6 A 88 LYS ASN LEU PHE LEU ARG LYS GLY LYS PRO CYS THR VAL
SEQRES 7 A 88 GLY PHE CYS ASP MET ASN GLY LYS CYS GLU
HELIX 1 1 CYS A 2 GLN A 7 1 6
HELIX 2 2 THR A 16 LYS A 21 5 6
SHEET 1 A 3 GLU A 9 CYS A 11 0
SHEET 2 A 3 CYS A 23 ARG A 25 -1 O CYS A 23 N CYS A 11
SHEET 3 A 3 CYS A 31 PRO A 33 -1 O VAL A 32 N CYS A 24
SHEET 1 B 3 LYS A 48 PRO A 49 0
SHEET 2 B 3 PHE A 54 ASP A 56 -1 O CYS A 55 N LYS A 48
SHEET 3 B 3 LYS A 60 CYS A 61 -1 O LYS A 60 N ASP A 56
SSBOND 1 CYS A 2 CYS A 24 1555 1555 2.03
SSBOND 2 CYS A 11 CYS A 31 1555 1555 2.03
SSBOND 3 CYS A 13 CYS A 23 1555 1555 2.04
SSBOND 4 CYS A 20 CYS A 55 1555 1555 2.03
SSBOND 5 CYS A 50 CYS A 61 1555 1555 2.02
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
(ATOM LINES ARE NOT SHOWN.)
END
