HEADER HYDROLASE 18-MAY-07 2PZF
TITLE MINIMAL HUMAN CFTR FIRST NUCLEOTIDE BINDING DOMAIN AS A HEAD-TO-TAIL
TITLE 2 DIMER WITH DELTA F508
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CFTR NBD1 387-646;
COMPND 5 SYNONYM: CFTR,ATP-BINDING CASSETTE SUB-FAMILY C MEMBER 7,CHANNEL
COMPND 6 CONDUCTANCE-CONTROLLING ATPASE,CAMP-DEPENDENT CHLORIDE CHANNEL;
COMPND 7 EC: 3.6.3.49;
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: CFTR, ABCC7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON+RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET26B
KEYWDS NBD, ABC TRANSPORTER, CFTR, F508, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.ATWELL,K.CONNERS,S.EMTAGE,T.GHEYI,N.R.GLENN,J.HENDLE,H.A.LEWIS,
AUTHOR 2 F.LU,L.A.RODGERS,R.ROMERO,J.M.SAUDER,D.SMITH,H.TIEN,S.R.WASSERMAN,
AUTHOR 3 X.ZHAO
REVDAT 11 30-AUG-23 2PZF 1 REMARK LINK
REVDAT 10 14-NOV-18 2PZF 1 AUTHOR
REVDAT 9 18-OCT-17 2PZF 1 REMARK
REVDAT 8 14-JUN-17 2PZF 1 COMPND
REVDAT 7 13-JUL-11 2PZF 1 VERSN
REVDAT 6 30-JUN-10 2PZF 1 JRNL
REVDAT 5 24-FEB-09 2PZF 1 VERSN
REVDAT 4 30-SEP-08 2PZF 1
REVDAT 3 26-AUG-08 2PZF 1 JRNL
REVDAT 2 05-AUG-08 2PZF 1 REMARK
REVDAT 1 09-OCT-07 2PZF 0
JRNL AUTH S.ATWELL,C.G.BROUILLETTE,K.CONNERS,S.EMTAGE,T.GHEYI,
JRNL AUTH 2 W.B.GUGGINO,J.HENDLE,J.F.HUNT,H.A.LEWIS,F.LU,
JRNL AUTH 3 I.I.PROTASEVICH,L.A.RODGERS,R.ROMERO,S.R.WASSERMAN,
JRNL AUTH 4 P.C.WEBER,D.WETMORE,F.F.ZHANG,X.ZHAO
JRNL TITL STRUCTURES OF A MINIMAL HUMAN CFTR FIRST NUCLEOTIDE-BINDING
JRNL TITL 2 DOMAIN AS A MONOMER, HEAD-TO-TAIL HOMODIMER, AND PATHOGENIC
JRNL TITL 3 MUTANT.
JRNL REF PROTEIN ENG.DES.SEL. V. 23 375 2010
JRNL REFN ISSN 1741-0126
JRNL PMID 20150177
JRNL DOI 10.1093/PROTEIN/GZQ004
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.ATWELL,K.CONNERS,S.EMTAGE,T.GHEYI,H.LEWIS,F.LU,R.ROMERO,
REMARK 1 AUTH 2 X.ZHAO
REMARK 1 TITL STRUCTURE OF THE HUMAN CFTR NBD1 DOMAIN AS A HOMODIMER:
REMARK 1 TITL 2 INSIGHTS AND APPLICATIONS
REMARK 1 REF PEDIATR.PULMONOL.SUPPL. V. 30 100 2007
REMARK 1 REFN ISSN 1054-187X
REMARK 1 PMID 17729305
REMARK 1 DOI 10.1002/PPUL.20699
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.12
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 29187
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1493
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3254
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.91300
REMARK 3 B22 (A**2) : 0.58700
REMARK 3 B33 (A**2) : -1.49900
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2PZF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000042956.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-FEB-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9797
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29245
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 25.583
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.12700
REMARK 200 R SYM (I) : 0.12700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 0.78600
REMARK 200 R SYM FOR SHELL (I) : 0.78600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2PZE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 9.5MG/ML NBD1, 0.15M NACL,
REMARK 280 0.01M METHIONINE, 0.01M HEPES PH 7.5, 10% GLYCEROL, 0.001M TCEP,
REMARK 280 0.002M ATP; WELL: 0.1M TRIS PH 8.5, 35% PEG 4K, 0.2M NAACETATE;
REMARK 280 CRYO: 25% DMSO, VAPOR DIFFUSION, TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 21.57600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.23550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.33100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.23550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.57600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.33100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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 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 GLU A 402
REMARK 465 GLU A 403
REMARK 465 GLN A 637
REMARK 465 PRO A 638
REMARK 465 SER B 386
REMARK 465 LEU B 387
REMARK 465 GLN B 637
REMARK 465 PRO B 638
REMARK 465 ASP B 639
REMARK 465 PHE B 640
REMARK 465 SER B 641
REMARK 465 SER B 642
REMARK 465 LYS B 643
REMARK 465 LEU B 644
REMARK 465 MET B 645
REMARK 465 GLY B 646
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 THR A 388 OG1 CG2
REMARK 470 THR A 389 OG1 CG2
REMARK 470 LYS A 442 CG CD CE NZ
REMARK 470 LYS A 447 CG CD CE NZ
REMARK 470 ARG A 450 NE CZ NH1 NH2
REMARK 470 LYS A 481 CG CD CE NZ
REMARK 470 LYS A 483 CG CD CE NZ
REMARK 470 TYR A 512 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 528 CG CD OE1 OE2
REMARK 470 LYS A 532 CG CD CE NZ
REMARK 470 PHE A 533 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 535 CG CD OE1 OE2
REMARK 470 LYS A 536 CG CD CE NZ
REMARK 470 ASP A 537 CG OD1 OD2
REMARK 470 ASN A 538 CG OD1 ND2
REMARK 470 ILE A 539 CG1 CG2 CD1
REMARK 470 GLU A 543 CG CD OE1 OE2
REMARK 470 LYS A 584 CD CE NZ
REMARK 470 GLU A 588 CG CD OE1 OE2
REMARK 470 SER A 605 OG
REMARK 470 GLU A 608 CG CD OE1 OE2
REMARK 470 LYS A 611 CG CD CE NZ
REMARK 470 LYS A 612 CD CE NZ
REMARK 470 ASN A 635 CG OD1 ND2
REMARK 470 SER A 642 OG
REMARK 470 LYS A 643 CG CD CE NZ
REMARK 470 THR B 389 OG1 CG2
REMARK 470 GLU B 395 CG CD OE1 OE2
REMARK 470 GLU B 402 CG CD OE1 OE2
REMARK 470 GLU B 403 CG CD OE1 OE2
REMARK 470 LYS B 442 CG CD CE NZ
REMARK 470 ASP B 443 CG OD1 OD2
REMARK 470 ARG B 450 NE CZ NH1 NH2
REMARK 470 GLU B 479 CG CD OE1 OE2
REMARK 470 LYS B 481 CD CE NZ
REMARK 470 LYS B 483 CG CD CE NZ
REMARK 470 VAL B 510 CG1 CG2
REMARK 470 SER B 511 OG
REMARK 470 GLU B 514 CG CD OE1 OE2
REMARK 470 ARG B 518 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 528 CG CD OE1 OE2
REMARK 470 LYS B 532 CG CD CE NZ
REMARK 470 LYS B 536 CG CD CE NZ
REMARK 470 ILE B 546 CG1 CG2 CD1
REMARK 470 LYS B 593 CD CE NZ
REMARK 470 LYS B 606 CE NZ
REMARK 470 MET B 607 SD CE
REMARK 470 GLU B 608 CG CD OE1 OE2
REMARK 470 LYS B 612 CD CE NZ
REMARK 470 GLN B 634 CG CD OE1 NE2
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 LYS A 536 -124.11 60.42
REMARK 500 CYS A 590 -66.66 -93.92
REMARK 500 LYS A 593 -63.25 -101.15
REMARK 500 SER B 531 2.94 -68.81
REMARK 500 LYS B 536 -131.02 47.90
REMARK 500 CYS B 590 -68.77 -90.04
REMARK 500 LYS B 593 -63.42 -103.90
REMARK 500 GLU B 621 48.14 39.42
REMARK 500
REMARK 500 REMARK: NULL
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 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XMI RELATED DB: PDB
REMARK 900 HUMAN CFTR NBD1 389-678(F429S,F508A,H667R)
REMARK 900 RELATED ID: 1XMJ RELATED DB: PDB
REMARK 900 HUMAN CFTR NBD1 389-678(F409L,F429S,F433L,DEL508,G550E,R553Q,R555K,
REMARK 900 H667R)
REMARK 900 RELATED ID: 2BB0 RELATED DB: PDB
REMARK 900 HUMAN CFTR NBD1 389-678(F409L,F429S,F433L,G550E,R553Q,R555K,H667R)
REMARK 900 RELATED ID: 2BBS RELATED DB: PDB
REMARK 900 HUMAN CFTR NBD1 389-678(F429S,F494N,DEL508,Q637R)
REMARK 900 RELATED ID: 2BBT RELATED DB: PDB
REMARK 900 HUMAN CFTR NBD1 389-678(F494N,DEL508,Q637R)
REMARK 900 RELATED ID: 1R0Z RELATED DB: PDB
REMARK 900 MOUSE CFTR NBD1 389-673
REMARK 900 RELATED ID: 1R10 RELATED DB: PDB
REMARK 900 MOUSE CFTR NBD1 389-673
REMARK 900 RELATED ID: 2IXE RELATED DB: PDB
REMARK 900 HOMODIMER OF HUMAN TAP1 NBD(D645N) WITH ATP
REMARK 900 RELATED ID: 1L2T RELATED DB: PDB
REMARK 900 HOMODIMER OF METHANOCOCCUS JANNASCHII MJ0796(E171Q)
REMARK 900 RELATED ID: 1Q12 RELATED DB: PDB
REMARK 900 HOMODIMER OF E. COLI MALK
REMARK 900 RELATED ID: 1XEF RELATED DB: PDB
REMARK 900 HOMODIMER OF E. COLI HLYB NBD 467-707(H662A)
REMARK 900 RELATED ID: 2HYD RELATED DB: PDB
REMARK 900 HOMODIMER OF S. AUREUS ABC TRANSPORTER SAV1866
REMARK 900 RELATED ID: 2PZE RELATED DB: PDB
REMARK 900 HUMAN NBD1 387-646(DEL 405-436)
REMARK 900 RELATED ID: 2PZG RELATED DB: PDB
REMARK 900 HUMAN NBD1 375-646(DEL 405-436)
DBREF 2PZF A 387 404 UNP P13569 CFTR_HUMAN 387 404
DBREF 2PZF A 437 646 UNP P13569 CFTR_HUMAN 437 646
DBREF 2PZF B 387 404 UNP P13569 CFTR_HUMAN 387 404
DBREF 2PZF B 437 646 UNP P13569 CFTR_HUMAN 437 646
SEQADV 2PZF SER A 386 UNP P13569 EXPRESSION TAG
SEQADV 2PZF MET A 470 UNP P13569 VAL 470 VARIANT
SEQADV 2PZF A UNP P13569 PHE 508 DELETION
SEQADV 2PZF SER B 386 UNP P13569 EXPRESSION TAG
SEQADV 2PZF MET B 470 UNP P13569 VAL 470 VARIANT
SEQADV 2PZF B UNP P13569 PHE 508 DELETION
SEQRES 1 A 228 SER LEU THR THR THR GLU VAL VAL MET GLU ASN VAL THR
SEQRES 2 A 228 ALA PHE TRP GLU GLU GLY GLY THR PRO VAL LEU LYS ASP
SEQRES 3 A 228 ILE ASN PHE LYS ILE GLU ARG GLY GLN LEU LEU ALA VAL
SEQRES 4 A 228 ALA GLY SER THR GLY ALA GLY LYS THR SER LEU LEU MET
SEQRES 5 A 228 MET ILE MET GLY GLU LEU GLU PRO SER GLU GLY LYS ILE
SEQRES 6 A 228 LYS HIS SER GLY ARG ILE SER PHE CYS SER GLN PHE SER
SEQRES 7 A 228 TRP ILE MET PRO GLY THR ILE LYS GLU ASN ILE ILE GLY
SEQRES 8 A 228 VAL SER TYR ASP GLU TYR ARG TYR ARG SER VAL ILE LYS
SEQRES 9 A 228 ALA CYS GLN LEU GLU GLU ASP ILE SER LYS PHE ALA GLU
SEQRES 10 A 228 LYS ASP ASN ILE VAL LEU GLY GLU GLY GLY ILE THR LEU
SEQRES 11 A 228 SER GLY GLY GLN ARG ALA ARG ILE SER LEU ALA ARG ALA
SEQRES 12 A 228 VAL TYR LYS ASP ALA ASP LEU TYR LEU LEU ASP SER PRO
SEQRES 13 A 228 PHE GLY TYR LEU ASP VAL LEU THR GLU LYS GLU ILE PHE
SEQRES 14 A 228 GLU SER CYS VAL CYS LYS LEU MET ALA ASN LYS THR ARG
SEQRES 15 A 228 ILE LEU VAL THR SER LYS MET GLU HIS LEU LYS LYS ALA
SEQRES 16 A 228 ASP LYS ILE LEU ILE LEU HIS GLU GLY SER SER TYR PHE
SEQRES 17 A 228 TYR GLY THR PHE SER GLU LEU GLN ASN LEU GLN PRO ASP
SEQRES 18 A 228 PHE SER SER LYS LEU MET GLY
SEQRES 1 B 228 SER LEU THR THR THR GLU VAL VAL MET GLU ASN VAL THR
SEQRES 2 B 228 ALA PHE TRP GLU GLU GLY GLY THR PRO VAL LEU LYS ASP
SEQRES 3 B 228 ILE ASN PHE LYS ILE GLU ARG GLY GLN LEU LEU ALA VAL
SEQRES 4 B 228 ALA GLY SER THR GLY ALA GLY LYS THR SER LEU LEU MET
SEQRES 5 B 228 MET ILE MET GLY GLU LEU GLU PRO SER GLU GLY LYS ILE
SEQRES 6 B 228 LYS HIS SER GLY ARG ILE SER PHE CYS SER GLN PHE SER
SEQRES 7 B 228 TRP ILE MET PRO GLY THR ILE LYS GLU ASN ILE ILE GLY
SEQRES 8 B 228 VAL SER TYR ASP GLU TYR ARG TYR ARG SER VAL ILE LYS
SEQRES 9 B 228 ALA CYS GLN LEU GLU GLU ASP ILE SER LYS PHE ALA GLU
SEQRES 10 B 228 LYS ASP ASN ILE VAL LEU GLY GLU GLY GLY ILE THR LEU
SEQRES 11 B 228 SER GLY GLY GLN ARG ALA ARG ILE SER LEU ALA ARG ALA
SEQRES 12 B 228 VAL TYR LYS ASP ALA ASP LEU TYR LEU LEU ASP SER PRO
SEQRES 13 B 228 PHE GLY TYR LEU ASP VAL LEU THR GLU LYS GLU ILE PHE
SEQRES 14 B 228 GLU SER CYS VAL CYS LYS LEU MET ALA ASN LYS THR ARG
SEQRES 15 B 228 ILE LEU VAL THR SER LYS MET GLU HIS LEU LYS LYS ALA
SEQRES 16 B 228 ASP LYS ILE LEU ILE LEU HIS GLU GLY SER SER TYR PHE
SEQRES 17 B 228 TYR GLY THR PHE SER GLU LEU GLN ASN LEU GLN PRO ASP
SEQRES 18 B 228 PHE SER SER LYS LEU MET GLY
HET MG A 3 1
HET ATP A 1 31
HET MG B 4 1
HET ATP B 2 31
HETNAM MG MAGNESIUM ION
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 3 MG 2(MG 2+)
FORMUL 4 ATP 2(C10 H16 N5 O13 P3)
FORMUL 7 HOH *130(H2 O)
HELIX 1 1 GLY A 463 MET A 472 1 10
HELIX 2 2 ILE A 502 GLY A 509 1 7
HELIX 3 3 ASP A 513 CYS A 524 1 12
HELIX 4 4 LEU A 526 PHE A 533 1 8
HELIX 5 5 GLU A 535 ASN A 538 5 4
HELIX 6 6 SER A 549 LYS A 564 1 16
HELIX 7 7 ASP A 579 CYS A 590 1 12
HELIX 8 8 LYS A 606 LYS A 612 1 7
HELIX 9 9 THR A 629 ASN A 635 1 7
HELIX 10 10 ASP A 639 MET A 645 1 7
HELIX 11 11 GLY B 463 MET B 472 1 10
HELIX 12 12 ILE B 502 GLY B 509 1 7
HELIX 13 13 ASP B 513 CYS B 524 1 12
HELIX 14 14 LEU B 526 SER B 531 1 6
HELIX 15 15 GLU B 535 ASN B 538 5 4
HELIX 16 16 SER B 549 LYS B 564 1 16
HELIX 17 17 ASP B 579 CYS B 590 1 12
HELIX 18 18 LYS B 606 ALA B 613 1 8
HELIX 19 19 THR B 629 LEU B 636 1 8
SHEET 1 A 3 LEU A 441 GLU A 449 0
SHEET 2 A 3 THR A 390 ALA A 399 -1 N GLU A 391 O ILE A 448
SHEET 3 A 3 GLU A 479 HIS A 484 -1 O LYS A 483 N VAL A 393
SHEET 1 B 6 ILE A 488 CYS A 491 0
SHEET 2 B 6 LEU A 568 ASP A 572 1 O LEU A 570 N SER A 489
SHEET 3 B 6 THR A 599 VAL A 603 1 O ILE A 601 N LEU A 571
SHEET 4 B 6 LEU A 453 ALA A 457 1 N VAL A 456 O LEU A 602
SHEET 5 B 6 LYS A 615 HIS A 620 1 O LEU A 619 N ALA A 457
SHEET 6 B 6 SER A 623 GLY A 628 -1 O TYR A 625 N ILE A 618
SHEET 1 C 2 GLY A 500 THR A 501 0
SHEET 2 C 2 VAL A 540 LEU A 541 -1 O LEU A 541 N GLY A 500
SHEET 1 D 3 LEU B 441 GLU B 449 0
SHEET 2 D 3 THR B 390 ALA B 399 -1 N MET B 394 O PHE B 446
SHEET 3 D 3 GLU B 479 HIS B 484 -1 O LYS B 481 N GLU B 395
SHEET 1 E 6 ILE B 488 CYS B 491 0
SHEET 2 E 6 LEU B 568 ASP B 572 1 O LEU B 570 N CYS B 491
SHEET 3 E 6 ARG B 600 VAL B 603 1 O ILE B 601 N TYR B 569
SHEET 4 E 6 LEU B 453 ALA B 457 1 N LEU B 454 O ARG B 600
SHEET 5 E 6 LYS B 615 HIS B 620 1 O LEU B 619 N ALA B 457
SHEET 6 E 6 SER B 623 GLY B 628 -1 O GLY B 628 N ILE B 616
SHEET 1 F 2 GLY B 500 THR B 501 0
SHEET 2 F 2 VAL B 540 LEU B 541 -1 O LEU B 541 N GLY B 500
LINK C GLY A 404 N GLY A 437 1555 1555 1.34
LINK C GLY B 404 N GLY B 437 1555 1555 1.33
SITE 1 AC1 5 ATP A 1 THR A 465 GLN A 493 HOH A 647
SITE 2 AC1 5 HOH A 648
SITE 1 AC2 5 ATP B 2 THR B 465 GLN B 493 HOH B 647
SITE 2 AC2 5 HOH B 648
SITE 1 AC3 22 MG A 3 TRP A 401 VAL A 440 THR A 460
SITE 2 AC3 22 GLY A 461 ALA A 462 GLY A 463 LYS A 464
SITE 3 AC3 22 THR A 465 SER A 466 GLN A 493 HOH A 647
SITE 4 AC3 22 HOH A 648 HOH A 649 HOH A 686 PHE B 533
SITE 5 AC3 22 THR B 547 SER B 549 GLY B 550 GLY B 551
SITE 6 AC3 22 GLN B 552 HOH B 654
SITE 1 AC4 21 THR A 547 SER A 549 GLY A 550 GLY A 551
SITE 2 AC4 21 GLN A 552 MG B 4 TRP B 401 VAL B 440
SITE 3 AC4 21 THR B 460 GLY B 461 ALA B 462 GLY B 463
SITE 4 AC4 21 LYS B 464 THR B 465 SER B 466 GLN B 493
SITE 5 AC4 21 HOH B 647 HOH B 648 HOH B 649 HOH B 655
SITE 6 AC4 21 HOH B 696
CRYST1 43.152 92.662 106.471 90.00 90.00 90.00 P 21 21 21 8
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 0.023174 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010792 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009392 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
