HEADER TRANSPORT PROTEIN 17-OCT-05 2BBT
TITLE HUMAN DELTAF508 NBD1 WITH TWO SOLUBLIZING MUTATIONS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 389-678;
COMPND 5 SYNONYM: CFTR, CAMP-DEPENDENT CHLORIDE CHANNEL;
COMPND 6 ENGINEERED: YES;
COMPND 7 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: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODON+RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET26B-DERIVED
KEYWDS ATP BINDING CASSETTE, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.A.LEWIS,M.C.KEARINS,K.CONNERS,X.ZHAO,F.LU,J.M.SAUDER,S.EMTAGE
REVDAT 7 23-AUG-23 2BBT 1 REMARK
REVDAT 6 20-OCT-21 2BBT 1 REMARK SEQADV LINK
REVDAT 5 14-NOV-18 2BBT 1 AUTHOR
REVDAT 4 18-OCT-17 2BBT 1 REMARK
REVDAT 3 16-FEB-10 2BBT 1 JRNL
REVDAT 2 24-FEB-09 2BBT 1 VERSN
REVDAT 1 01-NOV-05 2BBT 0
JRNL AUTH H.A.LEWIS,C.WANG,X.ZHAO,Y.HAMURO,K.CONNERS,M.C.KEARINS,F.LU,
JRNL AUTH 2 J.M.SAUDER,K.S.MOLNAR,S.J.COALES,P.C.MALONEY,W.B.GUGGINO,
JRNL AUTH 3 D.R.WETMORE,P.C.WEBER,J.F.HUNT
JRNL TITL STRUCTURE AND DYNAMICS OF NBD1 FROM CFTR CHARACTERIZED USING
JRNL TITL 2 CRYSTALLOGRAPHY AND HYDROGEN/DEUTERIUM EXCHANGE MASS
JRNL TITL 3 SPECTROMETRY.
JRNL REF J.MOL.BIOL. V. 396 406 2010
JRNL REFN ISSN 0022-2836
JRNL PMID 19944699
JRNL DOI 10.1016/J.JMB.2009.11.051
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH-HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.7
REMARK 3 NUMBER OF REFLECTIONS : 23718
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) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1213
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3974
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 129
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.31400
REMARK 3 B22 (A**2) : -1.47800
REMARK 3 B33 (A**2) : 1.16400
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 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.006 ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 1.029 ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; 4.897 ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; 0.065 ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; 0.002 ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; 1.158 ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; 1.989 ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; 2.367 ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; 3.634 ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT CORRECTION
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2BBT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034915.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.5
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) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23718
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 63.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -4.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1XMJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.28
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% PEG4000, 0.2M LICL, 50MM TRIS PH
REMARK 280 7.5, 3MM ATP, 5MM MGCL2, 2MM TCEP, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 280K
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 32.70250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 66.38850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.84300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.38850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.70250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.84300
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
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 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 SER A 388
REMARK 465 THR A 389
REMARK 465 GLN A 414
REMARK 465 ASN A 415
REMARK 465 ASN A 416
REMARK 465 ASN A 417
REMARK 465 ASN A 418
REMARK 465 ARG A 419
REMARK 465 LYS A 420
REMARK 465 THR A 421
REMARK 465 SER A 422
REMARK 465 ASN A 423
REMARK 465 GLY A 424
REMARK 465 ASP A 425
REMARK 465 ASP A 426
REMARK 465 SER A 427
REMARK 465 LEU A 428
REMARK 465 PHE A 429
REMARK 465 PHE A 430
REMARK 465 SER A 431
REMARK 465 ASN A 432
REMARK 465 PHE A 433
REMARK 465 SER A 434
REMARK 465 LEU A 435
REMARK 465 LEU A 436
REMARK 465 GLU A 543
REMARK 465 GLY A 544
REMARK 465 LYS A 643
REMARK 465 LEU A 644
REMARK 465 MET A 645
REMARK 465 GLY A 646
REMARK 465 CYS A 647
REMARK 465 SER A 670
REMARK 465 LEU A 671
REMARK 465 GLU A 672
REMARK 465 GLY A 673
REMARK 465 ASP A 674
REMARK 465 ALA A 675
REMARK 465 PRO A 676
REMARK 465 VAL A 677
REMARK 465 SER A 678
REMARK 465 SER B 388
REMARK 465 ARG B 419
REMARK 465 LYS B 420
REMARK 465 THR B 421
REMARK 465 SER B 422
REMARK 465 ASN B 423
REMARK 465 GLY B 424
REMARK 465 ASP B 425
REMARK 465 ASP B 426
REMARK 465 SER B 427
REMARK 465 LEU B 428
REMARK 465 PHE B 429
REMARK 465 PHE B 430
REMARK 465 SER B 431
REMARK 465 ASN B 432
REMARK 465 PHE B 433
REMARK 465 SER B 434
REMARK 465 LEU B 435
REMARK 465 LEU B 436
REMARK 465 GLY B 437
REMARK 465 GLY B 542
REMARK 465 GLU B 543
REMARK 465 GLY B 544
REMARK 465 GLY B 646
REMARK 465 CYS B 647
REMARK 465 GLU B 672
REMARK 465 GLY B 673
REMARK 465 ASP B 674
REMARK 465 ALA B 675
REMARK 465 PRO B 676
REMARK 465 VAL B 677
REMARK 465 SER B 678
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 GLU A 410 CG CD OE1 OE2
REMARK 470 LYS A 411 CG CD CE NZ
REMARK 470 LYS A 413 CE NZ
REMARK 470 GLN A 634 CG CD OE1 NE2
REMARK 470 LEU A 636 CG CD1 CD2
REMARK 470 ARG A 637 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 639 CG OD1 OD2
REMARK 470 ARG A 668 NE CZ NH1 NH2
REMARK 470 GLU B 410 CD OE1 OE2
REMARK 470 GLN B 414 CD OE1 NE2
REMARK 470 SER B 642 OG
REMARK 470 LYS B 643 CG CD CE NZ
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 PRO A 499 99.54 -61.94
REMARK 500 LYS A 536 -127.16 60.67
REMARK 500 CYS A 590 -70.47 -83.58
REMARK 500 LYS A 593 -73.14 -81.78
REMARK 500 LYS B 536 -118.52 57.06
REMARK 500 CYS B 590 -69.24 -94.17
REMARK 500 LYS B 593 -61.98 -98.27
REMARK 500 SER B 649 -11.26 -163.91
REMARK 500 HIS B 667 30.14 -144.04
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 3 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP A 1 O2G
REMARK 620 2 ATP A 1 O2B 88.4
REMARK 620 3 HOH A 132 O 100.7 102.3
REMARK 620 4 THR A 465 OG1 165.1 83.9 93.5
REMARK 620 5 GLN A 493 OE1 95.8 158.9 97.2 87.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 4 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP B 2 O2G
REMARK 620 2 ATP B 2 O2B 82.2
REMARK 620 3 HOH B 116 O 84.3 89.6
REMARK 620 4 THR B 465 OG1 161.8 82.0 86.6
REMARK 620 5 GLN B 493 OE1 120.3 156.4 99.0 76.7
REMARK 620 N 1 2 3 4
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: 2BBO RELATED DB: PDB
REMARK 900 HUMAN NBD1 WITH PHE508
REMARK 900 RELATED ID: 2BBS RELATED DB: PDB
REMARK 900 HUMAN DELTAF508 NBD1 WITH THREE SOLUBILIZING MUTATIONS
DBREF 2BBT A 389 678 UNP P13569 CFTR_HUMAN 389 678
DBREF 2BBT B 389 678 UNP P13569 CFTR_HUMAN 389 678
SEQADV 2BBT SER A 388 UNP P13569 THR 388 CLONING ARTIFACT
SEQADV 2BBT ASN A 494 UNP P13569 PHE 494 ENGINEERED MUTATION
SEQADV 2BBT A UNP P13569 PHE 508 DELETION
SEQADV 2BBT ARG A 637 UNP P13569 GLN 637 ENGINEERED MUTATION
SEQADV 2BBT SER B 388 UNP P13569 THR 388 CLONING ARTIFACT
SEQADV 2BBT ASN B 494 UNP P13569 PHE 494 ENGINEERED MUTATION
SEQADV 2BBT B UNP P13569 PHE 508 DELETION
SEQADV 2BBT ARG B 637 UNP P13569 GLN 637 ENGINEERED MUTATION
SEQRES 1 A 290 SER THR THR GLU VAL VAL MET GLU ASN VAL THR ALA PHE
SEQRES 2 A 290 TRP GLU GLU GLY PHE GLY GLU LEU PHE GLU LYS ALA LYS
SEQRES 3 A 290 GLN ASN ASN ASN ASN ARG LYS THR SER ASN GLY ASP ASP
SEQRES 4 A 290 SER LEU PHE PHE SER ASN PHE SER LEU LEU GLY THR PRO
SEQRES 5 A 290 VAL LEU LYS ASP ILE ASN PHE LYS ILE GLU ARG GLY GLN
SEQRES 6 A 290 LEU LEU ALA VAL ALA GLY SER THR GLY ALA GLY LYS THR
SEQRES 7 A 290 SER LEU LEU MET MET ILE MET GLY GLU LEU GLU PRO SER
SEQRES 8 A 290 GLU GLY LYS ILE LYS HIS SER GLY ARG ILE SER PHE CYS
SEQRES 9 A 290 SER GLN ASN SER TRP ILE MET PRO GLY THR ILE LYS GLU
SEQRES 10 A 290 ASN ILE ILE GLY VAL SER TYR ASP GLU TYR ARG TYR ARG
SEQRES 11 A 290 SER VAL ILE LYS ALA CYS GLN LEU GLU GLU ASP ILE SER
SEQRES 12 A 290 LYS PHE ALA GLU LYS ASP ASN ILE VAL LEU GLY GLU GLY
SEQRES 13 A 290 GLY ILE THR LEU SER GLY GLY GLN ARG ALA ARG ILE SER
SEQRES 14 A 290 LEU ALA ARG ALA VAL TYR LYS ASP ALA ASP LEU TYR LEU
SEQRES 15 A 290 LEU ASP SER PRO PHE GLY TYR LEU ASP VAL LEU THR GLU
SEQRES 16 A 290 LYS GLU ILE PHE GLU SER CYS VAL CYS LYS LEU MET ALA
SEQRES 17 A 290 ASN LYS THR ARG ILE LEU VAL THR SER LYS MET GLU HIS
SEQRES 18 A 290 LEU LYS LYS ALA ASP LYS ILE LEU ILE LEU HIS GLU GLY
SEQRES 19 A 290 SER SER TYR PHE TYR GLY THR PHE SER GLU LEU GLN ASN
SEQRES 20 A 290 LEU ARG PRO ASP PHE SER SER LYS LEU MET GLY CYS ASP
SEQRES 21 A 290 SER PHE ASP GLN PHE SER ALA GLU ARG ARG ASN SER ILE
SEQRES 22 A 290 LEU THR GLU THR LEU HIS ARG PHE SER LEU GLU GLY ASP
SEQRES 23 A 290 ALA PRO VAL SER
SEQRES 1 B 290 SER THR THR GLU VAL VAL MET GLU ASN VAL THR ALA PHE
SEQRES 2 B 290 TRP GLU GLU GLY PHE GLY GLU LEU PHE GLU LYS ALA LYS
SEQRES 3 B 290 GLN ASN ASN ASN ASN ARG LYS THR SER ASN GLY ASP ASP
SEQRES 4 B 290 SER LEU PHE PHE SER ASN PHE SER LEU LEU GLY THR PRO
SEQRES 5 B 290 VAL LEU LYS ASP ILE ASN PHE LYS ILE GLU ARG GLY GLN
SEQRES 6 B 290 LEU LEU ALA VAL ALA GLY SER THR GLY ALA GLY LYS THR
SEQRES 7 B 290 SER LEU LEU MET MET ILE MET GLY GLU LEU GLU PRO SER
SEQRES 8 B 290 GLU GLY LYS ILE LYS HIS SER GLY ARG ILE SER PHE CYS
SEQRES 9 B 290 SER GLN ASN SER TRP ILE MET PRO GLY THR ILE LYS GLU
SEQRES 10 B 290 ASN ILE ILE GLY VAL SER TYR ASP GLU TYR ARG TYR ARG
SEQRES 11 B 290 SER VAL ILE LYS ALA CYS GLN LEU GLU GLU ASP ILE SER
SEQRES 12 B 290 LYS PHE ALA GLU LYS ASP ASN ILE VAL LEU GLY GLU GLY
SEQRES 13 B 290 GLY ILE THR LEU SER GLY GLY GLN ARG ALA ARG ILE SER
SEQRES 14 B 290 LEU ALA ARG ALA VAL TYR LYS ASP ALA ASP LEU TYR LEU
SEQRES 15 B 290 LEU ASP SER PRO PHE GLY TYR LEU ASP VAL LEU THR GLU
SEQRES 16 B 290 LYS GLU ILE PHE GLU SER CYS VAL CYS LYS LEU MET ALA
SEQRES 17 B 290 ASN LYS THR ARG ILE LEU VAL THR SER LYS MET GLU HIS
SEQRES 18 B 290 LEU LYS LYS ALA ASP LYS ILE LEU ILE LEU HIS GLU GLY
SEQRES 19 B 290 SER SER TYR PHE TYR GLY THR PHE SER GLU LEU GLN ASN
SEQRES 20 B 290 LEU ARG PRO ASP PHE SER SER LYS LEU MET GLY CYS ASP
SEQRES 21 B 290 SER PHE ASP GLN PHE SER ALA GLU ARG ARG ASN SER ILE
SEQRES 22 B 290 LEU THR GLU THR LEU HIS ARG PHE SER LEU GLU GLY ASP
SEQRES 23 B 290 ALA PRO VAL SER
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 *129(H2 O)
HELIX 1 1 GLU A 402 LYS A 413 1 12
HELIX 2 2 GLY A 463 MET A 472 1 10
HELIX 3 3 THR A 501 GLY A 509 1 8
HELIX 4 4 ASP A 513 CYS A 524 1 12
HELIX 5 5 LEU A 526 SER A 531 1 6
HELIX 6 6 GLU A 535 ILE A 539 5 5
HELIX 7 7 SER A 549 LYS A 564 1 16
HELIX 8 8 ASP A 579 CYS A 590 1 12
HELIX 9 9 LYS A 606 ALA A 613 1 8
HELIX 10 10 THR A 629 ARG A 637 1 9
HELIX 11 11 ARG A 637 SER A 642 1 6
HELIX 12 12 SER A 654 PHE A 669 1 16
HELIX 13 13 GLY B 404 ASN B 418 1 15
HELIX 14 14 GLY B 463 MET B 472 1 10
HELIX 15 15 ILE B 502 GLY B 509 1 7
HELIX 16 16 ASP B 513 CYS B 524 1 12
HELIX 17 17 LEU B 526 PHE B 533 1 8
HELIX 18 18 GLU B 535 ASN B 538 5 4
HELIX 19 19 SER B 549 LYS B 564 1 16
HELIX 20 20 ASP B 579 CYS B 590 1 12
HELIX 21 21 LYS B 606 ALA B 613 1 8
HELIX 22 22 THR B 629 ARG B 637 1 9
HELIX 23 23 ARG B 637 LEU B 644 1 8
HELIX 24 24 SER B 654 GLU B 664 1 11
SHEET 1 A 3 LEU A 441 ILE A 448 0
SHEET 2 A 3 VAL A 392 ALA A 399 -1 N MET A 394 O PHE A 446
SHEET 3 A 3 GLU A 479 LYS A 483 -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 CYS A 491
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 GLY A 458 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 GLY A 628 N ILE A 616
SHEET 1 C 3 LEU B 441 ILE B 448 0
SHEET 2 C 3 VAL B 392 ALA B 399 -1 N MET B 394 O PHE B 446
SHEET 3 C 3 PRO B 477 LYS B 483 -1 O SER B 478 N THR B 398
SHEET 1 D 6 ILE B 488 CYS B 491 0
SHEET 2 D 6 LEU B 568 ASP B 572 1 O LEU B 570 N CYS B 491
SHEET 3 D 6 ARG B 600 VAL B 603 1 O ILE B 601 N LEU B 571
SHEET 4 D 6 LEU B 453 GLY B 458 1 N LEU B 454 O LEU B 602
SHEET 5 D 6 LYS B 615 HIS B 620 1 O LEU B 617 N ALA B 457
SHEET 6 D 6 SER B 623 GLY B 628 -1 O GLY B 628 N ILE B 616
SHEET 1 E 2 GLY B 500 THR B 501 0
SHEET 2 E 2 VAL B 540 LEU B 541 -1 O LEU B 541 N GLY B 500
LINK O2G ATP A 1 MG MG A 3 1555 1555 1.97
LINK O2B ATP A 1 MG MG A 3 1555 1555 2.18
LINK MG MG A 3 O HOH A 132 1555 1555 1.99
LINK MG MG A 3 OG1 THR A 465 1555 1555 2.10
LINK MG MG A 3 OE1 GLN A 493 1555 1555 2.46
LINK O2G ATP B 2 MG MG B 4 1555 1555 1.99
LINK O2B ATP B 2 MG MG B 4 1555 1555 2.17
LINK MG MG B 4 O HOH B 116 1555 1555 2.29
LINK MG MG B 4 OG1 THR B 465 1555 1555 2.17
LINK MG MG B 4 OE1 GLN B 493 1555 1555 2.24
SITE 1 AC1 4 ATP A 1 HOH A 132 THR A 465 GLN A 493
SITE 1 AC2 4 ATP B 2 HOH B 116 THR B 465 GLN B 493
SITE 1 AC3 16 MG A 3 HOH A 30 HOH A 42 HOH A 53
SITE 2 AC3 16 HOH A 132 TRP A 401 VAL A 440 THR A 460
SITE 3 AC3 16 GLY A 461 ALA A 462 GLY A 463 LYS A 464
SITE 4 AC3 16 THR A 465 SER A 466 GLN A 493 ASN B 597
SITE 1 AC4 12 MG B 4 HOH B 116 TRP B 401 VAL B 440
SITE 2 AC4 12 THR B 460 GLY B 461 ALA B 462 GLY B 463
SITE 3 AC4 12 LYS B 464 THR B 465 SER B 466 GLN B 493
CRYST1 65.405 65.686 132.777 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 0.015289 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015224 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007531 0.00000
(ATOM LINES ARE NOT SHOWN.)
END