HEADER TRANSPORT PROTEIN 14-JUN-16 5KHK
TITLE HCN2 CNBD IN COMPLEX WITH 2-AMINOPURINE RIBOSIDE-3', 5'-CYCLIC
TITLE 2 MONOPHOSPHATE (2-NH2-CPUMP)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM/SODIUM HYPERPOLARIZATION-ACTIVATED CYCLIC
COMPND 3 NUCLEOTIDE-GATED CHANNEL 2;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 443-643;
COMPND 6 SYNONYM: BRAIN CYCLIC NUCLEOTIDE-GATED CHANNEL 2,BCNG-2,
COMPND 7 HYPERPOLARIZATION-ACTIVATED CATION CHANNEL 1,HAC-1;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: HCN2, BCNG2, HAC1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASIMD;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS PROTEIN-LIGAND COMPLEX, CYCILC NUCLEOTIDE BINDING DOMAIN, ION
KEYWDS 2 TRANSPORT, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR L.C.T.NG,I.PUTRENKO,V.BARONAS,F.VAN PETEGEM,E.A.ACCILI
REVDAT 3 27-SEP-23 5KHK 1 JRNL REMARK
REVDAT 2 19-OCT-16 5KHK 1 JRNL
REVDAT 1 14-SEP-16 5KHK 0
JRNL AUTH L.C.NG,I.PUTRENKO,V.BARONAS,F.VAN PETEGEM,E.A.ACCILI
JRNL TITL CYCLIC PURINE AND PYRIMIDINE NUCLEOTIDES BIND TO THE HCN2
JRNL TITL 2 ION CHANNEL AND VARIABLY PROMOTE C-TERMINAL DOMAIN
JRNL TITL 3 INTERACTIONS AND OPENING.
JRNL REF STRUCTURE V. 24 1629 2016
JRNL REFN ISSN 0969-2126
JRNL PMID 27568927
JRNL DOI 10.1016/J.STR.2016.06.024
REMARK 2
REMARK 2 RESOLUTION. 2.07 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.07
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 13132
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 692
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.07
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.12
REMARK 3 REFLECTION IN BIN (WORKING SET) : 912
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.38
REMARK 3 BIN R VALUE (WORKING SET) : 0.3220
REMARK 3 BIN FREE R VALUE SET COUNT : 46
REMARK 3 BIN FREE R VALUE : 0.4370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1612
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 52
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.46
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.25000
REMARK 3 B22 (A**2) : 0.25000
REMARK 3 B33 (A**2) : -0.51000
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): 0.238
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.199
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.147
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.397
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1702 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1583 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2306 ; 1.736 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3628 ; 0.800 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 210 ; 5.769 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 85 ;32.149 ;23.176
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 293 ;17.482 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;16.578 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 247 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1942 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 424 ; 0.001 ; 0.020
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 ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; 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 : NULL
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: MOLECULAR REPLACEMENT
REMARK 4
REMARK 4 5KHK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-16.
REMARK 100 THE DEPOSITION ID IS D_1000222238.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-FEB-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033200
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : 1000 UM THICK SENSOR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13521
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
REMARK 200 RESOLUTION RANGE LOW (A) : 38.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 13.86
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.9900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.76700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.080
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1Q5O
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM NACL, 0.1 MM SODIUM CITRATE PH
REMARK 280 4.6, 12% PEG 400, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 21 2
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 -Y+1/2,X+1/2,Z
REMARK 290 4555 Y+1/2,-X+1/2,Z
REMARK 290 5555 -X+1/2,Y+1/2,-Z
REMARK 290 6555 X+1/2,-Y+1/2,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 48.21450
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 48.21450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 48.21450
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 48.21450
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 48.21450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.21450
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 48.21450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.21450
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 96.42900
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 48.21450
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 -48.21450
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 48.21450
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 48.21450
REMARK 350 BIOMT3 4 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 A 812 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 SER A 440
REMARK 465 ASN A 441
REMARK 465 ALA A 442
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 ASP A 443 CG OD1 OD2
REMARK 470 LYS A 464 CG CD CE NZ
REMARK 470 LYS A 552 CG CD CE NZ
REMARK 470 LYS A 567 CG CD CE NZ
REMARK 470 ASN A 569 CG OD1 ND2
REMARK 470 LYS A 570 CG CD CE NZ
REMARK 470 GLU A 616 CG CD OE1 OE2
REMARK 470 GLU A 617 CG CD OE1 OE2
REMARK 470 ARG A 623 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 638 CG CD CE NZ
REMARK 470 LYS A 639 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 NE ARG A 446 O HOH A 801 2.03
REMARK 500 NH2 ARG A 596 O HOH A 802 2.14
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 ASP A 522 CB - CG - OD1 ANGL. DEV. = 7.7 DEGREES
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 ASN A 569 -9.65 119.63
REMARK 500 ASP A 576 130.98 -39.91
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 6SZ A 701
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5KHG RELATED DB: PDB
REMARK 900 RELATED ID: 5KHH RELATED DB: PDB
REMARK 900 RELATED ID: 5KHI RELATED DB: PDB
REMARK 900 RELATED ID: 5KHJ RELATED DB: PDB
DBREF 5KHK A 443 643 UNP O88703 HCN2_MOUSE 443 643
SEQADV 5KHK SER A 440 UNP O88703 EXPRESSION TAG
SEQADV 5KHK ASN A 441 UNP O88703 EXPRESSION TAG
SEQADV 5KHK ALA A 442 UNP O88703 EXPRESSION TAG
SEQRES 1 A 204 SER ASN ALA ASP SER SER ARG ARG GLN TYR GLN GLU LYS
SEQRES 2 A 204 TYR LYS GLN VAL GLU GLN TYR MET SER PHE HIS LYS LEU
SEQRES 3 A 204 PRO ALA ASP PHE ARG GLN LYS ILE HIS ASP TYR TYR GLU
SEQRES 4 A 204 HIS ARG TYR GLN GLY LYS MET PHE ASP GLU ASP SER ILE
SEQRES 5 A 204 LEU GLY GLU LEU ASN GLY PRO LEU ARG GLU GLU ILE VAL
SEQRES 6 A 204 ASN PHE ASN CSX ARG LYS LEU VAL ALA SER MET PRO LEU
SEQRES 7 A 204 PHE ALA ASN ALA ASP PRO ASN PHE VAL THR ALA MET LEU
SEQRES 8 A 204 THR LYS LEU LYS PHE GLU VAL PHE GLN PRO GLY ASP TYR
SEQRES 9 A 204 ILE ILE ARG GLU GLY THR ILE GLY LYS LYS MET TYR PHE
SEQRES 10 A 204 ILE GLN HIS GLY VAL VAL SER VAL LEU THR LYS GLY ASN
SEQRES 11 A 204 LYS GLU MET LYS LEU SER ASP GLY SER TYR PHE GLY GLU
SEQRES 12 A 204 ILE CYS LEU LEU THR ARG GLY ARG ARG THR ALA SER VAL
SEQRES 13 A 204 ARG ALA ASP THR TYR CYS ARG LEU TYR SER LEU SER VAL
SEQRES 14 A 204 ASP ASN PHE ASN GLU VAL LEU GLU GLU TYR PRO MET MET
SEQRES 15 A 204 ARG ARG ALA PHE GLU THR VAL ALA ILE ASP ARG LEU ASP
SEQRES 16 A 204 ARG ILE GLY LYS LYS ASN SER ILE LEU
MODRES 5KHK CSX A 508 CYS MODIFIED RESIDUE
HET CSX A 508 7
HET 6SZ A 701 22
HETNAM CSX S-OXY CYSTEINE
HETNAM 6SZ 2-AMINOPURINE RIBOSIDE-3',5'-CYCLIC MONOPHOSPHATE
HETSYN 6SZ 2-NH2-CPUMP
FORMUL 1 CSX C3 H7 N O3 S
FORMUL 2 6SZ C10 H12 N5 O6 P
FORMUL 3 HOH *52(H2 O)
HELIX 1 AA1 ASP A 443 HIS A 463 1 21
HELIX 2 AA2 PRO A 466 GLN A 482 1 17
HELIX 3 AA3 ASP A 487 LEU A 495 1 9
HELIX 4 AA4 ASN A 496 CSX A 508 1 13
HELIX 5 AA5 CSX A 508 MET A 515 1 8
HELIX 6 AA6 MET A 515 ASN A 520 1 6
HELIX 7 AA7 ASP A 522 THR A 531 1 10
HELIX 8 AA8 GLY A 581 ARG A 588 1 8
HELIX 9 AA9 VAL A 608 TYR A 618 1 11
HELIX 10 AB1 PRO A 619 ARG A 635 1 17
SHEET 1 AA1 4 LYS A 534 PHE A 538 0
SHEET 2 AA1 4 CYS A 601 SER A 607 -1 O LEU A 603 N GLU A 536
SHEET 3 AA1 4 LYS A 553 HIS A 559 -1 N HIS A 559 O ARG A 602
SHEET 4 AA1 4 TYR A 579 PHE A 580 -1 O PHE A 580 N TYR A 555
SHEET 1 AA2 4 TYR A 543 ILE A 545 0
SHEET 2 AA2 4 SER A 594 ALA A 597 -1 O VAL A 595 N ILE A 545
SHEET 3 AA2 4 VAL A 562 LEU A 565 -1 N LEU A 565 O SER A 594
SHEET 4 AA2 4 GLU A 571 LEU A 574 -1 O MET A 572 N VAL A 564
LINK C ASN A 507 N CSX A 508 1555 1555 1.33
LINK C CSX A 508 N ARG A 509 1555 1555 1.33
SITE 1 AC1 13 VAL A 564 MET A 572 LEU A 574 PHE A 580
SITE 2 AC1 13 GLY A 581 GLU A 582 ILE A 583 CYS A 584
SITE 3 AC1 13 ARG A 591 THR A 592 ALA A 593 ARG A 632
SITE 4 AC1 13 ILE A 636
CRYST1 96.429 96.429 46.423 90.00 90.00 90.00 P 4 21 2 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 0.010370 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010370 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021541 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
