HEADER MEMBRANE PROTEIN 18-FEB-10 3LUT
TITLE A STRUCTURAL MODEL FOR THE FULL-LENGTH SHAKER POTASSIUM CHANNEL KV1.2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VOLTAGE-GATED POTASSIUM CHANNEL SUBUNIT BETA-2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: K(+) CHANNEL SUBUNIT BETA-2, KV-BETA-2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY A MEMBER 2;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: VOLTAGE-GATED POTASSIUM CHANNEL SUBUNIT KV1.2, RBK2, RCK5,
COMPND 10 RAK;
COMPND 11 ENGINEERED: YES;
COMPND 12 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: KCNAB2, CKBETA2, KCNB3;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 10 ORGANISM_COMMON: RAT;
SOURCE 11 ORGANISM_TAXID: 10116;
SOURCE 12 GENE: KCNA2;
SOURCE 13 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS VOLTAGE GATING, POTASSIUM CHANNEL, KV1.2, GATING CHARGES, NORMAL-MODE
KEYWDS 2 ANALYSIS, ION TRANSPORT, IONIC CHANNEL, NADP, PHOSPHOPROTEIN,
KEYWDS 3 POTASSIUM, POTASSIUM TRANSPORT, TRANSPORT, VOLTAGE-GATED CHANNEL,
KEYWDS 4 GLYCOPROTEIN, LIPOPROTEIN, MEMBRANE, PALMITATE, TRANSMEMBRANE,
KEYWDS 5 MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR X.CHEN,F.NI,Q.WANG,J.MA
REVDAT 5 21-FEB-24 3LUT 1 REMARK
REVDAT 4 13-OCT-21 3LUT 1 REMARK SEQADV LINK
REVDAT 3 26-OCT-11 3LUT 1 REMARK VERSN
REVDAT 2 07-JUL-10 3LUT 1 JRNL
REVDAT 1 23-JUN-10 3LUT 0
JRNL AUTH X.CHEN,Q.WANG,F.NI,J.MA
JRNL TITL STRUCTURE OF THE FULL-LENGTH SHAKER POTASSIUM CHANNEL KV1.2
JRNL TITL 2 BY NORMAL-MODE-BASED X-RAY CRYSTALLOGRAPHIC REFINEMENT.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 11352 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20534430
JRNL DOI 10.1073/PNAS.1000142107
REMARK 0
REMARK 0 THIS ENTRY 3LUT REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL
REMARK 0 STRUCTURAL DATA (R2A79SF) DETERMINED BY AUTHORS OF THE PDB ENTRY
REMARK 0 2A79: LONG,S.B., CAMPBELL,E.B., MACKINNON,R.
REMARK 0 ORIGINAL DATA REFERENCE 1
REMARK 0 PDB ID: 2A79
REMARK 0 AUTH S.B.LONG,E.B.CAMPBELL,R.MACKINNON
REMARK 0 TITL CRYSTAL STRUCTURE OF A MAMMALIAN VOLTAGE-DEPENDENT SHAKER
REMARK 0 TITL 2 FAMILY K+ CHANNEL
REMARK 0 REF SCIENCE V. 309 897 2005
REMARK 0 REFN ISSN 0036-8075
REMARK 0 PMID 16002581
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.B.LONG,X.TAO,E.B.CAMPBELL,R.MACKINNON
REMARK 1 TITL ATOMIC STRUCTURE OF A VOLTAGE-DEPENDENT K+ CHANNEL
REMARK 1 TITL 2 INALIPIDMEMBRANE-LIKE ENVIRONMENT
REMARK 1 REF NATURE V. 450 376 2007
REMARK 1 REFN ISSN 0028-0836
REMARK 1 PMID 18004376
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 31566
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1776
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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1990
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE SET COUNT : 128
REMARK 3 BIN FREE R VALUE : 0.3230
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5708
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 86
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 123.3
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.10000
REMARK 3 B22 (A**2) : -3.10000
REMARK 3 B33 (A**2) : 6.20000
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): 0.403
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.280
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.226
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 26.941
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.922
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5894 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7989 ; 1.210 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 714 ; 4.998 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 265 ;34.655 ;23.434
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1009 ;17.325 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;16.013 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 880 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4435 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3072 ; 0.263 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4146 ; 0.314 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 250 ; 0.168 ; 0.200
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): 174 ; 0.324 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.200 ; 0.200
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 : BABINET MODEL WITH MASK
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 3LUT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1000057757.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : M
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
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: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: AUTHOR USED THE SF DATA FROM ENTRY 2A79.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
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,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+1/2,Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 56.80250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 56.80250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 130.23650
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 56.80250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 56.80250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 130.23650
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 56.80250
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 56.80250
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 130.23650
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 56.80250
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 56.80250
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 130.23650
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 34450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 143810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -190.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 227.21000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 227.21000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 227.21000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 227.21000
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 K K B 500 LIES ON A SPECIAL POSITION.
REMARK 375 K K B 501 LIES ON A SPECIAL POSITION.
REMARK 375 K K B 502 LIES ON A SPECIAL POSITION.
REMARK 375 K K B 503 LIES ON A SPECIAL POSITION.
REMARK 375 K K B 504 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 MET A 1
REMARK 465 TYR A 2
REMARK 465 PRO A 3
REMARK 465 GLU A 4
REMARK 465 SER A 5
REMARK 465 THR A 6
REMARK 465 THR A 7
REMARK 465 GLY A 8
REMARK 465 SER A 9
REMARK 465 PRO A 10
REMARK 465 ALA A 11
REMARK 465 ARG A 12
REMARK 465 LEU A 13
REMARK 465 SER A 14
REMARK 465 LEU A 15
REMARK 465 ARG A 16
REMARK 465 GLN A 17
REMARK 465 THR A 18
REMARK 465 GLY A 19
REMARK 465 SER A 20
REMARK 465 PRO A 21
REMARK 465 GLY A 22
REMARK 465 MET A 23
REMARK 465 ILE A 24
REMARK 465 TYR A 25
REMARK 465 SER A 26
REMARK 465 THR A 27
REMARK 465 ARG A 28
REMARK 465 TYR A 29
REMARK 465 GLY A 30
REMARK 465 SER A 31
REMARK 465 PRO A 32
REMARK 465 LYS A 33
REMARK 465 ARG A 34
REMARK 465 GLN A 35
REMARK 465 LYS A 362
REMARK 465 LYS A 363
REMARK 465 ASP A 364
REMARK 465 TYR A 365
REMARK 465 ARG A 366
REMARK 465 SER A 367
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 VAL B 3
REMARK 465 ALA B 4
REMARK 465 THR B 5
REMARK 465 GLY B 6
REMARK 465 ASP B 7
REMARK 465 PRO B 8
REMARK 465 VAL B 9
REMARK 465 ASP B 10
REMARK 465 GLU B 11
REMARK 465 ALA B 12
REMARK 465 ALA B 13
REMARK 465 ALA B 14
REMARK 465 LEU B 15
REMARK 465 PRO B 16
REMARK 465 GLY B 17
REMARK 465 HIS B 18
REMARK 465 PRO B 19
REMARK 465 GLN B 20
REMARK 465 ASP B 21
REMARK 465 THR B 22
REMARK 465 TYR B 23
REMARK 465 ASP B 24
REMARK 465 PRO B 25
REMARK 465 GLU B 26
REMARK 465 ALA B 27
REMARK 465 ASP B 28
REMARK 465 HIS B 29
REMARK 465 GLU B 30
REMARK 465 CYS B 31
REMARK 465 GLU B 422
REMARK 465 GLY B 423
REMARK 465 GLU B 424
REMARK 465 GLU B 425
REMARK 465 GLN B 426
REMARK 465 ALA B 427
REMARK 465 GLN B 428
REMARK 465 TYR B 429
REMARK 465 LEU B 430
REMARK 465 GLN B 431
REMARK 465 VAL B 432
REMARK 465 THR B 433
REMARK 465 SER B 434
REMARK 465 CYS B 435
REMARK 465 PRO B 436
REMARK 465 LYS B 437
REMARK 465 ILE B 438
REMARK 465 PRO B 439
REMARK 465 SER B 440
REMARK 465 SER B 441
REMARK 465 PRO B 442
REMARK 465 ASP B 443
REMARK 465 LEU B 444
REMARK 465 LYS B 445
REMARK 465 LYS B 446
REMARK 465 SER B 447
REMARK 465 ARG B 448
REMARK 465 SER B 449
REMARK 465 ALA B 450
REMARK 465 SER B 451
REMARK 465 THR B 452
REMARK 465 ILE B 453
REMARK 465 SER B 454
REMARK 465 LYS B 455
REMARK 465 SER B 456
REMARK 465 ASP B 457
REMARK 465 TYR B 458
REMARK 465 MET B 459
REMARK 465 GLU B 460
REMARK 465 ILE B 461
REMARK 465 GLN B 462
REMARK 465 GLU B 463
REMARK 465 GLY B 464
REMARK 465 VAL B 465
REMARK 465 ASN B 466
REMARK 465 ASN B 467
REMARK 465 SER B 468
REMARK 465 ASN B 469
REMARK 465 GLU B 470
REMARK 465 ASP B 471
REMARK 465 PHE B 472
REMARK 465 ARG B 473
REMARK 465 GLU B 474
REMARK 465 GLU B 475
REMARK 465 ASN B 476
REMARK 465 LEU B 477
REMARK 465 LYS B 478
REMARK 465 THR B 479
REMARK 465 ALA B 480
REMARK 465 ASN B 481
REMARK 465 CYS B 482
REMARK 465 THR B 483
REMARK 465 LEU B 484
REMARK 465 ALA B 485
REMARK 465 ASN B 486
REMARK 465 THR B 487
REMARK 465 ASN B 488
REMARK 465 TYR B 489
REMARK 465 VAL B 490
REMARK 465 ASN B 491
REMARK 465 ILE B 492
REMARK 465 THR B 493
REMARK 465 LYS B 494
REMARK 465 MET B 495
REMARK 465 LEU B 496
REMARK 465 THR B 497
REMARK 465 ASP B 498
REMARK 465 VAL B 499
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 ARG B 240 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 290 CG CD1 CD2
REMARK 470 VAL B 381 CG1 CG2
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 OH TYR B 415 NH2 ARG B 419 2.04
REMARK 500 OD2 ASP B 259 NH2 ARG B 309 2.10
REMARK 500 O GLY B 199 CB TYR B 205 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH2 ARG B 297 OH TYR B 347 3755 2.18
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 PRO B 245 CD PRO B 245 N 0.118
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 VAL A 58 -41.77 70.81
REMARK 500 PHE A 120 -56.91 -175.18
REMARK 500 VAL A 227 -60.20 -102.15
REMARK 500 ALA A 247 58.25 36.10
REMARK 500 LEU A 278 34.17 -98.04
REMARK 500 GLU B 136 56.80 -95.80
REMARK 500 PRO B 141 -74.80 -48.13
REMARK 500 PHE B 145 -145.48 55.84
REMARK 500 SER B 158 -141.60 -88.25
REMARK 500 LEU B 185 -79.43 -66.42
REMARK 500 GLU B 193 -130.17 -178.57
REMARK 500 PHE B 202 -155.98 -157.87
REMARK 500 SER B 206 -71.55 -54.66
REMARK 500 PHE B 242 23.58 -63.18
REMARK 500 ALA B 243 -90.56 -106.38
REMARK 500 SER B 246 178.63 176.58
REMARK 500 ALA B 248 -131.59 -168.76
REMARK 500 PHE B 250 -72.32 -125.26
REMARK 500 THR B 252 -89.92 -15.75
REMARK 500 ASN B 253 102.91 -169.25
REMARK 500 LEU B 274 12.76 -164.88
REMARK 500 ALA B 275 56.37 -96.44
REMARK 500 LYS B 277 -74.08 -95.33
REMARK 500 GLN B 286 -104.56 13.08
REMARK 500 LYS B 306 -39.37 -35.12
REMARK 500 LEU B 307 -33.88 -38.40
REMARK 500 SER B 308 -8.15 -57.16
REMARK 500 ASP B 355 -1.01 74.52
REMARK 500 GLN B 357 105.17 -33.90
REMARK 500 PHE B 358 105.51 -33.52
REMARK 500 SER B 360 109.72 -15.26
REMARK 500 ILE B 361 -38.83 -35.94
REMARK 500 THR B 373 -8.08 -45.96
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 K B 500 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 374 OG1
REMARK 620 2 THR B 374 O 52.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 502 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 375 O
REMARK 620 2 GLY B 376 O 58.1
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 368
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2A79 RELATED DB: PDB
REMARK 900 THE ORIGINAL STRUCTURAL MODEL WE USE FOR NORMAL-MODE-BASED
REMARK 900 REFINEMENT. THIS ENTRY 3LUT REFLECTS AN ALTERNATIVE MODELING OF X-
REMARK 900 RAY DATA R2A79SF
REMARK 900 RELATED ID: 2R9R RELATED DB: PDB
REMARK 900 A CHIMERA KV1.2-KV2.1 STRUCTURE AT A HIGHER RESOLUTION WE USE IN
REMARK 900 MULTIPLE-CRYSTAL AVERAGING.
DBREF 3LUT A 1 367 UNP P62483 KCAB2_RAT 1 367
DBREF 3LUT B 1 499 UNP P63142 KCNA2_RAT 1 499
SEQADV 3LUT GLN B 207 UNP P63142 ASN 207 ENGINEERED MUTATION
SEQRES 1 A 367 MET TYR PRO GLU SER THR THR GLY SER PRO ALA ARG LEU
SEQRES 2 A 367 SER LEU ARG GLN THR GLY SER PRO GLY MET ILE TYR SER
SEQRES 3 A 367 THR ARG TYR GLY SER PRO LYS ARG GLN LEU GLN PHE TYR
SEQRES 4 A 367 ARG ASN LEU GLY LYS SER GLY LEU ARG VAL SER CYS LEU
SEQRES 5 A 367 GLY LEU GLY THR TRP VAL THR PHE GLY GLY GLN ILE THR
SEQRES 6 A 367 ASP GLU MET ALA GLU HIS LEU MET THR LEU ALA TYR ASP
SEQRES 7 A 367 ASN GLY ILE ASN LEU PHE ASP THR ALA GLU VAL TYR ALA
SEQRES 8 A 367 ALA GLY LYS ALA GLU VAL VAL LEU GLY ASN ILE ILE LYS
SEQRES 9 A 367 LYS LYS GLY TRP ARG ARG SER SER LEU VAL ILE THR THR
SEQRES 10 A 367 LYS ILE PHE TRP GLY GLY LYS ALA GLU THR GLU ARG GLY
SEQRES 11 A 367 LEU SER ARG LYS HIS ILE ILE GLU GLY LEU LYS ALA SER
SEQRES 12 A 367 LEU GLU ARG LEU GLN LEU GLU TYR VAL ASP VAL VAL PHE
SEQRES 13 A 367 ALA ASN ARG PRO ASP PRO ASN THR PRO MET GLU GLU THR
SEQRES 14 A 367 VAL ARG ALA MET THR HIS VAL ILE ASN GLN GLY MET ALA
SEQRES 15 A 367 MET TYR TRP GLY THR SER ARG TRP SER SER MET GLU ILE
SEQRES 16 A 367 MET GLU ALA TYR SER VAL ALA ARG GLN PHE ASN LEU ILE
SEQRES 17 A 367 PRO PRO ILE CYS GLU GLN ALA GLU TYR HIS MET PHE GLN
SEQRES 18 A 367 ARG GLU LYS VAL GLU VAL GLN LEU PRO GLU LEU PHE HIS
SEQRES 19 A 367 LYS ILE GLY VAL GLY ALA MET THR TRP SER PRO LEU ALA
SEQRES 20 A 367 CYS GLY ILE VAL SER GLY LYS TYR ASP SER GLY ILE PRO
SEQRES 21 A 367 PRO TYR SER ARG ALA SER LEU LYS GLY TYR GLN TRP LEU
SEQRES 22 A 367 LYS ASP LYS ILE LEU SER GLU GLU GLY ARG ARG GLN GLN
SEQRES 23 A 367 ALA LYS LEU LYS GLU LEU GLN ALA ILE ALA GLU ARG LEU
SEQRES 24 A 367 GLY CYS THR LEU PRO GLN LEU ALA ILE ALA TRP CYS LEU
SEQRES 25 A 367 ARG ASN GLU GLY VAL SER SER VAL LEU LEU GLY ALA SER
SEQRES 26 A 367 ASN ALA GLU GLN LEU MET GLU ASN ILE GLY ALA ILE GLN
SEQRES 27 A 367 VAL LEU PRO LYS LEU SER SER SER ILE VAL HIS GLU ILE
SEQRES 28 A 367 ASP SER ILE LEU GLY ASN LYS PRO TYR SER LYS LYS ASP
SEQRES 29 A 367 TYR ARG SER
SEQRES 1 B 499 MET THR VAL ALA THR GLY ASP PRO VAL ASP GLU ALA ALA
SEQRES 2 B 499 ALA LEU PRO GLY HIS PRO GLN ASP THR TYR ASP PRO GLU
SEQRES 3 B 499 ALA ASP HIS GLU CYS CYS GLU ARG VAL VAL ILE ASN ILE
SEQRES 4 B 499 SER GLY LEU ARG PHE GLU THR GLN LEU LYS THR LEU ALA
SEQRES 5 B 499 GLN PHE PRO GLU THR LEU LEU GLY ASP PRO LYS LYS ARG
SEQRES 6 B 499 MET ARG TYR PHE ASP PRO LEU ARG ASN GLU TYR PHE PHE
SEQRES 7 B 499 ASP ARG ASN ARG PRO SER PHE ASP ALA ILE LEU TYR TYR
SEQRES 8 B 499 TYR GLN SER GLY GLY ARG LEU ARG ARG PRO VAL ASN VAL
SEQRES 9 B 499 PRO LEU ASP ILE PHE SER GLU GLU ILE ARG PHE TYR GLU
SEQRES 10 B 499 LEU GLY GLU GLU ALA MET GLU MET PHE ARG GLU ASP GLU
SEQRES 11 B 499 GLY TYR ILE LYS GLU GLU GLU ARG PRO LEU PRO GLU ASN
SEQRES 12 B 499 GLU PHE GLN ARG GLN VAL TRP LEU LEU PHE GLU TYR PRO
SEQRES 13 B 499 GLU SER SER GLY PRO ALA ARG ILE ILE ALA ILE VAL SER
SEQRES 14 B 499 VAL MET VAL ILE LEU ILE SER ILE VAL SER PHE CYS LEU
SEQRES 15 B 499 GLU THR LEU PRO ILE PHE ARG ASP GLU ASN GLU ASP MET
SEQRES 16 B 499 HIS GLY GLY GLY VAL THR PHE HIS THR TYR SER GLN SER
SEQRES 17 B 499 THR ILE GLY TYR GLN GLN SER THR SER PHE THR ASP PRO
SEQRES 18 B 499 PHE PHE ILE VAL GLU THR LEU CYS ILE ILE TRP PHE SER
SEQRES 19 B 499 PHE GLU PHE LEU VAL ARG PHE PHE ALA CYS PRO SER LYS
SEQRES 20 B 499 ALA GLY PHE PHE THR ASN ILE MET ASN ILE ILE ASP ILE
SEQRES 21 B 499 VAL ALA ILE ILE PRO TYR PHE ILE THR LEU GLY THR GLU
SEQRES 22 B 499 LEU ALA GLU LYS PRO GLU ASP ALA GLN GLN GLY GLN GLN
SEQRES 23 B 499 ALA MET SER LEU ALA ILE LEU ARG VAL ILE ARG LEU VAL
SEQRES 24 B 499 ARG VAL PHE ARG ILE PHE LYS LEU SER ARG HIS SER LYS
SEQRES 25 B 499 GLY LEU GLN ILE LEU GLY GLN THR LEU LYS ALA SER MET
SEQRES 26 B 499 ARG GLU LEU GLY LEU LEU ILE PHE PHE LEU PHE ILE GLY
SEQRES 27 B 499 VAL ILE LEU PHE SER SER ALA VAL TYR PHE ALA GLU ALA
SEQRES 28 B 499 ASP GLU ARG ASP SER GLN PHE PRO SER ILE PRO ASP ALA
SEQRES 29 B 499 PHE TRP TRP ALA VAL VAL SER MET THR THR VAL GLY TYR
SEQRES 30 B 499 GLY ASP MET VAL PRO THR THR ILE GLY GLY LYS ILE VAL
SEQRES 31 B 499 GLY SER LEU CYS ALA ILE ALA GLY VAL LEU THR ILE ALA
SEQRES 32 B 499 LEU PRO VAL PRO VAL ILE VAL SER ASN PHE ASN TYR PHE
SEQRES 33 B 499 TYR HIS ARG GLU THR GLU GLY GLU GLU GLN ALA GLN TYR
SEQRES 34 B 499 LEU GLN VAL THR SER CYS PRO LYS ILE PRO SER SER PRO
SEQRES 35 B 499 ASP LEU LYS LYS SER ARG SER ALA SER THR ILE SER LYS
SEQRES 36 B 499 SER ASP TYR MET GLU ILE GLN GLU GLY VAL ASN ASN SER
SEQRES 37 B 499 ASN GLU ASP PHE ARG GLU GLU ASN LEU LYS THR ALA ASN
SEQRES 38 B 499 CYS THR LEU ALA ASN THR ASN TYR VAL ASN ILE THR LYS
SEQRES 39 B 499 MET LEU THR ASP VAL
HET NAP A 368 48
HET K B 500 1
HET K B 501 1
HET K B 502 1
HET K B 503 1
HET K B 504 1
HET K B 505 1
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM K POTASSIUM ION
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 3 NAP C21 H28 N7 O17 P3
FORMUL 4 K 6(K 1+)
FORMUL 10 HOH *86(H2 O)
HELIX 1 1 THR A 65 ASN A 79 1 15
HELIX 2 2 VAL A 89 ALA A 92 5 4
HELIX 3 3 GLY A 93 GLY A 107 1 15
HELIX 4 4 ARG A 109 LEU A 113 5 5
HELIX 5 5 ALA A 125 ARG A 129 5 5
HELIX 6 6 SER A 132 GLN A 148 1 17
HELIX 7 7 PRO A 165 GLN A 179 1 15
HELIX 8 8 SER A 191 ASN A 206 1 16
HELIX 9 9 ARG A 222 VAL A 227 1 6
HELIX 10 10 VAL A 227 GLY A 237 1 11
HELIX 11 11 LEU A 246 GLY A 253 5 8
HELIX 12 12 SER A 263 LEU A 267 5 5
HELIX 13 13 TYR A 270 LEU A 278 1 9
HELIX 14 14 SER A 279 LEU A 299 1 21
HELIX 15 15 THR A 302 ARG A 313 1 12
HELIX 16 16 ASN A 326 GLY A 335 1 10
HELIX 17 17 GLY A 335 LEU A 340 1 6
HELIX 18 18 PRO A 341 LEU A 343 5 3
HELIX 19 19 SER A 344 GLY A 356 1 13
HELIX 20 20 LEU B 48 GLN B 53 1 6
HELIX 21 21 ASP B 61 MET B 66 1 6
HELIX 22 22 ASN B 81 SER B 94 1 14
HELIX 23 23 PRO B 105 TYR B 116 1 12
HELIX 24 24 GLY B 119 GLY B 131 1 13
HELIX 25 25 LEU B 140 PHE B 145 1 6
HELIX 26 26 TRP B 150 SER B 158 1 9
HELIX 27 27 ARG B 163 LEU B 185 1 23
HELIX 28 28 PHE B 202 SER B 206 5 5
HELIX 29 29 THR B 219 ARG B 240 1 22
HELIX 30 30 ASN B 253 LEU B 270 1 18
HELIX 31 31 PRO B 278 GLN B 283 1 6
HELIX 32 32 SER B 289 ARG B 303 1 15
HELIX 33 33 ILE B 304 HIS B 310 5 7
HELIX 34 34 SER B 311 SER B 324 1 14
HELIX 35 35 SER B 324 ALA B 351 1 28
HELIX 36 36 SER B 360 THR B 373 1 14
HELIX 37 37 GLY B 386 LEU B 404 1 19
HELIX 38 38 PRO B 405 THR B 421 1 17
SHEET 1 A 2 TYR A 39 ASN A 41 0
SHEET 2 A 2 ARG A 48 SER A 50 -1 O VAL A 49 N ARG A 40
SHEET 1 B 9 LEU A 52 GLY A 55 0
SHEET 2 B 9 LEU A 83 ALA A 87 1 O LEU A 83 N LEU A 54
SHEET 3 B 9 VAL A 114 ILE A 119 1 O THR A 116 N PHE A 84
SHEET 4 B 9 VAL A 152 ALA A 157 1 O PHE A 156 N ILE A 119
SHEET 5 B 9 ALA A 182 SER A 188 1 O GLY A 186 N VAL A 155
SHEET 6 B 9 CYS A 212 GLU A 216 1 O CYS A 212 N THR A 187
SHEET 7 B 9 GLY A 239 TRP A 243 1 O GLY A 239 N GLU A 213
SHEET 8 B 9 VAL A 317 LEU A 322 1 O LEU A 321 N THR A 242
SHEET 9 B 9 LEU A 52 GLY A 55 1 N GLY A 53 O LEU A 322
SHEET 1 C 4 LEU B 42 GLN B 47 0
SHEET 2 C 4 ARG B 34 ILE B 39 -1 N ILE B 37 O PHE B 44
SHEET 3 C 4 GLU B 75 PHE B 78 1 O TYR B 76 N ASN B 38
SHEET 4 C 4 PHE B 69 ASP B 70 -1 N ASP B 70 O GLU B 75
LINK OG1 THR B 374 K K B 500 1555 1555 2.80
LINK O THR B 374 K K B 500 1555 1555 3.29
LINK O THR B 374 K K B 501 1555 1555 2.84
LINK O VAL B 375 K K B 502 1555 1555 3.13
LINK O GLY B 376 K K B 502 1555 1555 3.19
LINK O GLY B 376 K K B 503 1555 1555 3.20
SITE 1 AC1 31 GLY A 55 THR A 56 TRP A 57 GLN A 63
SITE 2 AC1 31 ASP A 85 TYR A 90 ASN A 158 SER A 188
SITE 3 AC1 31 ARG A 189 GLN A 214 TRP A 243 SER A 244
SITE 4 AC1 31 PRO A 245 LEU A 246 ALA A 247 CYS A 248
SITE 5 AC1 31 GLY A 249 SER A 252 LYS A 254 ARG A 264
SITE 6 AC1 31 LEU A 321 GLY A 323 SER A 325 GLN A 329
SITE 7 AC1 31 GLU A 332 ASN A 333 HOH A 395 HOH A 409
SITE 8 AC1 31 HOH A 410 HOH A 419 HOH A 435
SITE 1 AC2 2 THR B 374 K B 501
SITE 1 AC3 4 THR B 374 VAL B 375 K B 500 K B 502
SITE 1 AC4 4 VAL B 375 GLY B 376 K B 501 K B 503
SITE 1 AC5 2 GLY B 376 K B 502
CRYST1 113.605 113.605 260.473 90.00 90.00 90.00 I 4 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 0.008802 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008802 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003839 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
