HEADER TRANSPORT 04-DEC-13 4CHV
TITLE THE ELECTRON CRYSTALLOGRAPHY STRUCTURE OF THE CAMP-BOUND POTASSIUM
TITLE 2 CHANNEL MLOK1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIC NUCLEOTIDE-GATED POTASSIUM CHANNEL MLL3241;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: MLOTIK1 CHANNEL;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: CAMP PRESENT IN BUFFER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MESORHIZOBIUM LOTI;
SOURCE 3 ORGANISM_TAXID: 381;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PASK90
KEYWDS TRANSPORT, 2DX, VOLTAGE GATED POTASSIUM CHANNEL, CNBD, 2D CRYSTAL
EXPDTA ELECTRON CRYSTALLOGRAPHY
AUTHOR J.KOWAL,M.CHAMI,P.BAUMGARTNER,M.ARHEIT,P.L.CHIU,M.RANGL,S.SCHEURING,
AUTHOR 2 G.F.SCHROEDER,C.M.NIMIGEAN,H.STAHLBERG
REVDAT 3 24-APR-19 4CHV 1 REMARK
REVDAT 2 12-FEB-14 4CHV 1 JRNL
REVDAT 1 15-JAN-14 4CHV 0
JRNL AUTH J.KOWAL,M.CHAMI,P.BAUMGARTNER,M.ARHEIT,P.L.CHIU,M.RANGL,
JRNL AUTH 2 S.SCHEURING,G.F.SCHROEDER,C.M.NIMIGEAN,H.STAHLBERG
JRNL TITL LIGAND-INDUCED STRUCTURAL CHANGES IN THE CYCLIC
JRNL TITL 2 NUCLEOTIDE-MODULATED POTASSIUM CHANNEL MLOK1
JRNL REF NAT.COMMUN. V. 5 3106 2014
JRNL REFN ESSN 2041-1723
JRNL PMID 24469021
JRNL DOI 10.1038/NCOMMS4106
REMARK 2
REMARK 2 RESOLUTION. 7.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 7.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : NULL
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10340
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : 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 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4CHV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.
REMARK 100 THE DEPOSITION ID IS D_1290059153.
REMARK 240
REMARK 240 EXPERIMENTAL DETAILS
REMARK 240 RECONSTRUCTION METHOD : CRYSTALLOGRAPHY
REMARK 240 SAMPLE TYPE : 2D ARRAY
REMARK 240 SPECIMEN TYPE : 2D CRYSTAL IN VITREOUS ICE
REMARK 240 DATA ACQUISITION
REMARK 240 DATE OF DATA COLLECTION : NULL
REMARK 240 TEMPERATURE (KELVIN) : NULL
REMARK 240 PH : NULL
REMARK 240 NUMBER OF CRYSTALS USED : NULL
REMARK 240 MICROSCOPE MODEL : FEI/PHILIPS CM200FEG
REMARK 240 DETECTOR TYPE : KODAK SO-163 FILM
REMARK 240 ACCELERATION VOLTAGE (KV) : 200
REMARK 240 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 240 RESOLUTION RANGE HIGH (A) : NULL
REMARK 240 RESOLUTION RANGE LOW (A) : NULL
REMARK 240 DATA SCALING SOFTWARE : NULL
REMARK 240 COMPLETENESS FOR RANGE (%) : NULL
REMARK 240 DATA REDUNDANCY : NULL
REMARK 240 IN THE HIGHEST RESOLUTION SHELL
REMARK 240 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) :NULL
REMARK 240 HIGHEST RESOLUTION SHELL, RANGE LOW (A) :NULL
REMARK 240 COMPLETENESS FOR SHELL (%) : NULL
REMARK 240 DATA REDUNDANCY IN SHELL : NULL
REMARK 240 R MERGE FOR SHELL (I) : NULL
REMARK 240 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 240 SOFTWARE USED : NULL
REMARK 240 STARTING MODEL : NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 MET A 1
REMARK 465 SER A 2
REMARK 465 VAL A 3
REMARK 465 LEU A 4
REMARK 465 PRO A 5
REMARK 465 PHE A 6
REMARK 465 ALA A 351
REMARK 465 ALA A 352
REMARK 465 ALA A 353
REMARK 465 SER A 354
REMARK 465 ALA A 355
REMARK 465 HIS A 356
REMARK 465 HIS A 357
REMARK 465 HIS A 358
REMARK 465 HIS A 359
REMARK 465 HIS A 360
REMARK 465 HIS A 361
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 VAL B 3
REMARK 465 LEU B 4
REMARK 465 PRO B 5
REMARK 465 PHE B 6
REMARK 465 ALA B 351
REMARK 465 ALA B 352
REMARK 465 ALA B 353
REMARK 465 SER B 354
REMARK 465 ALA B 355
REMARK 465 HIS B 356
REMARK 465 HIS B 357
REMARK 465 HIS B 358
REMARK 465 HIS B 359
REMARK 465 HIS B 360
REMARK 465 HIS B 361
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 VAL C 3
REMARK 465 LEU C 4
REMARK 465 PRO C 5
REMARK 465 PHE C 6
REMARK 465 ALA C 351
REMARK 465 ALA C 352
REMARK 465 ALA C 353
REMARK 465 SER C 354
REMARK 465 ALA C 355
REMARK 465 HIS C 356
REMARK 465 HIS C 357
REMARK 465 HIS C 358
REMARK 465 HIS C 359
REMARK 465 HIS C 360
REMARK 465 HIS C 361
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 VAL D 3
REMARK 465 LEU D 4
REMARK 465 PRO D 5
REMARK 465 PHE D 6
REMARK 465 ALA D 351
REMARK 465 ALA D 352
REMARK 465 ALA D 353
REMARK 465 SER D 354
REMARK 465 ALA D 355
REMARK 465 HIS D 356
REMARK 465 HIS D 357
REMARK 465 HIS D 358
REMARK 465 HIS D 359
REMARK 465 HIS D 360
REMARK 465 HIS D 361
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 GLY A 350 CA C O
REMARK 470 GLY B 350 CA C O
REMARK 470 GLY C 350 CA C O
REMARK 470 GLY D 350 CA C O
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 ND2 ASN D 226 CG1 VAL D 248 0.65
REMARK 500 CD1 LEU D 229 CD1 LEU D 320 1.55
REMARK 500 O VAL D 218 OD1 ASP D 222 1.77
REMARK 500 O VAL D 218 OD2 ASP D 222 1.78
REMARK 500 ND2 ASN D 226 CB VAL D 248 1.84
REMARK 500 CD1 LEU D 7 O ILE D 262 1.84
REMARK 500 CG ASN D 226 CG1 VAL D 248 1.85
REMARK 500 O VAL D 218 CG ASP D 222 1.87
REMARK 500 CD1 LEU A 7 O ILE A 262 1.94
REMARK 500 CD1 LEU C 7 O ILE C 262 1.96
REMARK 500 CD1 LEU B 7 O ILE B 262 1.97
REMARK 500 O ASP C 222 ND2 ASN C 226 2.05
REMARK 500 O ARG D 220 CE1 PHE D 223 2.05
REMARK 500 O TRP C 227 CB ALA C 231 2.10
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 TYR A 178 C TYR A 178 O 0.142
REMARK 500 TYR B 178 C TYR B 178 O 0.143
REMARK 500 ALA B 253 C ALA B 253 O 0.128
REMARK 500 TYR C 178 C TYR C 178 O 0.144
REMARK 500 ALA C 253 C ALA C 253 O 0.125
REMARK 500 TYR D 178 C TYR D 178 O 0.143
REMARK 500 ALA D 253 C ALA D 253 O 0.128
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 ARG A 252 N - CA - CB ANGL. DEV. = -12.6 DEGREES
REMARK 500 PRO A 306 C - N - CA ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG B 252 N - CA - CB ANGL. DEV. = -14.0 DEGREES
REMARK 500 PRO B 257 N - CA - CB ANGL. DEV. = -8.3 DEGREES
REMARK 500 PRO B 306 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG C 252 N - CA - CB ANGL. DEV. = -11.4 DEGREES
REMARK 500 PRO C 306 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG D 252 N - CA - CB ANGL. DEV. = -13.0 DEGREES
REMARK 500 PRO D 257 N - CA - CB ANGL. DEV. = -8.0 DEGREES
REMARK 500 PRO D 306 C - N - CA ANGL. DEV. = 11.2 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 ILE A 9 -89.96 -120.12
REMARK 500 PRO A 12 45.51 -65.52
REMARK 500 THR A 29 26.75 -41.91
REMARK 500 VAL A 67 -60.00 -100.01
REMARK 500 THR A 72 -82.92 -164.56
REMARK 500 PRO A 95 -126.94 -9.90
REMARK 500 ALA A 102 -30.00 -34.35
REMARK 500 VAL A 103 -17.47 -40.80
REMARK 500 PHE A 114 -79.87 -90.01
REMARK 500 THR A 175 10.07 119.09
REMARK 500 ARG A 254 122.06 157.52
REMARK 500 PRO A 257 -159.98 -109.87
REMARK 500 PRO A 287 106.44 -22.13
REMARK 500 PRO A 306 -159.95 -1.21
REMARK 500 ARG A 349 50.50 -99.25
REMARK 500 ILE B 9 -100.01 -130.10
REMARK 500 ALA B 11 -79.59 -45.00
REMARK 500 THR B 29 46.04 -60.09
REMARK 500 ALA B 65 130.02 170.15
REMARK 500 VAL B 67 69.97 -170.01
REMARK 500 VAL B 68 89.99 140.52
REMARK 500 THR B 72 -81.11 -161.36
REMARK 500 ALA B 102 -29.61 -33.64
REMARK 500 VAL B 103 -16.47 -39.97
REMARK 500 PHE B 114 -79.96 -89.98
REMARK 500 THR B 175 13.54 111.31
REMARK 500 TRP B 227 -76.09 -114.38
REMARK 500 ALA B 231 -28.10 -34.03
REMARK 500 PRO B 257 -139.98 -127.15
REMARK 500 PRO B 306 -160.97 -19.91
REMARK 500 ARG B 349 51.74 -98.00
REMARK 500 ILE C 9 -99.98 -130.04
REMARK 500 ALA C 11 -79.30 -39.95
REMARK 500 THR C 29 20.03 -50.00
REMARK 500 VAL C 67 106.32 -179.10
REMARK 500 VAL C 68 113.75 39.97
REMARK 500 THR C 72 -80.04 -160.27
REMARK 500 ALA C 102 -28.71 -34.28
REMARK 500 VAL C 103 -17.81 -40.06
REMARK 500 PHE C 114 -79.94 -90.02
REMARK 500 THR C 175 18.08 113.63
REMARK 500 PRO C 257 -149.98 -120.02
REMARK 500 PRO C 306 -163.36 -19.97
REMARK 500 ARG C 349 49.87 -98.33
REMARK 500 ILE D 9 -99.99 -130.00
REMARK 500 ALA D 11 -82.03 -43.16
REMARK 500 THR D 29 45.34 -60.01
REMARK 500 VAL D 67 19.96 -169.94
REMARK 500 VAL D 68 30.00 -150.02
REMARK 500 THR D 72 -81.06 -161.06
REMARK 500
REMARK 500 THIS ENTRY HAS 57 RAMACHANDRAN OUTLIERS.
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 A1350 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 175 O
REMARK 620 2 THR A 175 O 54.4
REMARK 620 3 THR B 175 O 83.1 54.0
REMARK 620 4 THR C 175 O 54.2 76.3 53.1
REMARK 620 5 THR A 176 O 94.5 101.7 151.3 143.6
REMARK 620 6 THR B 176 O 141.5 100.0 105.6 156.4 60.0
REMARK 620 7 THR C 176 O 155.2 147.5 103.6 110.7 90.6 60.4
REMARK 620 8 THR D 176 O 104.3 152.1 149.6 107.1 58.7 87.2 58.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B1350 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 178 O
REMARK 620 2 GLY D 177 O 83.2
REMARK 620 3 GLY A 177 O 86.3 82.8
REMARK 620 4 GLY B 177 O 135.7 138.8 86.5
REMARK 620 5 TYR B 178 O 49.7 132.9 93.5 87.3
REMARK 620 6 TYR C 178 O 73.0 122.9 143.3 87.7 50.0
REMARK 620 7 TYR D 178 O 47.4 78.7 131.5 134.4 69.0 47.0
REMARK 620 8 GLY C 177 O 133.2 76.9 131.4 80.9 132.1 83.1 87.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 1350
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1350
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CHW RELATED DB: PDB
REMARK 900 THE ELECTRON CRYSTALLOGRAPHY STRUCTURE OF THE CAMP-FREE POTASSIUM
REMARK 900 CHANNEL MLOK1
REMARK 900 RELATED ID: EMD-2526 RELATED DB: EMDB
REMARK 900 THE ELECTRON CRYSTALLOGRAPHY STRUCTURE OF THE CAMP-BOUND POTASSIUM
REMARK 900 CHANNEL MLOK1
DBREF 4CHV A 1 355 UNP Q98GN8 CNGK1_RHILO 1 355
DBREF 4CHV B 1 355 UNP Q98GN8 CNGK1_RHILO 1 355
DBREF 4CHV C 1 355 UNP Q98GN8 CNGK1_RHILO 1 355
DBREF 4CHV D 1 355 UNP Q98GN8 CNGK1_RHILO 1 355
SEQADV 4CHV HIS A 356 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS A 357 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS A 358 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS A 359 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS A 360 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS A 361 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS B 356 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS B 357 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS B 358 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS B 359 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS B 360 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS B 361 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS C 356 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS C 357 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS C 358 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS C 359 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS C 360 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS C 361 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS D 356 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS D 357 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS D 358 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS D 359 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS D 360 UNP Q98GN8 EXPRESSION TAG
SEQADV 4CHV HIS D 361 UNP Q98GN8 EXPRESSION TAG
SEQRES 1 A 361 MET SER VAL LEU PRO PHE LEU ARG ILE TYR ALA PRO LEU
SEQRES 2 A 361 ASN ALA VAL LEU ALA ALA PRO GLY LEU LEU ALA VAL ALA
SEQRES 3 A 361 ALA LEU THR ILE PRO ASP MET SER GLY ARG SER ARG LEU
SEQRES 4 A 361 ALA LEU ALA ALA LEU LEU ALA VAL ILE TRP GLY ALA TYR
SEQRES 5 A 361 LEU LEU GLN LEU ALA ALA THR LEU LEU LYS ARG ARG ALA
SEQRES 6 A 361 GLY VAL VAL ARG ASP ARG THR PRO LYS ILE ALA ILE ASP
SEQRES 7 A 361 VAL LEU ALA VAL LEU VAL PRO LEU ALA ALA PHE LEU LEU
SEQRES 8 A 361 ASP GLY SER PRO ASP TRP SER LEU TYR CYS ALA VAL TRP
SEQRES 9 A 361 LEU LEU LYS PRO LEU ARG ASP SER THR PHE PHE PRO VAL
SEQRES 10 A 361 LEU GLY ARG VAL LEU ALA ASN GLU ALA ARG ASN LEU ILE
SEQRES 11 A 361 GLY VAL THR THR LEU PHE GLY VAL VAL LEU PHE ALA VAL
SEQRES 12 A 361 ALA LEU ALA ALA TYR VAL ILE GLU ARG ASP ILE GLN PRO
SEQRES 13 A 361 GLU LYS PHE GLY SER ILE PRO GLN ALA MET TRP TRP ALA
SEQRES 14 A 361 VAL VAL THR LEU SER THR THR GLY TYR GLY ASP THR ILE
SEQRES 15 A 361 PRO GLN SER PHE ALA GLY ARG VAL LEU ALA GLY ALA VAL
SEQRES 16 A 361 MET MET SER GLY ILE GLY ILE PHE GLY LEU TRP ALA GLY
SEQRES 17 A 361 ILE LEU ALA THR GLY PHE TYR GLN GLU VAL ARG ARG GLY
SEQRES 18 A 361 ASP PHE VAL ARG ASN TRP GLN LEU VAL ALA ALA VAL PRO
SEQRES 19 A 361 LEU PHE GLN LYS LEU GLY PRO ALA VAL LEU VAL GLU ILE
SEQRES 20 A 361 VAL ARG ALA LEU ARG ALA ARG THR VAL PRO ALA GLY ALA
SEQRES 21 A 361 VAL ILE CYS ARG ILE GLY GLU PRO GLY ASP ARG MET PHE
SEQRES 22 A 361 PHE VAL VAL GLU GLY SER VAL SER VAL ALA THR PRO ASN
SEQRES 23 A 361 PRO VAL GLU LEU GLY PRO GLY ALA PHE PHE GLY GLU MET
SEQRES 24 A 361 ALA LEU ILE SER GLY GLU PRO ARG SER ALA THR VAL SER
SEQRES 25 A 361 ALA ALA THR THR VAL SER LEU LEU SER LEU HIS SER ALA
SEQRES 26 A 361 ASP PHE GLN MET LEU CYS SER SER SER PRO GLU ILE ALA
SEQRES 27 A 361 GLU ILE PHE ARG LYS THR ALA LEU GLU ARG ARG GLY ALA
SEQRES 28 A 361 ALA ALA SER ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 B 361 MET SER VAL LEU PRO PHE LEU ARG ILE TYR ALA PRO LEU
SEQRES 2 B 361 ASN ALA VAL LEU ALA ALA PRO GLY LEU LEU ALA VAL ALA
SEQRES 3 B 361 ALA LEU THR ILE PRO ASP MET SER GLY ARG SER ARG LEU
SEQRES 4 B 361 ALA LEU ALA ALA LEU LEU ALA VAL ILE TRP GLY ALA TYR
SEQRES 5 B 361 LEU LEU GLN LEU ALA ALA THR LEU LEU LYS ARG ARG ALA
SEQRES 6 B 361 GLY VAL VAL ARG ASP ARG THR PRO LYS ILE ALA ILE ASP
SEQRES 7 B 361 VAL LEU ALA VAL LEU VAL PRO LEU ALA ALA PHE LEU LEU
SEQRES 8 B 361 ASP GLY SER PRO ASP TRP SER LEU TYR CYS ALA VAL TRP
SEQRES 9 B 361 LEU LEU LYS PRO LEU ARG ASP SER THR PHE PHE PRO VAL
SEQRES 10 B 361 LEU GLY ARG VAL LEU ALA ASN GLU ALA ARG ASN LEU ILE
SEQRES 11 B 361 GLY VAL THR THR LEU PHE GLY VAL VAL LEU PHE ALA VAL
SEQRES 12 B 361 ALA LEU ALA ALA TYR VAL ILE GLU ARG ASP ILE GLN PRO
SEQRES 13 B 361 GLU LYS PHE GLY SER ILE PRO GLN ALA MET TRP TRP ALA
SEQRES 14 B 361 VAL VAL THR LEU SER THR THR GLY TYR GLY ASP THR ILE
SEQRES 15 B 361 PRO GLN SER PHE ALA GLY ARG VAL LEU ALA GLY ALA VAL
SEQRES 16 B 361 MET MET SER GLY ILE GLY ILE PHE GLY LEU TRP ALA GLY
SEQRES 17 B 361 ILE LEU ALA THR GLY PHE TYR GLN GLU VAL ARG ARG GLY
SEQRES 18 B 361 ASP PHE VAL ARG ASN TRP GLN LEU VAL ALA ALA VAL PRO
SEQRES 19 B 361 LEU PHE GLN LYS LEU GLY PRO ALA VAL LEU VAL GLU ILE
SEQRES 20 B 361 VAL ARG ALA LEU ARG ALA ARG THR VAL PRO ALA GLY ALA
SEQRES 21 B 361 VAL ILE CYS ARG ILE GLY GLU PRO GLY ASP ARG MET PHE
SEQRES 22 B 361 PHE VAL VAL GLU GLY SER VAL SER VAL ALA THR PRO ASN
SEQRES 23 B 361 PRO VAL GLU LEU GLY PRO GLY ALA PHE PHE GLY GLU MET
SEQRES 24 B 361 ALA LEU ILE SER GLY GLU PRO ARG SER ALA THR VAL SER
SEQRES 25 B 361 ALA ALA THR THR VAL SER LEU LEU SER LEU HIS SER ALA
SEQRES 26 B 361 ASP PHE GLN MET LEU CYS SER SER SER PRO GLU ILE ALA
SEQRES 27 B 361 GLU ILE PHE ARG LYS THR ALA LEU GLU ARG ARG GLY ALA
SEQRES 28 B 361 ALA ALA SER ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 C 361 MET SER VAL LEU PRO PHE LEU ARG ILE TYR ALA PRO LEU
SEQRES 2 C 361 ASN ALA VAL LEU ALA ALA PRO GLY LEU LEU ALA VAL ALA
SEQRES 3 C 361 ALA LEU THR ILE PRO ASP MET SER GLY ARG SER ARG LEU
SEQRES 4 C 361 ALA LEU ALA ALA LEU LEU ALA VAL ILE TRP GLY ALA TYR
SEQRES 5 C 361 LEU LEU GLN LEU ALA ALA THR LEU LEU LYS ARG ARG ALA
SEQRES 6 C 361 GLY VAL VAL ARG ASP ARG THR PRO LYS ILE ALA ILE ASP
SEQRES 7 C 361 VAL LEU ALA VAL LEU VAL PRO LEU ALA ALA PHE LEU LEU
SEQRES 8 C 361 ASP GLY SER PRO ASP TRP SER LEU TYR CYS ALA VAL TRP
SEQRES 9 C 361 LEU LEU LYS PRO LEU ARG ASP SER THR PHE PHE PRO VAL
SEQRES 10 C 361 LEU GLY ARG VAL LEU ALA ASN GLU ALA ARG ASN LEU ILE
SEQRES 11 C 361 GLY VAL THR THR LEU PHE GLY VAL VAL LEU PHE ALA VAL
SEQRES 12 C 361 ALA LEU ALA ALA TYR VAL ILE GLU ARG ASP ILE GLN PRO
SEQRES 13 C 361 GLU LYS PHE GLY SER ILE PRO GLN ALA MET TRP TRP ALA
SEQRES 14 C 361 VAL VAL THR LEU SER THR THR GLY TYR GLY ASP THR ILE
SEQRES 15 C 361 PRO GLN SER PHE ALA GLY ARG VAL LEU ALA GLY ALA VAL
SEQRES 16 C 361 MET MET SER GLY ILE GLY ILE PHE GLY LEU TRP ALA GLY
SEQRES 17 C 361 ILE LEU ALA THR GLY PHE TYR GLN GLU VAL ARG ARG GLY
SEQRES 18 C 361 ASP PHE VAL ARG ASN TRP GLN LEU VAL ALA ALA VAL PRO
SEQRES 19 C 361 LEU PHE GLN LYS LEU GLY PRO ALA VAL LEU VAL GLU ILE
SEQRES 20 C 361 VAL ARG ALA LEU ARG ALA ARG THR VAL PRO ALA GLY ALA
SEQRES 21 C 361 VAL ILE CYS ARG ILE GLY GLU PRO GLY ASP ARG MET PHE
SEQRES 22 C 361 PHE VAL VAL GLU GLY SER VAL SER VAL ALA THR PRO ASN
SEQRES 23 C 361 PRO VAL GLU LEU GLY PRO GLY ALA PHE PHE GLY GLU MET
SEQRES 24 C 361 ALA LEU ILE SER GLY GLU PRO ARG SER ALA THR VAL SER
SEQRES 25 C 361 ALA ALA THR THR VAL SER LEU LEU SER LEU HIS SER ALA
SEQRES 26 C 361 ASP PHE GLN MET LEU CYS SER SER SER PRO GLU ILE ALA
SEQRES 27 C 361 GLU ILE PHE ARG LYS THR ALA LEU GLU ARG ARG GLY ALA
SEQRES 28 C 361 ALA ALA SER ALA HIS HIS HIS HIS HIS HIS
SEQRES 1 D 361 MET SER VAL LEU PRO PHE LEU ARG ILE TYR ALA PRO LEU
SEQRES 2 D 361 ASN ALA VAL LEU ALA ALA PRO GLY LEU LEU ALA VAL ALA
SEQRES 3 D 361 ALA LEU THR ILE PRO ASP MET SER GLY ARG SER ARG LEU
SEQRES 4 D 361 ALA LEU ALA ALA LEU LEU ALA VAL ILE TRP GLY ALA TYR
SEQRES 5 D 361 LEU LEU GLN LEU ALA ALA THR LEU LEU LYS ARG ARG ALA
SEQRES 6 D 361 GLY VAL VAL ARG ASP ARG THR PRO LYS ILE ALA ILE ASP
SEQRES 7 D 361 VAL LEU ALA VAL LEU VAL PRO LEU ALA ALA PHE LEU LEU
SEQRES 8 D 361 ASP GLY SER PRO ASP TRP SER LEU TYR CYS ALA VAL TRP
SEQRES 9 D 361 LEU LEU LYS PRO LEU ARG ASP SER THR PHE PHE PRO VAL
SEQRES 10 D 361 LEU GLY ARG VAL LEU ALA ASN GLU ALA ARG ASN LEU ILE
SEQRES 11 D 361 GLY VAL THR THR LEU PHE GLY VAL VAL LEU PHE ALA VAL
SEQRES 12 D 361 ALA LEU ALA ALA TYR VAL ILE GLU ARG ASP ILE GLN PRO
SEQRES 13 D 361 GLU LYS PHE GLY SER ILE PRO GLN ALA MET TRP TRP ALA
SEQRES 14 D 361 VAL VAL THR LEU SER THR THR GLY TYR GLY ASP THR ILE
SEQRES 15 D 361 PRO GLN SER PHE ALA GLY ARG VAL LEU ALA GLY ALA VAL
SEQRES 16 D 361 MET MET SER GLY ILE GLY ILE PHE GLY LEU TRP ALA GLY
SEQRES 17 D 361 ILE LEU ALA THR GLY PHE TYR GLN GLU VAL ARG ARG GLY
SEQRES 18 D 361 ASP PHE VAL ARG ASN TRP GLN LEU VAL ALA ALA VAL PRO
SEQRES 19 D 361 LEU PHE GLN LYS LEU GLY PRO ALA VAL LEU VAL GLU ILE
SEQRES 20 D 361 VAL ARG ALA LEU ARG ALA ARG THR VAL PRO ALA GLY ALA
SEQRES 21 D 361 VAL ILE CYS ARG ILE GLY GLU PRO GLY ASP ARG MET PHE
SEQRES 22 D 361 PHE VAL VAL GLU GLY SER VAL SER VAL ALA THR PRO ASN
SEQRES 23 D 361 PRO VAL GLU LEU GLY PRO GLY ALA PHE PHE GLY GLU MET
SEQRES 24 D 361 ALA LEU ILE SER GLY GLU PRO ARG SER ALA THR VAL SER
SEQRES 25 D 361 ALA ALA THR THR VAL SER LEU LEU SER LEU HIS SER ALA
SEQRES 26 D 361 ASP PHE GLN MET LEU CYS SER SER SER PRO GLU ILE ALA
SEQRES 27 D 361 GLU ILE PHE ARG LYS THR ALA LEU GLU ARG ARG GLY ALA
SEQRES 28 D 361 ALA ALA SER ALA HIS HIS HIS HIS HIS HIS
HET K A1350 1
HET K B1350 1
HETNAM K POTASSIUM ION
FORMUL 5 K 2(K 1+)
HELIX 1 1 PRO A 12 THR A 29 1 18
HELIX 2 2 SER A 34 LYS A 62 1 29
HELIX 3 3 THR A 72 ASP A 92 1 21
HELIX 4 4 TRP A 97 ALA A 102 1 6
HELIX 5 5 VAL A 103 SER A 112 5 10
HELIX 6 6 PHE A 114 GLU A 125 1 12
HELIX 7 7 GLU A 125 ARG A 152 1 28
HELIX 8 8 GLN A 155 GLY A 160 1 6
HELIX 9 9 SER A 161 THR A 175 1 15
HELIX 10 10 SER A 185 VAL A 233 1 49
HELIX 11 11 PRO A 234 LEU A 239 5 6
HELIX 12 12 GLY A 240 LEU A 251 1 12
HELIX 13 13 GLU A 298 GLY A 304 1 7
HELIX 14 14 HIS A 323 SER A 334 1 12
HELIX 15 15 SER A 334 ARG A 349 1 16
HELIX 16 16 PRO B 12 THR B 29 1 18
HELIX 17 17 SER B 34 LYS B 62 1 29
HELIX 18 18 THR B 72 ASP B 92 1 21
HELIX 19 19 TRP B 97 ALA B 102 1 6
HELIX 20 20 VAL B 103 SER B 112 5 10
HELIX 21 21 PHE B 114 GLU B 125 1 12
HELIX 22 22 GLU B 125 ARG B 152 1 28
HELIX 23 23 GLN B 155 GLY B 160 1 6
HELIX 24 24 SER B 161 THR B 175 1 15
HELIX 25 25 SER B 185 ARG B 225 1 41
HELIX 26 26 LEU B 229 VAL B 233 5 5
HELIX 27 27 VAL B 233 LEU B 239 5 7
HELIX 28 28 GLY B 240 LEU B 251 1 12
HELIX 29 29 GLU B 298 GLY B 304 1 7
HELIX 30 30 HIS B 323 SER B 334 1 12
HELIX 31 31 SER B 334 ARG B 349 1 16
HELIX 32 32 PRO C 12 ALA C 18 1 7
HELIX 33 33 ALA C 18 THR C 29 1 12
HELIX 34 34 SER C 34 LYS C 62 1 29
HELIX 35 35 THR C 72 ASP C 92 1 21
HELIX 36 36 TRP C 97 ALA C 102 1 6
HELIX 37 37 VAL C 103 SER C 112 5 10
HELIX 38 38 PHE C 114 GLU C 125 1 12
HELIX 39 39 GLU C 125 ARG C 152 1 28
HELIX 40 40 GLN C 155 GLY C 160 1 6
HELIX 41 41 SER C 161 THR C 175 1 15
HELIX 42 42 SER C 185 VAL C 230 1 46
HELIX 43 43 VAL C 233 LEU C 239 5 7
HELIX 44 44 GLY C 240 LEU C 251 1 12
HELIX 45 45 GLY C 297 GLY C 304 1 8
HELIX 46 46 HIS C 323 SER C 334 1 12
HELIX 47 47 SER C 334 ARG C 349 1 16
HELIX 48 48 PRO D 12 THR D 29 1 18
HELIX 49 49 SER D 34 LYS D 62 1 29
HELIX 50 50 THR D 72 ASP D 92 1 21
HELIX 51 51 TRP D 97 ALA D 102 1 6
HELIX 52 52 VAL D 103 SER D 112 5 10
HELIX 53 53 PHE D 114 GLU D 125 1 12
HELIX 54 54 GLU D 125 ARG D 152 1 28
HELIX 55 55 SER D 161 THR D 175 1 15
HELIX 56 56 SER D 185 VAL D 233 1 49
HELIX 57 57 PRO D 234 LEU D 239 5 6
HELIX 58 58 GLY D 240 LEU D 251 1 12
HELIX 59 59 GLY D 297 GLY D 304 1 8
HELIX 60 60 HIS D 323 SER D 334 1 12
HELIX 61 61 SER D 334 ARG D 349 1 16
SHEET 1 AA 4 THR A 255 VAL A 256 0
SHEET 2 AA 4 VAL A 317 LEU A 322 -1 O VAL A 317 N VAL A 256
SHEET 3 AA 4 MET A 272 GLU A 277 -1 O MET A 272 N LEU A 322
SHEET 4 AA 4 ALA A 294 PHE A 296 -1 O ALA A 294 N VAL A 275
SHEET 1 AB 4 VAL A 261 CYS A 263 0
SHEET 2 AB 4 VAL A 311 ALA A 313 -1 O VAL A 311 N CYS A 263
SHEET 3 AB 4 VAL A 280 VAL A 282 -1 O SER A 281 N SER A 312
SHEET 4 AB 4 VAL A 288 LEU A 290 -1 O VAL A 288 N VAL A 282
SHEET 1 BA 4 ARG B 252 VAL B 256 0
SHEET 2 BA 4 VAL B 317 LEU B 322 -1 O VAL B 317 N VAL B 256
SHEET 3 BA 4 MET B 272 GLU B 277 -1 O MET B 272 N LEU B 322
SHEET 4 BA 4 ALA B 294 PHE B 296 -1 O ALA B 294 N VAL B 275
SHEET 1 BB 4 VAL B 261 CYS B 263 0
SHEET 2 BB 4 VAL B 311 ALA B 313 -1 O VAL B 311 N CYS B 263
SHEET 3 BB 4 VAL B 280 VAL B 282 -1 O SER B 281 N SER B 312
SHEET 4 BB 4 VAL B 288 LEU B 290 -1 O VAL B 288 N VAL B 282
SHEET 1 CA 4 ARG C 252 VAL C 256 0
SHEET 2 CA 4 VAL C 317 LEU C 322 -1 O VAL C 317 N VAL C 256
SHEET 3 CA 4 MET C 272 GLU C 277 -1 O MET C 272 N LEU C 322
SHEET 4 CA 4 ALA C 294 PHE C 296 -1 O ALA C 294 N VAL C 275
SHEET 1 CB 4 VAL C 261 CYS C 263 0
SHEET 2 CB 4 VAL C 311 ALA C 313 -1 O VAL C 311 N CYS C 263
SHEET 3 CB 4 VAL C 280 VAL C 282 -1 O SER C 281 N SER C 312
SHEET 4 CB 4 VAL C 288 LEU C 290 -1 O VAL C 288 N VAL C 282
SHEET 1 DA 4 ARG D 252 VAL D 256 0
SHEET 2 DA 4 VAL D 317 LEU D 322 -1 O VAL D 317 N VAL D 256
SHEET 3 DA 4 MET D 272 GLU D 277 -1 O MET D 272 N LEU D 322
SHEET 4 DA 4 ALA D 294 PHE D 296 -1 O ALA D 294 N VAL D 275
SHEET 1 DB 4 VAL D 261 CYS D 263 0
SHEET 2 DB 4 VAL D 311 ALA D 313 -1 O VAL D 311 N CYS D 263
SHEET 3 DB 4 VAL D 280 VAL D 282 -1 O SER D 281 N SER D 312
SHEET 4 DB 4 VAL D 288 LEU D 290 -1 O VAL D 288 N VAL D 282
LINK K K A1350 O THR D 175 1555 1555 2.52
LINK K K A1350 O THR A 175 1555 1555 2.64
LINK K K A1350 O THR B 175 1555 1555 2.53
LINK K K A1350 O THR C 175 1555 1555 2.62
LINK K K A1350 O THR A 176 1555 1555 2.53
LINK K K A1350 O THR B 176 1555 1555 2.54
LINK K K A1350 O THR C 176 1555 1555 2.47
LINK K K A1350 O THR D 176 1555 1555 2.56
LINK K K B1350 O TYR A 178 1555 1555 2.87
LINK K K B1350 O GLY D 177 1555 1555 2.53
LINK K K B1350 O GLY A 177 1555 1555 2.50
LINK K K B1350 O GLY B 177 1555 1555 2.48
LINK K K B1350 O TYR B 178 1555 1555 2.89
LINK K K B1350 O TYR C 178 1555 1555 2.92
LINK K K B1350 O TYR D 178 1555 1555 3.15
LINK K K B1350 O GLY C 177 1555 1555 2.58
SITE 1 AC1 8 GLY A 177 TYR A 178 GLY B 177 TYR B 178
SITE 2 AC1 8 GLY C 177 TYR C 178 GLY D 177 TYR D 178
SITE 1 AC2 8 THR A 175 THR A 176 THR B 175 THR B 176
SITE 2 AC2 8 THR C 175 THR C 176 THR D 175 THR D 176
CRYST1 104.325 104.325 104.325 90.00 90.00 90.00 P 1 4
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 0.009585 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009585 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009585 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
