HEADER SIGNALING PROTEIN 04-NOV-18 6MZB
TITLE CRYO-EM STRUCTURE OF PHOSPHODIESTERASE 6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ROD CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE SUBUNIT
COMPND 3 BETA;
COMPND 4 CHAIN: B;
COMPND 5 SYNONYM: GMP-PDE BETA;
COMPND 6 EC: 3.1.4.35;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: ROD CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE SUBUNIT
COMPND 10 ALPHA;
COMPND 11 CHAIN: A;
COMPND 12 SYNONYM: GMP-PDE ALPHA,PDE V-B1;
COMPND 13 EC: 3.1.4.35;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: RETINAL ROD RHODOPSIN-SENSITIVE CGMP 3',5'-CYCLIC
COMPND 17 PHOSPHODIESTERASE SUBUNIT GAMMA;
COMPND 18 CHAIN: C, D;
COMPND 19 SYNONYM: GMP-PDE GAMMA;
COMPND 20 EC: 3.1.4.35;
COMPND 21 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: EYE;
SOURCE 6 TISSUE: RETINA;
SOURCE 7 GENE: PDE6B, PDEB;
SOURCE 8 EXPRESSION_SYSTEM: BOS TAURUS;
SOURCE 9 EXPRESSION_SYSTEM_COMMON: BOVINE;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9913;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 13 ORGANISM_COMMON: BOVINE;
SOURCE 14 ORGANISM_TAXID: 9913;
SOURCE 15 ORGAN: EYE;
SOURCE 16 TISSUE: RETINA;
SOURCE 17 GENE: PDE6A, PDEA;
SOURCE 18 EXPRESSION_SYSTEM: BOS TAURUS;
SOURCE 19 EXPRESSION_SYSTEM_COMMON: BOVINE;
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 9913;
SOURCE 21 MOL_ID: 3;
SOURCE 22 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 23 ORGANISM_COMMON: BOVINE;
SOURCE 24 ORGANISM_TAXID: 9913;
SOURCE 25 ORGAN: EYE;
SOURCE 26 TISSUE: RETINA;
SOURCE 27 GENE: PDE6G, PDEG;
SOURCE 28 EXPRESSION_SYSTEM: BOS TAURUS;
SOURCE 29 EXPRESSION_SYSTEM_COMMON: BOVINE;
SOURCE 30 EXPRESSION_SYSTEM_TAXID: 9913
KEYWDS GAF DOMAIN, PHOSPHOHYDROLASE, G PROTEIN-COUPLED RECEPTOR SIGNALING,
KEYWDS 2 SIGNALING PROTEIN
EXPDTA ELECTRON MICROSCOPY
AUTHOR S.GULATI,K.PALCZEWSKI
REVDAT 4 19-MAY-21 6MZB 1 COMPND REMARK HET HETNAM
REVDAT 4 2 1 FORMUL HELIX SHEET SSBOND
REVDAT 4 3 1 LINK SITE ATOM
REVDAT 3 18-DEC-19 6MZB 1 SCALE
REVDAT 2 13-MAR-19 6MZB 1 JRNL
REVDAT 1 06-MAR-19 6MZB 0
JRNL AUTH S.GULATI,K.PALCZEWSKI,A.ENGEL,H.STAHLBERG,L.KOVACIK
JRNL TITL CRYO-EM STRUCTURE OF PHOSPHODIESTERASE 6 REVEALS INSIGHTS
JRNL TITL 2 INTO THE ALLOSTERIC REGULATION OF TYPE I PHOSPHODIESTERASES.
JRNL REF SCI ADV V. 5 V4322 2019
JRNL REFN ESSN 2375-2548
JRNL PMID 30820458
JRNL DOI 10.1126/SCIADV.AAV4322
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : NULL
REMARK 3 RECONSTRUCTION SCHEMA : NULL
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : NULL
REMARK 3 REFINEMENT PROTOCOL : NULL
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.400
REMARK 3 NUMBER OF PARTICLES : 43597
REMARK 3 CTF CORRECTION METHOD : NONE
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 6MZB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1000237800.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : PHOSPHODIESTERASE 6
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI TITAN KRIOS
REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K)
REMARK 245 MINIMUM DEFOCUS (NM) : NULL
REMARK 245 MAXIMUM DEFOCUS (NM) : NULL
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : NULL
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 8000.00
REMARK 245 ILLUMINATION MODE : OTHER
REMARK 245 NOMINAL MAGNIFICATION : NULL
REMARK 245 CALIBRATED MAGNIFICATION : NULL
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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: 18280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 85370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, 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 B 1
REMARK 465 SER B 2
REMARK 465 LEU B 3
REMARK 465 SER B 4
REMARK 465 GLU B 5
REMARK 465 GLY B 6
REMARK 465 GLN B 7
REMARK 465 VAL B 8
REMARK 465 HIS B 9
REMARK 465 ARG B 10
REMARK 465 PHE B 11
REMARK 465 LEU B 12
REMARK 465 ASP B 13
REMARK 465 GLN B 14
REMARK 465 ASN B 15
REMARK 465 PRO B 16
REMARK 465 GLY B 17
REMARK 465 GLN B 825
REMARK 465 LYS B 826
REMARK 465 LYS B 827
REMARK 465 GLU B 828
REMARK 465 THR B 829
REMARK 465 THR B 830
REMARK 465 ALA B 831
REMARK 465 LYS B 832
REMARK 465 LYS B 833
REMARK 465 VAL B 834
REMARK 465 GLY B 835
REMARK 465 THR B 836
REMARK 465 GLU B 837
REMARK 465 ILE B 838
REMARK 465 CYS B 839
REMARK 465 ASN B 840
REMARK 465 GLY B 841
REMARK 465 GLY B 842
REMARK 465 PRO B 843
REMARK 465 ALA B 844
REMARK 465 PRO B 845
REMARK 465 ARG B 846
REMARK 465 SER B 847
REMARK 465 SER B 848
REMARK 465 THR B 849
REMARK 465 CYS B 850
REMARK 465 ARG B 851
REMARK 465 ILE B 852
REMARK 465 LEU B 853
REMARK 465 MET A 1
REMARK 465 GLY A 2
REMARK 465 GLU A 3
REMARK 465 VAL A 4
REMARK 465 THR A 5
REMARK 465 ALA A 6
REMARK 465 GLU A 7
REMARK 465 GLN A 828
REMARK 465 LYS A 829
REMARK 465 GLN A 830
REMARK 465 GLN A 831
REMARK 465 ALA A 832
REMARK 465 ALA A 833
REMARK 465 ASN A 834
REMARK 465 GLN A 835
REMARK 465 ALA A 836
REMARK 465 ALA A 837
REMARK 465 ALA A 838
REMARK 465 GLY A 839
REMARK 465 SER A 840
REMARK 465 GLN A 841
REMARK 465 HIS A 842
REMARK 465 GLY A 843
REMARK 465 GLY A 844
REMARK 465 LYS A 845
REMARK 465 GLN A 846
REMARK 465 PRO A 847
REMARK 465 GLY A 848
REMARK 465 GLY A 849
REMARK 465 GLY A 850
REMARK 465 PRO A 851
REMARK 465 ALA A 852
REMARK 465 SER A 853
REMARK 465 LYS A 854
REMARK 465 SER A 855
REMARK 465 CYS A 856
REMARK 465 CYS A 857
REMARK 465 VAL A 858
REMARK 465 GLN A 859
REMARK 465 MET C 1
REMARK 465 ASN C 2
REMARK 465 LEU C 3
REMARK 465 GLU C 4
REMARK 465 PRO C 5
REMARK 465 PRO C 6
REMARK 465 LYS C 7
REMARK 465 ALA C 8
REMARK 465 GLU C 9
REMARK 465 PRO C 42
REMARK 465 PRO C 43
REMARK 465 LYS C 44
REMARK 465 LYS C 45
REMARK 465 GLY C 46
REMARK 465 VAL C 47
REMARK 465 GLN C 48
REMARK 465 GLY C 49
REMARK 465 PHE C 50
REMARK 465 GLY C 51
REMARK 465 ASP C 52
REMARK 465 ASP C 53
REMARK 465 ILE C 54
REMARK 465 PRO C 55
REMARK 465 GLY C 56
REMARK 465 MET C 57
REMARK 465 GLU C 58
REMARK 465 GLY C 59
REMARK 465 LEU C 60
REMARK 465 GLY C 61
REMARK 465 THR C 62
REMARK 465 ASP C 63
REMARK 465 ILE C 64
REMARK 465 THR C 65
REMARK 465 VAL C 66
REMARK 465 ILE C 67
REMARK 465 CYS C 68
REMARK 465 PRO C 69
REMARK 465 TRP C 70
REMARK 465 GLU C 71
REMARK 465 MET D 1
REMARK 465 ASN D 2
REMARK 465 LEU D 3
REMARK 465 GLU D 4
REMARK 465 PRO D 5
REMARK 465 PRO D 6
REMARK 465 LYS D 7
REMARK 465 ALA D 8
REMARK 465 GLU D 9
REMARK 465 SER D 40
REMARK 465 LYS D 41
REMARK 465 PRO D 42
REMARK 465 PRO D 43
REMARK 465 LYS D 44
REMARK 465 LYS D 45
REMARK 465 GLY D 46
REMARK 465 VAL D 47
REMARK 465 GLN D 48
REMARK 465 GLY D 49
REMARK 465 PHE D 50
REMARK 465 GLY D 51
REMARK 465 ASP D 52
REMARK 465 ASP D 53
REMARK 465 ILE D 54
REMARK 465 PRO D 55
REMARK 465 GLY D 56
REMARK 465 MET D 57
REMARK 465 GLU D 58
REMARK 465 GLY D 59
REMARK 465 LEU D 60
REMARK 465 GLY D 61
REMARK 465 THR D 62
REMARK 465 ASP D 63
REMARK 465 ILE D 64
REMARK 465 THR D 65
REMARK 465 VAL D 66
REMARK 465 ILE D 67
REMARK 465 CYS D 68
REMARK 465 PRO D 69
REMARK 465 TRP D 70
REMARK 465 GLU D 71
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 25 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 823 CG CD OE1 OE2
REMARK 470 ASP B 824 CG OD1 OD2
REMARK 470 GLU A 8 CG CD OE1 OE2
REMARK 470 VAL A 9 CG1 CG2
REMARK 470 GLU A 10 CG CD OE1 OE2
REMARK 470 LYS A 11 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 HG1 THR A 693 OE1 GLN A 694 1.53
REMARK 500 HE1 TRP B 290 OE2 GLU A 709 1.57
REMARK 500 O VAL A 685 HG SER A 688 1.58
REMARK 500 O GLY A 801 HD22 ASN A 805 1.58
REMARK 500 OD1 ASN A 645 H PHE A 647 1.59
REMARK 500 O PHE B 287 NZ LYS A 677 2.01
REMARK 500 OH TYR B 170 OD1 ASN B 194 2.08
REMARK 500 OG1 THR B 667 OD2 ASP B 718 2.19
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 B 32 70.44 49.05
REMARK 500 ALA B 35 -1.58 68.10
REMARK 500 ASP B 38 -4.82 77.39
REMARK 500 ASN B 101 46.17 37.83
REMARK 500 LEU B 196 -97.61 62.59
REMARK 500 CYS B 200 31.65 -141.38
REMARK 500 THR B 202 130.91 -36.75
REMARK 500 SER B 332 79.75 -160.47
REMARK 500 ASN B 390 40.08 -109.33
REMARK 500 LYS B 391 -6.37 74.01
REMARK 500 ASP B 500 59.13 36.97
REMARK 500 THR B 641 -1.22 63.21
REMARK 500 SER B 720 -169.00 -78.60
REMARK 500 ALA B 721 -6.11 76.14
REMARK 500 GLU B 766 49.66 -86.37
REMARK 500 THR B 780 17.76 55.25
REMARK 500 LEU A 52 -7.87 72.71
REMARK 500 LYS A 186 -5.23 72.60
REMARK 500 ASN A 196 160.90 69.69
REMARK 500 ALA A 299 75.65 52.72
REMARK 500 ASN A 392 58.44 -95.75
REMARK 500 LYS A 393 -2.76 72.49
REMARK 500 ASN A 405 136.67 -39.10
REMARK 500 LYS A 459 142.75 -171.83
REMARK 500 ILE A 468 -61.41 -105.84
REMARK 500 SER A 643 -1.03 67.43
REMARK 500 ASN A 649 50.97 -92.30
REMARK 500 GLU A 696 31.77 -93.85
REMARK 500 ASP A 704 -38.43 -38.51
REMARK 500 GLN A 705 -74.52 68.59
REMARK 500 LEU A 721 50.75 -93.28
REMARK 500 GLN A 754 62.20 61.91
REMARK 500 THR A 782 19.63 53.38
REMARK 500 SER C 12 -6.34 74.25
REMARK 500 ALA C 13 -71.38 62.98
REMARK 500 SER C 40 53.40 -92.77
REMARK 500 PRO D 23 46.06 -84.27
REMARK 500 ARG D 33 141.53 71.36
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 ZN B 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 561 NE2
REMARK 620 2 HIS B 597 NE2 111.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 901 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 563 NE2
REMARK 620 2 HIS A 599 NE2 95.4
REMARK 620 3 ASP A 600 OD2 122.6 86.5
REMARK 620 4 ASP A 720 OD1 103.4 100.8 132.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 902 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 600 OD1
REMARK 620 2 ASP A 600 OD2 50.6
REMARK 620 N 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-9297 RELATED DB: EMDB
REMARK 900 CRYO-EM STRUCTURE OF PHOSPHODIESTERASE 6 AT 3.4 A
DBREF 6MZB B 1 853 UNP P23439 PDE6B_BOVIN 1 853
DBREF 6MZB A 1 859 UNP P11541 PDE6A_BOVIN 1 859
DBREF 6MZB C 1 87 UNP P04972 CNRG_BOVIN 1 87
DBREF 6MZB D 1 87 UNP P04972 CNRG_BOVIN 1 87
SEQRES 1 B 853 MET SER LEU SER GLU GLY GLN VAL HIS ARG PHE LEU ASP
SEQRES 2 B 853 GLN ASN PRO GLY PHE ALA ASP GLN TYR PHE GLY ARG LYS
SEQRES 3 B 853 LEU SER PRO GLU ASP VAL ALA ASN ALA CYS GLU ASP GLY
SEQRES 4 B 853 CYS PRO GLU GLY CYS THR SER PHE ARG GLU LEU CYS GLN
SEQRES 5 B 853 VAL GLU GLU SER ALA ALA LEU PHE GLU LEU VAL GLN ASP
SEQRES 6 B 853 MET GLN GLU ASN VAL ASN MET GLU ARG VAL VAL PHE LYS
SEQRES 7 B 853 ILE LEU ARG ARG LEU CYS SER ILE LEU HIS ALA ASP ARG
SEQRES 8 B 853 CYS SER LEU PHE MET TYR ARG GLN ARG ASN GLY VAL ALA
SEQRES 9 B 853 GLU LEU ALA THR ARG LEU PHE SER VAL GLN PRO ASP SER
SEQRES 10 B 853 VAL LEU GLU ASP CYS LEU VAL PRO PRO ASP SER GLU ILE
SEQRES 11 B 853 VAL PHE PRO LEU ASP ILE GLY VAL VAL GLY HIS VAL ALA
SEQRES 12 B 853 GLN THR LYS LYS MET VAL ASN VAL GLN ASP VAL MET GLU
SEQRES 13 B 853 CYS PRO HIS PHE SER SER PHE ALA ASP GLU LEU THR ASP
SEQRES 14 B 853 TYR VAL THR ARG ASN ILE LEU ALA THR PRO ILE MET ASN
SEQRES 15 B 853 GLY LYS ASP VAL VAL ALA VAL ILE MET ALA VAL ASN LYS
SEQRES 16 B 853 LEU ASP GLY PRO CYS PHE THR SER GLU ASP GLU ASP VAL
SEQRES 17 B 853 PHE LEU LYS TYR LEU ASN PHE GLY THR LEU ASN LEU LYS
SEQRES 18 B 853 ILE TYR HIS LEU SER TYR LEU HIS ASN CYS GLU THR ARG
SEQRES 19 B 853 ARG GLY GLN VAL LEU LEU TRP SER ALA ASN LYS VAL PHE
SEQRES 20 B 853 GLU GLU LEU THR ASP ILE GLU ARG GLN PHE HIS LYS ALA
SEQRES 21 B 853 PHE TYR THR VAL ARG ALA TYR LEU ASN CYS ASP ARG TYR
SEQRES 22 B 853 SER VAL GLY LEU LEU ASP MET THR LYS GLU LYS GLU PHE
SEQRES 23 B 853 PHE ASP VAL TRP PRO VAL LEU MET GLY GLU ALA GLN ALA
SEQRES 24 B 853 TYR SER GLY PRO ARG THR PRO ASP GLY ARG GLU ILE LEU
SEQRES 25 B 853 PHE TYR LYS VAL ILE ASP TYR ILE LEU HIS GLY LYS GLU
SEQRES 26 B 853 ASP ILE LYS VAL ILE PRO SER PRO PRO ALA ASP HIS TRP
SEQRES 27 B 853 ALA LEU ALA SER GLY LEU PRO THR TYR VAL ALA GLU SER
SEQRES 28 B 853 GLY PHE ILE CYS ASN ILE MET ASN ALA PRO ALA ASP GLU
SEQRES 29 B 853 MET PHE ASN PHE GLN GLU GLY PRO LEU ASP ASP SER GLY
SEQRES 30 B 853 TRP ILE VAL LYS ASN VAL LEU SER MET PRO ILE VAL ASN
SEQRES 31 B 853 LYS LYS GLU GLU ILE VAL GLY VAL ALA THR PHE TYR ASN
SEQRES 32 B 853 ARG LYS ASP GLY LYS PRO PHE ASP GLU GLN ASP GLU VAL
SEQRES 33 B 853 LEU MET GLU SER LEU THR GLN PHE LEU GLY TRP SER VAL
SEQRES 34 B 853 LEU ASN THR ASP THR TYR ASP LYS MET ASN LYS LEU GLU
SEQRES 35 B 853 ASN ARG LYS ASP ILE ALA GLN ASP MET VAL LEU TYR HIS
SEQRES 36 B 853 VAL ARG CYS ASP ARG GLU GLU ILE GLN LEU ILE LEU PRO
SEQRES 37 B 853 THR ARG GLU ARG LEU GLY LYS GLU PRO ALA ASP CYS GLU
SEQRES 38 B 853 GLU ASP GLU LEU GLY LYS ILE LEU LYS GLU VAL LEU PRO
SEQRES 39 B 853 GLY PRO ALA LYS PHE ASP ILE TYR GLU PHE HIS PHE SER
SEQRES 40 B 853 ASP LEU GLU CYS THR GLU LEU GLU LEU VAL LYS CYS GLY
SEQRES 41 B 853 ILE GLN MET TYR TYR GLU LEU GLY VAL VAL ARG LYS PHE
SEQRES 42 B 853 GLN ILE PRO GLN GLU VAL LEU VAL ARG PHE LEU PHE SER
SEQRES 43 B 853 VAL SER LYS GLY TYR ARG ARG ILE THR TYR HIS ASN TRP
SEQRES 44 B 853 ARG HIS GLY PHE ASN VAL ALA GLN THR MET PHE THR LEU
SEQRES 45 B 853 LEU MET THR GLY LYS LEU LYS SER TYR TYR THR ASP LEU
SEQRES 46 B 853 GLU ALA PHE ALA MET VAL THR ALA GLY LEU CYS HIS ASP
SEQRES 47 B 853 ILE ASP HIS ARG GLY THR ASN ASN LEU TYR GLN MET LYS
SEQRES 48 B 853 SER GLN ASN PRO LEU ALA LYS LEU HIS GLY SER SER ILE
SEQRES 49 B 853 LEU GLU ARG HIS HIS LEU GLU PHE GLY LYS PHE LEU LEU
SEQRES 50 B 853 SER GLU GLU THR LEU ASN ILE TYR GLN ASN LEU ASN ARG
SEQRES 51 B 853 ARG GLN HIS GLU HIS VAL ILE HIS LEU MET ASP ILE ALA
SEQRES 52 B 853 ILE ILE ALA THR ASP LEU ALA LEU TYR PHE LYS LYS ARG
SEQRES 53 B 853 THR MET PHE GLN LYS ILE VAL ASP GLU SER LYS ASN TYR
SEQRES 54 B 853 GLU ASP ARG LYS SER TRP VAL GLU TYR LEU SER LEU GLU
SEQRES 55 B 853 THR THR ARG LYS GLU ILE VAL MET ALA MET MET MET THR
SEQRES 56 B 853 ALA CYS ASP LEU SER ALA ILE THR LYS PRO TRP GLU VAL
SEQRES 57 B 853 GLN SER LYS VAL ALA LEU LEU VAL ALA ALA GLU PHE TRP
SEQRES 58 B 853 GLU GLN GLY ASP LEU GLU ARG THR VAL LEU ASP GLN GLN
SEQRES 59 B 853 PRO ILE PRO MET MET ASP ARG ASN LYS ALA ALA GLU LEU
SEQRES 60 B 853 PRO LYS LEU GLN VAL GLY PHE ILE ASP PHE VAL CYS THR
SEQRES 61 B 853 PHE VAL TYR LYS GLU PHE SER ARG PHE HIS GLU GLU ILE
SEQRES 62 B 853 LEU PRO MET PHE ASP ARG LEU GLN ASN ASN ARG LYS GLU
SEQRES 63 B 853 TRP LYS ALA LEU ALA ASP GLU TYR GLU ALA LYS VAL LYS
SEQRES 64 B 853 ALA LEU GLU GLU ASP GLN LYS LYS GLU THR THR ALA LYS
SEQRES 65 B 853 LYS VAL GLY THR GLU ILE CYS ASN GLY GLY PRO ALA PRO
SEQRES 66 B 853 ARG SER SER THR CYS ARG ILE LEU
SEQRES 1 A 859 MET GLY GLU VAL THR ALA GLU GLU VAL GLU LYS PHE LEU
SEQRES 2 A 859 ASP SER ASN VAL SER PHE ALA LYS GLN TYR TYR ASN LEU
SEQRES 3 A 859 ARG TYR ARG ALA LYS VAL ILE SER ASP LEU LEU GLY PRO
SEQRES 4 A 859 ARG GLU ALA ALA VAL ASP PHE SER ASN TYR HIS ALA LEU
SEQRES 5 A 859 ASN SER VAL GLU GLU SER GLU ILE ILE PHE ASP LEU LEU
SEQRES 6 A 859 ARG ASP PHE GLN ASP ASN LEU GLN ALA GLU LYS CYS VAL
SEQRES 7 A 859 PHE ASN VAL MET LYS LYS LEU CYS PHE LEU LEU GLN ALA
SEQRES 8 A 859 ASP ARG MET SER LEU PHE MET TYR ARG ALA ARG ASN GLY
SEQRES 9 A 859 ILE ALA GLU LEU ALA THR ARG LEU PHE ASN VAL HIS LYS
SEQRES 10 A 859 ASP ALA VAL LEU GLU GLU CYS LEU VAL ALA PRO ASP SER
SEQRES 11 A 859 GLU ILE VAL PHE PRO LEU ASP MET GLY VAL VAL GLY HIS
SEQRES 12 A 859 VAL ALA LEU SER LYS LYS ILE VAL ASN VAL PRO ASN THR
SEQRES 13 A 859 GLU GLU ASP GLU HIS PHE CYS ASP PHE VAL ASP THR LEU
SEQRES 14 A 859 THR GLU TYR GLN THR LYS ASN ILE LEU ALA SER PRO ILE
SEQRES 15 A 859 MET ASN GLY LYS ASP VAL VAL ALA ILE ILE MET VAL VAL
SEQRES 16 A 859 ASN LYS VAL ASP GLY PRO HIS PHE THR GLU ASN ASP GLU
SEQRES 17 A 859 GLU ILE LEU LEU LYS TYR LEU ASN PHE ALA ASN LEU ILE
SEQRES 18 A 859 MET LYS VAL PHE HIS LEU SER TYR LEU HIS ASN CYS GLU
SEQRES 19 A 859 THR ARG ARG GLY GLN ILE LEU LEU TRP SER GLY SER LYS
SEQRES 20 A 859 VAL PHE GLU GLU LEU THR ASP ILE GLU ARG GLN PHE HIS
SEQRES 21 A 859 LYS ALA LEU TYR THR VAL ARG ALA PHE LEU ASN CYS ASP
SEQRES 22 A 859 ARG TYR SER VAL GLY LEU LEU ASP MET THR LYS GLN LYS
SEQRES 23 A 859 GLU PHE PHE ASP VAL TRP PRO VAL LEU MET GLY GLU ALA
SEQRES 24 A 859 PRO PRO TYR ALA GLY PRO ARG THR PRO ASP GLY ARG GLU
SEQRES 25 A 859 ILE ASN PHE TYR LYS VAL ILE ASP TYR ILE LEU HIS GLY
SEQRES 26 A 859 LYS GLU ASP ILE LYS VAL ILE PRO ASN PRO PRO PRO ASP
SEQRES 27 A 859 HIS TRP ALA LEU VAL SER GLY LEU PRO THR TYR VAL ALA
SEQRES 28 A 859 GLN ASN GLY LEU ILE CYS ASN ILE MET ASN ALA PRO SER
SEQRES 29 A 859 GLU ASP PHE PHE ALA PHE GLN LYS GLU PRO LEU ASP GLU
SEQRES 30 A 859 SER GLY TRP MET ILE LYS ASN VAL LEU SER MET PRO ILE
SEQRES 31 A 859 VAL ASN LYS LYS GLU GLU ILE VAL GLY VAL ALA THR PHE
SEQRES 32 A 859 TYR ASN ARG LYS ASP GLY LYS PRO PHE ASP GLU MET ASP
SEQRES 33 A 859 GLU THR LEU MET GLU SER LEU THR GLN PHE LEU GLY TRP
SEQRES 34 A 859 SER VAL LEU ASN PRO ASP THR TYR GLU LEU MET ASN LYS
SEQRES 35 A 859 LEU GLU ASN ARG LYS ASP ILE PHE GLN ASP MET VAL LYS
SEQRES 36 A 859 TYR HIS VAL LYS CYS ASP ASN GLU GLU ILE GLN THR ILE
SEQRES 37 A 859 LEU LYS THR ARG GLU VAL TYR GLY LYS GLU PRO TRP GLU
SEQRES 38 A 859 CYS GLU GLU GLU GLU LEU ALA GLU ILE LEU GLN GLY GLU
SEQRES 39 A 859 LEU PRO ASP ALA ASP LYS TYR GLU ILE ASN LYS PHE HIS
SEQRES 40 A 859 PHE SER ASP LEU PRO LEU THR GLU LEU GLU LEU VAL LYS
SEQRES 41 A 859 CYS GLY ILE GLN MET TYR TYR GLU LEU LYS VAL VAL ASP
SEQRES 42 A 859 LYS PHE HIS ILE PRO GLN GLU ALA LEU VAL ARG PHE MET
SEQRES 43 A 859 TYR SER LEU SER LYS GLY TYR ARG ARG ILE THR TYR HIS
SEQRES 44 A 859 ASN TRP ARG HIS GLY PHE ASN VAL GLY GLN THR MET PHE
SEQRES 45 A 859 SER LEU LEU VAL THR GLY LYS LEU LYS ARG TYR PHE THR
SEQRES 46 A 859 ASP LEU GLU ALA LEU ALA MET VAL THR ALA ALA PHE CYS
SEQRES 47 A 859 HIS ASP ILE ASP HIS ARG GLY THR ASN ASN LEU TYR GLN
SEQRES 48 A 859 MET LYS SER GLN ASN PRO LEU ALA LYS LEU HIS GLY SER
SEQRES 49 A 859 SER ILE LEU GLU ARG HIS HIS LEU GLU PHE GLY LYS THR
SEQRES 50 A 859 LEU LEU ARG ASP GLU SER LEU ASN ILE PHE GLN ASN LEU
SEQRES 51 A 859 ASN ARG ARG GLN HIS GLU HIS ALA ILE HIS MET MET ASP
SEQRES 52 A 859 ILE ALA ILE ILE ALA THR ASP LEU ALA LEU TYR PHE LYS
SEQRES 53 A 859 LYS ARG THR MET PHE GLN LYS ILE VAL ASP GLN SER LYS
SEQRES 54 A 859 THR TYR GLU THR GLN GLN GLU TRP THR GLN TYR MET MET
SEQRES 55 A 859 LEU ASP GLN THR ARG LYS GLU ILE VAL MET ALA MET MET
SEQRES 56 A 859 MET THR ALA CYS ASP LEU SER ALA ILE THR LYS PRO TRP
SEQRES 57 A 859 GLU VAL GLN SER LYS VAL ALA LEU LEU VAL ALA ALA GLU
SEQRES 58 A 859 PHE TRP GLU GLN GLY ASP LEU GLU ARG THR VAL LEU GLN
SEQRES 59 A 859 GLN ASN PRO ILE PRO MET MET ASP ARG ASN LYS ALA ASP
SEQRES 60 A 859 GLU LEU PRO LYS LEU GLN VAL GLY PHE ILE ASP PHE VAL
SEQRES 61 A 859 CYS THR PHE VAL TYR LYS GLU PHE SER ARG PHE HIS GLU
SEQRES 62 A 859 GLU ILE THR PRO MET LEU ASP GLY ILE THR ASN ASN ARG
SEQRES 63 A 859 LYS GLU TRP LYS ALA LEU ALA ASP GLU TYR GLU THR LYS
SEQRES 64 A 859 MET LYS GLY LEU GLU GLU GLU LYS GLN LYS GLN GLN ALA
SEQRES 65 A 859 ALA ASN GLN ALA ALA ALA GLY SER GLN HIS GLY GLY LYS
SEQRES 66 A 859 GLN PRO GLY GLY GLY PRO ALA SER LYS SER CYS CYS VAL
SEQRES 67 A 859 GLN
SEQRES 1 C 87 MET ASN LEU GLU PRO PRO LYS ALA GLU ILE ARG SER ALA
SEQRES 2 C 87 THR ARG VAL MET GLY GLY PRO VAL THR PRO ARG LYS GLY
SEQRES 3 C 87 PRO PRO LYS PHE LYS GLN ARG GLN THR ARG GLN PHE LYS
SEQRES 4 C 87 SER LYS PRO PRO LYS LYS GLY VAL GLN GLY PHE GLY ASP
SEQRES 5 C 87 ASP ILE PRO GLY MET GLU GLY LEU GLY THR ASP ILE THR
SEQRES 6 C 87 VAL ILE CYS PRO TRP GLU ALA PHE ASN HIS LEU GLU LEU
SEQRES 7 C 87 HIS GLU LEU ALA GLN TYR GLY ILE ILE
SEQRES 1 D 87 MET ASN LEU GLU PRO PRO LYS ALA GLU ILE ARG SER ALA
SEQRES 2 D 87 THR ARG VAL MET GLY GLY PRO VAL THR PRO ARG LYS GLY
SEQRES 3 D 87 PRO PRO LYS PHE LYS GLN ARG GLN THR ARG GLN PHE LYS
SEQRES 4 D 87 SER LYS PRO PRO LYS LYS GLY VAL GLN GLY PHE GLY ASP
SEQRES 5 D 87 ASP ILE PRO GLY MET GLU GLY LEU GLY THR ASP ILE THR
SEQRES 6 D 87 VAL ILE CYS PRO TRP GLU ALA PHE ASN HIS LEU GLU LEU
SEQRES 7 D 87 HIS GLU LEU ALA GLN TYR GLY ILE ILE
HET ZN B 901 1
HET MG B 902 1
HET 35G B 903 34
HET ZN A 901 1
HET MG A 902 1
HET 35G A 903 34
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
HETNAM 35G GUANOSINE-3',5'-MONOPHOSPHATE
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 MG 2(MG 2+)
FORMUL 7 35G 2(C10 H12 N5 O7 P)
HELIX 1 AA1 PHE B 47 MET B 66 1 20
HELIX 2 AA2 ASN B 71 HIS B 88 1 18
HELIX 3 AA3 VAL B 118 LEU B 123 1 6
HELIX 4 AA4 PRO B 125 GLU B 129 5 5
HELIX 5 AA5 GLY B 137 LYS B 146 1 10
HELIX 6 AA6 SER B 162 LEU B 167 1 6
HELIX 7 AA7 THR B 202 LEU B 213 1 12
HELIX 8 AA8 GLY B 216 PHE B 247 1 32
HELIX 9 AA9 ASP B 252 VAL B 264 1 13
HELIX 10 AB1 TRP B 290 MET B 294 5 5
HELIX 11 AB2 LEU B 344 SER B 351 1 8
HELIX 12 AB3 ASP B 411 SER B 428 1 18
HELIX 13 AB4 VAL B 429 ARG B 457 1 29
HELIX 14 AB5 ASP B 459 ILE B 466 5 8
HELIX 15 AB6 PRO B 468 LEU B 473 1 6
HELIX 16 AB7 GLU B 481 LEU B 493 1 13
HELIX 17 AB8 THR B 512 LEU B 527 1 16
HELIX 18 AB9 PRO B 536 TYR B 551 1 16
HELIX 19 AC1 ASN B 558 GLY B 576 1 19
HELIX 20 AC2 THR B 583 CYS B 596 1 14
HELIX 21 AC3 ASN B 605 GLN B 613 1 9
HELIX 22 AC4 ASN B 614 HIS B 620 1 7
HELIX 23 AC5 LEU B 625 LEU B 637 1 13
HELIX 24 AC6 ASN B 649 THR B 667 1 19
HELIX 25 AC7 ASP B 668 LYS B 675 1 8
HELIX 26 AC8 ARG B 676 SER B 686 1 11
HELIX 27 AC9 ASP B 691 SER B 700 1 10
HELIX 28 AD1 GLU B 702 LEU B 719 1 18
HELIX 29 AD2 PRO B 725 LEU B 751 1 27
HELIX 30 AD3 ILE B 756 ALA B 764 5 9
HELIX 31 AD4 GLU B 766 VAL B 778 1 13
HELIX 32 AD5 PHE B 781 HIS B 790 1 10
HELIX 33 AD6 ILE B 793 GLU B 823 1 31
HELIX 34 AD7 LYS A 11 ASN A 16 1 6
HELIX 35 AD8 ALA A 20 ASP A 35 1 16
HELIX 36 AD9 VAL A 55 ARG A 66 1 12
HELIX 37 AE1 GLU A 75 LEU A 89 1 15
HELIX 38 AE2 VAL A 120 CYS A 124 5 5
HELIX 39 AE3 MET A 138 LYS A 148 1 11
HELIX 40 AE4 ASN A 155 ASP A 159 5 5
HELIX 41 AE5 ASP A 164 THR A 170 1 7
HELIX 42 AE6 THR A 204 LEU A 215 1 12
HELIX 43 AE7 LEU A 215 LEU A 220 1 6
HELIX 44 AE8 ILE A 221 GLU A 250 1 30
HELIX 45 AE9 ASP A 254 VAL A 266 1 13
HELIX 46 AF1 GLU A 287 ASP A 290 5 4
HELIX 47 AF2 VAL A 291 GLY A 297 1 7
HELIX 48 AF3 GLY A 345 GLY A 354 1 10
HELIX 49 AF4 ASP A 413 SER A 430 1 18
HELIX 50 AF5 VAL A 431 VAL A 458 1 28
HELIX 51 AF6 ASP A 461 GLN A 466 1 6
HELIX 52 AF7 GLU A 478 CYS A 482 5 5
HELIX 53 AF8 GLU A 483 GLY A 493 1 11
HELIX 54 AF9 ASP A 497 GLU A 502 1 6
HELIX 55 AG1 THR A 514 LEU A 529 1 16
HELIX 56 AG2 VAL A 531 HIS A 536 1 6
HELIX 57 AG3 PRO A 538 TYR A 553 1 16
HELIX 58 AG4 ASN A 560 THR A 577 1 18
HELIX 59 AG5 THR A 585 CYS A 598 1 14
HELIX 60 AG6 ASN A 607 GLN A 615 1 9
HELIX 61 AG7 ASN A 616 HIS A 622 1 7
HELIX 62 AG8 SER A 625 ARG A 640 1 16
HELIX 63 AG9 ASN A 651 THR A 669 1 19
HELIX 64 AH1 ASP A 670 LYS A 677 1 8
HELIX 65 AH2 THR A 679 LYS A 689 1 11
HELIX 66 AH3 GLU A 696 GLN A 705 1 10
HELIX 67 AH4 GLN A 705 LEU A 721 1 17
HELIX 68 AH5 SER A 722 LYS A 726 5 5
HELIX 69 AH6 PRO A 727 GLN A 754 1 28
HELIX 70 AH7 ILE A 758 ASP A 767 5 10
HELIX 71 AH8 GLU A 768 VAL A 780 1 13
HELIX 72 AH9 PHE A 783 HIS A 792 1 10
HELIX 73 AI1 THR A 796 LYS A 827 1 32
HELIX 74 AI2 LEU C 78 TYR C 84 1 7
HELIX 75 AI3 GLU D 77 LEU D 81 5 5
SHEET 1 AA1 5 LEU B 110 VAL B 113 0
SHEET 2 AA1 5 CYS B 92 MET B 96 -1 N CYS B 92 O VAL B 113
SHEET 3 AA1 5 ASP B 185 ALA B 192 -1 O VAL B 189 N PHE B 95
SHEET 4 AA1 5 ILE B 175 ASN B 182 -1 N ILE B 180 O VAL B 187
SHEET 5 AA1 5 VAL B 149 VAL B 151 -1 N VAL B 149 O ALA B 177
SHEET 1 AA2 2 ARG B 98 ARG B 100 0
SHEET 2 AA2 2 VAL B 103 GLU B 105 -1 O GLU B 105 N ARG B 98
SHEET 1 AA3 6 LYS B 328 ILE B 330 0
SHEET 2 AA3 6 PHE B 313 ILE B 320 -1 N VAL B 316 O ILE B 330
SHEET 3 AA3 6 ARG B 272 LEU B 278 -1 N VAL B 275 O ILE B 317
SHEET 4 AA3 6 ILE B 395 PHE B 401 -1 O VAL B 398 N GLY B 276
SHEET 5 AA3 6 LEU B 384 VAL B 389 -1 N ILE B 388 O VAL B 396
SHEET 6 AA3 6 CYS B 355 ASN B 356 -1 N CYS B 355 O SER B 385
SHEET 1 AA4 6 VAL A 133 PHE A 134 0
SHEET 2 AA4 6 ILE A 105 VAL A 115 -1 N LEU A 108 O PHE A 134
SHEET 3 AA4 6 ASP A 92 ARG A 102 -1 N ARG A 100 O GLU A 107
SHEET 4 AA4 6 ASP A 187 VAL A 195 -1 O ILE A 191 N PHE A 97
SHEET 5 AA4 6 ILE A 177 ASN A 184 -1 N ASN A 184 O ASP A 187
SHEET 6 AA4 6 VAL A 151 ASN A 152 -1 N VAL A 151 O ALA A 179
SHEET 1 AA5 6 ASP A 328 PRO A 333 0
SHEET 2 AA5 6 PHE A 315 ILE A 322 -1 N ILE A 322 O ASP A 328
SHEET 3 AA5 6 ARG A 274 LEU A 280 -1 N VAL A 277 O ILE A 319
SHEET 4 AA5 6 ILE A 397 PHE A 403 -1 O THR A 402 N SER A 276
SHEET 5 AA5 6 VAL A 385 VAL A 391 -1 N ILE A 390 O VAL A 398
SHEET 6 AA5 6 CYS A 357 ILE A 359 -1 N ILE A 359 O VAL A 385
SSBOND 1 CYS B 84 CYS B 92 1555 1555 2.03
LINK NE2 HIS B 561 ZN ZN B 901 1555 1555 2.30
LINK NE2 HIS B 597 ZN ZN B 901 1555 1555 2.30
LINK NE2 HIS A 563 ZN ZN A 901 1555 1555 2.30
LINK NE2 HIS A 599 ZN ZN A 901 1555 1555 2.30
LINK OD2 ASP A 600 ZN ZN A 901 1555 1555 1.91
LINK OD1 ASP A 600 MG MG A 902 1555 1555 2.30
LINK OD2 ASP A 600 MG MG A 902 1555 1555 2.74
LINK OD1 ASP A 720 ZN ZN A 901 1555 1555 1.96
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
