HEADER SIGNALING PROTEIN 01-NOV-17 5YPH
TITLE P62/SQSTM1 ZZ DOMAIN WITH ILE-PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 78 KDA GLUCOSE-REGULATED PROTEIN,SEQUESTOSOME-1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GRP-78,EBI3-ASSOCIATED PROTEIN OF 60 KDA,P60,
COMPND 5 PHOSPHOTYROSINE-INDEPENDENT LIGAND FOR THE LCK SH2 DOMAIN OF 62 KDA,
COMPND 6 UBIQUITIN-BINDING PROTEIN P62;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HSPA5, GRP78, SQSTM1, ORCA, OSIL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS COMPLEX, P62/SQSTM1, ZZ DOMAIN, AUTOPHAGY, N-END RULE, SIGNALING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.H.KWON,L.KIM,H.K.SONG
REVDAT 3 22-NOV-23 5YPH 1 REMARK
REVDAT 2 03-OCT-18 5YPH 1 TITLE
REVDAT 1 29-AUG-18 5YPH 0
JRNL AUTH D.H.KWON,O.H.PARK,L.KIM,Y.O.JUNG,Y.PARK,H.JEONG,J.HYUN,
JRNL AUTH 2 Y.K.KIM,H.K.SONG
JRNL TITL INSIGHTS INTO DEGRADATION MECHANISM OF N-END RULE SUBSTRATES
JRNL TITL 2 BY P62/SQSTM1 AUTOPHAGY ADAPTER.
JRNL REF NAT COMMUN V. 9 3291 2018
JRNL REFN ESSN 2041-1723
JRNL PMID 30120248
JRNL DOI 10.1038/S41467-018-05825-X
REMARK 2
REMARK 2 RESOLUTION. 1.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 9011
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.151
REMARK 3 R VALUE (WORKING SET) : 0.147
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.120
REMARK 3 FREE R VALUE TEST SET COUNT : 912
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 17.9096 - 3.1114 0.98 1251 139 0.1595 0.1674
REMARK 3 2 3.1114 - 2.4717 0.97 1190 138 0.1540 0.1902
REMARK 3 3 2.4717 - 2.1599 0.96 1172 135 0.1490 0.2025
REMARK 3 4 2.1599 - 1.9627 0.94 1155 133 0.1370 0.2191
REMARK 3 5 1.9627 - 1.8221 0.93 1138 124 0.1319 0.1815
REMARK 3 6 1.8221 - 1.7148 0.92 1126 121 0.1303 0.1813
REMARK 3 7 1.7148 - 1.6290 0.89 1067 122 0.1186 0.1906
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.000
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 762
REMARK 3 ANGLE : 1.305 1030
REMARK 3 CHIRALITY : 0.073 112
REMARK 3 PLANARITY : 0.011 137
REMARK 3 DIHEDRAL : 6.252 458
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5YPH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-NOV-17.
REMARK 100 THE DEPOSITION ID IS D_1300005680.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-16
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9011
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.629
REMARK 200 RESOLUTION RANGE LOW (A) : 17.910
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.0
REMARK 200 DATA REDUNDANCY : 3.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5YP7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 16.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM PHOSPHATE, POTASSIUM PHOSPHATE,
REMARK 280 MGCL2, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 16.69050
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PHE A 48
REMARK 465 GLY A 49
REMARK 465 HIS A 50
REMARK 465 LEU A 51
REMARK 465 SER A 52
REMARK 465 GLU A 53
REMARK 465 GLY A 54
REMARK 465 PHE A 55
REMARK 465 SER A 56
REMARK 465 SER B 46
REMARK 465 PRO B 47
REMARK 465 PHE B 48
REMARK 465 GLY B 49
REMARK 465 HIS B 50
REMARK 465 LEU B 51
REMARK 465 SER B 52
REMARK 465 GLU B 53
REMARK 465 GLY B 54
REMARK 465 PHE B 55
REMARK 465 SER B 56
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 O HOH B 234 O HOH B 241 2.12
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 CYS A 7 -0.69 -140.79
REMARK 500 ASP A 23 30.97 71.82
REMARK 500 ASP B 23 41.57 -155.74
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 A 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 4 SG
REMARK 620 2 CYS A 7 SG 110.6
REMARK 620 3 CYS A 27 SG 109.8 115.3
REMARK 620 4 CYS A 30 SG 106.4 107.8 106.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 102 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 18 SG
REMARK 620 2 CYS A 21 SG 119.0
REMARK 620 3 HIS A 36 NE2 107.1 114.2
REMARK 620 4 HIS A 39 ND1 100.5 107.6 107.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 4 SG
REMARK 620 2 CYS B 7 SG 107.0
REMARK 620 3 CYS B 27 SG 110.6 118.6
REMARK 620 4 CYS B 30 SG 104.6 109.0 106.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 102 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 18 SG
REMARK 620 2 CYS B 21 SG 119.9
REMARK 620 3 HIS B 36 NE2 112.2 110.4
REMARK 620 4 HIS B 39 ND1 102.3 107.0 103.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 102
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ILE (-3 POSITION) IS SYNTHETIC RESIDUE GENERATED BY SPECIAL ENZYME
DBREF 5YPH A -2 1 UNP P11021 GRP78_HUMAN 19 22
DBREF 5YPH A 2 56 UNP Q13501 SQSTM_HUMAN 126 180
DBREF 5YPH B -2 1 UNP P11021 GRP78_HUMAN 19 22
DBREF 5YPH B 2 56 UNP Q13501 SQSTM_HUMAN 126 180
SEQADV 5YPH ILE A -3 UNP P11021 SEE SEQUENCE DETAILS
SEQADV 5YPH ILE B -3 UNP P11021 SEE SEQUENCE DETAILS
SEQRES 1 A 60 ILE GLU GLU GLU ASP VAL ILE CYS ASP GLY CYS ASN GLY
SEQRES 2 A 60 PRO VAL VAL GLY THR ARG TYR LYS CYS SER VAL CYS PRO
SEQRES 3 A 60 ASP TYR ASP LEU CYS SER VAL CYS GLU GLY LYS GLY LEU
SEQRES 4 A 60 HIS ARG GLY HIS THR LYS LEU ALA PHE PRO SER PRO PHE
SEQRES 5 A 60 GLY HIS LEU SER GLU GLY PHE SER
SEQRES 1 B 60 ILE GLU GLU GLU ASP VAL ILE CYS ASP GLY CYS ASN GLY
SEQRES 2 B 60 PRO VAL VAL GLY THR ARG TYR LYS CYS SER VAL CYS PRO
SEQRES 3 B 60 ASP TYR ASP LEU CYS SER VAL CYS GLU GLY LYS GLY LEU
SEQRES 4 B 60 HIS ARG GLY HIS THR LYS LEU ALA PHE PRO SER PRO PHE
SEQRES 5 B 60 GLY HIS LEU SER GLU GLY PHE SER
HET ZN A 101 1
HET ZN A 102 1
HET ZN B 101 1
HET ZN B 102 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 4(ZN 2+)
FORMUL 7 HOH *117(H2 O)
HELIX 1 AA1 CYS A 27 LYS A 33 1 7
HELIX 2 AA2 CYS B 27 LYS B 33 1 7
SHEET 1 AA1 3 ASP A 25 LEU A 26 0
SHEET 2 AA1 3 THR A 14 CYS A 18 -1 N TYR A 16 O LEU A 26
SHEET 3 AA1 3 LYS A 41 PRO A 45 -1 O PHE A 44 N ARG A 15
SHEET 1 AA2 3 ASP B 25 LEU B 26 0
SHEET 2 AA2 3 ARG B 15 CYS B 18 -1 N TYR B 16 O LEU B 26
SHEET 3 AA2 3 LYS B 41 PHE B 44 -1 O PHE B 44 N ARG B 15
LINK SG CYS A 4 ZN ZN A 101 1555 1555 2.35
LINK SG CYS A 7 ZN ZN A 101 1555 1555 2.34
LINK SG CYS A 18 ZN ZN A 102 1555 1555 2.33
LINK SG CYS A 21 ZN ZN A 102 1555 1555 2.28
LINK SG CYS A 27 ZN ZN A 101 1555 1555 2.37
LINK SG CYS A 30 ZN ZN A 101 1555 1555 2.35
LINK NE2 HIS A 36 ZN ZN A 102 1555 1555 1.99
LINK ND1 HIS A 39 ZN ZN A 102 1555 1555 2.09
LINK SG CYS B 4 ZN ZN B 101 1555 1555 2.31
LINK SG CYS B 7 ZN ZN B 101 1555 1555 2.29
LINK SG CYS B 18 ZN ZN B 102 1555 1555 2.31
LINK SG CYS B 21 ZN ZN B 102 1555 1555 2.25
LINK SG CYS B 27 ZN ZN B 101 1555 1555 2.34
LINK SG CYS B 30 ZN ZN B 101 1555 1555 2.36
LINK NE2 HIS B 36 ZN ZN B 102 1555 1555 1.99
LINK ND1 HIS B 39 ZN ZN B 102 1555 1555 2.11
SITE 1 AC1 4 CYS A 4 CYS A 7 CYS A 27 CYS A 30
SITE 1 AC2 4 CYS A 18 CYS A 21 HIS A 36 HIS A 39
SITE 1 AC3 4 CYS B 4 CYS B 7 CYS B 27 CYS B 30
SITE 1 AC4 4 CYS B 18 CYS B 21 HIS B 36 HIS B 39
CRYST1 33.658 33.381 35.019 90.00 103.61 90.00 P 1 21 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 0.029711 0.000000 0.007195 0.00000
SCALE2 0.000000 0.029957 0.000000 0.00000
SCALE3 0.000000 0.000000 0.029381 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
