HEADER TRANSCRIPTION 18-MAY-14 4PLL
TITLE STRUCTURE OF THE CHROMODAOMAIN OF MRG2 IN COMPLEX WITH H3K36ME3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AT1G02740;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 51-123;
COMPND 5 SYNONYM: MRG FAMILY PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: H3K36ME3;
COMPND 9 CHAIN: C, D;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: AT1G02740;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 10 ORGANISM_TAXID: 3702;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CHROMODOMAIN, H3K36ME3, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.LIU,Y.HUANG
REVDAT 3 27-DEC-23 4PLL 1 REMARK
REVDAT 2 04-MAY-16 4PLL 1 JRNL
REVDAT 1 22-JUL-15 4PLL 0
JRNL AUTH Z.BU,Y.YU,Z.LI,Y.LIU,W.JIANG,Y.HUANG,A.W.DONG
JRNL TITL REGULATION OF ARABIDOPSIS FLOWERING BY THE HISTONE MARK
JRNL TITL 2 READERS MRG1/2 VIA INTERACTION WITH CONSTANS TO MODULATE FT
JRNL TITL 3 EXPRESSION.
JRNL REF PLOS GENET. V. 10 04617 2014
JRNL REFN ESSN 1553-7404
JRNL PMID 25211338
JRNL DOI 10.1371/JOURNAL.PGEN.1004617
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.430
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 6489
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.244
REMARK 3 R VALUE (WORKING SET) : 0.240
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.920
REMARK 3 FREE R VALUE TEST SET COUNT : 644
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 28.5764 - 4.4414 1.00 1228 136 0.2205 0.2638
REMARK 3 2 4.4414 - 3.5273 1.00 1174 131 0.2166 0.2652
REMARK 3 3 3.5273 - 3.0821 1.00 1166 130 0.2635 0.2793
REMARK 3 4 3.0821 - 2.8005 0.99 1138 129 0.3073 0.3252
REMARK 3 5 2.8005 - 2.6000 0.97 1139 118 0.3195 0.3747
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.460
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.280
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 : 0.010 1055
REMARK 3 ANGLE : 1.330 1418
REMARK 3 CHIRALITY : 0.059 134
REMARK 3 PLANARITY : 0.006 170
REMARK 3 DIHEDRAL : 19.901 372
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 4PLL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000201609.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 6489
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.09400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.5, 30% POLYETHYLENE
REMARK 280 GLYCOL MONOMETHYL ETHER 5000, 0.2M AMMONIUM SULFATE, PH 8.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 9.99233
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 19.98467
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 14.98850
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 24.98083
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 4.99617
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 GLY A 49
REMARK 465 SER A 50
REMARK 465 SER A 107
REMARK 465 ASP A 108
REMARK 465 GLU A 109
REMARK 465 ASN A 110
REMARK 465 ILE A 111
REMARK 465 GLU A 112
REMARK 465 LYS A 113
REMARK 465 GLN A 114
REMARK 465 LYS A 115
REMARK 465 GLU A 116
REMARK 465 GLN A 117
REMARK 465 GLY A 118
REMARK 465 LEU A 119
REMARK 465 LYS A 120
REMARK 465 GLN A 121
REMARK 465 GLN A 122
REMARK 465 GLY A 123
REMARK 465 GLY B 49
REMARK 465 SER B 50
REMARK 465 SER B 107
REMARK 465 ASP B 108
REMARK 465 GLU B 109
REMARK 465 ASN B 110
REMARK 465 ILE B 111
REMARK 465 GLU B 112
REMARK 465 LYS B 113
REMARK 465 GLN B 114
REMARK 465 LYS B 115
REMARK 465 GLU B 116
REMARK 465 GLN B 117
REMARK 465 GLY B 118
REMARK 465 LEU B 119
REMARK 465 LYS B 120
REMARK 465 GLN B 121
REMARK 465 GLN B 122
REMARK 465 GLY B 123
REMARK 465 ALA C 31
REMARK 465 THR C 32
REMARK 465 GLY C 33
REMARK 465 GLY C 34
REMARK 465 VAL C 35
REMARK 465 LYS C 37
REMARK 465 PRO C 38
REMARK 465 HIS C 39
REMARK 465 ARG C 40
REMARK 465 TYR C 41
REMARK 465 ALA D 31
REMARK 465 THR D 32
REMARK 465 GLY D 33
REMARK 465 GLY D 34
REMARK 465 VAL D 35
REMARK 465 LYS D 37
REMARK 465 PRO D 38
REMARK 465 HIS D 39
REMARK 465 ARG D 40
REMARK 465 TYR D 41
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 GLU A 68 O HOH A 201 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 SER A 63 -132.99 60.11
REMARK 500 ASN A 91 165.54 -29.62
REMARK 500 SER B 63 -123.80 62.91
REMARK 500 ASN B 79 11.23 52.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PL6 RELATED DB: PDB
REMARK 900 RELATED ID: 4PLI RELATED DB: PDB
DBREF 4PLL A 51 123 UNP Q4V3E2 Q4V3E2_ARATH 51 123
DBREF 4PLL B 51 123 UNP Q4V3E2 Q4V3E2_ARATH 51 123
DBREF 4PLL C 31 41 PDB 4PLL 4PLL 31 41
DBREF 4PLL D 31 41 PDB 4PLL 4PLL 31 41
SEQADV 4PLL GLY A 49 UNP Q4V3E2 EXPRESSION TAG
SEQADV 4PLL SER A 50 UNP Q4V3E2 EXPRESSION TAG
SEQADV 4PLL GLY B 49 UNP Q4V3E2 EXPRESSION TAG
SEQADV 4PLL SER B 50 UNP Q4V3E2 EXPRESSION TAG
SEQRES 1 A 75 GLY SER HIS PHE GLU GLU GLY GLU ARG VAL LEU ALA LYS
SEQRES 2 A 75 HIS SER ASP CYS PHE TYR GLU ALA LYS VAL LEU LYS VAL
SEQRES 3 A 75 GLU PHE LYS ASP ASN GLU TRP LYS TYR PHE VAL HIS TYR
SEQRES 4 A 75 ILE GLY TRP ASN LYS SER TRP ASP GLU TRP ILE ARG LEU
SEQRES 5 A 75 ASP CYS LEU LEU LYS HIS SER ASP GLU ASN ILE GLU LYS
SEQRES 6 A 75 GLN LYS GLU GLN GLY LEU LYS GLN GLN GLY
SEQRES 1 B 75 GLY SER HIS PHE GLU GLU GLY GLU ARG VAL LEU ALA LYS
SEQRES 2 B 75 HIS SER ASP CYS PHE TYR GLU ALA LYS VAL LEU LYS VAL
SEQRES 3 B 75 GLU PHE LYS ASP ASN GLU TRP LYS TYR PHE VAL HIS TYR
SEQRES 4 B 75 ILE GLY TRP ASN LYS SER TRP ASP GLU TRP ILE ARG LEU
SEQRES 5 B 75 ASP CYS LEU LEU LYS HIS SER ASP GLU ASN ILE GLU LYS
SEQRES 6 B 75 GLN LYS GLU GLN GLY LEU LYS GLN GLN GLY
SEQRES 1 C 11 ALA THR GLY GLY VAL M3L LYS PRO HIS ARG TYR
SEQRES 1 D 11 ALA THR GLY GLY VAL M3L LYS PRO HIS ARG TYR
HET M3L C 36 12
HET M3L D 36 12
HETNAM M3L N-TRIMETHYLLYSINE
FORMUL 3 M3L 2(C9 H21 N2 O2 1+)
FORMUL 5 HOH *8(H2 O)
HELIX 1 AA1 ASN A 91 ASP A 95 5 5
HELIX 2 AA2 ARG A 99 ASP A 101 5 3
HELIX 3 AA3 ARG B 99 ASP B 101 5 3
SHEET 1 AA1 5 GLU A 96 ILE A 98 0
SHEET 2 AA1 5 GLU A 80 TYR A 87 -1 N TYR A 83 O ILE A 98
SHEET 3 AA1 5 CYS A 65 LYS A 77 -1 N LYS A 70 O HIS A 86
SHEET 4 AA1 5 ARG A 57 HIS A 62 -1 N ALA A 60 O TYR A 67
SHEET 5 AA1 5 LEU A 103 LYS A 105 -1 O LEU A 104 N LEU A 59
SHEET 1 AA2 5 GLU B 96 ILE B 98 0
SHEET 2 AA2 5 GLU B 80 TYR B 87 -1 N VAL B 85 O GLU B 96
SHEET 3 AA2 5 CYS B 65 LYS B 77 -1 N LYS B 70 O HIS B 86
SHEET 4 AA2 5 ARG B 57 HIS B 62 -1 N HIS B 62 O CYS B 65
SHEET 5 AA2 5 LEU B 103 LEU B 104 -1 O LEU B 104 N LEU B 59
SSBOND 1 CYS A 65 CYS B 65 1555 1555 2.01
CRYST1 109.157 109.157 29.977 90.00 90.00 120.00 P 61 12
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 0.009161 0.005289 0.000000 0.00000
SCALE2 0.000000 0.010578 0.000000 0.00000
SCALE3 0.000000 0.000000 0.033359 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
