HEADER TRANSPORT PROTEIN 01-AUG-13 4LZV
TITLE BOVINE BETA-LACTOGLOBULIN CRYSTALLIZED IN THE PRESENCE OF 20 MM ZINC
TITLE 2 CHLORIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTOGLOBULIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 17-178;
COMPND 5 SYNONYM: BETA-LG
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.OELKER,G.ZOCHER,T.STEHLE
REVDAT 3 20-SEP-23 4LZV 1 REMARK LINK
REVDAT 2 07-MAR-18 4LZV 1 REMARK
REVDAT 1 06-AUG-14 4LZV 0
JRNL AUTH A.SAUTER,M.OELKER,G.ZOCHER,F.ZHANG,T.STEHLE,F.SCHREIBER
JRNL TITL NON-CLASSICAL PATHWAYS OF PROTEIN CRYSTALLIZATION IN THE
JRNL TITL 2 PRESENCE OF MULTIVALENT METAL IONS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.44 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0025
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) : 2.44
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 6365
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) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 12.000
REMARK 3 FREE R VALUE TEST SET COUNT : 868
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) : 2.44
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.50
REMARK 3 REFLECTION IN BIN (WORKING SET) : 439
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.2370
REMARK 3 BIN FREE R VALUE SET COUNT : 59
REMARK 3 BIN FREE R VALUE : 0.2480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1252
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 10
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.29000
REMARK 3 B22 (A**2) : 0.29000
REMARK 3 B33 (A**2) : -0.94000
REMARK 3 B12 (A**2) : 0.15000
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): 0.522
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.266
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.178
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.918
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.930
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1291 ; 0.004 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1259 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1745 ; 0.871 ; 1.994
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2922 ; 0.644 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 160 ; 4.551 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 55 ;29.158 ;26.364
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 246 ;11.067 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ; 4.582 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 202 ; 0.054 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1426 ; 0.002 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 250 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 640 ; 1.513 ; 8.158
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 639 ; 1.505 ; 8.157
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 800 ; 2.328 ;10.700
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 651 ; 2.349 ; 8.659
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): 1825 ; 3.092 ;33.858
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 4 A 162
REMARK 3 ORIGIN FOR THE GROUP (A): 58.8554 -15.3031 3.3378
REMARK 3 T TENSOR
REMARK 3 T11: 0.0155 T22: 0.0572
REMARK 3 T33: 0.0034 T12: -0.0079
REMARK 3 T13: 0.0023 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 2.0787 L22: 4.0868
REMARK 3 L33: 3.6801 L12: -0.0899
REMARK 3 L13: 0.1946 L23: 0.7774
REMARK 3 S TENSOR
REMARK 3 S11: 0.0228 S12: 0.0207 S13: 0.0631
REMARK 3 S21: -0.1364 S22: 0.0222 S23: -0.0203
REMARK 3 S31: -0.1293 S32: -0.0464 S33: -0.0450
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4LZV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081288.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2380
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7223
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.440
REMARK 200 RESOLUTION RANGE LOW (A) : 38.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 8.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.5700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.44
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 14.86
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: PDB ENTRY 3PH5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 MM ZINC CHLORIDE, PH 5.9, BATCH,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 27.16667
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 13.58333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 13.58333
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 27.16667
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -137.0 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 13.58333
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 LEU A 1
REMARK 465 ILE A 2
REMARK 465 VAL A 3
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 GLN A 5 CD OE1 NE2
REMARK 470 LYS A 91 CE NZ
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 ALA A 34 162.36 80.20
REMARK 500 TYR A 99 -41.84 79.19
REMARK 500 LYS A 101 -57.10 -126.66
REMARK 500 GLN A 159 -127.92 51.62
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 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 51 OE1
REMARK 620 2 GLU A 51 OE2 54.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 53 OD2
REMARK 620 2 GLU A 74 OE1 99.9
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 ZN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PH5 RELATED DB: PDB
REMARK 900 RELATED ID: 3PH6 RELATED DB: PDB
REMARK 900 RELATED ID: 4LZU RELATED DB: PDB
DBREF 4LZV A 1 162 UNP P02754 LACB_BOVIN 17 178
SEQRES 1 A 162 LEU ILE VAL THR GLN THR MET LYS GLY LEU ASP ILE GLN
SEQRES 2 A 162 LYS VAL ALA GLY THR TRP TYR SER LEU ALA MET ALA ALA
SEQRES 3 A 162 SER ASP ILE SER LEU LEU ASP ALA GLN SER ALA PRO LEU
SEQRES 4 A 162 ARG VAL TYR VAL GLU GLU LEU LYS PRO THR PRO GLU GLY
SEQRES 5 A 162 ASP LEU GLU ILE LEU LEU GLN LYS TRP GLU ASN GLY GLU
SEQRES 6 A 162 CYS ALA GLN LYS LYS ILE ILE ALA GLU LYS THR LYS ILE
SEQRES 7 A 162 PRO ALA VAL PHE LYS ILE ASP ALA LEU ASN GLU ASN LYS
SEQRES 8 A 162 VAL LEU VAL LEU ASP THR ASP TYR LYS LYS TYR LEU LEU
SEQRES 9 A 162 PHE CYS MET GLU ASN SER ALA GLU PRO GLU GLN SER LEU
SEQRES 10 A 162 ALA CYS GLN CYS LEU VAL ARG THR PRO GLU VAL ASP ASP
SEQRES 11 A 162 GLU ALA LEU GLU LYS PHE ASP LYS ALA LEU LYS ALA LEU
SEQRES 12 A 162 PRO MET HIS ILE ARG LEU SER PHE ASN PRO THR GLN LEU
SEQRES 13 A 162 GLU GLU GLN CYS HIS ILE
HET ZN A 201 1
HET ZN A 202 1
HET ZN A 203 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 3(ZN 2+)
FORMUL 5 HOH *10(H2 O)
HELIX 1 1 ASP A 11 ALA A 16 5 6
HELIX 2 2 ASP A 28 LEU A 32 5 5
HELIX 3 3 ASP A 129 LYS A 141 1 13
HELIX 4 4 ASN A 152 GLN A 159 1 8
SHEET 1 A10 GLY A 17 THR A 18 0
SHEET 2 A10 VAL A 41 PRO A 48 -1 O LEU A 46 N GLY A 17
SHEET 3 A10 LEU A 54 GLU A 62 -1 O GLU A 55 N LYS A 47
SHEET 4 A10 GLU A 65 LYS A 75 -1 O ALA A 67 N LYS A 60
SHEET 5 A10 VAL A 81 ALA A 86 -1 O LYS A 83 N GLU A 74
SHEET 6 A10 GLU A 89 THR A 97 -1 O VAL A 92 N PHE A 82
SHEET 7 A10 TYR A 102 GLU A 108 -1 O LEU A 104 N ASP A 96
SHEET 8 A10 ALA A 118 VAL A 123 -1 O LEU A 122 N LEU A 103
SHEET 9 A10 TYR A 20 ALA A 26 -1 N ALA A 25 O CYS A 119
SHEET 10 A10 ILE A 147 SER A 150 -1 O LEU A 149 N MET A 24
SSBOND 1 CYS A 66 CYS A 160 1555 1555 2.06
SSBOND 2 CYS A 106 CYS A 119 1555 1555 2.04
LINK OE1 GLU A 51 ZN ZN A 201 1555 1555 2.02
LINK OE2 GLU A 51 ZN ZN A 201 1555 1555 2.63
LINK OD2 ASP A 53 ZN ZN A 202 1555 1555 2.02
LINK OE1 GLU A 74 ZN ZN A 202 1555 1555 2.02
LINK NE2 HIS A 146 ZN ZN A 203 1555 1555 2.15
SITE 1 AC1 1 GLU A 51
SITE 1 AC2 3 ASP A 53 GLU A 74 HIS A 161
SITE 1 AC3 1 HIS A 146
CRYST1 89.820 89.820 40.750 90.00 90.00 120.00 P 32 2 1 6
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 0.011133 0.006428 0.000000 0.00000
SCALE2 0.000000 0.012856 0.000000 0.00000
SCALE3 0.000000 0.000000 0.024540 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
