HEADER TRANSPORT PROTEIN 14-NOV-13 4NLJ
TITLE CRYSTAL STRUCTURE OF SHEEP BETA-LACTOGLOBULIN (SPACE GROUP P1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTOGLOBULIN-1/B;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 19-180;
COMPND 5 SYNONYM: BETA-LG;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE 3 ORGANISM_COMMON: DOMESTIC SHEEP,LAMBS,WILD SHEEP;
SOURCE 4 ORGANISM_TAXID: 9940
KEYWDS LIPOCALIN, TRANSPORT, MILK, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.I.LOCH,M.MOLENDA,M.KOPEC,S.SWIATEK,K.LEWINSKI
REVDAT 4 08-NOV-23 4NLJ 1 REMARK
REVDAT 3 10-DEC-14 4NLJ 1 JRNL
REVDAT 2 19-MAR-14 4NLJ 1 JRNL
REVDAT 1 12-MAR-14 4NLJ 0
JRNL AUTH J.I.LOCH,M.MOLENDA,M.KOPEC,S.SWIATEK,K.LEWINSKI
JRNL TITL STRUCTURE OF TWO CRYSTAL FORMS OF SHEEP BETA-LACTOGLOBULIN
JRNL TITL 2 WITH EF-LOOP IN CLOSED CONFORMATION
JRNL REF BIOPOLYMERS V. 101 886 2014
JRNL REFN ISSN 0006-3525
JRNL PMID 25098178
JRNL DOI 10.1002/BIP.22471
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 53791
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2852
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3832
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 193
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2516
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 386
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
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): 0.076
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.052
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.290
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2910 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4001 ; 1.542 ; 1.995
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 389 ; 6.353 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 124 ;32.380 ;26.935
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 570 ;13.915 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;20.093 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 452 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2202 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1442 ; 0.840 ; 1.214
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1846 ; 1.415 ; 1.819
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1468 ; 1.337 ; 1.406
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): 4834 ; 5.033 ;11.617
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 : NULL
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4NLJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1000083354.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : SEALED TUBE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OXFORD DIFFRACTION ENHANCE ULTRA
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : MULTILAYER X-RAY OPTICS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : AGILENT ATLAS CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56652
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 14.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.03500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.40100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: 1QG5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1M AMMONIUM SULPHATE, 0.05M TRIS
REMARK 280 -HCL, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 ILE B 1
REMARK 465 ILE B 2
REMARK 465 VAL B 3
REMARK 465 THR B 4
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 LEU B 140 CA - CB - CG ANGL. DEV. = 18.9 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 ASP A 33 47.04 -87.90
REMARK 500 ALA A 34 157.12 94.83
REMARK 500 TYR A 99 -43.27 73.38
REMARK 500 LYS A 101 -52.30 -132.47
REMARK 500 LYS A 101 -50.83 -133.26
REMARK 500 GLU A 112 69.18 -153.92
REMARK 500 GLN A 159 -124.81 26.32
REMARK 500 CYS A 160 -19.50 105.29
REMARK 500 CYS A 160 44.20 -91.18
REMARK 500 ALA B 34 145.93 97.66
REMARK 500 ASP B 96 149.86 -174.42
REMARK 500 TYR B 99 -46.59 71.99
REMARK 500 LYS B 101 -50.63 -132.81
REMARK 500 GLU B 112 72.64 -158.99
REMARK 500 SER B 116 -1.99 -150.75
REMARK 500 CYS B 160 78.88 8.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 158 GLN A 159 149.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE ORIGINAL NUMBERS OF HOHS HAVE BEEN RENUMBERED.
REMARK 600 ORIGINAL RENUMBERED
REMARK 600 HOH(204, CHAIN B) HOH(201, CHAIN B).
REMARK 600 HOH(205, CHAIN B) HOH(202, CHAIN B).
REMARK 600 HOH(206, CHAIN B) HOH(203, CHAIN B).
REMARK 600 HOH(201, CHAIN A) HOH(204, CHAIN B).
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NLI RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THESE CONFLICTS ARE DUE TO NATURAL VARIANT.
DBREF 4NLJ A 1 162 UNP P67976 LACB_SHEEP 19 180
DBREF 4NLJ B 1 162 UNP P67976 LACB_SHEEP 19 180
SEQADV 4NLJ TYR A 20 UNP P67976 HIS 38 SEE REMARK 999
SEQADV 4NLJ TYR B 20 UNP P67976 HIS 38 SEE REMARK 999
SEQRES 1 A 162 ILE 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 ASN 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 ASN
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 ALA PHE ASN PRO THR GLN LEU
SEQRES 13 A 162 GLU GLY GLN CYS HIS VAL
SEQRES 1 B 162 ILE ILE VAL THR GLN THR MET LYS GLY LEU ASP ILE GLN
SEQRES 2 B 162 LYS VAL ALA GLY THR TRP TYR SER LEU ALA MET ALA ALA
SEQRES 3 B 162 SER ASP ILE SER LEU LEU ASP ALA GLN SER ALA PRO LEU
SEQRES 4 B 162 ARG VAL TYR VAL GLU GLU LEU LYS PRO THR PRO GLU GLY
SEQRES 5 B 162 ASN LEU GLU ILE LEU LEU GLN LYS TRP GLU ASN GLY GLU
SEQRES 6 B 162 CYS ALA GLN LYS LYS ILE ILE ALA GLU LYS THR LYS ILE
SEQRES 7 B 162 PRO ALA VAL PHE LYS ILE ASP ALA LEU ASN GLU ASN LYS
SEQRES 8 B 162 VAL LEU VAL LEU ASP THR ASP TYR LYS LYS TYR LEU LEU
SEQRES 9 B 162 PHE CYS MET GLU ASN SER ALA GLU PRO GLU GLN SER LEU
SEQRES 10 B 162 ALA CYS GLN CYS LEU VAL ARG THR PRO GLU VAL ASP ASN
SEQRES 11 B 162 GLU ALA LEU GLU LYS PHE ASP LYS ALA LEU LYS ALA LEU
SEQRES 12 B 162 PRO MET HIS ILE ARG LEU ALA PHE ASN PRO THR GLN LEU
SEQRES 13 B 162 GLU GLY GLN CYS HIS VAL
HET SO4 A 201 5
HET SO4 B 201 5
HET SO4 B 202 5
HET SO4 B 203 5
HET SO4 B 204 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 5(O4 S 2-)
FORMUL 8 HOH *386(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 GLU A 112 SER A 116 5 5
HELIX 4 4 ASP A 129 LYS A 141 1 13
HELIX 5 5 ASN A 152 GLU A 157 1 6
HELIX 6 6 ASP B 11 ALA B 16 5 6
HELIX 7 7 ASP B 28 LEU B 32 5 5
HELIX 8 8 GLU B 112 SER B 116 5 5
HELIX 9 9 ASP B 129 LEU B 140 1 12
HELIX 10 10 ASN B 152 GLN B 159 1 8
SHEET 1 A20 GLY A 17 THR A 18 0
SHEET 2 A20 TYR A 42 PRO A 48 -1 O LEU A 46 N GLY A 17
SHEET 3 A20 LEU A 54 GLU A 62 -1 O GLN A 59 N TYR A 42
SHEET 4 A20 GLU A 65 LYS A 75 -1 O LYS A 69 N LEU A 58
SHEET 5 A20 VAL A 81 ASP A 85 -1 O LYS A 83 N GLU A 74
SHEET 6 A20 GLU A 89 THR A 97 -1 O VAL A 92 N PHE A 82
SHEET 7 A20 TYR A 102 GLU A 108 -1 O LEU A 104 N ASP A 96
SHEET 8 A20 ALA A 118 VAL A 123 -1 O LEU A 122 N LEU A 103
SHEET 9 A20 TYR A 20 ALA A 26 -1 N ALA A 25 O CYS A 119
SHEET 10 A20 ILE A 147 ALA A 150 -1 O LEU A 149 N MET A 24
SHEET 11 A20 ILE B 147 ALA B 150 -1 O ARG B 148 N ARG A 148
SHEET 12 A20 TYR B 20 ALA B 26 -1 N MET B 24 O LEU B 149
SHEET 13 A20 ALA B 118 VAL B 123 -1 O CYS B 119 N ALA B 25
SHEET 14 A20 TYR B 102 GLU B 108 -1 N LEU B 103 O LEU B 122
SHEET 15 A20 GLU B 89 THR B 97 -1 N ASP B 96 O LEU B 104
SHEET 16 A20 VAL B 81 ASP B 85 -1 N PHE B 82 O VAL B 92
SHEET 17 A20 GLU B 65 LYS B 75 -1 N GLU B 74 O LYS B 83
SHEET 18 A20 LEU B 54 GLU B 62 -1 N LEU B 54 O ALA B 73
SHEET 19 A20 TYR B 42 PRO B 48 -1 N GLU B 44 O LEU B 57
SHEET 20 A20 GLY B 17 THR B 18 -1 N GLY B 17 O LEU B 46
SSBOND 1 CYS A 66 CYS A 160 1555 1555 2.02
SSBOND 2 CYS A 106 CYS A 119 1555 1555 2.06
SSBOND 3 CYS B 66 CYS B 160 1555 1555 2.04
SSBOND 4 CYS B 106 CYS B 119 1555 1555 2.03
SITE 1 AC1 7 LYS A 69 ALA A 86 LEU A 87 HOH A 431
SITE 2 AC1 7 HOH A 432 HOH A 433 HOH A 434
SITE 1 AC2 6 THR B 76 LYS B 77 LYS B 83 HOH B 361
SITE 2 AC2 6 HOH B 421 HOH B 422
SITE 1 AC3 9 LYS A 77 GLN A 155 ASP B 28 ILE B 29
SITE 2 AC3 9 SER B 30 HOH B 322 HOH B 417 HOH B 418
SITE 3 AC3 9 HOH B 466
SITE 1 AC4 6 THR B 49 PRO B 50 GLU B 51 ASN B 53
SITE 2 AC4 6 HOH B 419 HOH B 420
SITE 1 AC5 7 HOH A 370 HOH A 383 LYS B 69 ALA B 86
SITE 2 AC5 7 LEU B 87 HOH B 414 HOH B 416
CRYST1 36.180 47.540 50.240 70.40 76.56 72.10 P 1 2
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 0.027638 -0.008929 -0.004233 0.00000
SCALE2 0.000000 0.022106 -0.006579 0.00000
SCALE3 0.000000 0.000000 0.021353 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
