HEADER TRANSPORT PROTEIN 02-MAR-16 5IJF
TITLE CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN IN THE PRESENCE OF 0.5 MM
TITLE 2 ZINC AT PH 9.0
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERUM ALBUMIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 25-609
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: BLOOD
KEYWDS STRUCTURAL GENOMICS, PSI-BIOLOGY, NEW YORK STRUCTURAL GENOMICS
KEYWDS 2 RESEARCH CONSORTIUM, NYSGRC, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.B.HANDING,I.G.SHABALIN,D.R.COOPER,M.GRABOWSKI,S.C.ALMO,W.MINOR,NEW
AUTHOR 2 YORK STRUCTURAL GENOMICS RESEARCH CONSORTIUM (NYSGRC)
REVDAT 7 27-SEP-23 5IJF 1 REMARK
REVDAT 6 13-APR-22 5IJF 1 AUTHOR JRNL
REVDAT 5 23-MAR-22 5IJF 1 REMARK
REVDAT 4 31-OCT-18 5IJF 1 COMPND SOURCE
REVDAT 3 13-DEC-17 5IJF 1 JRNL
REVDAT 2 20-SEP-17 5IJF 1 REMARK
REVDAT 1 16-MAR-16 5IJF 0
JRNL AUTH K.B.HANDING,I.G.SHABALIN,O.KASSAAR,S.KHAZAIPOUL,
JRNL AUTH 2 C.A.BLINDAUER,A.J.STEWART,M.CHRUSZCZ,W.MINOR
JRNL TITL CIRCULATORY ZINC TRANSPORT IS CONTROLLED BY DISTINCT
JRNL TITL 2 INTERDOMAIN SITES ON MAMMALIAN ALBUMINS.
JRNL REF CHEM SCI V. 7 6635 2016
JRNL REFN ISSN 2041-6520
JRNL PMID 28567254
JRNL DOI 10.1039/C6SC02267G
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 18566
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 949
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) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1252
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.74
REMARK 3 BIN R VALUE (WORKING SET) : 0.3850
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.4870
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4279
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 40
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 105.0
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.76000
REMARK 3 B22 (A**2) : 14.13000
REMARK 3 B33 (A**2) : -6.37000
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): 1.073
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.383
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.438
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 49.517
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4391 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3952 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5974 ; 1.160 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9055 ; 0.906 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 570 ; 5.226 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 189 ;37.351 ;24.392
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 669 ;14.798 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;15.653 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 683 ; 0.058 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5051 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 985 ; 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): 2286 ; 8.238 ; 5.060
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2285 ; 8.232 ; 5.060
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2854 ;11.491 ; 7.603
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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 : 6
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 3 A 115
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0670 9.3980 -19.4720
REMARK 3 T TENSOR
REMARK 3 T11: 0.6938 T22: 0.4093
REMARK 3 T33: 0.4676 T12: 0.3174
REMARK 3 T13: 0.1549 T23: 0.2178
REMARK 3 L TENSOR
REMARK 3 L11: 7.2169 L22: 1.3922
REMARK 3 L33: 5.9885 L12: 0.4079
REMARK 3 L13: -0.2883 L23: 0.7859
REMARK 3 S TENSOR
REMARK 3 S11: -0.3026 S12: -0.1742 S13: -0.1889
REMARK 3 S21: -0.4007 S22: -0.1314 S23: 0.1264
REMARK 3 S31: 0.7007 S32: 1.3185 S33: 0.4341
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 116 A 185
REMARK 3 ORIGIN FOR THE GROUP (A): -8.1190 7.8840 -22.5140
REMARK 3 T TENSOR
REMARK 3 T11: 0.5991 T22: 0.2052
REMARK 3 T33: 0.6720 T12: -0.1173
REMARK 3 T13: 0.1691 T23: -0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 5.6860 L22: 1.2495
REMARK 3 L33: 7.9448 L12: 1.3591
REMARK 3 L13: 0.1191 L23: 2.7365
REMARK 3 S TENSOR
REMARK 3 S11: -0.5985 S12: 0.3127 S13: -0.8843
REMARK 3 S21: 0.2094 S22: -0.2627 S23: 0.1091
REMARK 3 S31: 1.0294 S32: -1.0044 S33: 0.8612
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 186 A 385
REMARK 3 ORIGIN FOR THE GROUP (A): 0.0250 24.3610 6.0820
REMARK 3 T TENSOR
REMARK 3 T11: 0.4178 T22: 0.2737
REMARK 3 T33: 0.4674 T12: 0.0438
REMARK 3 T13: 0.1209 T23: 0.0600
REMARK 3 L TENSOR
REMARK 3 L11: 2.4859 L22: 3.4115
REMARK 3 L33: 5.5914 L12: -0.6513
REMARK 3 L13: -1.9784 L23: 0.4684
REMARK 3 S TENSOR
REMARK 3 S11: 0.0012 S12: -0.7277 S13: 0.0014
REMARK 3 S21: 0.4705 S22: -0.0438 S23: 0.3368
REMARK 3 S31: -0.1594 S32: 0.3197 S33: 0.0427
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 386 A 445
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5480 37.0140 -14.2490
REMARK 3 T TENSOR
REMARK 3 T11: 0.3863 T22: 0.5113
REMARK 3 T33: 0.5072 T12: 0.1305
REMARK 3 T13: 0.0327 T23: -0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 9.5816 L22: 3.0765
REMARK 3 L33: 6.5146 L12: -0.8244
REMARK 3 L13: -0.2746 L23: -4.0961
REMARK 3 S TENSOR
REMARK 3 S11: 0.3638 S12: -0.3946 S13: 0.0793
REMARK 3 S21: 0.0970 S22: 0.5721 S23: 0.5925
REMARK 3 S31: -0.2461 S32: -0.7721 S33: -0.9360
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 446 A 499
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4000 39.4910 -12.3940
REMARK 3 T TENSOR
REMARK 3 T11: 0.5928 T22: 0.2610
REMARK 3 T33: 0.6140 T12: 0.0151
REMARK 3 T13: 0.0692 T23: -0.1033
REMARK 3 L TENSOR
REMARK 3 L11: 6.6211 L22: 5.8589
REMARK 3 L33: 5.9478 L12: -1.6108
REMARK 3 L13: 0.8781 L23: -4.9360
REMARK 3 S TENSOR
REMARK 3 S11: 0.4635 S12: 0.7381 S13: 0.9358
REMARK 3 S21: 0.1246 S22: -0.5651 S23: -0.3146
REMARK 3 S31: -0.6491 S32: 0.4780 S33: 0.1015
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 500 A 582
REMARK 3 ORIGIN FOR THE GROUP (A): -16.2360 40.6080 -35.0400
REMARK 3 T TENSOR
REMARK 3 T11: 0.4082 T22: 0.5792
REMARK 3 T33: 0.5855 T12: 0.2982
REMARK 3 T13: -0.0936 T23: -0.3021
REMARK 3 L TENSOR
REMARK 3 L11: 8.9155 L22: 1.4016
REMARK 3 L33: 6.8387 L12: 3.3863
REMARK 3 L13: 3.0155 L23: 0.7405
REMARK 3 S TENSOR
REMARK 3 S11: 0.2748 S12: 0.5325 S13: 1.1640
REMARK 3 S21: 0.0174 S22: -0.0170 S23: 0.6428
REMARK 3 S31: -0.1674 S32: 0.1998 S33: -0.2578
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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: U VALUES : WITH TLS ADDED HYDROGENS
REMARK 3 HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 5IJF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000218913.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-MAR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : DIAMOND [111]
REMARK 200 OPTICS : BERYLLIUM LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19741
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.81800
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: MOLREP
REMARK 200 STARTING MODEL: 1AO6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 UL OF 90 MG/ML PROTEIN IN 20 MM
REMARK 280 K2HPO4 PH 7.5 BUFFER WAS MIXED WITH 0.2 UL OF THE WELL CONDITION
REMARK 280 (0.1 M MMT BUFFER PH 9.0, 23 % PEG 1500, 1 MM ZNCL2) AND
REMARK 280 EQUILIBRATED AGAINST WELL SOLUTION IN 96 WELL 3 DROP
REMARK 280 CRYSTALLIZATION PLATE (SWISSCI), VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.01800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.01800
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 39.30700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 60.78000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.30700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 60.78000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.01800
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.30700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 60.78000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.01800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.30700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 60.78000
REMARK 290 SMTRY3 8 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 ASP A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 78
REMARK 465 THR A 79
REMARK 465 LEU A 80
REMARK 465 ARG A 81
REMARK 465 GLU A 82
REMARK 465 THR A 83
REMARK 465 TYR A 84
REMARK 465 GLY A 85
REMARK 465 LEU A 583
REMARK 465 GLY A 584
REMARK 465 LEU A 585
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 HIS A 3 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 4 CG CD CE NZ
REMARK 470 SER A 5 OG
REMARK 470 HIS A 9 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 12 CG CD CE NZ
REMARK 470 GLU A 17 CG CD OE1 OE2
REMARK 470 LYS A 20 CD CE NZ
REMARK 470 GLU A 48 CG CD OE1 OE2
REMARK 470 SER A 58 OG
REMARK 470 GLU A 60 CG CD OE1 OE2
REMARK 470 ASP A 63 CG OD1 OD2
REMARK 470 LYS A 64 CG CD CE NZ
REMARK 470 LEU A 69 CG CD1 CD2
REMARK 470 VAL A 77 CG1 CG2
REMARK 470 GLU A 86 CG CD OE1 OE2
REMARK 470 MET A 87 CG SD CE
REMARK 470 GLU A 119 CG CD OE1 OE2
REMARK 470 ASP A 121 CG OD1 OD2
REMARK 470 ASP A 129 CG OD1 OD2
REMARK 470 LYS A 136 CE NZ
REMARK 470 LYS A 205 CE NZ
REMARK 470 LYS A 225 CG CD CE NZ
REMARK 470 LYS A 262 CG CD CE NZ
REMARK 470 LYS A 276 CG CD CE NZ
REMARK 470 GLU A 277 CG CD OE1 OE2
REMARK 470 LEU A 283 CG CD1 CD2
REMARK 470 SER A 312 OG
REMARK 470 LYS A 313 CG CD CE NZ
REMARK 470 ASP A 314 CG OD1 OD2
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 GLU A 321 CG CD OE1 OE2
REMARK 470 LYS A 323 CG CD CE NZ
REMARK 470 VAL A 325 CG1 CG2
REMARK 470 LYS A 351 CG CD CE NZ
REMARK 470 LYS A 359 CG CD CE NZ
REMARK 470 ASP A 365 CG OD1 OD2
REMARK 470 GLU A 368 CG CD OE1 OE2
REMARK 470 TYR A 370 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 372 CE NZ
REMARK 470 VAL A 373 CG1 CG2
REMARK 470 GLU A 376 CG CD OE1 OE2
REMARK 470 LYS A 378 CG CD CE NZ
REMARK 470 GLU A 382 CG CD OE1 OE2
REMARK 470 LEU A 387 CG CD1 CD2
REMARK 470 LYS A 389 CG CD CE NZ
REMARK 470 GLU A 396 CG CD OE1 OE2
REMARK 470 LYS A 439 CG CD CE NZ
REMARK 470 LYS A 444 CG CD CE NZ
REMARK 470 GLU A 465 CG CD OE1 OE2
REMARK 470 LYS A 466 CG CD CE NZ
REMARK 470 LYS A 475 CG CD CE NZ
REMARK 470 VAL A 493 CG1 CG2
REMARK 470 VAL A 498 CG1 CG2
REMARK 470 LYS A 500 CG CD CE NZ
REMARK 470 GLU A 505 CG CD OE1 OE2
REMARK 470 THR A 508 OG1 CG2
REMARK 470 ASP A 512 CG OD1 OD2
REMARK 470 ILE A 513 CG1 CG2 CD1
REMARK 470 SER A 517 OG
REMARK 470 GLU A 520 CG CD OE1 OE2
REMARK 470 ARG A 521 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 524 CG CD CE NZ
REMARK 470 LYS A 525 CG CD CE NZ
REMARK 470 LYS A 541 CG CD CE NZ
REMARK 470 GLU A 542 CG CD OE1 OE2
REMARK 470 LYS A 545 CG CD CE NZ
REMARK 470 ASP A 550 CG OD1 OD2
REMARK 470 GLU A 556 CG CD OE1 OE2
REMARK 470 LYS A 557 CG CD CE NZ
REMARK 470 LYS A 560 CG CD CE NZ
REMARK 470 ASP A 563 CG OD1 OD2
REMARK 470 GLU A 565 CG CD OE1 OE2
REMARK 470 GLU A 570 CG CD OE1 OE2
REMARK 470 GLU A 571 CG CD OE1 OE2
REMARK 470 LYS A 573 CG CD CE NZ
REMARK 470 LYS A 574 CG CD CE NZ
REMARK 470 LEU A 575 CG CD1 CD2
REMARK 470 VAL A 576 CG1 CG2
REMARK 470 GLN A 580 CG CD OE1 NE2
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 ASN A 61 -7.85 75.76
REMARK 500 PRO A 118 -178.34 -62.78
REMARK 500 ILE A 271 -61.11 -106.98
REMARK 500 GLU A 280 44.37 -106.67
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 601 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 67 NE2
REMARK 620 2 HIS A 247 ND1 120.1
REMARK 620 3 ASP A 249 OD1 76.9 157.5
REMARK 620 4 ASP A 249 OD2 121.1 101.3 56.2
REMARK 620 5 HOH A 717 O 102.3 95.4 94.9 114.1
REMARK 620 N 1 2 3 4
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 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5IIH RELATED DB: PDB
REMARK 900 RELATED ID: 5HOZ RELATED DB: PDB
REMARK 900 RELATED ID: 5IIU RELATED DB: PDB
REMARK 900 RELATED ID: 5IIX RELATED DB: PDB
REMARK 900 RELATED ID: 5IJ5 RELATED DB: PDB
REMARK 900 RELATED ID: 5IJE RELATED DB: PDB
DBREF 5IJF A 1 585 UNP P02768 ALBU_HUMAN 25 609
SEQRES 1 A 585 ASP ALA HIS LYS SER GLU VAL ALA HIS ARG PHE LYS ASP
SEQRES 2 A 585 LEU GLY GLU GLU ASN PHE LYS ALA LEU VAL LEU ILE ALA
SEQRES 3 A 585 PHE ALA GLN TYR LEU GLN GLN CYS PRO PHE GLU ASP HIS
SEQRES 4 A 585 VAL LYS LEU VAL ASN GLU VAL THR GLU PHE ALA LYS THR
SEQRES 5 A 585 CYS VAL ALA ASP GLU SER ALA GLU ASN CYS ASP LYS SER
SEQRES 6 A 585 LEU HIS THR LEU PHE GLY ASP LYS LEU CYS THR VAL ALA
SEQRES 7 A 585 THR LEU ARG GLU THR TYR GLY GLU MET ALA ASP CYS CYS
SEQRES 8 A 585 ALA LYS GLN GLU PRO GLU ARG ASN GLU CYS PHE LEU GLN
SEQRES 9 A 585 HIS LYS ASP ASP ASN PRO ASN LEU PRO ARG LEU VAL ARG
SEQRES 10 A 585 PRO GLU VAL ASP VAL MET CYS THR ALA PHE HIS ASP ASN
SEQRES 11 A 585 GLU GLU THR PHE LEU LYS LYS TYR LEU TYR GLU ILE ALA
SEQRES 12 A 585 ARG ARG HIS PRO TYR PHE TYR ALA PRO GLU LEU LEU PHE
SEQRES 13 A 585 PHE ALA LYS ARG TYR LYS ALA ALA PHE THR GLU CYS CYS
SEQRES 14 A 585 GLN ALA ALA ASP LYS ALA ALA CYS LEU LEU PRO LYS LEU
SEQRES 15 A 585 ASP GLU LEU ARG ASP GLU GLY LYS ALA SER SER ALA LYS
SEQRES 16 A 585 GLN ARG LEU LYS CYS ALA SER LEU GLN LYS PHE GLY GLU
SEQRES 17 A 585 ARG ALA PHE LYS ALA TRP ALA VAL ALA ARG LEU SER GLN
SEQRES 18 A 585 ARG PHE PRO LYS ALA GLU PHE ALA GLU VAL SER LYS LEU
SEQRES 19 A 585 VAL THR ASP LEU THR LYS VAL HIS THR GLU CYS CYS HIS
SEQRES 20 A 585 GLY ASP LEU LEU GLU CYS ALA ASP ASP ARG ALA ASP LEU
SEQRES 21 A 585 ALA LYS TYR ILE CYS GLU ASN GLN ASP SER ILE SER SER
SEQRES 22 A 585 LYS LEU LYS GLU CYS CYS GLU LYS PRO LEU LEU GLU LYS
SEQRES 23 A 585 SER HIS CYS ILE ALA GLU VAL GLU ASN ASP GLU MET PRO
SEQRES 24 A 585 ALA ASP LEU PRO SER LEU ALA ALA ASP PHE VAL GLU SER
SEQRES 25 A 585 LYS ASP VAL CYS LYS ASN TYR ALA GLU ALA LYS ASP VAL
SEQRES 26 A 585 PHE LEU GLY MET PHE LEU TYR GLU TYR ALA ARG ARG HIS
SEQRES 27 A 585 PRO ASP TYR SER VAL VAL LEU LEU LEU ARG LEU ALA LYS
SEQRES 28 A 585 THR TYR GLU THR THR LEU GLU LYS CYS CYS ALA ALA ALA
SEQRES 29 A 585 ASP PRO HIS GLU CYS TYR ALA LYS VAL PHE ASP GLU PHE
SEQRES 30 A 585 LYS PRO LEU VAL GLU GLU PRO GLN ASN LEU ILE LYS GLN
SEQRES 31 A 585 ASN CYS GLU LEU PHE GLU GLN LEU GLY GLU TYR LYS PHE
SEQRES 32 A 585 GLN ASN ALA LEU LEU VAL ARG TYR THR LYS LYS VAL PRO
SEQRES 33 A 585 GLN VAL SER THR PRO THR LEU VAL GLU VAL SER ARG ASN
SEQRES 34 A 585 LEU GLY LYS VAL GLY SER LYS CYS CYS LYS HIS PRO GLU
SEQRES 35 A 585 ALA LYS ARG MET PRO CYS ALA GLU ASP TYR LEU SER VAL
SEQRES 36 A 585 VAL LEU ASN GLN LEU CYS VAL LEU HIS GLU LYS THR PRO
SEQRES 37 A 585 VAL SER ASP ARG VAL THR LYS CYS CYS THR GLU SER LEU
SEQRES 38 A 585 VAL ASN ARG ARG PRO CYS PHE SER ALA LEU GLU VAL ASP
SEQRES 39 A 585 GLU THR TYR VAL PRO LYS GLU PHE ASN ALA GLU THR PHE
SEQRES 40 A 585 THR PHE HIS ALA ASP ILE CYS THR LEU SER GLU LYS GLU
SEQRES 41 A 585 ARG GLN ILE LYS LYS GLN THR ALA LEU VAL GLU LEU VAL
SEQRES 42 A 585 LYS HIS LYS PRO LYS ALA THR LYS GLU GLN LEU LYS ALA
SEQRES 43 A 585 VAL MET ASP ASP PHE ALA ALA PHE VAL GLU LYS CYS CYS
SEQRES 44 A 585 LYS ALA ASP ASP LYS GLU THR CYS PHE ALA GLU GLU GLY
SEQRES 45 A 585 LYS LYS LEU VAL ALA ALA SER GLN ALA ALA LEU GLY LEU
HET ZN A 601 1
HET UNL A 602 4
HET UNL A 603 4
HETNAM ZN ZINC ION
HETNAM UNL UNKNOWN LIGAND
FORMUL 2 ZN ZN 2+
FORMUL 5 HOH *40(H2 O)
HELIX 1 AA1 SER A 5 GLY A 15 1 11
HELIX 2 AA2 GLY A 15 LEU A 31 1 17
HELIX 3 AA3 PRO A 35 ASP A 56 1 22
HELIX 4 AA4 SER A 65 CYS A 75 1 11
HELIX 5 AA5 MET A 87 CYS A 91 1 5
HELIX 6 AA6 PRO A 96 HIS A 105 1 10
HELIX 7 AA7 GLU A 119 ASN A 130 1 12
HELIX 8 AA8 ASN A 130 HIS A 146 1 17
HELIX 9 AA9 TYR A 150 CYS A 169 1 20
HELIX 10 AB1 ASP A 173 GLY A 207 1 35
HELIX 11 AB2 GLY A 207 PHE A 223 1 17
HELIX 12 AB3 GLU A 227 HIS A 247 1 21
HELIX 13 AB4 ASP A 249 ASN A 267 1 19
HELIX 14 AB5 GLU A 277 LYS A 281 5 5
HELIX 15 AB6 PRO A 282 GLU A 292 1 11
HELIX 16 AB7 LEU A 305 VAL A 310 1 6
HELIX 17 AB8 ASP A 314 ALA A 322 1 9
HELIX 18 AB9 ALA A 322 ARG A 337 1 16
HELIX 19 AC1 SER A 342 CYS A 361 1 20
HELIX 20 AC2 ASP A 365 ALA A 371 1 7
HELIX 21 AC3 LYS A 372 GLU A 376 5 5
HELIX 22 AC4 PHE A 377 GLY A 399 1 23
HELIX 23 AC5 GLY A 399 VAL A 415 1 17
HELIX 24 AC6 SER A 419 CYS A 438 1 20
HELIX 25 AC7 PRO A 441 ALA A 443 5 3
HELIX 26 AC8 LYS A 444 THR A 467 1 24
HELIX 27 AC9 SER A 470 SER A 480 1 11
HELIX 28 AD1 ASN A 483 LEU A 491 1 9
HELIX 29 AD2 ALA A 511 LEU A 516 1 6
HELIX 30 AD3 SER A 517 LYS A 536 1 20
HELIX 31 AD4 THR A 540 LYS A 560 1 21
HELIX 32 AD5 ASP A 563 ALA A 582 1 20
SSBOND 1 CYS A 53 CYS A 62 1555 1555 2.04
SSBOND 2 CYS A 75 CYS A 91 1555 1555 2.04
SSBOND 3 CYS A 90 CYS A 101 1555 1555 2.05
SSBOND 4 CYS A 124 CYS A 169 1555 1555 2.04
SSBOND 5 CYS A 168 CYS A 177 1555 1555 2.04
SSBOND 6 CYS A 200 CYS A 246 1555 1555 2.02
SSBOND 7 CYS A 245 CYS A 253 1555 1555 2.06
SSBOND 8 CYS A 265 CYS A 279 1555 1555 2.02
SSBOND 9 CYS A 278 CYS A 289 1555 1555 2.04
SSBOND 10 CYS A 316 CYS A 361 1555 1555 2.04
SSBOND 11 CYS A 360 CYS A 369 1555 1555 2.02
SSBOND 12 CYS A 392 CYS A 438 1555 1555 2.03
SSBOND 13 CYS A 437 CYS A 448 1555 1555 2.04
SSBOND 14 CYS A 461 CYS A 477 1555 1555 2.03
SSBOND 15 CYS A 476 CYS A 487 1555 1555 2.06
SSBOND 16 CYS A 514 CYS A 559 1555 1555 2.03
SSBOND 17 CYS A 558 CYS A 567 1555 1555 2.04
LINK NE2 HIS A 67 ZN ZN A 601 1555 1555 2.06
LINK ND1 HIS A 247 ZN ZN A 601 1555 1555 2.12
LINK OD1 ASP A 249 ZN ZN A 601 1555 1555 2.59
LINK OD2 ASP A 249 ZN ZN A 601 1555 1555 1.99
LINK ZN ZN A 601 O HOH A 717 1555 1555 2.00
CISPEP 1 GLU A 95 PRO A 96 0 2.17
SITE 1 AC1 4 HIS A 67 HIS A 247 ASP A 249 HOH A 717
CRYST1 78.614 121.560 140.036 90.00 90.00 90.00 C 2 2 21 8
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 0.012720 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008226 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007141 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
