HEADER IMMUNE SYSTEM 01-FEB-11 3QKG
TITLE CRYSTAL STRUCTURE OF ALPHA-1-MICROGLOBULIN AT 2.3 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN AMBP;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIPOCALIN;
COMPND 5 SYNONYM: ALPHA-1-MICROGLOBULIN, PROTEIN HC, ALPHA-1
COMPND 6 MICROGLYCOPROTEIN, COMPLEX-FORMING GLYCOPROTEIN HETEROGENEOUS IN
COMPND 7 CHARGE, INTER-ALPHA-TRYPSIN INHIBITOR LIGHT CHAIN, ITI-LC, BIKUNIN,
COMPND 8 EDC1, HI-30, URONIC-ACID-RICH PROTEIN, TRYPSTATIN;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: AMBP, HCP, ITIL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K-12;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PA1M2
KEYWDS BETA BARREL, BINDING PROTEIN, BOUND CHROMOPHORE, HUMAN PLASMA, IMMUNE
KEYWDS 2 SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR W.MEINING,A.SKERRA
REVDAT 4 08-NOV-17 3QKG 1 REMARK
REVDAT 3 19-JUN-13 3QKG 1 JRNL
REVDAT 2 20-JUN-12 3QKG 1 JRNL
REVDAT 1 08-FEB-12 3QKG 0
JRNL AUTH W.MEINING,A.SKERRA
JRNL TITL THE CRYSTAL STRUCTURE OF HUMAN ALPHA(1)-MICROGLOBULIN
JRNL TITL 2 REVEALS A POTENTIAL HAEM-BINDING SITE.
JRNL REF BIOCHEM.J. V. 445 175 2012
JRNL REFN ISSN 0264-6021
JRNL PMID 22512701
JRNL DOI 10.1042/BJ20120448
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 9044
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 452
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 655
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.3400
REMARK 3 BIN FREE R VALUE SET COUNT : 31
REMARK 3 BIN FREE R VALUE : 0.4850
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1317
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 7
REMARK 3 SOLVENT ATOMS : 47
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.94
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.35000
REMARK 3 B22 (A**2) : -2.35000
REMARK 3 B33 (A**2) : 3.52000
REMARK 3 B12 (A**2) : -1.17000
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): 0.309
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.237
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.224
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.515
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1353 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1829 ; 1.703 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 163 ; 7.447 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 62 ;36.585 ;23.548
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 237 ;20.913 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;24.331 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 199 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1011 ; 0.008 ; 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): 812 ; 0.896 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1316 ; 1.674 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 541 ; 2.708 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 513 ; 4.428 ; 4.500
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 : 3
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 8 A 34
REMARK 3 ORIGIN FOR THE GROUP (A): -18.1030 16.9850 -1.2880
REMARK 3 T TENSOR
REMARK 3 T11: 0.5226 T22: 0.3116
REMARK 3 T33: 0.0604 T12: -0.0737
REMARK 3 T13: -0.0008 T23: 0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 6.7347 L22: 6.0569
REMARK 3 L33: 6.7829 L12: 2.4013
REMARK 3 L13: -0.7132 L23: 1.1743
REMARK 3 S TENSOR
REMARK 3 S11: -0.4377 S12: 0.2940 S13: -0.2103
REMARK 3 S21: 0.1032 S22: 0.2054 S23: -0.0532
REMARK 3 S31: 0.2347 S32: 0.3580 S33: 0.2323
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 35 A 79
REMARK 3 ORIGIN FOR THE GROUP (A): -15.8210 12.5320 12.0420
REMARK 3 T TENSOR
REMARK 3 T11: 1.6242 T22: 0.9307
REMARK 3 T33: 0.4704 T12: -0.0650
REMARK 3 T13: -0.0420 T23: 0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 1.3449 L22: 4.0462
REMARK 3 L33: 5.0214 L12: 2.5567
REMARK 3 L13: 6.5378 L23: -6.0837
REMARK 3 S TENSOR
REMARK 3 S11: -0.0763 S12: -0.5462 S13: -0.3688
REMARK 3 S21: 1.3359 S22: -0.0883 S23: -0.1471
REMARK 3 S31: 0.0993 S32: 0.3715 S33: 0.1646
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 80 A 171
REMARK 3 ORIGIN FOR THE GROUP (A): -22.4660 15.2970 4.0240
REMARK 3 T TENSOR
REMARK 3 T11: 0.5163 T22: 0.4512
REMARK 3 T33: 0.0725 T12: -0.0848
REMARK 3 T13: -0.0110 T23: 0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 2.3128 L22: 6.0564
REMARK 3 L33: 2.1614 L12: 2.9719
REMARK 3 L13: -1.1821 L23: -0.8751
REMARK 3 S TENSOR
REMARK 3 S11: 0.0077 S12: -0.1102 S13: 0.0179
REMARK 3 S21: 0.3647 S22: 0.0516 S23: -0.0337
REMARK 3 S31: -0.0595 S32: 0.1959 S33: -0.0593
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3QKG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063757.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 105
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : SI-111 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10877
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.170
REMARK 200 RESOLUTION RANGE LOW (A) : 46.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 10.40
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 1.38000
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: MRBUMP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.06
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL, 1.1 M SODIUM CITRATE,
REMARK 280 PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 53.50333
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 26.75167
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 26.75167
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 53.50333
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 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 GLY A 1
REMARK 465 PRO A 2
REMARK 465 VAL A 3
REMARK 465 PRO A 4
REMARK 465 THR A 5
REMARK 465 PRO A 6
REMARK 465 PRO A 7
REMARK 465 GLY A 172
REMARK 465 GLU A 173
REMARK 465 GLN A 174
REMARK 465 GLU A 175
REMARK 465 PRO A 176
REMARK 465 GLU A 177
REMARK 465 PRO A 178
REMARK 465 ILE A 179
REMARK 465 LEU A 180
REMARK 465 ILE A 181
REMARK 465 PRO A 182
REMARK 465 ARG A 183
REMARK 465 SER A 184
REMARK 465 ALA A 185
REMARK 465 TRP A 186
REMARK 465 SER A 187
REMARK 465 HIS A 188
REMARK 465 PRO A 189
REMARK 465 GLN A 190
REMARK 465 PHE A 191
REMARK 465 GLU A 192
REMARK 465 LYS A 193
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 OE2 GLU A 110 NH1 ARG A 139 1.97
REMARK 500 N SER A 159 O HOH A 241 2.01
REMARK 500 O PRO A 156 O ASP A 158 2.12
REMARK 500 O HOH A 196 O HOH A 198 2.15
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 ARG A 43 2.28 -53.40
REMARK 500 LYS A 69 -124.92 54.72
REMARK 500 THR A 82 -164.16 -123.61
REMARK 500 ASN A 96 33.08 72.19
REMARK 500 TYR A 108 -45.60 73.00
REMARK 500 GLU A 110 -48.24 -137.87
REMARK 500 LEU A 138 -97.52 -74.19
REMARK 500 ARG A 139 100.83 110.67
REMARK 500 ASP A 158 174.40 -58.64
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 NI A 194 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 199 O
REMARK 620 2 HIS A 122 NE2 92.8
REMARK 620 3 HOH A 196 O 178.5 87.6
REMARK 620 4 HOH A 198 O 124.1 95.2 57.3
REMARK 620 5 HOH A 197 O 107.6 159.1 72.2 69.6
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 NI A 194
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 195
DBREF 3QKG A 1 183 UNP P02760 AMBP_HUMAN 20 202
SEQADV 3QKG SER A 34 UNP P02760 CYS 53 ENGINEERED MUTATION
SEQADV 3QKG SER A 184 UNP P02760 EXPRESSION TAG
SEQADV 3QKG ALA A 185 UNP P02760 EXPRESSION TAG
SEQADV 3QKG TRP A 186 UNP P02760 EXPRESSION TAG
SEQADV 3QKG SER A 187 UNP P02760 EXPRESSION TAG
SEQADV 3QKG HIS A 188 UNP P02760 EXPRESSION TAG
SEQADV 3QKG PRO A 189 UNP P02760 EXPRESSION TAG
SEQADV 3QKG GLN A 190 UNP P02760 EXPRESSION TAG
SEQADV 3QKG PHE A 191 UNP P02760 EXPRESSION TAG
SEQADV 3QKG GLU A 192 UNP P02760 EXPRESSION TAG
SEQADV 3QKG LYS A 193 UNP P02760 EXPRESSION TAG
SEQRES 1 A 193 GLY PRO VAL PRO THR PRO PRO ASP ASN ILE GLN VAL GLN
SEQRES 2 A 193 GLU ASN PHE ASN ILE SER ARG ILE TYR GLY LYS TRP TYR
SEQRES 3 A 193 ASN LEU ALA ILE GLY SER THR SER PRO TRP LEU LYS LYS
SEQRES 4 A 193 ILE MET ASP ARG MET THR VAL SER THR LEU VAL LEU GLY
SEQRES 5 A 193 GLU GLY ALA THR GLU ALA GLU ILE SER MET THR SER THR
SEQRES 6 A 193 ARG TRP ARG LYS GLY VAL CYS GLU GLU THR SER GLY ALA
SEQRES 7 A 193 TYR GLU LYS THR ASP THR ASP GLY LYS PHE LEU TYR HIS
SEQRES 8 A 193 LYS SER LYS TRP ASN ILE THR MET GLU SER TYR VAL VAL
SEQRES 9 A 193 HIS THR ASN TYR ASP GLU TYR ALA ILE PHE LEU THR LYS
SEQRES 10 A 193 LYS PHE SER ARG HIS HIS GLY PRO THR ILE THR ALA LYS
SEQRES 11 A 193 LEU TYR GLY ARG ALA PRO GLN LEU ARG GLU THR LEU LEU
SEQRES 12 A 193 GLN ASP PHE ARG VAL VAL ALA GLN GLY VAL GLY ILE PRO
SEQRES 13 A 193 GLU ASP SER ILE PHE THR MET ALA ASP ARG GLY GLU CYS
SEQRES 14 A 193 VAL PRO GLY GLU GLN GLU PRO GLU PRO ILE LEU ILE PRO
SEQRES 15 A 193 ARG SER ALA TRP SER HIS PRO GLN PHE GLU LYS
HET NI A 194 1
HET GOL A 195 6
HETNAM NI NICKEL (II) ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 NI NI 2+
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *47(H2 O)
HELIX 1 1 ASN A 17 TYR A 22 5 6
HELIX 2 2 SER A 34 MET A 41 1 8
HELIX 3 3 ARG A 139 VAL A 153 1 15
SHEET 1 A10 ILE A 160 THR A 162 0
SHEET 2 A10 GLY A 23 SER A 32 -1 N ILE A 30 O PHE A 161
SHEET 3 A10 THR A 126 GLY A 133 -1 O GLY A 133 N TYR A 26
SHEET 4 A10 TYR A 111 LYS A 118 -1 N THR A 116 O THR A 128
SHEET 5 A10 ILE A 97 THR A 106 -1 N GLU A 100 O LYS A 117
SHEET 6 A10 LYS A 87 LYS A 92 -1 N LYS A 92 O ILE A 97
SHEET 7 A10 CYS A 72 LYS A 81 -1 N GLU A 80 O LEU A 89
SHEET 8 A10 GLU A 59 TRP A 67 -1 N SER A 64 O THR A 75
SHEET 9 A10 SER A 47 GLU A 53 -1 N VAL A 50 O THR A 63
SHEET 10 A10 GLY A 23 SER A 32 -1 N ASN A 27 O SER A 47
SSBOND 1 CYS A 72 CYS A 169 1555 1555 2.05
LINK NI NI A 194 O HOH A 199 1555 1555 1.73
LINK NE2 HIS A 122 NI NI A 194 1555 1555 1.94
LINK NI NI A 194 O HOH A 196 1555 1555 2.24
LINK NI NI A 194 O HOH A 198 1555 1555 2.25
LINK NI NI A 194 O HOH A 197 1555 1555 2.26
SITE 1 AC1 6 HIS A 122 HIS A 123 HOH A 196 HOH A 197
SITE 2 AC1 6 HOH A 198 HOH A 199
SITE 1 AC2 6 TRP A 67 GLY A 70 CYS A 72 VAL A 170
SITE 2 AC2 6 PRO A 171 HOH A 220
CRYST1 66.721 66.721 80.255 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 0.014988 0.008653 0.000000 0.00000
SCALE2 0.000000 0.017306 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012460 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
