HEADER IMMUNE SYSTEM 29-MAR-06 2GIT
TITLE HUMAN CLASS I MHC HLA-A2 IN COMPLEX WITH THE MODIFIED HTLV-1 TAX (Y5K-
TITLE 2 4-[3-INDOLYL]-BUTYRIC ACID) PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN;
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: HUMAN CLASS I MAJOR HISTOCOMPATIBILITY COMPLEX HEAVY CHAIN;
COMPND 5 SYNONYM: MHC CLASS I ANTIGEN A*2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 9 CHAIN: B, E;
COMPND 10 FRAGMENT: BETA-2-MICROGLOBULIN;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: TRANSCRIPTIONAL ACTIVATOR TAX;
COMPND 14 CHAIN: C, F;
COMPND 15 FRAGMENT: HTLV-1 TAX PEPTIDE;
COMPND 16 ENGINEERED: YES;
COMPND 17 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: HLA-A, HLAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHN1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: B2M;
SOURCE 16 MOL_ID: 3;
SOURCE 17 SYNTHETIC: YES;
SOURCE 18 OTHER_DETAILS: COMMERCIAL SYNTHESIS FOR THE PEPTIDE
KEYWDS HTLV-1 TAX PEPTIDE, HAPTENATED PEPTIDE, LYSINE-4-(3-INDOLYL)-BUTYRIC
KEYWDS 2 ACID, MHC CLASS I, HLA-A2, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR O.Y.BORBULEVYCH,B.M.BAKER
REVDAT 4 30-AUG-23 2GIT 1 REMARK SEQADV LINK
REVDAT 3 13-JUL-11 2GIT 1 VERSN
REVDAT 2 24-FEB-09 2GIT 1 VERSN
REVDAT 1 03-OCT-06 2GIT 0
JRNL AUTH S.J.GAGNON,O.Y.BORBULEVYCH,R.L.DAVIS-HARRISON,R.V.TURNER,
JRNL AUTH 2 M.DAMIRJIAN,A.WOJNAROWICZ,W.E.BIDDISON,B.M.BAKER
JRNL TITL T CELL RECEPTOR RECOGNITION VIA COOPERATIVE CONFORMATIONAL
JRNL TITL 2 PLASTICITY.
JRNL REF J.MOL.BIOL. V. 363 228 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16962135
JRNL DOI 10.1016/J.JMB.2006.08.045
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 3 NUMBER OF REFLECTIONS : 82640
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; 5% OF THE DATA SET
REMARK 3 R VALUE (WORKING + TEST SET) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4395
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.75
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4214
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 62.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE SET COUNT : 215
REMARK 3 BIN FREE R VALUE : 0.2800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6313
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 788
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 18.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.93000
REMARK 3 B22 (A**2) : -1.11000
REMARK 3 B33 (A**2) : -1.46000
REMARK 3 B12 (A**2) : 0.47000
REMARK 3 B13 (A**2) : 0.66000
REMARK 3 B23 (A**2) : 0.47000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.117
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.115
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.081
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.822
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6579 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8906 ; 1.729 ; 1.929
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 762 ; 6.356 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 351 ;31.237 ;23.105
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1069 ;14.733 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 57 ;19.120 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 907 ; 0.142 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5133 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2800 ; 0.155 ; 0.080
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4400 ; 0.311 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1133 ; 0.205 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.123 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 41 ; 0.109 ; 0.080
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 52 ; 0.181 ; 0.500
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): 3852 ; 0.947 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6196 ; 1.664 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2880 ; 2.771 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2710 ; 4.333 ; 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 183 A 275 4
REMARK 3 1 D 183 D 275 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 749 ; 0.26 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 749 ; 1.17 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 0 B 99 4
REMARK 3 1 E 0 E 99 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 B (A): 831 ; 0.27 ; 0.50
REMARK 3 MEDIUM THERMAL 2 B (A**2): 831 ; 0.92 ; 2.00
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 182
REMARK 3 RESIDUE RANGE : C 1 C 9
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6378 14.0647 6.8388
REMARK 3 T TENSOR
REMARK 3 T11: -0.0900 T22: -0.0677
REMARK 3 T33: -0.0548 T12: 0.0012
REMARK 3 T13: -0.0034 T23: -0.0175
REMARK 3 L TENSOR
REMARK 3 L11: 1.0881 L22: 1.4963
REMARK 3 L33: 2.2172 L12: 0.1291
REMARK 3 L13: 0.0414 L23: -0.3048
REMARK 3 S TENSOR
REMARK 3 S11: -0.0446 S12: -0.0265 S13: 0.1421
REMARK 3 S21: 0.0548 S22: -0.0073 S23: 0.0141
REMARK 3 S31: -0.1543 S32: 0.0444 S33: 0.0519
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 183 A 275
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5994 -19.4809 -6.4668
REMARK 3 T TENSOR
REMARK 3 T11: -0.0402 T22: -0.0580
REMARK 3 T33: -0.0832 T12: -0.0011
REMARK 3 T13: -0.0013 T23: -0.0073
REMARK 3 L TENSOR
REMARK 3 L11: 1.5189 L22: 3.5636
REMARK 3 L33: 2.6527 L12: -1.3713
REMARK 3 L13: -1.1394 L23: 1.6638
REMARK 3 S TENSOR
REMARK 3 S11: 0.0358 S12: 0.1195 S13: -0.0911
REMARK 3 S21: -0.2482 S22: -0.0098 S23: 0.0199
REMARK 3 S31: 0.1838 S32: 0.0587 S33: -0.0261
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 : B 0 B 99
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9662 -4.9426 -7.0060
REMARK 3 T TENSOR
REMARK 3 T11: -0.1060 T22: -0.0467
REMARK 3 T33: -0.0486 T12: -0.0005
REMARK 3 T13: 0.0050 T23: 0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 1.6738 L22: 3.5846
REMARK 3 L33: 1.4110 L12: 1.4780
REMARK 3 L13: -0.2258 L23: -0.4646
REMARK 3 S TENSOR
REMARK 3 S11: -0.0406 S12: 0.0893 S13: 0.0130
REMARK 3 S21: -0.2047 S22: 0.0789 S23: 0.2733
REMARK 3 S31: 0.0888 S32: -0.1006 S33: -0.0384
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 182
REMARK 3 RESIDUE RANGE : F 1 F 9
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9421 -13.2305 26.1622
REMARK 3 T TENSOR
REMARK 3 T11: -0.0673 T22: -0.0462
REMARK 3 T33: -0.0576 T12: -0.0091
REMARK 3 T13: 0.0105 T23: 0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 0.9011 L22: 2.0574
REMARK 3 L33: 1.8147 L12: -0.2371
REMARK 3 L13: 0.0059 L23: 0.4390
REMARK 3 S TENSOR
REMARK 3 S11: -0.0670 S12: 0.0235 S13: 0.0969
REMARK 3 S21: 0.0183 S22: 0.0262 S23: -0.0990
REMARK 3 S31: -0.1779 S32: 0.0531 S33: 0.0408
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 : D 183 D 275
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9766 -42.3493 39.1365
REMARK 3 T TENSOR
REMARK 3 T11: -0.1604 T22: -0.0570
REMARK 3 T33: -0.0639 T12: 0.0001
REMARK 3 T13: 0.0116 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 3.7964 L22: 2.1628
REMARK 3 L33: 3.0960 L12: 1.2878
REMARK 3 L13: -2.6481 L23: -0.8013
REMARK 3 S TENSOR
REMARK 3 S11: 0.0594 S12: 0.0427 S13: -0.1154
REMARK 3 S21: -0.0321 S22: -0.0619 S23: -0.0271
REMARK 3 S31: 0.0485 S32: -0.1633 S33: 0.0025
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 : E 0 E 99
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7344 -36.1067 39.7756
REMARK 3 T TENSOR
REMARK 3 T11: -0.1745 T22: -0.0491
REMARK 3 T33: -0.0730 T12: -0.0116
REMARK 3 T13: 0.0297 T23: -0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 0.8367 L22: 3.9438
REMARK 3 L33: 2.0501 L12: -0.4249
REMARK 3 L13: 0.2631 L23: 0.1678
REMARK 3 S TENSOR
REMARK 3 S11: -0.0045 S12: -0.0262 S13: -0.0614
REMARK 3 S21: 0.1151 S22: 0.0211 S23: -0.1510
REMARK 3 S31: 0.0893 S32: -0.0209 S33: -0.0166
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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: THE SIDE CHAIN OF LYI (RES 5 CHAIN C,F)
REMARK 3 IS DISORDERED AND WAS NOT MODELED.
REMARK 4
REMARK 4 2GIT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037171.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
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 : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : BLU-ICE (GM/CA)
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87035
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.08700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 66.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.23900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.130
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: PDB ENTRY 2AV1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350 24%, MES 0.025M, HCOOH 0.1M,
REMARK 280 PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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, 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6300 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 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 LYS C 5 CE NZ
REMARK 470 LYS F 5 NZ
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 VAL E 85 CB - CA - C ANGL. DEV. = -13.5 DEGREES
REMARK 500 VAL E 85 CG1 - CB - CG2 ANGL. DEV. = 11.2 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 29 -127.54 49.96
REMARK 500 SER A 195 -153.68 -138.92
REMARK 500 TRP B 60 -6.52 79.86
REMARK 500 ARG B 97 53.32 -67.50
REMARK 500 ASP B 98 2.28 -168.27
REMARK 500 ASP D 29 -126.50 51.28
REMARK 500 HIS D 114 105.31 -160.22
REMARK 500 TRP E 60 -4.09 77.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 3-INDOLYL-BUTYRIC ACID (LIGAND CODE 3IB)
REMARK 600 IS COVALENTLY BONDED TO LYS 5 IN CHAIN C
REMARK 600 AND F. COORDINATES WERE NOT INCLUDED
REMARK 600 BECAUSE THE LIGAND WAS DISORDERED.
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 NA B 816 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 83 OD1
REMARK 620 2 HIS B 84 O 75.3
REMARK 620 3 LEU B 87 O 88.2 80.0
REMARK 620 4 HOH B 882 O 174.9 99.9 89.2
REMARK 620 5 HOH B 904 O 92.4 167.0 104.3 92.6
REMARK 620 6 HOH B 923 O 82.2 76.5 156.2 98.6 97.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 816
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT E 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT E 811
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 812
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 813
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 814
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 815
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DUZ RELATED DB: PDB
REMARK 900 HTLV-1 TAX PEPTIDE BOUND TO HLA-A2
REMARK 900 RELATED ID: 2AV1 RELATED DB: PDB
REMARK 900 HTLV-1 TAX PEPTIDE BOUND TO HLA-A2 (E63Q,K66A)
REMARK 900 RELATED ID: 2AV7 RELATED DB: PDB
REMARK 900 HTLV-1 TAX PEPTIDE BOUND TO HLA-A2 (K66A)
DBREF 2GIT A 1 275 UNP Q9TQH5 1A02_HUMAN 25 299
DBREF 2GIT D 1 275 UNP Q9TQH5 1A02_HUMAN 25 299
DBREF 2GIT B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 2GIT E 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 2GIT C 1 9 PDB 2GIT 2GIT 1 9
DBREF 2GIT F 1 9 PDB 2GIT 2GIT 1 9
SEQADV 2GIT MET B 0 UNP P61769 INITIATING METHIONINE
SEQADV 2GIT MET E 0 UNP P61769 INITIATING METHIONINE
SEQRES 1 A 275 GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER
SEQRES 2 A 275 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 A 275 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 275 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 A 275 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG
SEQRES 6 A 275 LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU
SEQRES 7 A 275 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 A 275 SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY
SEQRES 9 A 275 SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA
SEQRES 10 A 275 TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU
SEQRES 11 A 275 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR
SEQRES 12 A 275 LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU
SEQRES 13 A 275 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 A 275 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 A 275 ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER
SEQRES 16 A 275 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE
SEQRES 17 A 275 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 A 275 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 A 275 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 A 275 VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS
SEQRES 21 A 275 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG
SEQRES 22 A 275 TRP GLU
SEQRES 1 B 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 B 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 B 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 B 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 B 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 B 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 B 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 B 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 C 9 LEU LEU PHE GLY LYS PRO VAL TYR VAL
SEQRES 1 D 275 GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER
SEQRES 2 D 275 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 D 275 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 D 275 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 D 275 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG
SEQRES 6 D 275 LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU
SEQRES 7 D 275 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 D 275 SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY
SEQRES 9 D 275 SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA
SEQRES 10 D 275 TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU
SEQRES 11 D 275 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR
SEQRES 12 D 275 LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU
SEQRES 13 D 275 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 D 275 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 D 275 ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER
SEQRES 16 D 275 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE
SEQRES 17 D 275 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 D 275 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 D 275 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 D 275 VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS
SEQRES 21 D 275 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG
SEQRES 22 D 275 TRP GLU
SEQRES 1 E 100 MET ILE GLN ARG THR PRO LYS ILE GLN VAL TYR SER ARG
SEQRES 2 E 100 HIS PRO ALA GLU ASN GLY LYS SER ASN PHE LEU ASN CYS
SEQRES 3 E 100 TYR VAL SER GLY PHE HIS PRO SER ASP ILE GLU VAL ASP
SEQRES 4 E 100 LEU LEU LYS ASN GLY GLU ARG ILE GLU LYS VAL GLU HIS
SEQRES 5 E 100 SER ASP LEU SER PHE SER LYS ASP TRP SER PHE TYR LEU
SEQRES 6 E 100 LEU TYR TYR THR GLU PHE THR PRO THR GLU LYS ASP GLU
SEQRES 7 E 100 TYR ALA CYS ARG VAL ASN HIS VAL THR LEU SER GLN PRO
SEQRES 8 E 100 LYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 F 9 LEU LEU PHE GLY LYS PRO VAL TYR VAL
HET GOL A 802 6
HET NA B 816 1
HET GOL B 803 6
HET FMT B 809 3
HET FMT B 810 3
HET FMT C 813 3
HET GOL D 804 6
HET GOL D 805 6
HET GOL D 806 6
HET FMT D 808 3
HET FMT D 812 3
HET FMT D 814 3
HET FMT D 815 3
HET GOL E 801 6
HET FMT E 807 3
HET FMT E 811 3
HETNAM GOL GLYCEROL
HETNAM NA SODIUM ION
HETNAM FMT FORMIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 GOL 6(C3 H8 O3)
FORMUL 8 NA NA 1+
FORMUL 10 FMT 9(C H2 O2)
FORMUL 23 HOH *788(H2 O)
HELIX 1 1 ALA A 49 GLU A 53 5 5
HELIX 2 2 GLY A 56 TYR A 85 1 30
HELIX 3 3 MET A 138 ALA A 150 1 13
HELIX 4 4 HIS A 151 GLY A 162 1 12
HELIX 5 5 GLY A 162 GLY A 175 1 14
HELIX 6 6 GLY A 175 GLN A 180 1 6
HELIX 7 7 THR A 225 THR A 228 5 4
HELIX 8 8 GLN A 253 GLN A 255 5 3
HELIX 9 9 ALA D 49 GLU D 53 5 5
HELIX 10 10 GLY D 56 TYR D 85 1 30
HELIX 11 11 ASP D 137 ALA D 150 1 14
HELIX 12 12 HIS D 151 GLY D 162 1 12
HELIX 13 13 GLY D 162 GLY D 175 1 14
HELIX 14 14 GLY D 175 GLN D 180 1 6
HELIX 15 15 THR D 225 THR D 228 5 4
HELIX 16 16 GLN D 253 GLN D 255 5 3
SHEET 1 A 8 GLU A 46 PRO A 47 0
SHEET 2 A 8 THR A 31 ASP A 37 -1 N ARG A 35 O GLU A 46
SHEET 3 A 8 ARG A 21 VAL A 28 -1 N GLY A 26 O PHE A 33
SHEET 4 A 8 HIS A 3 VAL A 12 -1 N ARG A 6 O TYR A 27
SHEET 5 A 8 THR A 94 VAL A 103 -1 O VAL A 103 N HIS A 3
SHEET 6 A 8 PHE A 109 TYR A 118 -1 O LEU A 110 N ASP A 102
SHEET 7 A 8 LYS A 121 LEU A 126 -1 O LEU A 126 N HIS A 114
SHEET 8 A 8 TRP A 133 ALA A 135 -1 O THR A 134 N ALA A 125
SHEET 1 B 4 LYS A 186 ALA A 193 0
SHEET 2 B 4 GLU A 198 PHE A 208 -1 O THR A 200 N HIS A 192
SHEET 3 B 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203
SHEET 4 B 4 GLU A 229 LEU A 230 -1 N GLU A 229 O ALA A 246
SHEET 1 C 4 LYS A 186 ALA A 193 0
SHEET 2 C 4 GLU A 198 PHE A 208 -1 O THR A 200 N HIS A 192
SHEET 3 C 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203
SHEET 4 C 4 ARG A 234 PRO A 235 -1 N ARG A 234 O GLN A 242
SHEET 1 D 4 GLU A 222 ASP A 223 0
SHEET 2 D 4 THR A 214 ARG A 219 -1 N ARG A 219 O GLU A 222
SHEET 3 D 4 TYR A 257 GLN A 262 -1 O HIS A 260 N THR A 216
SHEET 4 D 4 LEU A 270 LEU A 272 -1 O LEU A 272 N CYS A 259
SHEET 1 E 4 LYS B 6 SER B 11 0
SHEET 2 E 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 E 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25
SHEET 4 E 4 GLU B 50 HIS B 51 -1 N GLU B 50 O TYR B 67
SHEET 1 F 4 LYS B 6 SER B 11 0
SHEET 2 F 4 ASN B 21 PHE B 30 -1 O ASN B 24 N TYR B 10
SHEET 3 F 4 PHE B 62 PHE B 70 -1 O TYR B 66 N CYS B 25
SHEET 4 F 4 SER B 55 PHE B 56 -1 N SER B 55 O TYR B 63
SHEET 1 G 4 GLU B 44 ARG B 45 0
SHEET 2 G 4 GLU B 36 LYS B 41 -1 N LYS B 41 O GLU B 44
SHEET 3 G 4 TYR B 78 ASN B 83 -1 O ARG B 81 N ASP B 38
SHEET 4 G 4 LYS B 91 LYS B 94 -1 O LYS B 91 N VAL B 82
SHEET 1 H 8 GLU D 46 PRO D 47 0
SHEET 2 H 8 THR D 31 ASP D 37 -1 N ARG D 35 O GLU D 46
SHEET 3 H 8 ARG D 21 VAL D 28 -1 N GLY D 26 O PHE D 33
SHEET 4 H 8 HIS D 3 VAL D 12 -1 N ARG D 6 O TYR D 27
SHEET 5 H 8 THR D 94 VAL D 103 -1 O VAL D 103 N HIS D 3
SHEET 6 H 8 PHE D 109 TYR D 118 -1 O ARG D 111 N ASP D 102
SHEET 7 H 8 LYS D 121 LEU D 126 -1 O ILE D 124 N TYR D 116
SHEET 8 H 8 TRP D 133 ALA D 135 -1 O THR D 134 N ALA D 125
SHEET 1 I 4 LYS D 186 ALA D 193 0
SHEET 2 I 4 GLU D 198 PHE D 208 -1 O TRP D 204 N HIS D 188
SHEET 3 I 4 PHE D 241 PRO D 250 -1 O ALA D 245 N CYS D 203
SHEET 4 I 4 GLU D 229 LEU D 230 -1 N GLU D 229 O ALA D 246
SHEET 1 J 4 LYS D 186 ALA D 193 0
SHEET 2 J 4 GLU D 198 PHE D 208 -1 O TRP D 204 N HIS D 188
SHEET 3 J 4 PHE D 241 PRO D 250 -1 O ALA D 245 N CYS D 203
SHEET 4 J 4 ARG D 234 PRO D 235 -1 N ARG D 234 O GLN D 242
SHEET 1 K 4 GLU D 222 ASP D 223 0
SHEET 2 K 4 THR D 214 ARG D 219 -1 N ARG D 219 O GLU D 222
SHEET 3 K 4 TYR D 257 GLN D 262 -1 O HIS D 260 N THR D 216
SHEET 4 K 4 LEU D 270 ARG D 273 -1 O LEU D 272 N CYS D 259
SHEET 1 L 4 LYS E 6 SER E 11 0
SHEET 2 L 4 ASN E 21 PHE E 30 -1 O ASN E 24 N TYR E 10
SHEET 3 L 4 PHE E 62 PHE E 70 -1 O THR E 68 N LEU E 23
SHEET 4 L 4 GLU E 50 HIS E 51 -1 N GLU E 50 O TYR E 67
SHEET 1 M 4 LYS E 6 SER E 11 0
SHEET 2 M 4 ASN E 21 PHE E 30 -1 O ASN E 24 N TYR E 10
SHEET 3 M 4 PHE E 62 PHE E 70 -1 O THR E 68 N LEU E 23
SHEET 4 M 4 SER E 55 PHE E 56 -1 N SER E 55 O TYR E 63
SHEET 1 N 4 GLU E 44 ARG E 45 0
SHEET 2 N 4 GLU E 36 LYS E 41 -1 N LYS E 41 O GLU E 44
SHEET 3 N 4 TYR E 78 ASN E 83 -1 O ALA E 79 N LEU E 40
SHEET 4 N 4 LYS E 91 LYS E 94 -1 O VAL E 93 N CYS E 80
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.13
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.07
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.02
SSBOND 4 CYS D 101 CYS D 164 1555 1555 2.11
SSBOND 5 CYS D 203 CYS D 259 1555 1555 2.05
SSBOND 6 CYS E 25 CYS E 80 1555 1555 1.99
LINK OD1 ASN B 83 NA NA B 816 1555 1555 2.65
LINK O HIS B 84 NA NA B 816 1555 1555 2.68
LINK O LEU B 87 NA NA B 816 1555 1555 2.39
LINK NA NA B 816 O HOH B 882 1555 1555 2.21
LINK NA NA B 816 O HOH B 904 1555 1555 2.33
LINK NA NA B 816 O HOH B 923 1555 1555 2.50
CISPEP 1 TYR A 209 PRO A 210 0 -0.29
CISPEP 2 HIS B 31 PRO B 32 0 -5.57
CISPEP 3 TYR D 209 PRO D 210 0 -0.01
CISPEP 4 HIS E 31 PRO E 32 0 -1.38
SITE 1 AC1 6 ASN B 83 HIS B 84 LEU B 87 HOH B 882
SITE 2 AC1 6 HOH B 904 HOH B 923
SITE 1 AC2 8 TRP D 204 ARG D 234 GLN D 242 SER E 11
SITE 2 AC2 8 PRO E 14 ARG E 97 HOH E 825 HOH E 896
SITE 1 AC3 6 TYR A 27 ASP A 29 ASP A 30 HOH A 845
SITE 2 AC3 6 HOH A 950 FMT B 810
SITE 1 AC4 7 ARG A 234 GLN A 242 TYR B 10 SER B 11
SITE 2 AC4 7 HIS B 13 PRO B 14 HOH B 835
SITE 1 AC5 7 THR D 31 GLN D 32 ARG D 48 PRO D 50
SITE 2 AC5 7 HOH D1014 HOH D1018 HOH D1071
SITE 1 AC6 5 ASP D 223 GLN D 224 THR D 225 GLN D 226
SITE 2 AC6 5 ASP D 227
SITE 1 AC7 4 ARG D 131 GLU D 154 HOH D 889 HOH D 987
SITE 1 AC8 3 LYS E 6 ILE E 7 HOH E 933
SITE 1 AC9 6 THR D 31 ARG D 181 TYR D 209 GLY D 239
SITE 2 AC9 6 HOH D1018 HOH D1068
SITE 1 BC1 3 LYS B 91 ILE B 92 HOH B 928
SITE 1 BC2 3 GOL A 802 SER B 57 HOH B 844
SITE 1 BC3 2 ASN E 83 HIS E 84
SITE 1 BC4 3 MET D 138 THR D 142 HIS D 191
SITE 1 BC5 4 LEU C 2 PHE C 3 GLY C 4 HOH C 452
SITE 1 BC6 4 THR B 86 SER B 88 ASP D 220 ARG D 256
SITE 1 BC7 3 MET D 98 TYR D 113 GLN D 115
CRYST1 50.384 62.709 74.773 82.00 76.22 78.18 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 0.019848 -0.004155 -0.004494 0.00000
SCALE2 0.000000 0.016292 -0.001557 0.00000
SCALE3 0.000000 0.000000 0.013833 0.00000
(ATOM LINES ARE NOT SHOWN.)
END