HEADER IMMUNE SYSTEM 15-MAR-07 2P5E
TITLE CRYSTAL STRUCTURES OF HIGH AFFINITY HUMAN T-CELL RECEPTORS BOUND TO
TITLE 2 PMHC REVEAL NATIVE DIAGONAL BINDING GEOMETRY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAINS ALPHA 1, ALPHA2 AND ALPHA3, RESIDUES
COMPND 5 25-299;
COMPND 6 SYNONYM: MHC CLASS I ANTIGEN A*2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: BETA-2 MICROGLOBULIN, RESIDUES 21-119;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: CANCER/TESTIS ANTIGEN 1B;
COMPND 15 CHAIN: C;
COMPND 16 FRAGMENT: RESIDUES 157-165;
COMPND 17 SYNONYM: L ANTIGEN FAMILY MEMBER 2, LAGE-2 PROTEIN, AUTOIMMUNOGENIC
COMPND 18 CANCER/TESTIS ANTIGEN NY-ESO-1;
COMPND 19 ENGINEERED: YES;
COMPND 20 MOL_ID: 4;
COMPND 21 MOLECULE: T-CELL RECEPTOR, ALPHA CHAIN;
COMPND 22 CHAIN: D;
COMPND 23 ENGINEERED: YES;
COMPND 24 MOL_ID: 5;
COMPND 25 MOLECULE: HYPOTHETICAL PROTEIN;
COMPND 26 CHAIN: E;
COMPND 27 ENGINEERED: 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: PEX078;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PEX050;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HOMO SAPIENS
SOURCE 24 (HUMANS);
SOURCE 25 MOL_ID: 4;
SOURCE 26 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 27 ORGANISM_COMMON: HUMAN;
SOURCE 28 ORGANISM_TAXID: 9606;
SOURCE 29 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 30 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 31 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 32 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 33 EXPRESSION_SYSTEM_PLASMID: PGMT7;
SOURCE 34 MOL_ID: 5;
SOURCE 35 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 36 ORGANISM_COMMON: HUMAN;
SOURCE 37 ORGANISM_TAXID: 9606;
SOURCE 38 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 39 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 40 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 41 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 42 EXPRESSION_SYSTEM_PLASMID: PGMT7
KEYWDS T-CELL RECEPTOR, CDR3, PHAGE DISPLAY, MUTANT, HIGH AFFINITY, NY-ESO-
KEYWDS 2 1, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR M.SAMI,P.J.RIZKALLAH,S.DUNN,Y.LI,R.MOYSEY,A.VUIDEPOT,E.BASTON,
AUTHOR 2 P.TODOROV,P.MOLLOY,F.GAO,J.M.BOULTER,B.K.JAKOBSEN
REVDAT 5 27-DEC-23 2P5E 1 LINK
REVDAT 4 30-AUG-23 2P5E 1 SEQADV LINK
REVDAT 3 13-JUL-11 2P5E 1 VERSN
REVDAT 2 24-FEB-09 2P5E 1 VERSN
REVDAT 1 25-SEP-07 2P5E 0
JRNL AUTH M.SAMI,P.J.RIZKALLAH,S.DUNN,P.MOLLOY,R.MOYSEY,A.VUIDEPOT,
JRNL AUTH 2 E.BASTON,P.TODOROV,L.YI,F.GAO,J.M.BOULTER,B.K.JAKOBSEN
JRNL TITL CRYSTAL STRUCTURES OF HIGH AFFINITY HUMAN T-CELL RECEPTORS
JRNL TITL 2 BOUND TO PEPTIDE MAJOR HISTOCOMPATIBILITY COMPLEX REVEAL
JRNL TITL 3 NATIVE DIAGONAL BINDING GEOMETRY
JRNL REF PROTEIN ENG.DES.SEL. V. 20 397 2007
JRNL REFN ISSN 1741-0126
JRNL PMID 17644531
JRNL DOI 10.1093/PROTEIN/GZM033
REMARK 2
REMARK 2 RESOLUTION. 1.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 117.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 66411
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3552
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) : 1.89
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.94
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4475
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE SET COUNT : 240
REMARK 3 BIN FREE R VALUE : 0.3620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6568
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 93
REMARK 3 SOLVENT ATOMS : 739
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.29000
REMARK 3 B22 (A**2) : 0.30000
REMARK 3 B33 (A**2) : -1.16000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.52000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.156
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.153
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.111
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.074
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6915 ; 0.017 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 4691 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9412 ; 1.173 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11347 ; 0.710 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 837 ; 2.817 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 342 ;24.273 ;23.830
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1105 ; 8.812 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;10.558 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 989 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7708 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1449 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1430 ; 0.196 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 5260 ; 0.213 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3220 ; 0.187 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): 3598 ; 0.092 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 979 ; 0.230 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): 4 ; 0.191 ; 0.500
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.019 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 44 ; 0.185 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 104 ; 0.226 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 45 ; 0.318 ; 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): 5262 ; 3.072 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1659 ; 0.860 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6703 ; 3.544 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3290 ; 5.409 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2703 ; 7.091 ; 6.000
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 : 8
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 1 A 180
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8288 -2.5121 40.6213
REMARK 3 T TENSOR
REMARK 3 T11: -0.0848 T22: -0.1070
REMARK 3 T33: -0.0802 T12: 0.0284
REMARK 3 T13: 0.0111 T23: 0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 1.2966 L22: 0.7292
REMARK 3 L33: 1.8137 L12: -0.0416
REMARK 3 L13: -0.8640 L23: -0.1931
REMARK 3 S TENSOR
REMARK 3 S11: -0.0310 S12: 0.0066 S13: -0.0659
REMARK 3 S21: 0.0236 S22: -0.0140 S23: 0.0090
REMARK 3 S31: 0.0855 S32: 0.1186 S33: 0.0450
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 185 A 274
REMARK 3 ORIGIN FOR THE GROUP (A): 11.8696 -10.0952 75.6826
REMARK 3 T TENSOR
REMARK 3 T11: -0.0297 T22: 0.1095
REMARK 3 T33: -0.0358 T12: -0.0175
REMARK 3 T13: -0.0172 T23: -0.0323
REMARK 3 L TENSOR
REMARK 3 L11: 0.9247 L22: 0.9099
REMARK 3 L33: 2.8726 L12: 0.1651
REMARK 3 L13: 0.1900 L23: -1.0148
REMARK 3 S TENSOR
REMARK 3 S11: 0.0554 S12: -0.2726 S13: -0.0083
REMARK 3 S21: 0.1119 S22: -0.0216 S23: -0.0779
REMARK 3 S31: -0.1640 S32: 0.3882 S33: -0.0338
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): 4.4083 -20.2245 56.9110
REMARK 3 T TENSOR
REMARK 3 T11: -0.0501 T22: -0.1087
REMARK 3 T33: -0.0801 T12: 0.0008
REMARK 3 T13: -0.0046 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 2.0280 L22: 2.4276
REMARK 3 L33: 1.9772 L12: 0.6101
REMARK 3 L13: -1.2753 L23: -0.6695
REMARK 3 S TENSOR
REMARK 3 S11: -0.0141 S12: -0.0233 S13: -0.1015
REMARK 3 S21: -0.1223 S22: -0.0584 S23: 0.0179
REMARK 3 S31: 0.2579 S32: -0.0297 S33: 0.0724
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 : C 1 C 9
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7036 0.5556 32.5599
REMARK 3 T TENSOR
REMARK 3 T11: -0.0231 T22: -0.0269
REMARK 3 T33: -0.0609 T12: 0.0345
REMARK 3 T13: -0.0029 T23: -0.0066
REMARK 3 L TENSOR
REMARK 3 L11: 1.0650 L22: 3.6430
REMARK 3 L33: 1.2212 L12: -0.4988
REMARK 3 L13: -1.1229 L23: 0.1696
REMARK 3 S TENSOR
REMARK 3 S11: -0.0148 S12: -0.0978 S13: -0.2118
REMARK 3 S21: 0.1790 S22: 0.0033 S23: 0.3012
REMARK 3 S31: -0.1006 S32: 0.2372 S33: 0.0115
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 1 D 110
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0162 15.5124 15.1694
REMARK 3 T TENSOR
REMARK 3 T11: -0.0337 T22: -0.0207
REMARK 3 T33: -0.0265 T12: -0.0146
REMARK 3 T13: -0.0292 T23: 0.0417
REMARK 3 L TENSOR
REMARK 3 L11: 1.9897 L22: 1.1960
REMARK 3 L33: 3.1489 L12: 0.7825
REMARK 3 L13: -1.4533 L23: -0.6497
REMARK 3 S TENSOR
REMARK 3 S11: 0.0255 S12: 0.1286 S13: 0.1786
REMARK 3 S21: 0.0039 S22: -0.0131 S23: -0.0519
REMARK 3 S31: -0.3630 S32: 0.1004 S33: -0.0124
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 : D 115 D 191
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2335 17.3856 -19.8545
REMARK 3 T TENSOR
REMARK 3 T11: 0.0104 T22: 0.1010
REMARK 3 T33: -0.0195 T12: -0.0682
REMARK 3 T13: -0.0156 T23: 0.0569
REMARK 3 L TENSOR
REMARK 3 L11: 1.8729 L22: 3.7244
REMARK 3 L33: 2.9899 L12: 0.6469
REMARK 3 L13: -0.3027 L23: -0.5066
REMARK 3 S TENSOR
REMARK 3 S11: -0.1024 S12: 0.1956 S13: 0.1470
REMARK 3 S21: -0.1678 S22: 0.1195 S23: 0.3156
REMARK 3 S31: -0.4396 S32: -0.0375 S33: -0.0171
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 110
REMARK 3 ORIGIN FOR THE GROUP (A): 8.0433 -0.7255 11.2251
REMARK 3 T TENSOR
REMARK 3 T11: -0.1269 T22: -0.0293
REMARK 3 T33: -0.0907 T12: 0.0091
REMARK 3 T13: -0.0218 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 0.5465 L22: 0.8074
REMARK 3 L33: 2.0724 L12: -0.1875
REMARK 3 L13: 0.6706 L23: -0.1770
REMARK 3 S TENSOR
REMARK 3 S11: -0.0031 S12: 0.0912 S13: -0.0556
REMARK 3 S21: -0.0384 S22: -0.0270 S23: 0.0060
REMARK 3 S31: 0.1601 S32: -0.0135 S33: 0.0301
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 120 E 241
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4065 2.9472 -17.4513
REMARK 3 T TENSOR
REMARK 3 T11: -0.0746 T22: -0.0179
REMARK 3 T33: -0.0920 T12: -0.0285
REMARK 3 T13: -0.0117 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 1.8186 L22: 0.8446
REMARK 3 L33: 1.4263 L12: 0.5452
REMARK 3 L13: 0.1385 L23: -0.2097
REMARK 3 S TENSOR
REMARK 3 S11: -0.0123 S12: 0.1114 S13: 0.0023
REMARK 3 S21: -0.0683 S22: 0.0020 S23: -0.0186
REMARK 3 S31: -0.0692 S32: 0.1865 S33: 0.0103
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 2P5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000041987.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUL-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 3
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.488
REMARK 200 MONOCHROMATOR : SI (III)
REMARK 200 OPTICS : MIRROR + MONOCHROMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69966
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.887
REMARK 200 RESOLUTION RANGE LOW (A) : 117.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 2F53
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 85 MM HEPES, 8.5% ISOPROPANOL, 17% PEG
REMARK 280 4000, 15% GLYCEROL, PH 7.5, VAPOR DIFFUSION, TEMPERATURE 293K,
REMARK 280 PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 25.88550
REMARK 290 SMTRY3 2 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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 14010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -134.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 SER D 194
REMARK 465 ALA E 242
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 O HOH E 955 O HOH E 982 1.90
REMARK 500 O HOH D 835 O HOH D 889 2.00
REMARK 500 O HOH E 976 O HOH E 1034 2.05
REMARK 500 OE1 GLN E 222 O HOH E 961 2.13
REMARK 500 O SER D 69 N GLY D 71 2.14
REMARK 500 O GLU B 74 O HOH B 959 2.15
REMARK 500 O HOH A 1030 O HOH A 1048 2.15
REMARK 500 O HOH A 933 O HOH B 990 2.15
REMARK 500 O HOH D 890 O HOH D 915 2.17
REMARK 500 O SER E 165 O HOH E 1094 2.17
REMARK 500 O HOH A 1085 O HOH A 1118 2.17
REMARK 500 ND2 ASN A 86 O HOH A 918 2.18
REMARK 500 O HOH A 1003 O HOH D 854 2.18
REMARK 500 O HOH D 885 O HOH D 899 2.18
REMARK 500 O HOH E 1028 O HOH E 1104 2.18
REMARK 500 OG SER D 168 O HOH D 853 2.19
REMARK 500 O HOH D 907 O HOH E 1083 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASN E 217 O HOH E 960 2545 2.16
REMARK 500
REMARK 500 REMARK: NULL
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 CYS D 162 CA - CB - SG ANGL. DEV. = 8.5 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 PRO A 15 113.44 -27.65
REMARK 500 ASP A 29 -125.02 60.88
REMARK 500 SER A 195 -164.06 -160.67
REMARK 500 ASN B 21 -169.04 -164.44
REMARK 500 PRO B 32 -178.01 -69.44
REMARK 500 TRP B 60 -4.75 80.58
REMARK 500 SER D 70 34.60 -36.88
REMARK 500 ALA D 79 65.47 35.13
REMARK 500 ALA D 86 177.54 173.24
REMARK 500 ASP D 120 59.34 -149.29
REMARK 500 SER D 132 -9.59 -58.29
REMARK 500 SER D 151 92.99 -43.96
REMARK 500 ASN D 181 47.29 -102.76
REMARK 500 ASN D 192 -167.55 58.02
REMARK 500 ILE E 44 -60.01 -92.63
REMARK 500 SER E 85 -178.96 -172.52
REMARK 500 LEU E 94 49.64 -101.95
REMARK 500 ASN E 96 -121.96 60.46
REMARK 500 ASP E 182 32.48 -97.33
REMARK 500 TRP E 220 111.68 -161.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 800 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 83 OD1
REMARK 620 2 LEU B 87 O 108.4
REMARK 620 3 HOH B 922 O 96.0 153.7
REMARK 620 N 1 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2F53 RELATED DB: PDB
REMARK 900 CLONE 49-50
REMARK 900 RELATED ID: 2F54 RELATED DB: PDB
REMARK 900 WILD TYPE
REMARK 900 RELATED ID: 2BNR RELATED DB: PDB
REMARK 900 WILD TYPE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 NO SUITABLE DATABASE REFERENCE WAS FOUND FOR CHAINS
REMARK 999 D AND E AT TIME OF PROCESSING
DBREF 2P5E A 1 276 UNP P01892 1A02_HUMAN 25 300
DBREF 2P5E B 2 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 2P5E C 1 9 UNP P78358 CTG1B_HUMAN 157 165
DBREF 2P5E D 1 92 UNP A2NVQ1 A2NVQ1_HUMAN 20 111
DBREF 2P5E E 1 241 UNP Q2YDB4 Q2YDB4_HUMAN 22 263
SEQADV 2P5E MET B 0 UNP P61769 INSERTION
SEQADV 2P5E CYS B 91 UNP P61769 LYS 111 CONFLICT
SEQRES 1 A 276 GLY SER HIS SER MET ARG TYR PHE PHE THR SER VAL SER
SEQRES 2 A 276 ARG PRO GLY ARG GLY GLU PRO ARG PHE ILE ALA VAL GLY
SEQRES 3 A 276 TYR VAL ASP ASP THR GLN PHE VAL ARG PHE ASP SER ASP
SEQRES 4 A 276 ALA ALA SER GLN ARG MET GLU PRO ARG ALA PRO TRP ILE
SEQRES 5 A 276 GLU GLN GLU GLY PRO GLU TYR TRP ASP GLY GLU THR ARG
SEQRES 6 A 276 LYS VAL LYS ALA HIS SER GLN THR HIS ARG VAL ASP LEU
SEQRES 7 A 276 GLY THR LEU ARG GLY TYR TYR ASN GLN SER GLU ALA GLY
SEQRES 8 A 276 SER HIS THR VAL GLN ARG MET TYR GLY CYS ASP VAL GLY
SEQRES 9 A 276 SER ASP TRP ARG PHE LEU ARG GLY TYR HIS GLN TYR ALA
SEQRES 10 A 276 TYR ASP GLY LYS ASP TYR ILE ALA LEU LYS GLU ASP LEU
SEQRES 11 A 276 ARG SER TRP THR ALA ALA ASP MET ALA ALA GLN THR THR
SEQRES 12 A 276 LYS HIS LYS TRP GLU ALA ALA HIS VAL ALA GLU GLN LEU
SEQRES 13 A 276 ARG ALA TYR LEU GLU GLY THR CYS VAL GLU TRP LEU ARG
SEQRES 14 A 276 ARG TYR LEU GLU ASN GLY LYS GLU THR LEU GLN ARG THR
SEQRES 15 A 276 ASP ALA PRO LYS THR HIS MET THR HIS HIS ALA VAL SER
SEQRES 16 A 276 ASP HIS GLU ALA THR LEU ARG CYS TRP ALA LEU SER PHE
SEQRES 17 A 276 TYR PRO ALA GLU ILE THR LEU THR TRP GLN ARG ASP GLY
SEQRES 18 A 276 GLU ASP GLN THR GLN ASP THR GLU LEU VAL GLU THR ARG
SEQRES 19 A 276 PRO ALA GLY ASP GLY THR PHE GLN LYS TRP ALA ALA VAL
SEQRES 20 A 276 VAL VAL PRO SER GLY GLN GLU GLN ARG TYR THR CYS HIS
SEQRES 21 A 276 VAL GLN HIS GLU GLY LEU PRO LYS PRO LEU THR LEU ARG
SEQRES 22 A 276 TRP GLU PRO
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 CYS ILE VAL LYS TRP ASP ARG ASP MET
SEQRES 1 C 9 SER LEU LEU MET TRP ILE THR GLN CYS
SEQRES 1 D 195 MET LYS GLN GLU VAL THR GLN ILE PRO ALA ALA LEU SER
SEQRES 2 D 195 VAL PRO GLU GLY GLU ASN LEU VAL LEU ASN CYS SER PHE
SEQRES 3 D 195 THR ASP SER ALA ILE TYR ASN LEU GLN TRP PHE ARG GLN
SEQRES 4 D 195 ASP PRO GLY LYS GLY LEU THR SER LEU LEU LEU ILE THR
SEQRES 5 D 195 PRO TRP GLN ARG GLU GLN THR SER GLY ARG LEU ASN ALA
SEQRES 6 D 195 SER LEU ASP LYS SER SER GLY SER SER THR LEU TYR ILE
SEQRES 7 D 195 ALA ALA SER GLN PRO GLY ASP SER ALA THR TYR LEU CYS
SEQRES 8 D 195 ALA VAL ARG PRO LEU LEU ASP GLY THR TYR ILE PRO THR
SEQRES 9 D 195 PHE GLY ARG GLY THR SER LEU ILE VAL HIS PRO TYR ILE
SEQRES 10 D 195 GLN ASN PRO ASP PRO ALA VAL TYR GLN LEU ARG ASP SER
SEQRES 11 D 195 LYS SER SER ASP LYS SER VAL CYS LEU PHE THR ASP PHE
SEQRES 12 D 195 ASP SER GLN THR ASN VAL SER GLN SER LYS ASP SER ASP
SEQRES 13 D 195 VAL TYR ILE THR ASP LYS CYS VAL LEU ASP MET ARG SER
SEQRES 14 D 195 MET ASP PHE LYS SER ASN SER ALA VAL ALA TRP SER ASN
SEQRES 15 D 195 LYS SER ASP PHE ALA CYS ALA ASN ALA PHE ASN ASN SER
SEQRES 1 E 242 GLY VAL THR GLN THR PRO LYS PHE GLN VAL LEU LYS THR
SEQRES 2 E 242 GLY GLN SER MET THR LEU GLN CYS ALA GLN ASP MET ASN
SEQRES 3 E 242 HIS GLU TYR MET SER TRP TYR ARG GLN ASP PRO GLY MET
SEQRES 4 E 242 GLY LEU ARG LEU ILE HIS TYR SER VAL ALA ILE GLN THR
SEQRES 5 E 242 THR ASP GLN GLY GLU VAL PRO ASN GLY TYR ASN VAL SER
SEQRES 6 E 242 ARG SER THR ILE GLU ASP PHE PRO LEU ARG LEU LEU SER
SEQRES 7 E 242 ALA ALA PRO SER GLN THR SER VAL TYR PHE CYS ALA SER
SEQRES 8 E 242 SER TYR LEU GLY ASN THR GLY GLU LEU PHE PHE GLY GLU
SEQRES 9 E 242 GLY SER ARG LEU THR VAL LEU GLU ASP LEU LYS ASN VAL
SEQRES 10 E 242 PHE PRO PRO GLU VAL ALA VAL PHE GLU PRO SER GLU ALA
SEQRES 11 E 242 GLU ILE SER HIS THR GLN LYS ALA THR LEU VAL CYS LEU
SEQRES 12 E 242 ALA THR GLY PHE TYR PRO ASP HIS VAL GLU LEU SER TRP
SEQRES 13 E 242 TRP VAL ASN GLY LYS GLU VAL HIS SER GLY VAL CYS THR
SEQRES 14 E 242 ASP PRO GLN PRO LEU LYS GLU GLN PRO ALA LEU ASN ASP
SEQRES 15 E 242 SER ARG TYR ALA LEU SER SER ARG LEU ARG VAL SER ALA
SEQRES 16 E 242 THR PHE TRP GLN ASP PRO ARG ASN HIS PHE ARG CYS GLN
SEQRES 17 E 242 VAL GLN PHE TYR GLY LEU SER GLU ASN ASP GLU TRP THR
SEQRES 18 E 242 GLN ASP ARG ALA LYS PRO VAL THR GLN ILE VAL SER ALA
SEQRES 19 E 242 GLU ALA TRP GLY ARG ALA ASP ALA
HET GOL A 902 6
HET GOL A 903 6
HET GOL A 904 6
HET GOL A 906 6
HET GOL A 907 6
HET MG B 800 1
HET SO4 B 805 5
HET GOL B 901 6
HET IPA C 909 4
HET SO4 D 801 5
HET SO4 D 802 5
HET SO4 E 803 5
HET SO4 E 804 5
HET EPE E 806 15
HET GOL E 905 6
HET GOL E 908 6
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETNAM SO4 SULFATE ION
HETNAM IPA ISOPROPYL ALCOHOL
HETNAM EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN IPA 2-PROPANOL
HETSYN EPE HEPES
FORMUL 6 GOL 8(C3 H8 O3)
FORMUL 11 MG MG 2+
FORMUL 12 SO4 5(O4 S 2-)
FORMUL 14 IPA C3 H8 O
FORMUL 19 EPE C8 H18 N2 O4 S
FORMUL 22 HOH *739(H2 O)
HELIX 1 1 PRO A 50 GLU A 55 5 6
HELIX 2 2 GLY A 56 TYR A 85 1 30
HELIX 3 3 ASP A 137 ALA A 150 1 14
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 GLN A 253 GLN A 255 5 3
HELIX 8 8 GLN D 81 SER D 85 5 5
HELIX 9 9 ARG D 167 ASP D 170 5 4
HELIX 10 10 ALA D 186 ALA D 190 5 5
HELIX 11 11 ALA E 80 THR E 84 5 5
HELIX 12 12 ASP E 113 VAL E 117 5 5
HELIX 13 13 SER E 128 GLN E 136 1 9
HELIX 14 14 ALA E 195 ASP E 200 1 6
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 PHE A 8 O VAL A 25
SHEET 5 A 8 THR A 94 VAL A 103 -1 O ARG A 97 N PHE A 9
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 TYR A 123 N TYR A 116
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 TRP A 204 N HIS A 188
SHEET 3 B 4 PHE A 241 PRO A 250 -1 O ALA A 245 N CYS A 203
SHEET 4 B 4 THR A 228 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 TRP A 204 N HIS A 188
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 GLN A 224 0
SHEET 2 D 4 THR A 214 ARG A 219 -1 N TRP A 217 O GLN A 224
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 ARG A 273 -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 THR B 68 N LEU B 23
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 THR B 68 N LEU B 23
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 ALA B 79 N LEU B 40
SHEET 4 G 4 CYS B 91 LYS B 94 -1 O CYS B 91 N VAL B 82
SHEET 1 H 5 VAL D 4 ILE D 7 0
SHEET 2 H 5 LEU D 19 PHE D 25 -1 O SER D 24 N THR D 5
SHEET 3 H 5 SER D 72 ILE D 77 -1 O LEU D 75 N LEU D 21
SHEET 4 H 5 LEU D 62 LEU D 66 -1 N ASN D 63 O TYR D 76
SHEET 5 H 5 GLU D 56 SER D 59 -1 N SER D 59 O LEU D 62
SHEET 1 I 5 ALA D 10 PRO D 14 0
SHEET 2 I 5 THR D 108 HIS D 113 1 O SER D 109 N LEU D 11
SHEET 3 I 5 ALA D 86 PRO D 94 -1 N ALA D 86 O LEU D 110
SHEET 4 I 5 ILE D 30 GLN D 38 -1 N PHE D 36 O LEU D 89
SHEET 5 I 5 LEU D 44 ILE D 50 -1 O LEU D 47 N TRP D 35
SHEET 1 J 4 ALA D 10 PRO D 14 0
SHEET 2 J 4 THR D 108 HIS D 113 1 O SER D 109 N LEU D 11
SHEET 3 J 4 ALA D 86 PRO D 94 -1 N ALA D 86 O LEU D 110
SHEET 4 J 4 THR D 103 PHE D 104 -1 O THR D 103 N VAL D 92
SHEET 1 K 8 VAL D 156 ILE D 158 0
SHEET 2 K 8 PHE D 171 SER D 180 -1 O TRP D 179 N TYR D 157
SHEET 3 K 8 SER D 135 THR D 140 -1 N CYS D 137 O ALA D 178
SHEET 4 K 8 ALA D 122 ASP D 128 -1 N TYR D 124 O LEU D 138
SHEET 5 K 8 GLU E 121 GLU E 126 -1 O GLU E 126 N ARG D 127
SHEET 6 K 8 LYS E 137 PHE E 147 -1 O VAL E 141 N PHE E 125
SHEET 7 K 8 TYR E 185 SER E 194 -1 O VAL E 193 N ALA E 138
SHEET 8 K 8 VAL E 167 THR E 169 -1 N CYS E 168 O ARG E 190
SHEET 1 L 8 CYS D 162 MET D 166 0
SHEET 2 L 8 PHE D 171 SER D 180 -1 O PHE D 171 N MET D 166
SHEET 3 L 8 SER D 135 THR D 140 -1 N CYS D 137 O ALA D 178
SHEET 4 L 8 ALA D 122 ASP D 128 -1 N TYR D 124 O LEU D 138
SHEET 5 L 8 GLU E 121 GLU E 126 -1 O GLU E 126 N ARG D 127
SHEET 6 L 8 LYS E 137 PHE E 147 -1 O VAL E 141 N PHE E 125
SHEET 7 L 8 TYR E 185 SER E 194 -1 O VAL E 193 N ALA E 138
SHEET 8 L 8 LEU E 174 LYS E 175 -1 N LEU E 174 O ALA E 186
SHEET 1 M 4 VAL E 2 THR E 5 0
SHEET 2 M 4 MET E 17 GLN E 23 -1 O GLN E 20 N THR E 5
SHEET 3 M 4 LEU E 74 LEU E 76 -1 O LEU E 76 N MET E 17
SHEET 4 M 4 TYR E 62 VAL E 64 -1 N ASN E 63 O ARG E 75
SHEET 1 N 6 PHE E 8 LYS E 12 0
SHEET 2 N 6 SER E 106 LEU E 111 1 O LEU E 111 N LEU E 11
SHEET 3 N 6 SER E 85 SER E 92 -1 N TYR E 87 O SER E 106
SHEET 4 N 6 TYR E 29 GLN E 35 -1 N TYR E 33 O PHE E 88
SHEET 5 N 6 ARG E 42 ALA E 49 -1 O ILE E 44 N TRP E 32
SHEET 6 N 6 THR E 52 GLN E 55 -1 O ASP E 54 N TYR E 46
SHEET 1 O 4 PHE E 8 LYS E 12 0
SHEET 2 O 4 SER E 106 LEU E 111 1 O LEU E 111 N LEU E 11
SHEET 3 O 4 SER E 85 SER E 92 -1 N TYR E 87 O SER E 106
SHEET 4 O 4 PHE E 101 PHE E 102 -1 O PHE E 101 N SER E 91
SHEET 1 P 4 LYS E 161 VAL E 163 0
SHEET 2 P 4 VAL E 152 VAL E 158 -1 N VAL E 158 O LYS E 161
SHEET 3 P 4 HIS E 204 PHE E 211 -1 O ARG E 206 N TRP E 157
SHEET 4 P 4 GLN E 230 TRP E 237 -1 O ALA E 236 N PHE E 205
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.12
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.05
SSBOND 3 CYS B 25 CYS B 80 1555 1555 2.01
SSBOND 4 CYS D 23 CYS D 90 1555 1555 2.01
SSBOND 5 CYS D 137 CYS D 187 1555 1555 2.02
SSBOND 6 CYS D 162 CYS E 168 1555 1555 2.00
SSBOND 7 CYS E 21 CYS E 89 1555 1555 2.01
SSBOND 8 CYS E 142 CYS E 207 1555 1555 1.96
LINK OD1 ASN B 83 MG MG B 800 1555 1555 2.46
LINK O LEU B 87 MG MG B 800 1555 1555 2.25
LINK MG MG B 800 O HOH B 922 1555 1555 1.97
CISPEP 1 TYR A 209 PRO A 210 0 0.12
CISPEP 2 HIS B 31 PRO B 32 0 0.32
CISPEP 3 ILE D 7 PRO D 8 0 -0.01
CISPEP 4 THR E 5 PRO E 6 0 -0.80
CISPEP 5 TYR E 148 PRO E 149 0 0.23
CRYST1 74.002 51.771 118.270 90.00 98.24 90.00 P 1 21 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 0.013513 0.000000 0.001957 0.00000
SCALE2 0.000000 0.019316 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008543 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
