HEADER IMMUNE SYSTEM 28-APR-06 2GTZ
TITLE HUMAN CLASS I MHC HLA-A2 IN COMPLEX WITH THE NONAMERIC MELAN-A/MART-
TITLE 2 1(27-35) PEPTIDE HAVING A28L SUBSTITUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HLA-A*0201 HEAVY CHAIN;
COMPND 3 CHAIN: A, D;
COMPND 4 FRAGMENT: HEAVY CHAIN;
COMPND 5 SYNONYM: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN; MHC
COMPND 6 CLASS I ANTIGEN A*2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: BETA-2-MICROGLOBULIN;
COMPND 10 CHAIN: B, E;
COMPND 11 SYNONYM: BETA-2-MICROGLOBULIN VARIANT PI 5.3;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: OCTAPEPTIDE FROM MELAN-A/MART-1;
COMPND 15 CHAIN: C, F;
COMPND 16 FRAGMENT: RESIDUES 27-35;
COMPND 17 SYNONYM: MELANOMA ANTIGEN RECOGNIZED BY T-CELLS 1;
COMPND 18 ENGINEERED: YES;
COMPND 19 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;
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 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: PHN1;
SOURCE 21 MOL_ID: 3;
SOURCE 22 SYNTHETIC: YES;
SOURCE 23 OTHER_DETAILS: COMMERCIAL SYNTHESIS FOR THE PEPTIDE
KEYWDS MELAN-A/MART-1 PEPTIDE, NONAPEPTIDE, MHC CLASS I, HLA-A2, A28L
KEYWDS 2 MUTATION, MELANOMA, CANCER VACCINES, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR O.Y.BORBULEVYCH,B.M.BAKER
REVDAT 6 30-AUG-23 2GTZ 1 REMARK
REVDAT 5 20-OCT-21 2GTZ 1 REMARK SEQADV LINK
REVDAT 4 13-JUL-11 2GTZ 1 VERSN
REVDAT 3 24-FEB-09 2GTZ 1 VERSN
REVDAT 2 02-OCT-07 2GTZ 1 JRNL
REVDAT 1 12-JUN-07 2GTZ 0
JRNL AUTH O.Y.BORBULEVYCH,F.K.INSAIDOO,T.K.BAXTER,D.J.POWELL,
JRNL AUTH 2 L.A.JOHNSON,N.P.RESTIFO,B.M.BAKER
JRNL TITL STRUCTURES OF MART-1(26/27-35) PEPTIDE/HLA-A2 COMPLEXES
JRNL TITL 2 REVEAL A REMARKABLE DISCONNECT BETWEEN ANTIGEN STRUCTURAL
JRNL TITL 3 HOMOLOGY AND T CELL RECOGNITION
JRNL REF J.MOL.BIOL. V. 372 1123 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17719062
JRNL DOI 10.1016/J.JMB.2007.07.025
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2
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 (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 83098
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4382
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) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4966
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE SET COUNT : 276
REMARK 3 BIN FREE R VALUE : 0.2980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6288
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 812
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 16.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.69000
REMARK 3 B22 (A**2) : 1.60000
REMARK 3 B33 (A**2) : -0.91000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.17000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.109
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.112
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.480
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6574 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8923 ; 1.710 ; 1.927
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 767 ; 6.135 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 349 ;32.731 ;23.152
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1082 ;14.818 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 57 ;20.887 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 923 ; 0.154 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5125 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2839 ; 0.162 ; 0.080
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4418 ; 0.309 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1138 ; 0.189 ; 0.500
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.192 ; 0.500
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 72 ; 0.124 ; 0.080
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 78 ; 0.199 ; 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 ; 0.939 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6235 ; 1.701 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2875 ; 2.882 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2688 ; 4.624 ; 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): 738 ; 0.24 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 738 ; 0.80 ; 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): 839 ; 0.35 ; 0.50
REMARK 3 MEDIUM THERMAL 2 B (A**2): 839 ; 0.82 ; 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): 24.0821 17.2932 35.4299
REMARK 3 T TENSOR
REMARK 3 T11: -0.0457 T22: -0.0569
REMARK 3 T33: -0.0606 T12: -0.0214
REMARK 3 T13: -0.0291 T23: 0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 2.0938 L22: 0.3416
REMARK 3 L33: 1.7916 L12: -0.1446
REMARK 3 L13: -1.1135 L23: -0.1817
REMARK 3 S TENSOR
REMARK 3 S11: -0.0401 S12: -0.2175 S13: -0.0846
REMARK 3 S21: 0.0850 S22: 0.0295 S23: -0.0453
REMARK 3 S31: 0.0442 S32: 0.0197 S33: 0.0106
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): -6.9055 14.1127 19.0802
REMARK 3 T TENSOR
REMARK 3 T11: -0.0699 T22: -0.1293
REMARK 3 T33: -0.0803 T12: 0.0063
REMARK 3 T13: -0.0067 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 1.9935 L22: 0.8629
REMARK 3 L33: 3.9128 L12: 0.3426
REMARK 3 L13: 1.2358 L23: 0.6350
REMARK 3 S TENSOR
REMARK 3 S11: 0.0205 S12: 0.0698 S13: -0.1226
REMARK 3 S21: -0.0435 S22: 0.0295 S23: -0.0061
REMARK 3 S31: 0.1443 S32: 0.0305 S33: -0.0500
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): 3.2702 32.1526 27.1208
REMARK 3 T TENSOR
REMARK 3 T11: -0.0464 T22: -0.1185
REMARK 3 T33: -0.0630 T12: -0.0066
REMARK 3 T13: 0.0214 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 4.1321 L22: 1.2615
REMARK 3 L33: 1.5422 L12: -0.5426
REMARK 3 L13: -0.6890 L23: 0.2277
REMARK 3 S TENSOR
REMARK 3 S11: 0.0793 S12: -0.0580 S13: 0.3575
REMARK 3 S21: 0.0534 S22: -0.0361 S23: 0.0609
REMARK 3 S31: -0.1597 S32: -0.0699 S33: -0.0432
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): 5.1701 -17.4682 20.3141
REMARK 3 T TENSOR
REMARK 3 T11: -0.0470 T22: -0.0419
REMARK 3 T33: -0.0426 T12: -0.0126
REMARK 3 T13: 0.0144 T23: -0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 1.9143 L22: 0.2835
REMARK 3 L33: 1.6477 L12: -0.1606
REMARK 3 L13: 0.7828 L23: 0.1176
REMARK 3 S TENSOR
REMARK 3 S11: -0.0237 S12: -0.2327 S13: 0.1132
REMARK 3 S21: 0.0717 S22: 0.0080 S23: 0.0576
REMARK 3 S31: -0.0300 S32: 0.0810 S33: 0.0157
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): 36.1701 -14.2728 3.7881
REMARK 3 T TENSOR
REMARK 3 T11: -0.0641 T22: -0.1061
REMARK 3 T33: -0.0774 T12: 0.0130
REMARK 3 T13: -0.0038 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 2.3782 L22: 0.9143
REMARK 3 L33: 3.8969 L12: 0.3478
REMARK 3 L13: -1.6614 L23: -0.3990
REMARK 3 S TENSOR
REMARK 3 S11: 0.0655 S12: 0.0560 S13: 0.1640
REMARK 3 S21: -0.0676 S22: 0.0073 S23: 0.0086
REMARK 3 S31: -0.1302 S32: -0.0906 S33: -0.0728
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): 26.1225 -32.2706 11.9185
REMARK 3 T TENSOR
REMARK 3 T11: -0.0697 T22: -0.0727
REMARK 3 T33: -0.0750 T12: -0.0014
REMARK 3 T13: -0.0113 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 3.4546 L22: 1.4473
REMARK 3 L33: 1.3812 L12: -0.5284
REMARK 3 L13: 0.2456 L23: -0.1662
REMARK 3 S TENSOR
REMARK 3 S11: 0.0066 S12: -0.1699 S13: -0.2370
REMARK 3 S21: 0.0260 S22: -0.0173 S23: -0.0482
REMARK 3 S31: 0.0901 S32: 0.1474 S33: 0.0107
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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GTZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000037546.
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87504
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 (%) : 97.0
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1000
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 (%) : 85.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.47900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1TVB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350 24%, MES 0.025M, NH4CL 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 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 42.15500
REMARK 290 SMTRY3 2 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: 5350 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 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: 4700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 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 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 ARG D 108 NE - CZ - NH1 ANGL. DEV. = 3.1 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 15 111.95 -35.32
REMARK 500 ASP A 29 -127.67 54.03
REMARK 500 LEU A 110 -60.60 -104.86
REMARK 500 HIS A 114 106.84 -160.90
REMARK 500 GLN A 180 54.79 -100.30
REMARK 500 SER A 195 -168.64 -165.51
REMARK 500 TRP B 60 -5.19 80.10
REMARK 500 ASP D 29 -127.14 51.51
REMARK 500 SER D 195 -166.12 -165.46
REMARK 500 GLN D 224 41.59 -102.71
REMARK 500 LYS E 48 57.78 -90.37
REMARK 500 TRP E 60 -2.64 81.23
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 NA B5001 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 83 OD1
REMARK 620 2 HIS B 84 O 81.8
REMARK 620 3 LEU B 87 O 96.7 81.2
REMARK 620 4 HOH B5072 O 85.0 84.7 165.4
REMARK 620 5 HOH B5079 O 176.5 97.8 86.7 91.5
REMARK 620 6 HOH B5088 O 93.1 170.0 91.0 103.4 87.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA E5002 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN E 83 OD1
REMARK 620 2 HIS E 84 O 75.1
REMARK 620 3 LEU E 87 O 94.3 80.1
REMARK 620 4 HOH E5102 O 80.0 78.0 158.0
REMARK 620 5 HOH E5119 O 63.8 124.7 68.5 125.4
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 NA B 5001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 5002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1006
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JF1 RELATED DB: PDB
REMARK 900 CLASS I MHC HLA-A2 IN COMPLEX WITH ALTERED DECAMERIC PEPTIDE FROM
REMARK 900 MELAN-A/MART-1
REMARK 900 RELATED ID: 1JHT RELATED DB: PDB
REMARK 900 CLASS I MHC HLA-A2 IN COMPLEX WITH ALTERED NONAMERIC PEPTIDE FROM
REMARK 900 MELAN-A/MART-1
REMARK 900 RELATED ID: 2GT9 RELATED DB: PDB
REMARK 900 CLASS I MHC HLA-A2 IN COMPLEX WITH THE DECAMERIC MELAN-A/MART-1(26-
REMARK 900 35) PEPTIDE
REMARK 900 RELATED ID: 2GUO RELATED DB: PDB
REMARK 900 CLASS I MHC HLA-A2 IN COMPLEX WITH THE NATIVE NONAMERIC MELAN-A/
REMARK 900 MART-1(27-35) PEPTIDE
REMARK 900 RELATED ID: 2GTW RELATED DB: PDB
REMARK 900 CLASS I MHC HLA-A2 IN COMPLEX WITH THE NONAMERIC MELAN-A/MART-1(27-
REMARK 900 35) PEPTIDE HAVING A27L SUBSTITUTION
DBREF 2GTZ A 1 275 UNP Q9TQH5 1A02_HUMAN 25 299
DBREF 2GTZ D 1 275 UNP Q9TQH5 1A02_HUMAN 25 299
DBREF 2GTZ B 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 2GTZ E 1 99 UNP P61769 B2MG_HUMAN 21 119
DBREF 2GTZ C 1 9 UNP Q16655 MAR1_HUMAN 28 36
DBREF 2GTZ F 1 9 UNP Q16655 MAR1_HUMAN 28 36
SEQADV 2GTZ MET B 0 UNP P61769 INITIATING METHIONINE
SEQADV 2GTZ MET E 0 UNP P61769 INITIATING METHIONINE
SEQADV 2GTZ LEU C 2 UNP Q16655 ALA 29 ENGINEERED MUTATION
SEQADV 2GTZ LEU F 2 UNP Q16655 ALA 29 ENGINEERED MUTATION
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 ALA LEU GLY ILE GLY ILE LEU THR 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 ALA LEU GLY ILE GLY ILE LEU THR VAL
HET GOL A1001 6
HET GOL A1002 6
HET GOL A1005 6
HET GOL A1006 6
HET NA B5001 1
HET GOL D1003 6
HET GOL D1004 6
HET NA E5002 1
HETNAM GOL GLYCEROL
HETNAM NA SODIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 GOL 6(C3 H8 O3)
FORMUL 11 NA 2(NA 1+)
FORMUL 15 HOH *812(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 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 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 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 VAL A 247 N LEU A 201
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 TRP A 204 N HIS A 188
SHEET 3 C 4 PHE A 241 PRO A 250 -1 O VAL A 247 N LEU A 201
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 ALA B 79 N LEU B 40
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 TYR D 99 N TYR D 7
SHEET 6 H 8 PHE D 109 TYR D 118 -1 O LEU D 110 N ASP D 102
SHEET 7 H 8 LYS D 121 LEU D 126 -1 O LEU D 126 N HIS D 114
SHEET 8 H 8 TRP D 133 THR D 134 -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 LEU D 272 -1 O LEU D 270 N VAL D 261
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 ARG E 81 N ASP E 38
SHEET 4 N 4 LYS E 91 LYS E 94 -1 O LYS E 91 N VAL E 82
SSBOND 1 CYS A 101 CYS A 164 1555 1555 2.11
SSBOND 2 CYS A 203 CYS A 259 1555 1555 2.00
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 1.99
SSBOND 6 CYS E 25 CYS E 80 1555 1555 2.02
LINK OD1 ASN B 83 NA NA B5001 1555 1555 2.65
LINK O HIS B 84 NA NA B5001 1555 1555 2.74
LINK O LEU B 87 NA NA B5001 1555 1555 2.42
LINK NA NA B5001 O HOH B5072 1555 1555 2.21
LINK NA NA B5001 O HOH B5079 1555 1555 2.21
LINK NA NA B5001 O HOH B5088 1555 1555 2.44
LINK OD1 ASN E 83 NA NA E5002 1555 1555 2.80
LINK O HIS E 84 NA NA E5002 1555 1555 2.75
LINK O LEU E 87 NA NA E5002 1555 1555 2.69
LINK NA NA E5002 O HOH E5102 1555 1555 2.66
LINK NA NA E5002 O HOH E5119 1555 1555 2.24
CISPEP 1 TYR A 209 PRO A 210 0 -0.45
CISPEP 2 HIS B 31 PRO B 32 0 -0.47
CISPEP 3 TYR D 209 PRO D 210 0 0.18
CISPEP 4 HIS E 31 PRO E 32 0 -0.75
SITE 1 AC1 6 ASN B 83 HIS B 84 LEU B 87 HOH B5072
SITE 2 AC1 6 HOH B5079 HOH B5088
SITE 1 AC2 5 ASN E 83 HIS E 84 LEU E 87 HOH E5102
SITE 2 AC2 5 HOH E5119
SITE 1 AC3 9 TYR A 84 ASN A 86 HIS A 191 HIS A 192
SITE 2 AC3 9 ALA A 193 HOH A1009 HOH A1079 HOH A1135
SITE 3 AC3 9 HOH A1149
SITE 1 AC4 9 ARG A 6 PHE A 8 TYR A 27 ASP A 29
SITE 2 AC4 9 ASP A 30 HOH A1033 HOH A1118 HOH A1193
SITE 3 AC4 9 TYR B 63
SITE 1 AC5 7 ARG D 6 ASP D 29 ASP D 30 HOH D1036
SITE 2 AC5 7 HOH D1200 HOH D1212 TYR E 63
SITE 1 AC6 9 TYR D 84 ASN D 86 HIS D 191 HIS D 192
SITE 2 AC6 9 ALA D 193 HOH D1009 HOH D1015 HOH D1148
SITE 3 AC6 9 HOH D1248
SITE 1 AC7 5 GLU A 58 TYR A 59 GLY A 62 GLU A 63
SITE 2 AC7 5 LYS A 66
SITE 1 AC8 3 GLU A 166 TRP A 167 ARG A 170
CRYST1 58.400 84.310 84.140 90.00 90.13 90.00 P 1 21 1 4
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 0.017123 0.000000 0.000039 0.00000
SCALE2 0.000000 0.011861 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011885 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
