HEADER TRANSFERASE/SIGNALING PROTEIN 30-APR-08 3CZU
TITLE CRYSTAL STRUCTURE OF THE HUMAN EPHRIN A2- EPHRIN A1 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPHRIN TYPE-A RECEPTOR 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: LIGAND BINDING DOMAIN: RESIDUES 23-202;
COMPND 5 SYNONYM: TYROSINE-PROTEIN KINASE RECEPTOR ECK, EPITHELIAL CELL
COMPND 6 KINASE;
COMPND 7 EC: 2.7.10.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: EPHRIN-A1;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: RESIDUES 17-171;
COMPND 13 SYNONYM: EPH-RELATED RECEPTOR TYROSINE KINASE LIGAND 1, LERK-1,
COMPND 14 IMMEDIATE EARLY RESPONSE PROTEIN B61, TUMOR NECROSIS FACTOR, ALPHA-
COMPND 15 INDUCED PROTEIN 4;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_TAXID: 9606;
SOURCE 4 GENE: EPHA2, ECK;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFHMSP-LIC-N;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: EFNA1, EPLG1, LERK1, TNFAIP4;
SOURCE 16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 17 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PFHMSP-LIC-N
KEYWDS ATP-BINDING, KINASE, NUCLEOTIDE-BINDING, RECEPTOR, TRANSFERASE,
KEYWDS 2 PHOSPHORYLATION, TRANSMEMBRANE, TYROSINE-PROTEIN KINASE,
KEYWDS 3 GLYCOPROTEIN, STRUCTURAL GENOMICS CONSORTIUM, SGC, PHOSPHOPROTEIN,
KEYWDS 4 GPI-ANCHOR, LIPOPROTEIN, TRANSFERASE-SIGNALING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.WALKER,L.YERMEKBAYEVA,A.SEITOVA,C.BUTLER-COLE,C.BOUNTRA,
AUTHOR 2 M.WIKSTROM,C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,S.DHE-PAGANON,
AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 5 13-JUL-11 3CZU 1 VERSN
REVDAT 4 30-JUN-10 3CZU 1 JRNL
REVDAT 3 09-JUN-10 3CZU 1 JRNL
REVDAT 2 24-FEB-09 3CZU 1 VERSN
REVDAT 1 12-AUG-08 3CZU 0
JRNL AUTH J.P.HIMANEN,L.YERMEKBAYEVA,P.W.JANES,J.R.WALKER,K.XU,
JRNL AUTH 2 L.ATAPATTU,K.R.RAJASHANKAR,A.MENSINGA,M.LACKMANN,
JRNL AUTH 3 D.B.NIKOLOV,S.DHE-PAGANON
JRNL TITL ARCHITECTURE OF EPH RECEPTOR CLUSTERS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 107 10860 2010
JRNL REFN ISSN 0027-8424
JRNL PMID 20505120
JRNL DOI 10.1073/PNAS.1004148107
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 17120
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 938
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.72
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1212
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.2490
REMARK 3 BIN FREE R VALUE SET COUNT : 62
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2473
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 72
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.19000
REMARK 3 B22 (A**2) : 0.19000
REMARK 3 B33 (A**2) : -0.28000
REMARK 3 B12 (A**2) : 0.09000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.325
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.237
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.177
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.245
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2606 ; 0.009 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3542 ; 1.225 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 306 ; 6.590 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 133 ;35.890 ;23.985
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 415 ;16.557 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;15.660 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 376 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2008 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 972 ; 0.191 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1732 ; 0.313 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 110 ; 0.102 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 21 ; 0.154 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.219 ; 0.200
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): 1565 ; 1.006 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2466 ; 1.703 ; 4.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1198 ; 2.206 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1076 ; 3.590 ; 7.000
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 : 20
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 27 A 39
REMARK 3 ORIGIN FOR THE GROUP (A): -58.1074 -6.6098 12.2467
REMARK 3 T TENSOR
REMARK 3 T11: 0.2015 T22: 0.1889
REMARK 3 T33: 0.3155 T12: -0.0915
REMARK 3 T13: 0.0645 T23: -0.0280
REMARK 3 L TENSOR
REMARK 3 L11: 3.3913 L22: 12.7192
REMARK 3 L33: 7.0482 L12: -6.5392
REMARK 3 L13: -1.0068 L23: 1.0790
REMARK 3 S TENSOR
REMARK 3 S11: 0.6961 S12: -0.3725 S13: -1.3543
REMARK 3 S21: -0.5038 S22: 0.0484 S23: 1.2196
REMARK 3 S31: 0.3602 S32: -0.5992 S33: -0.7445
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 40 A 54
REMARK 3 ORIGIN FOR THE GROUP (A): -41.0256 -1.0844 8.6363
REMARK 3 T TENSOR
REMARK 3 T11: 0.2963 T22: 0.2449
REMARK 3 T33: 0.1596 T12: 0.0450
REMARK 3 T13: 0.1308 T23: -0.0647
REMARK 3 L TENSOR
REMARK 3 L11: 9.7950 L22: 13.0796
REMARK 3 L33: 4.5110 L12: -0.7884
REMARK 3 L13: 0.6334 L23: -1.3898
REMARK 3 S TENSOR
REMARK 3 S11: 0.2807 S12: 0.7198 S13: 0.3649
REMARK 3 S21: -0.8784 S22: -0.0942 S23: -0.9349
REMARK 3 S31: -0.0168 S32: 0.6224 S33: -0.1866
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 55 A 64
REMARK 3 ORIGIN FOR THE GROUP (A): -44.8404 -16.9217 18.6600
REMARK 3 T TENSOR
REMARK 3 T11: 0.2841 T22: 0.1342
REMARK 3 T33: 0.1587 T12: -0.0617
REMARK 3 T13: 0.0689 T23: -0.0420
REMARK 3 L TENSOR
REMARK 3 L11: 13.1730 L22: 5.6575
REMARK 3 L33: 10.4444 L12: -7.6568
REMARK 3 L13: -3.1970 L23: 5.2744
REMARK 3 S TENSOR
REMARK 3 S11: -0.8329 S12: -0.3386 S13: -1.1570
REMARK 3 S21: 0.3786 S22: 0.6714 S23: 0.7772
REMARK 3 S31: 0.6939 S32: -0.6313 S33: 0.1615
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 65 A 81
REMARK 3 ORIGIN FOR THE GROUP (A): -37.7661 1.4059 16.6161
REMARK 3 T TENSOR
REMARK 3 T11: 0.2541 T22: 0.1541
REMARK 3 T33: 0.2018 T12: -0.0686
REMARK 3 T13: 0.1214 T23: -0.0863
REMARK 3 L TENSOR
REMARK 3 L11: 3.2395 L22: 6.7864
REMARK 3 L33: 6.4702 L12: -1.8754
REMARK 3 L13: 2.4824 L23: -3.9314
REMARK 3 S TENSOR
REMARK 3 S11: 0.0655 S12: 0.2769 S13: 0.6157
REMARK 3 S21: 0.7532 S22: -0.1249 S23: -0.3638
REMARK 3 S31: -0.5778 S32: 0.7553 S33: 0.0594
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 82 A 105
REMARK 3 ORIGIN FOR THE GROUP (A): -54.5138 1.6596 15.1282
REMARK 3 T TENSOR
REMARK 3 T11: 0.1982 T22: 0.2147
REMARK 3 T33: 0.2720 T12: 0.0329
REMARK 3 T13: 0.1043 T23: -0.0336
REMARK 3 L TENSOR
REMARK 3 L11: 2.6589 L22: 2.4419
REMARK 3 L33: 3.2006 L12: -0.8529
REMARK 3 L13: -0.2931 L23: -0.4490
REMARK 3 S TENSOR
REMARK 3 S11: 0.1189 S12: 0.2156 S13: 0.1776
REMARK 3 S21: 0.0225 S22: -0.0815 S23: 0.5680
REMARK 3 S31: -0.2840 S32: -0.7301 S33: -0.0374
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 106 A 113
REMARK 3 ORIGIN FOR THE GROUP (A): -30.1525 1.5259 30.7857
REMARK 3 T TENSOR
REMARK 3 T11: 0.5900 T22: 0.6596
REMARK 3 T33: 0.5702 T12: -0.0388
REMARK 3 T13: 0.0164 T23: -0.0757
REMARK 3 L TENSOR
REMARK 3 L11: 12.3581 L22: 10.7635
REMARK 3 L33: 42.7430 L12: 4.6342
REMARK 3 L13: 20.3430 L23: 16.7685
REMARK 3 S TENSOR
REMARK 3 S11: -1.3110 S12: 1.0406 S13: 1.8369
REMARK 3 S21: -1.3246 S22: 0.2845 S23: -2.4803
REMARK 3 S31: -2.4073 S32: 3.6113 S33: 1.0265
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 : A 114 A 152
REMARK 3 ORIGIN FOR THE GROUP (A): -47.5162 7.6842 15.3629
REMARK 3 T TENSOR
REMARK 3 T11: 0.2363 T22: 0.0067
REMARK 3 T33: 0.2551 T12: -0.0299
REMARK 3 T13: 0.1051 T23: -0.0836
REMARK 3 L TENSOR
REMARK 3 L11: 3.0808 L22: 3.0902
REMARK 3 L33: 11.2399 L12: -1.6615
REMARK 3 L13: 2.6785 L23: -3.0400
REMARK 3 S TENSOR
REMARK 3 S11: -0.0735 S12: -0.0915 S13: 0.5740
REMARK 3 S21: 0.2355 S22: 0.0943 S23: -0.0464
REMARK 3 S31: -0.7970 S32: -0.2930 S33: -0.0208
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 : A 153 A 166
REMARK 3 ORIGIN FOR THE GROUP (A): -43.2074 -9.4946 30.6354
REMARK 3 T TENSOR
REMARK 3 T11: 0.2895 T22: 0.1002
REMARK 3 T33: 0.1057 T12: -0.0641
REMARK 3 T13: 0.0625 T23: -0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 4.3884 L22: 7.3115
REMARK 3 L33: 10.1233 L12: -0.8871
REMARK 3 L13: 3.2113 L23: -2.9960
REMARK 3 S TENSOR
REMARK 3 S11: -0.1130 S12: -0.6685 S13: -0.4042
REMARK 3 S21: 1.3672 S22: 0.0492 S23: -0.3331
REMARK 3 S31: 0.3008 S32: 0.3730 S33: 0.0638
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 167 A 176
REMARK 3 ORIGIN FOR THE GROUP (A): -60.8776 9.1108 13.0299
REMARK 3 T TENSOR
REMARK 3 T11: 0.2628 T22: 0.2055
REMARK 3 T33: 0.3701 T12: 0.1012
REMARK 3 T13: 0.1686 T23: -0.0147
REMARK 3 L TENSOR
REMARK 3 L11: 6.2965 L22: 6.6067
REMARK 3 L33: 0.7103 L12: -4.4719
REMARK 3 L13: 0.2864 L23: 1.3432
REMARK 3 S TENSOR
REMARK 3 S11: 0.3164 S12: -0.3921 S13: 0.2178
REMARK 3 S21: 0.0650 S22: 0.5538 S23: 1.3658
REMARK 3 S31: -1.7703 S32: -1.4517 S33: -0.8702
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 177 A 201
REMARK 3 ORIGIN FOR THE GROUP (A): -53.2273 1.3171 15.5057
REMARK 3 T TENSOR
REMARK 3 T11: 0.2259 T22: 0.2002
REMARK 3 T33: 0.2058 T12: 0.0377
REMARK 3 T13: 0.1258 T23: -0.0740
REMARK 3 L TENSOR
REMARK 3 L11: 4.2582 L22: 4.9406
REMARK 3 L33: 2.9159 L12: -1.8207
REMARK 3 L13: 0.4512 L23: -0.9483
REMARK 3 S TENSOR
REMARK 3 S11: 0.1409 S12: -0.1205 S13: -0.0026
REMARK 3 S21: 0.0999 S22: 0.0900 S23: 0.4754
REMARK 3 S31: -0.2401 S32: -0.5194 S33: -0.2309
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 18 B 30
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0548 -20.6808 4.4233
REMARK 3 T TENSOR
REMARK 3 T11: 0.1868 T22: 0.2668
REMARK 3 T33: 0.1518 T12: -0.0026
REMARK 3 T13: 0.1842 T23: -0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 5.4551 L22: 9.6686
REMARK 3 L33: 7.8113 L12: -0.2726
REMARK 3 L13: 0.3989 L23: 7.1825
REMARK 3 S TENSOR
REMARK 3 S11: -0.1791 S12: 0.6328 S13: 0.1007
REMARK 3 S21: -0.8523 S22: 0.3557 S23: -0.6125
REMARK 3 S31: -0.2390 S32: 0.4141 S33: -0.1766
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 31 B 40
REMARK 3 ORIGIN FOR THE GROUP (A): -21.6639 -25.6666 8.3968
REMARK 3 T TENSOR
REMARK 3 T11: 0.1627 T22: 0.3399
REMARK 3 T33: 0.2854 T12: -0.0552
REMARK 3 T13: 0.2422 T23: -0.0923
REMARK 3 L TENSOR
REMARK 3 L11: 3.1405 L22: 24.2792
REMARK 3 L33: 10.0831 L12: -0.3240
REMARK 3 L13: 1.6531 L23: 14.7752
REMARK 3 S TENSOR
REMARK 3 S11: 0.0195 S12: -0.0786 S13: -0.1378
REMARK 3 S21: -0.8436 S22: 0.1714 S23: -1.6919
REMARK 3 S31: 0.3486 S32: 1.1540 S33: -0.1910
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 41 B 53
REMARK 3 ORIGIN FOR THE GROUP (A): -30.7129 -14.4633 8.5813
REMARK 3 T TENSOR
REMARK 3 T11: 0.1832 T22: 0.1656
REMARK 3 T33: 0.2334 T12: -0.0601
REMARK 3 T13: 0.1160 T23: -0.0568
REMARK 3 L TENSOR
REMARK 3 L11: 2.0183 L22: 2.9127
REMARK 3 L33: 5.5599 L12: 0.5532
REMARK 3 L13: 1.1316 L23: 1.5113
REMARK 3 S TENSOR
REMARK 3 S11: 0.2079 S12: 0.6215 S13: 0.5135
REMARK 3 S21: -0.6241 S22: -0.0536 S23: -0.5588
REMARK 3 S31: -0.2317 S32: 0.7008 S33: -0.1543
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 54 B 68
REMARK 3 ORIGIN FOR THE GROUP (A): -41.9904 -31.0528 1.0843
REMARK 3 T TENSOR
REMARK 3 T11: 0.3173 T22: 0.1509
REMARK 3 T33: 0.1020 T12: 0.0601
REMARK 3 T13: -0.0706 T23: -0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 10.4266 L22: 10.8405
REMARK 3 L33: 15.3941 L12: 4.2516
REMARK 3 L13: 0.2095 L23: 2.7553
REMARK 3 S TENSOR
REMARK 3 S11: 0.2145 S12: 1.0351 S13: -0.2160
REMARK 3 S21: -1.6327 S22: 0.0922 S23: 0.3829
REMARK 3 S31: 0.5432 S32: -0.8853 S33: -0.3068
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 69 B 76
REMARK 3 ORIGIN FOR THE GROUP (A): -29.5248 -25.4741 21.5982
REMARK 3 T TENSOR
REMARK 3 T11: 0.1503 T22: 0.2484
REMARK 3 T33: 0.1402 T12: 0.0024
REMARK 3 T13: -0.0013 T23: -0.0416
REMARK 3 L TENSOR
REMARK 3 L11: 12.1341 L22: 13.8983
REMARK 3 L33: 1.2032 L12: -3.0962
REMARK 3 L13: -3.5055 L23: -0.6857
REMARK 3 S TENSOR
REMARK 3 S11: 0.0822 S12: -1.9992 S13: 0.1648
REMARK 3 S21: 0.5496 S22: 0.0526 S23: -1.3872
REMARK 3 S31: 0.2612 S32: -0.3032 S33: -0.1349
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 77 B 91
REMARK 3 ORIGIN FOR THE GROUP (A): -34.2370 -26.4094 20.5791
REMARK 3 T TENSOR
REMARK 3 T11: 0.1612 T22: 0.1645
REMARK 3 T33: 0.1353 T12: -0.0626
REMARK 3 T13: 0.0131 T23: -0.1036
REMARK 3 L TENSOR
REMARK 3 L11: 4.0695 L22: 10.9653
REMARK 3 L33: 4.9057 L12: -2.2309
REMARK 3 L13: -1.2264 L23: -2.7730
REMARK 3 S TENSOR
REMARK 3 S11: 0.1587 S12: -0.2792 S13: 0.0267
REMARK 3 S21: 0.5904 S22: -0.0289 S23: -0.2225
REMARK 3 S31: 0.0691 S32: 0.2817 S33: -0.1298
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 92 B 101
REMARK 3 ORIGIN FOR THE GROUP (A): -45.0779 -22.4113 2.9885
REMARK 3 T TENSOR
REMARK 3 T11: 0.3783 T22: 0.0345
REMARK 3 T33: 0.2437 T12: 0.0356
REMARK 3 T13: -0.0272 T23: -0.0353
REMARK 3 L TENSOR
REMARK 3 L11: 10.6340 L22: 8.0814
REMARK 3 L33: 7.9286 L12: -1.0970
REMARK 3 L13: -0.7029 L23: -7.8525
REMARK 3 S TENSOR
REMARK 3 S11: 0.1995 S12: 0.0807 S13: 1.0434
REMARK 3 S21: -0.5520 S22: 0.0568 S23: 0.8050
REMARK 3 S31: -0.9114 S32: -0.1234 S33: -0.2563
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 102 B 110
REMARK 3 ORIGIN FOR THE GROUP (A): -33.3563 -12.5239 13.7938
REMARK 3 T TENSOR
REMARK 3 T11: 0.1690 T22: 0.1481
REMARK 3 T33: 0.2538 T12: 0.0223
REMARK 3 T13: 0.0629 T23: -0.0613
REMARK 3 L TENSOR
REMARK 3 L11: 10.9548 L22: 16.0046
REMARK 3 L33: 11.3982 L12: 9.1242
REMARK 3 L13: 5.1483 L23: 11.3847
REMARK 3 S TENSOR
REMARK 3 S11: -0.1606 S12: -0.4597 S13: 0.7622
REMARK 3 S21: -0.2914 S22: 0.0540 S23: 0.2411
REMARK 3 S31: -0.3560 S32: 0.2640 S33: 0.1065
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 111 B 119
REMARK 3 ORIGIN FOR THE GROUP (A): -35.6191 -10.1625 24.1578
REMARK 3 T TENSOR
REMARK 3 T11: 0.2739 T22: 0.2103
REMARK 3 T33: 0.1863 T12: -0.0842
REMARK 3 T13: 0.0009 T23: -0.1153
REMARK 3 L TENSOR
REMARK 3 L11: 23.1790 L22: 1.8734
REMARK 3 L33: 6.3017 L12: 6.3562
REMARK 3 L13: -10.0035 L23: -2.2345
REMARK 3 S TENSOR
REMARK 3 S11: -0.4075 S12: -0.9039 S13: -0.4803
REMARK 3 S21: -0.3327 S22: 0.4891 S23: -0.5081
REMARK 3 S31: -0.5601 S32: 0.3747 S33: -0.0815
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 120 B 149
REMARK 3 ORIGIN FOR THE GROUP (A): -28.2023 -24.4671 15.2514
REMARK 3 T TENSOR
REMARK 3 T11: 0.1373 T22: 0.3179
REMARK 3 T33: 0.1896 T12: 0.0011
REMARK 3 T13: 0.0495 T23: -0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 4.2634 L22: 8.6255
REMARK 3 L33: 1.7810 L12: 2.1371
REMARK 3 L13: -0.1236 L23: 0.3126
REMARK 3 S TENSOR
REMARK 3 S11: 0.0012 S12: 0.1135 S13: 0.0052
REMARK 3 S21: -0.0871 S22: 0.2285 S23: -0.8577
REMARK 3 S31: -0.0092 S32: 0.5573 S33: -0.2297
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS
REMARK 4
REMARK 4 3CZU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-08.
REMARK 100 THE RCSB ID CODE IS RCSB047413.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18122
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 20.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.7400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 21.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.71400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.509
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRIES 3C8X, 1SHW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14.9% PEG 4000, 0.1M SODIUM CITRATE PH
REMARK 280 5.6, 20% ISOPROPANOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 290.9K, PH 5.60
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 136.58600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 68.29300
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 102.43950
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 34.14650
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 170.73250
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 136.58600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 68.29300
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 34.14650
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 102.43950
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 170.73250
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.6 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 ALA A -4
REMARK 465 ALA A -3
REMARK 465 PRO A -2
REMARK 465 GLU A -1
REMARK 465 HIS A 0
REMARK 465 HIS A 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 ASP A 6
REMARK 465 TYR A 7
REMARK 465 ASP A 8
REMARK 465 ILE A 9
REMARK 465 PRO A 10
REMARK 465 THR A 11
REMARK 465 THR A 12
REMARK 465 GLU A 13
REMARK 465 ASN A 14
REMARK 465 LEU A 15
REMARK 465 TYR A 16
REMARK 465 PHE A 17
REMARK 465 GLN A 18
REMARK 465 GLY A 19
REMARK 465 ALA A 20
REMARK 465 MET A 21
REMARK 465 ASP A 22
REMARK 465 ALA A 23
REMARK 465 ALA A 24
REMARK 465 GLN A 25
REMARK 465 GLY A 26
REMARK 465 PRO A 202
REMARK 465 ALA B -10
REMARK 465 ALA B -9
REMARK 465 PRO B -8
REMARK 465 GLU B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 ASP B 0
REMARK 465 TYR B 1
REMARK 465 ASP B 2
REMARK 465 ILE B 3
REMARK 465 PRO B 4
REMARK 465 THR B 5
REMARK 465 THR B 6
REMARK 465 GLU B 7
REMARK 465 ASN B 8
REMARK 465 LEU B 9
REMARK 465 TYR B 10
REMARK 465 PHE B 11
REMARK 465 GLN B 12
REMARK 465 GLY B 13
REMARK 465 ALA B 14
REMARK 465 MET B 15
REMARK 465 ASP B 16
REMARK 465 ALA B 17
REMARK 465 ASP B 56
REMARK 465 HIS B 57
REMARK 465 LYS B 150
REMARK 465 ILE B 151
REMARK 465 THR B 152
REMARK 465 HIS B 153
REMARK 465 SER B 154
REMARK 465 PRO B 155
REMARK 465 GLN B 156
REMARK 465 ALA B 157
REMARK 465 HIS B 158
REMARK 465 VAL B 159
REMARK 465 ASN B 160
REMARK 465 PRO B 161
REMARK 465 GLN B 162
REMARK 465 GLU B 163
REMARK 465 LYS B 164
REMARK 465 ARG B 165
REMARK 465 LEU B 166
REMARK 465 ALA B 167
REMARK 465 ALA B 168
REMARK 465 ASP B 169
REMARK 465 ASP B 170
REMARK 465 PRO B 171
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 A 27 CD CE NZ
REMARK 470 LYS A 50 CG CD CE NZ
REMARK 470 ASP A 76 CG OD1 OD2
REMARK 470 ARG A 137 CZ NH1 NH2
REMARK 470 LYS A 176 CG CD CE NZ
REMARK 470 LYS A 200 CE NZ
REMARK 470 ASN B 34 CG OD1
REMARK 470 LYS B 98 CG CD CE NZ
REMARK 470 LYS B 118 NZ
REMARK 470 ARG B 139 CZ NH1 NH2
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 CYS A 70 54.13 -148.25
REMARK 500 ASP A 76 105.14 -56.83
REMARK 500 SER A 113 20.01 -70.61
REMARK 500 ASP B 19 -30.12 -143.79
REMARK 500 TYR B 37 108.56 -45.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MQB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF EPHRIN A2 (EPHA2)
REMARK 900 RECEPTOR PROTEIN KINASE
REMARK 900 RELATED ID: 3C8X RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE LIGAND BINDING DOMAIN OF HUMAN
REMARK 900 EPHRIN A2 (EPHA2) RECEPTOR PROTEIN KINASE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS STATE THAT THE CORRECT SEQUENCE IS PROVIDED IN
REMARK 999 GENBANK ENTRY NP_004422.
DBREF 3CZU A 23 202 UNP P29317 EPHA2_HUMAN 23 202
DBREF 3CZU B 17 171 UNP P20827 EFNA1_HUMAN 17 171
SEQADV 3CZU ALA A -4 UNP P29317 EXPRESSION TAG
SEQADV 3CZU ALA A -3 UNP P29317 EXPRESSION TAG
SEQADV 3CZU PRO A -2 UNP P29317 EXPRESSION TAG
SEQADV 3CZU GLU A -1 UNP P29317 EXPRESSION TAG
SEQADV 3CZU HIS A 0 UNP P29317 EXPRESSION TAG
SEQADV 3CZU HIS A 1 UNP P29317 EXPRESSION TAG
SEQADV 3CZU HIS A 2 UNP P29317 EXPRESSION TAG
SEQADV 3CZU HIS A 3 UNP P29317 EXPRESSION TAG
SEQADV 3CZU HIS A 4 UNP P29317 EXPRESSION TAG
SEQADV 3CZU HIS A 5 UNP P29317 EXPRESSION TAG
SEQADV 3CZU ASP A 6 UNP P29317 EXPRESSION TAG
SEQADV 3CZU TYR A 7 UNP P29317 EXPRESSION TAG
SEQADV 3CZU ASP A 8 UNP P29317 EXPRESSION TAG
SEQADV 3CZU ILE A 9 UNP P29317 EXPRESSION TAG
SEQADV 3CZU PRO A 10 UNP P29317 EXPRESSION TAG
SEQADV 3CZU THR A 11 UNP P29317 EXPRESSION TAG
SEQADV 3CZU THR A 12 UNP P29317 EXPRESSION TAG
SEQADV 3CZU GLU A 13 UNP P29317 EXPRESSION TAG
SEQADV 3CZU ASN A 14 UNP P29317 EXPRESSION TAG
SEQADV 3CZU LEU A 15 UNP P29317 EXPRESSION TAG
SEQADV 3CZU TYR A 16 UNP P29317 EXPRESSION TAG
SEQADV 3CZU PHE A 17 UNP P29317 EXPRESSION TAG
SEQADV 3CZU GLN A 18 UNP P29317 EXPRESSION TAG
SEQADV 3CZU GLY A 19 UNP P29317 EXPRESSION TAG
SEQADV 3CZU ALA A 20 UNP P29317 EXPRESSION TAG
SEQADV 3CZU MET A 21 UNP P29317 EXPRESSION TAG
SEQADV 3CZU ASP A 22 UNP P29317 EXPRESSION TAG
SEQADV 3CZU ILE A 94 UNP P29317 ASN 94 SEE REMARK 999
SEQADV 3CZU PHE A 95 UNP P29317 ASN 95 SEE REMARK 999
SEQADV 3CZU ILE A 96 UNP P29317 PHE 96 SEE REMARK 999
SEQADV 3CZU LYS A 99 UNP P29317 ASN 99 SEE REMARK 999
SEQADV 3CZU ALA B -10 UNP P20827 EXPRESSION TAG
SEQADV 3CZU ALA B -9 UNP P20827 EXPRESSION TAG
SEQADV 3CZU PRO B -8 UNP P20827 EXPRESSION TAG
SEQADV 3CZU GLU B -7 UNP P20827 EXPRESSION TAG
SEQADV 3CZU HIS B -6 UNP P20827 EXPRESSION TAG
SEQADV 3CZU HIS B -5 UNP P20827 EXPRESSION TAG
SEQADV 3CZU HIS B -4 UNP P20827 EXPRESSION TAG
SEQADV 3CZU HIS B -3 UNP P20827 EXPRESSION TAG
SEQADV 3CZU HIS B -2 UNP P20827 EXPRESSION TAG
SEQADV 3CZU HIS B -1 UNP P20827 EXPRESSION TAG
SEQADV 3CZU ASP B 0 UNP P20827 EXPRESSION TAG
SEQADV 3CZU TYR B 1 UNP P20827 EXPRESSION TAG
SEQADV 3CZU ASP B 2 UNP P20827 EXPRESSION TAG
SEQADV 3CZU ILE B 3 UNP P20827 EXPRESSION TAG
SEQADV 3CZU PRO B 4 UNP P20827 EXPRESSION TAG
SEQADV 3CZU THR B 5 UNP P20827 EXPRESSION TAG
SEQADV 3CZU THR B 6 UNP P20827 EXPRESSION TAG
SEQADV 3CZU GLU B 7 UNP P20827 EXPRESSION TAG
SEQADV 3CZU ASN B 8 UNP P20827 EXPRESSION TAG
SEQADV 3CZU LEU B 9 UNP P20827 EXPRESSION TAG
SEQADV 3CZU TYR B 10 UNP P20827 EXPRESSION TAG
SEQADV 3CZU PHE B 11 UNP P20827 EXPRESSION TAG
SEQADV 3CZU GLN B 12 UNP P20827 EXPRESSION TAG
SEQADV 3CZU GLY B 13 UNP P20827 EXPRESSION TAG
SEQADV 3CZU ALA B 14 UNP P20827 EXPRESSION TAG
SEQADV 3CZU MET B 15 UNP P20827 EXPRESSION TAG
SEQADV 3CZU ASP B 16 UNP P20827 EXPRESSION TAG
SEQADV 3CZU VAL B 159 UNP P20827 ASP 159 VARIANT
SEQRES 1 A 207 ALA ALA PRO GLU HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 A 207 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 A 207 ASP ALA ALA GLN GLY LYS GLU VAL VAL LEU LEU ASP PHE
SEQRES 4 A 207 ALA ALA ALA GLY GLY GLU LEU GLY TRP LEU THR HIS PRO
SEQRES 5 A 207 TYR GLY LYS GLY TRP ASP LEU MET GLN ASN ILE MET ASN
SEQRES 6 A 207 ASP MET PRO ILE TYR MET TYR SER VAL CYS ASN VAL MET
SEQRES 7 A 207 SER GLY ASP GLN ASP ASN TRP LEU ARG THR ASN TRP VAL
SEQRES 8 A 207 TYR ARG GLY GLU ALA GLU ARG ILE PHE ILE GLU LEU LYS
SEQRES 9 A 207 PHE THR VAL ARG ASP CYS ASN SER PHE PRO GLY GLY ALA
SEQRES 10 A 207 SER SER CYS LYS GLU THR PHE ASN LEU TYR TYR ALA GLU
SEQRES 11 A 207 SER ASP LEU ASP TYR GLY THR ASN PHE GLN LYS ARG LEU
SEQRES 12 A 207 PHE THR LYS ILE ASP THR ILE ALA PRO ASP GLU ILE THR
SEQRES 13 A 207 VAL SER SER ASP PHE GLU ALA ARG HIS VAL LYS LEU ASN
SEQRES 14 A 207 VAL GLU GLU ARG SER VAL GLY PRO LEU THR ARG LYS GLY
SEQRES 15 A 207 PHE TYR LEU ALA PHE GLN ASP ILE GLY ALA CYS VAL ALA
SEQRES 16 A 207 LEU LEU SER VAL ARG VAL TYR TYR LYS LYS CYS PRO
SEQRES 1 B 182 ALA ALA PRO GLU HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 B 182 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 B 182 ASP ALA ALA ASP ARG HIS THR VAL PHE TRP ASN SER SER
SEQRES 4 B 182 ASN PRO LYS PHE ARG ASN GLU ASP TYR THR ILE HIS VAL
SEQRES 5 B 182 GLN LEU ASN ASP TYR VAL ASP ILE ILE CYS PRO HIS TYR
SEQRES 6 B 182 GLU ASP HIS SER VAL ALA ASP ALA ALA MET GLU GLN TYR
SEQRES 7 B 182 ILE LEU TYR LEU VAL GLU HIS GLU GLU TYR GLN LEU CYS
SEQRES 8 B 182 GLN PRO GLN SER LYS ASP GLN VAL ARG TRP GLN CYS ASN
SEQRES 9 B 182 ARG PRO SER ALA LYS HIS GLY PRO GLU LYS LEU SER GLU
SEQRES 10 B 182 LYS PHE GLN ARG PHE THR PRO PHE THR LEU GLY LYS GLU
SEQRES 11 B 182 PHE LYS GLU GLY HIS SER TYR TYR TYR ILE SER LYS PRO
SEQRES 12 B 182 ILE HIS GLN HIS GLU ASP ARG CYS LEU ARG LEU LYS VAL
SEQRES 13 B 182 THR VAL SER GLY LYS ILE THR HIS SER PRO GLN ALA HIS
SEQRES 14 B 182 VAL ASN PRO GLN GLU LYS ARG LEU ALA ALA ASP ASP PRO
MODRES 3CZU ASN B 26 ASN GLYCOSYLATION SITE
HET NAG B 500 14
HET NAG B 501 14
HET MAN B 502 11
HETNAM NAG N-ACETYL-D-GLUCOSAMINE
HETNAM MAN ALPHA-D-MANNOSE
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 3 MAN C6 H12 O6
FORMUL 4 HOH *72(H2 O)
HELIX 1 1 ALA A 35 GLY A 38 5 4
HELIX 2 2 ASP A 104 PHE A 108 5 5
HELIX 3 3 GLN A 135 PHE A 139 5 5
HELIX 4 4 SER A 153 ALA A 158 1 6
HELIX 5 5 ASN B 29 ARG B 33 5 5
HELIX 6 6 ALA B 60 MET B 64 5 5
HELIX 7 7 GLU B 73 CYS B 80 1 8
HELIX 8 8 SER B 84 ASP B 86 5 3
SHEET 1 A 4 GLU A 28 ASP A 33 0
SHEET 2 A 4 CYS A 188 LYS A 199 -1 O VAL A 196 N LEU A 31
SHEET 3 A 4 MET A 62 CYS A 70 -1 N TYR A 67 O LEU A 191
SHEET 4 A 4 ASP A 53 MET A 59 -1 N ASN A 57 O ILE A 64
SHEET 1 B 4 GLU A 28 ASP A 33 0
SHEET 2 B 4 CYS A 188 LYS A 199 -1 O VAL A 196 N LEU A 31
SHEET 3 B 4 ILE A 94 VAL A 102 -1 N GLU A 97 O ARG A 195
SHEET 4 B 4 ASN A 164 VAL A 170 -1 O ARG A 168 N ILE A 96
SHEET 1 C 4 LEU A 44 HIS A 46 0
SHEET 2 C 4 ASN A 79 ARG A 82 -1 O TRP A 80 N HIS A 46
SHEET 3 C 4 GLY A 177 ASP A 184 -1 O ASP A 184 N ASN A 79
SHEET 4 C 4 VAL A 86 TYR A 87 -1 N VAL A 86 O PHE A 178
SHEET 1 D 5 LEU A 44 HIS A 46 0
SHEET 2 D 5 ASN A 79 ARG A 82 -1 O TRP A 80 N HIS A 46
SHEET 3 D 5 GLY A 177 ASP A 184 -1 O ASP A 184 N ASN A 79
SHEET 4 D 5 PHE A 119 SER A 126 -1 N TYR A 122 O ALA A 181
SHEET 5 D 5 THR A 140 ILE A 145 -1 O ILE A 145 N PHE A 119
SHEET 1 E 3 ARG B 20 PHE B 24 0
SHEET 2 E 3 TYR B 46 ILE B 50 1 O ASP B 48 N HIS B 21
SHEET 3 E 3 LYS B 103 LYS B 107 -1 O LEU B 104 N ILE B 49
SHEET 1 F 5 THR B 38 VAL B 41 0
SHEET 2 F 5 ARG B 142 VAL B 147 1 O THR B 146 N VAL B 41
SHEET 3 F 5 SER B 125 PRO B 132 -1 N TYR B 126 O VAL B 145
SHEET 4 F 5 TYR B 67 VAL B 72 -1 N TYR B 70 O ILE B 129
SHEET 5 F 5 VAL B 88 CYS B 92 -1 O CYS B 92 N TYR B 67
SSBOND 1 CYS A 70 CYS A 188 1555 1555 2.07
SSBOND 2 CYS A 105 CYS A 115 1555 1555 2.04
SSBOND 3 CYS B 51 CYS B 92 1555 1555 2.08
SSBOND 4 CYS B 80 CYS B 140 1555 1555 2.06
LINK ND2 ASN B 26 C1 NAG B 500 1555 1555 1.44
LINK O4 NAG B 500 C1 NAG B 501 1555 1555 1.43
LINK O4 NAG B 501 C1 MAN B 502 1555 1555 1.45
CISPEP 1 HIS A 46 PRO A 47 0 2.52
CISPEP 2 GLY A 171 PRO A 172 0 -1.28
SITE 1 AC1 6 PHE B 24 ASN B 26 ASN B 29 PRO B 52
SITE 2 AC1 6 HIS B 53 TYR B 54
SITE 1 AC2 3 SER A 113 CYS A 115 LYS A 116
CRYST1 99.431 99.431 204.879 90.00 90.00 120.00 P 65 2 2 12
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 0.010057 0.005807 0.000000 0.00000
SCALE2 0.000000 0.011613 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004881 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
