HEADER TRANSFERASE 20-MAY-09 3HIL
TITLE SAM DOMAIN OF HUMAN EPHRIN TYPE-A RECEPTOR 1 (EPHA1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPHRIN TYPE-A RECEPTOR 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SAM DOMAIN, UNP RESIDUES 911-974;
COMPND 5 SYNONYM: TYROSINE-PROTEIN KINASE RECEPTOR EPH;
COMPND 6 EC: 2.7.10.1;
COMPND 7 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: EPH, EPHA1, EPHT, EPHT1, MGC163163;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL
KEYWDS ATP-BINDING, KINASE, NUCLEOTIDE-BINDING, RECEPTOR, TRANSFERASE,
KEYWDS 2 TYROSINE-PROTEIN KINASE, STERILE ALPHA MOTIF, STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, SGC, GLYCOPROTEIN, MEMBRANE, PHOSPHOPROTEIN,
KEYWDS 4 POLYMORPHISM, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.WALKER,L.YERMEKBAYEVA,C.BUTLER-COLE,J.WEIGELT,C.BOUNTRA,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,S.DHE-PAGANON,STRUCTURAL
AUTHOR 3 GENOMICS CONSORTIUM (SGC)
REVDAT 2 06-SEP-23 3HIL 1 REMARK SEQADV
REVDAT 1 09-JUN-09 3HIL 0
JRNL AUTH J.R.WALKER,L.YERMEKBAYEVA,C.BUTLER-COLE,J.WEIGELT,C.BOUNTRA,
JRNL AUTH 2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,S.DHE-PAGANON
JRNL TITL SAM DOMAIN OF HUMAN EPHRIN TYPE-A RECEPTOR 1 (EPHA1).
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 8696
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.279
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 437
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 620
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 37
REMARK 3 BIN FREE R VALUE : 0.4430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 992
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 36
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.18000
REMARK 3 B22 (A**2) : 0.18000
REMARK 3 B33 (A**2) : -0.27000
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): 0.208
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.199
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.136
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.648
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1054 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1429 ; 1.393 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 131 ; 5.281 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 43 ;35.988 ;22.791
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 191 ;15.215 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;25.019 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 162 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 785 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 647 ; 0.694 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1047 ; 1.264 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 407 ; 2.271 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 382 ; 3.477 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 21
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 902 A 909
REMARK 3 ORIGIN FOR THE GROUP (A): -12.9544 4.9099 -1.9297
REMARK 3 T TENSOR
REMARK 3 T11: 0.2304 T22: 0.1450
REMARK 3 T33: 0.1765 T12: -0.0388
REMARK 3 T13: 0.0123 T23: 0.0925
REMARK 3 L TENSOR
REMARK 3 L11: 1.0242 L22: 10.0443
REMARK 3 L33: 9.2382 L12: -1.3026
REMARK 3 L13: -0.0619 L23: 3.0710
REMARK 3 S TENSOR
REMARK 3 S11: -0.0964 S12: 0.2296 S13: 0.3417
REMARK 3 S21: -0.6776 S22: 0.3496 S23: -0.1936
REMARK 3 S31: -0.6529 S32: 0.4857 S33: -0.2532
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 910 A 914
REMARK 3 ORIGIN FOR THE GROUP (A): -18.1048 3.2680 0.5654
REMARK 3 T TENSOR
REMARK 3 T11: 0.1844 T22: 0.1176
REMARK 3 T33: 0.1599 T12: 0.0363
REMARK 3 T13: 0.0069 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 6.5038 L22: 9.5791
REMARK 3 L33: 9.0960 L12: 3.7523
REMARK 3 L13: 0.8813 L23: 1.5641
REMARK 3 S TENSOR
REMARK 3 S11: 0.0826 S12: 0.4150 S13: 0.4863
REMARK 3 S21: -0.4371 S22: 0.0195 S23: 0.1116
REMARK 3 S31: -0.3108 S32: -0.0661 S33: -0.1021
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 915 A 919
REMARK 3 ORIGIN FOR THE GROUP (A): -22.6769 1.0600 4.6947
REMARK 3 T TENSOR
REMARK 3 T11: 0.1693 T22: 0.1161
REMARK 3 T33: 0.1366 T12: 0.0577
REMARK 3 T13: 0.0230 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 5.4688 L22: 6.1704
REMARK 3 L33: 9.6153 L12: 0.0809
REMARK 3 L13: -0.7371 L23: 6.7402
REMARK 3 S TENSOR
REMARK 3 S11: 0.1375 S12: 0.0524 S13: 0.3277
REMARK 3 S21: -0.2099 S22: -0.1871 S23: 0.3029
REMARK 3 S31: -0.2558 S32: -0.6034 S33: 0.0496
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 920 A 924
REMARK 3 ORIGIN FOR THE GROUP (A): -18.7497 6.6231 10.9442
REMARK 3 T TENSOR
REMARK 3 T11: 0.3323 T22: 0.1024
REMARK 3 T33: 0.3259 T12: 0.0512
REMARK 3 T13: 0.1247 T23: -0.0583
REMARK 3 L TENSOR
REMARK 3 L11: 7.1099 L22: 1.3996
REMARK 3 L33: 2.3624 L12: 1.3084
REMARK 3 L13: 2.4568 L23: 1.7732
REMARK 3 S TENSOR
REMARK 3 S11: 0.3303 S12: -0.2506 S13: 0.5558
REMARK 3 S21: -0.3201 S22: -0.2354 S23: -0.1039
REMARK 3 S31: -0.3473 S32: -0.2689 S33: -0.0950
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 925 A 930
REMARK 3 ORIGIN FOR THE GROUP (A): -12.5848 11.2297 10.0817
REMARK 3 T TENSOR
REMARK 3 T11: 0.4573 T22: 0.1568
REMARK 3 T33: 0.4123 T12: -0.0043
REMARK 3 T13: 0.0369 T23: -0.1147
REMARK 3 L TENSOR
REMARK 3 L11: 9.9490 L22: 9.1692
REMARK 3 L33: 2.3580 L12: 1.8558
REMARK 3 L13: -4.2082 L23: -3.0375
REMARK 3 S TENSOR
REMARK 3 S11: 0.4894 S12: -0.3473 S13: 1.6124
REMARK 3 S21: -0.0367 S22: 0.1076 S23: 0.0529
REMARK 3 S31: -0.1987 S32: 0.0939 S33: -0.5970
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 931 A 937
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5406 5.1834 4.4940
REMARK 3 T TENSOR
REMARK 3 T11: 0.1807 T22: 0.1435
REMARK 3 T33: 0.2727 T12: -0.0923
REMARK 3 T13: 0.0351 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 9.1280 L22: 9.1060
REMARK 3 L33: 6.1530 L12: -1.8666
REMARK 3 L13: 2.1978 L23: -0.2167
REMARK 3 S TENSOR
REMARK 3 S11: 0.1888 S12: 0.2811 S13: 0.7043
REMARK 3 S21: -0.1856 S22: 0.0142 S23: -0.3637
REMARK 3 S31: -0.7531 S32: 0.7717 S33: -0.2030
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 938 A 947
REMARK 3 ORIGIN FOR THE GROUP (A): -11.2822 0.4471 15.7318
REMARK 3 T TENSOR
REMARK 3 T11: 0.2754 T22: 0.3062
REMARK 3 T33: 0.1994 T12: -0.1059
REMARK 3 T13: -0.0494 T23: -0.1188
REMARK 3 L TENSOR
REMARK 3 L11: 3.7882 L22: 4.1225
REMARK 3 L33: 9.7965 L12: -1.5109
REMARK 3 L13: -4.6611 L23: 1.2582
REMARK 3 S TENSOR
REMARK 3 S11: 0.4608 S12: -0.7305 S13: 0.3056
REMARK 3 S21: 0.4125 S22: -0.1673 S23: -0.2197
REMARK 3 S31: -0.7385 S32: 0.8123 S33: -0.2934
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 948 A 953
REMARK 3 ORIGIN FOR THE GROUP (A): -19.5815 -4.0501 14.5827
REMARK 3 T TENSOR
REMARK 3 T11: 0.1210 T22: 0.1511
REMARK 3 T33: 0.1206 T12: 0.0480
REMARK 3 T13: 0.0551 T23: -0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 7.0450 L22: 7.7715
REMARK 3 L33: 5.2701 L12: 4.3809
REMARK 3 L13: -1.8146 L23: -2.2574
REMARK 3 S TENSOR
REMARK 3 S11: 0.0402 S12: -0.4586 S13: 0.1143
REMARK 3 S21: 0.1471 S22: -0.2148 S23: -0.0304
REMARK 3 S31: 0.1220 S32: -0.1153 S33: 0.1746
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 954 A 958
REMARK 3 ORIGIN FOR THE GROUP (A): -15.6610 -5.5794 8.8000
REMARK 3 T TENSOR
REMARK 3 T11: 0.1527 T22: 0.1291
REMARK 3 T33: 0.1327 T12: 0.0114
REMARK 3 T13: 0.0184 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 1.5225 L22: 1.5095
REMARK 3 L33: 9.4188 L12: -1.4398
REMARK 3 L13: 1.0453 L23: 0.1406
REMARK 3 S TENSOR
REMARK 3 S11: -0.0241 S12: -0.1441 S13: -0.0933
REMARK 3 S21: 0.0539 S22: 0.1212 S23: 0.0939
REMARK 3 S31: 0.1664 S32: -0.1598 S33: -0.0970
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 959 A 964
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6427 -3.9812 1.5876
REMARK 3 T TENSOR
REMARK 3 T11: 0.1667 T22: 0.1935
REMARK 3 T33: 0.1326 T12: -0.0212
REMARK 3 T13: 0.0119 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 3.4418 L22: 4.9268
REMARK 3 L33: 6.1620 L12: -3.4266
REMARK 3 L13: -2.2154 L23: -0.4106
REMARK 3 S TENSOR
REMARK 3 S11: 0.1771 S12: -0.1003 S13: 0.3363
REMARK 3 S21: -0.0684 S22: 0.0767 S23: -0.3023
REMARK 3 S31: -0.3148 S32: 0.3168 S33: -0.2538
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 903 B 909
REMARK 3 ORIGIN FOR THE GROUP (A): -26.4161 -6.9659 -4.8031
REMARK 3 T TENSOR
REMARK 3 T11: 0.0688 T22: 0.2602
REMARK 3 T33: 0.3865 T12: 0.0769
REMARK 3 T13: -0.1112 T23: -0.1144
REMARK 3 L TENSOR
REMARK 3 L11: 7.3129 L22: 5.9365
REMARK 3 L33: 8.6350 L12: 1.2185
REMARK 3 L13: -3.8440 L23: 3.9227
REMARK 3 S TENSOR
REMARK 3 S11: -0.0289 S12: 0.7640 S13: 0.6585
REMARK 3 S21: -0.4275 S22: -0.7877 S23: 1.4007
REMARK 3 S31: -0.1949 S32: -0.8147 S33: 0.8165
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 910 B 913
REMARK 3 ORIGIN FOR THE GROUP (A): -21.5421 -5.9205 -7.4634
REMARK 3 T TENSOR
REMARK 3 T11: 0.1671 T22: 0.2010
REMARK 3 T33: 0.1813 T12: 0.0507
REMARK 3 T13: -0.0570 T23: 0.0286
REMARK 3 L TENSOR
REMARK 3 L11: 9.5268 L22: 8.9188
REMARK 3 L33: 4.5952 L12: -0.9202
REMARK 3 L13: 1.3829 L23: 2.5605
REMARK 3 S TENSOR
REMARK 3 S11: -0.2378 S12: 0.3286 S13: 0.6272
REMARK 3 S21: -0.3549 S22: 0.2370 S23: 0.3688
REMARK 3 S31: -0.3906 S32: -0.6158 S33: 0.0008
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 914 B 918
REMARK 3 ORIGIN FOR THE GROUP (A): -17.1846 -3.9584 -8.7948
REMARK 3 T TENSOR
REMARK 3 T11: 0.2087 T22: 0.1715
REMARK 3 T33: 0.1768 T12: 0.0299
REMARK 3 T13: -0.0318 T23: 0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 0.9793 L22: 5.1375
REMARK 3 L33: 9.7935 L12: 0.5493
REMARK 3 L13: -2.4216 L23: 2.9265
REMARK 3 S TENSOR
REMARK 3 S11: 0.0587 S12: 0.0573 S13: 0.1438
REMARK 3 S21: -0.3858 S22: -0.0320 S23: 0.4392
REMARK 3 S31: -0.4844 S32: -0.2109 S33: -0.0267
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 919 B 923
REMARK 3 ORIGIN FOR THE GROUP (A): -16.8978 -10.7287 -15.5239
REMARK 3 T TENSOR
REMARK 3 T11: 0.3071 T22: 0.4956
REMARK 3 T33: 0.1598 T12: -0.0507
REMARK 3 T13: -0.1250 T23: 0.0583
REMARK 3 L TENSOR
REMARK 3 L11: 1.6228 L22: 6.0783
REMARK 3 L33: 9.8093 L12: 0.8453
REMARK 3 L13: 3.8763 L23: 3.0356
REMARK 3 S TENSOR
REMARK 3 S11: -0.3914 S12: 0.2754 S13: 0.2186
REMARK 3 S21: -0.7246 S22: -0.1343 S23: 0.1992
REMARK 3 S31: -0.9842 S32: 0.2148 S33: 0.5258
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 924 B 930
REMARK 3 ORIGIN FOR THE GROUP (A): -23.1721 -17.3572 -13.2058
REMARK 3 T TENSOR
REMARK 3 T11: 0.1369 T22: 0.1774
REMARK 3 T33: 0.1640 T12: 0.0038
REMARK 3 T13: -0.0518 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 7.7941 L22: 7.6565
REMARK 3 L33: 7.0129 L12: 4.1105
REMARK 3 L13: 2.2432 L23: 1.1044
REMARK 3 S TENSOR
REMARK 3 S11: -0.0569 S12: 0.4519 S13: 0.3076
REMARK 3 S21: -0.1399 S22: 0.0418 S23: 0.5133
REMARK 3 S31: -0.1421 S32: -0.4105 S33: 0.0150
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 931 B 936
REMARK 3 ORIGIN FOR THE GROUP (A): -25.2796 -16.4415 -3.6606
REMARK 3 T TENSOR
REMARK 3 T11: 0.1345 T22: 0.1963
REMARK 3 T33: 0.2212 T12: -0.0244
REMARK 3 T13: 0.0092 T23: -0.0336
REMARK 3 L TENSOR
REMARK 3 L11: 10.1270 L22: 6.3650
REMARK 3 L33: 7.3647 L12: -2.7086
REMARK 3 L13: 1.6129 L23: 0.8869
REMARK 3 S TENSOR
REMARK 3 S11: -0.0059 S12: -0.1842 S13: 0.0455
REMARK 3 S21: 0.2221 S22: -0.0735 S23: 0.5350
REMARK 3 S31: -0.0641 S32: -0.4990 S33: 0.0794
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 937 B 941
REMARK 3 ORIGIN FOR THE GROUP (A): -13.6677 -21.7400 -4.7721
REMARK 3 T TENSOR
REMARK 3 T11: 0.1428 T22: 0.1303
REMARK 3 T33: 0.1370 T12: -0.0152
REMARK 3 T13: -0.0361 T23: 0.0202
REMARK 3 L TENSOR
REMARK 3 L11: 8.8705 L22: 8.3789
REMARK 3 L33: 10.1888 L12: -2.1807
REMARK 3 L13: -3.8544 L23: 4.8431
REMARK 3 S TENSOR
REMARK 3 S11: -0.2253 S12: 0.0127 S13: -0.3075
REMARK 3 S21: 0.1848 S22: 0.0400 S23: 0.1202
REMARK 3 S31: 0.2079 S32: -0.1293 S33: 0.1853
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 942 B 945
REMARK 3 ORIGIN FOR THE GROUP (A): -12.3397 -21.6177 -10.9445
REMARK 3 T TENSOR
REMARK 3 T11: 0.1590 T22: 0.1815
REMARK 3 T33: 0.1662 T12: 0.0079
REMARK 3 T13: -0.0003 T23: -0.0203
REMARK 3 L TENSOR
REMARK 3 L11: 9.5954 L22: 6.6918
REMARK 3 L33: 8.0450 L12: 6.8662
REMARK 3 L13: 7.4238 L23: 7.3351
REMARK 3 S TENSOR
REMARK 3 S11: -0.0772 S12: 0.0872 S13: -0.7029
REMARK 3 S21: 0.0734 S22: 0.3565 S23: -0.2770
REMARK 3 S31: 0.0809 S32: 0.3919 S33: -0.2793
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 946 B 952
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9988 -14.6118 -11.6833
REMARK 3 T TENSOR
REMARK 3 T11: 0.1565 T22: 0.1448
REMARK 3 T33: 0.0686 T12: -0.0113
REMARK 3 T13: 0.0097 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 9.0072 L22: 6.5559
REMARK 3 L33: 3.9882 L12: 5.6456
REMARK 3 L13: 3.2673 L23: 3.3294
REMARK 3 S TENSOR
REMARK 3 S11: -0.4006 S12: 0.3821 S13: -0.1322
REMARK 3 S21: -0.5501 S22: 0.4731 S23: -0.1615
REMARK 3 S31: -0.3669 S32: 0.3015 S33: -0.0725
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 953 B 959
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8131 -10.7241 -4.8353
REMARK 3 T TENSOR
REMARK 3 T11: 0.1268 T22: 0.1155
REMARK 3 T33: 0.0805 T12: 0.0021
REMARK 3 T13: -0.0192 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 7.4597 L22: 2.0687
REMARK 3 L33: 8.4969 L12: 0.8606
REMARK 3 L13: -2.6432 L23: 2.0778
REMARK 3 S TENSOR
REMARK 3 S11: -0.1062 S12: 0.3161 S13: 0.1503
REMARK 3 S21: -0.2722 S22: 0.2177 S23: 0.0311
REMARK 3 S31: -0.1353 S32: 0.0693 S33: -0.1115
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 960 B 964
REMARK 3 ORIGIN FOR THE GROUP (A): -17.8724 -11.4317 1.7002
REMARK 3 T TENSOR
REMARK 3 T11: 0.0815 T22: 0.0922
REMARK 3 T33: 0.1133 T12: 0.0189
REMARK 3 T13: -0.0050 T23: 0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 7.9391 L22: 4.8512
REMARK 3 L33: 10.5994 L12: 2.1156
REMARK 3 L13: -2.1897 L23: 0.2393
REMARK 3 S TENSOR
REMARK 3 S11: 0.0620 S12: -0.1642 S13: -0.0800
REMARK 3 S21: 0.2195 S22: -0.0524 S23: 0.1258
REMARK 3 S31: 0.2840 S32: -0.0495 S33: -0.0096
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. 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 3HIL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000053178.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91700
REMARK 200 MONOCHROMATOR : HORIZONTAL BENT SI(111),
REMARK 200 ASYMMETRICALLY CUT WITH WATER
REMARK 200 COOLED CU BLOCK
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9138
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.50
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 43.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.84000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.640
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 ENTRY 2QKQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 3350, 0.3 M MG(NO4)2. PRIOR TO
REMARK 280 SETTING UP CRYSTALLIZATION PLATES, CHYMOTRYPSIN WAS ADDED TO THE
REMARK 280 PROTEIN SAMPLE AT A FINAL CONCENTRATION OF 0.57 MICROMOLAR., PH
REMARK 280 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.1K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 27.10233
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 54.20467
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 54.20467
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 27.10233
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 MET A 883
REMARK 465 HIS A 884
REMARK 465 HIS A 885
REMARK 465 HIS A 886
REMARK 465 HIS A 887
REMARK 465 HIS A 888
REMARK 465 HIS A 889
REMARK 465 SER A 890
REMARK 465 SER A 891
REMARK 465 GLY A 892
REMARK 465 ARG A 893
REMARK 465 GLU A 894
REMARK 465 ASN A 895
REMARK 465 LEU A 896
REMARK 465 TYR A 897
REMARK 465 PHE A 898
REMARK 465 GLN A 899
REMARK 465 GLY A 900
REMARK 465 ASP A 901
REMARK 465 MET B 883
REMARK 465 HIS B 884
REMARK 465 HIS B 885
REMARK 465 HIS B 886
REMARK 465 HIS B 887
REMARK 465 HIS B 888
REMARK 465 HIS B 889
REMARK 465 SER B 890
REMARK 465 SER B 891
REMARK 465 GLY B 892
REMARK 465 ARG B 893
REMARK 465 GLU B 894
REMARK 465 ASN B 895
REMARK 465 LEU B 896
REMARK 465 TYR B 897
REMARK 465 PHE B 898
REMARK 465 GLN B 899
REMARK 465 GLY B 900
REMARK 465 ASP B 901
REMARK 465 GLY B 902
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 ARG A 906 CD NE CZ NH1 NH2
REMARK 470 GLU A 937 CD OE1 OE2
REMARK 470 GLU A 941 CG CD OE1 OE2
REMARK 470 GLN A 945 CG CD OE1 NE2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 2
DBREF 3HIL A 901 964 UNP P21709 EPHA1_HUMAN 911 974
DBREF 3HIL B 901 964 UNP P21709 EPHA1_HUMAN 911 974
SEQADV 3HIL MET A 883 UNP P21709 EXPRESSION TAG
SEQADV 3HIL HIS A 884 UNP P21709 EXPRESSION TAG
SEQADV 3HIL HIS A 885 UNP P21709 EXPRESSION TAG
SEQADV 3HIL HIS A 886 UNP P21709 EXPRESSION TAG
SEQADV 3HIL HIS A 887 UNP P21709 EXPRESSION TAG
SEQADV 3HIL HIS A 888 UNP P21709 EXPRESSION TAG
SEQADV 3HIL HIS A 889 UNP P21709 EXPRESSION TAG
SEQADV 3HIL SER A 890 UNP P21709 EXPRESSION TAG
SEQADV 3HIL SER A 891 UNP P21709 EXPRESSION TAG
SEQADV 3HIL GLY A 892 UNP P21709 EXPRESSION TAG
SEQADV 3HIL ARG A 893 UNP P21709 EXPRESSION TAG
SEQADV 3HIL GLU A 894 UNP P21709 EXPRESSION TAG
SEQADV 3HIL ASN A 895 UNP P21709 EXPRESSION TAG
SEQADV 3HIL LEU A 896 UNP P21709 EXPRESSION TAG
SEQADV 3HIL TYR A 897 UNP P21709 EXPRESSION TAG
SEQADV 3HIL PHE A 898 UNP P21709 EXPRESSION TAG
SEQADV 3HIL GLN A 899 UNP P21709 EXPRESSION TAG
SEQADV 3HIL GLY A 900 UNP P21709 EXPRESSION TAG
SEQADV 3HIL MET B 883 UNP P21709 EXPRESSION TAG
SEQADV 3HIL HIS B 884 UNP P21709 EXPRESSION TAG
SEQADV 3HIL HIS B 885 UNP P21709 EXPRESSION TAG
SEQADV 3HIL HIS B 886 UNP P21709 EXPRESSION TAG
SEQADV 3HIL HIS B 887 UNP P21709 EXPRESSION TAG
SEQADV 3HIL HIS B 888 UNP P21709 EXPRESSION TAG
SEQADV 3HIL HIS B 889 UNP P21709 EXPRESSION TAG
SEQADV 3HIL SER B 890 UNP P21709 EXPRESSION TAG
SEQADV 3HIL SER B 891 UNP P21709 EXPRESSION TAG
SEQADV 3HIL GLY B 892 UNP P21709 EXPRESSION TAG
SEQADV 3HIL ARG B 893 UNP P21709 EXPRESSION TAG
SEQADV 3HIL GLU B 894 UNP P21709 EXPRESSION TAG
SEQADV 3HIL ASN B 895 UNP P21709 EXPRESSION TAG
SEQADV 3HIL LEU B 896 UNP P21709 EXPRESSION TAG
SEQADV 3HIL TYR B 897 UNP P21709 EXPRESSION TAG
SEQADV 3HIL PHE B 898 UNP P21709 EXPRESSION TAG
SEQADV 3HIL GLN B 899 UNP P21709 EXPRESSION TAG
SEQADV 3HIL GLY B 900 UNP P21709 EXPRESSION TAG
SEQRES 1 A 82 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 A 82 LEU TYR PHE GLN GLY ASP GLY ILE PRO TYR ARG THR VAL
SEQRES 3 A 82 SER GLU TRP LEU GLU SER ILE ARG MET LYS ARG TYR ILE
SEQRES 4 A 82 LEU HIS PHE HIS SER ALA GLY LEU ASP THR MET GLU CYS
SEQRES 5 A 82 VAL LEU GLU LEU THR ALA GLU ASP LEU THR GLN MET GLY
SEQRES 6 A 82 ILE THR LEU PRO GLY HIS GLN LYS ARG ILE LEU CYS SER
SEQRES 7 A 82 ILE GLN GLY PHE
SEQRES 1 B 82 MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN
SEQRES 2 B 82 LEU TYR PHE GLN GLY ASP GLY ILE PRO TYR ARG THR VAL
SEQRES 3 B 82 SER GLU TRP LEU GLU SER ILE ARG MET LYS ARG TYR ILE
SEQRES 4 B 82 LEU HIS PHE HIS SER ALA GLY LEU ASP THR MET GLU CYS
SEQRES 5 B 82 VAL LEU GLU LEU THR ALA GLU ASP LEU THR GLN MET GLY
SEQRES 6 B 82 ILE THR LEU PRO GLY HIS GLN LYS ARG ILE LEU CYS SER
SEQRES 7 B 82 ILE GLN GLY PHE
HET CL A 1 1
HET NO3 A 2 4
HETNAM CL CHLORIDE ION
HETNAM NO3 NITRATE ION
FORMUL 3 CL CL 1-
FORMUL 4 NO3 N O3 1-
FORMUL 5 HOH *36(H2 O)
HELIX 1 1 THR A 907 ILE A 915 1 9
HELIX 2 2 MET A 917 ARG A 919 5 3
HELIX 3 3 TYR A 920 ALA A 927 1 8
HELIX 4 4 THR A 931 LEU A 936 5 6
HELIX 5 5 THR A 939 MET A 946 1 8
HELIX 6 6 LEU A 950 PHE A 964 1 15
HELIX 7 7 THR B 907 ILE B 915 1 9
HELIX 8 8 MET B 917 ARG B 919 5 3
HELIX 9 9 TYR B 920 ALA B 927 1 8
HELIX 10 10 THR B 931 LEU B 936 5 6
HELIX 11 11 THR B 939 MET B 946 1 8
HELIX 12 12 LEU B 950 GLY B 963 1 14
CISPEP 1 GLY A 902 ILE A 903 0 6.77
SITE 1 AC1 2 THR A 931 GLU A 933
SITE 1 AC2 4 ARG A 916 MET A 917 LYS A 918 ARG A 919
CRYST1 52.286 52.286 81.307 90.00 90.00 120.00 P 31 2 1 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 0.019126 0.011042 0.000000 0.00000
SCALE2 0.000000 0.022084 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012299 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
