HEADER SIGNALING PROTEIN/SIGNALING PROTEIN REGU31-AUG-10 3OP0
TITLE CRYSTAL STRUCTURE OF CBL-C (CBL-3) TKB DOMAIN IN COMPLEX WITH EGFR
TITLE 2 PY1069 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIGNAL TRANSDUCTION PROTEIN CBL-C;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CBL N-TERMINAL, UNP RESIDUES 9-323;
COMPND 5 SYNONYM: SH3-BINDING PROTEIN CBL-C, SH3-BINDING PROTEIN CBL-3, RING
COMPND 6 FINGER PROTEIN 57;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;
COMPND 11 CHAIN: C, D;
COMPND 12 FRAGMENT: EGFR, UNP RESIDUES 1066-1076;
COMPND 13 SYNONYM: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-1, PROTO-ONCOGENE C-
COMPND 14 ERBB-1;
COMPND 15 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: CBL3, CBLC, RNF57;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC-CTHF;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, SIGNAL
KEYWDS 2 TRANSDUCTION PROTEIN, SH3-BINDING PROTEIN, SIGNALING PROTEIN-
KEYWDS 3 SIGNALING PROTEIN REGULATOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CHAIKUAD,K.GUO,C.D.O.COOPER,V.AYINAMPUDI,T.KROJER,E.UGOCHUKWU,
AUTHOR 2 J.R.C.MUNIZ,M.VOLLMAR,P.CANNING,F.VON DELFT,C.H.ARROWSMITH,
AUTHOR 3 J.WEIGELT,A.M.EDWARDS,C.BOUNTRA,A.BULLOCK,STRUCTURAL GENOMICS
AUTHOR 4 CONSORTIUM (SGC)
REVDAT 4 06-DEC-23 3OP0 1 REMARK
REVDAT 3 06-SEP-23 3OP0 1 REMARK SEQADV LINK
REVDAT 2 08-NOV-17 3OP0 1 REMARK
REVDAT 1 20-OCT-10 3OP0 0
JRNL AUTH A.CHAIKUAD,K.GUO,C.D.O.COOPER,V.AYINAMPUDI,T.KROJER,
JRNL AUTH 2 E.UGOCHUKWU,J.R.C.MUNIZ,M.VOLLMAR,P.CANNING,F.VON DELFT,
JRNL AUTH 3 C.H.ARROWSMITH,J.WEIGELT,A.M.EDWARDS,C.BOUNTRA,A.BULLOCK
JRNL TITL CRYSTAL STRUCTURE OF CBL-C (CBL-3) TKB DOMAIN IN COMPLEX
JRNL TITL 2 WITH EGFR PY1069 PEPTIDE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.52 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.52
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 28157
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1505
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) : 2.52
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.58
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2084
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.95
REMARK 3 BIN R VALUE (WORKING SET) : 0.3370
REMARK 3 BIN FREE R VALUE SET COUNT : 99
REMARK 3 BIN FREE R VALUE : 0.3270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5163
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 282
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.68000
REMARK 3 B22 (A**2) : 2.68000
REMARK 3 B33 (A**2) : -4.03000
REMARK 3 B12 (A**2) : 1.34000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.301
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.238
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.618
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.902
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5358 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3708 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7260 ; 1.543 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8949 ; 1.170 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 678 ;14.708 ; 5.118
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 245 ;33.330 ;22.571
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 831 ;16.615 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 50 ;18.520 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 774 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6008 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1146 ; 0.002 ; 0.020
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): 3316 ; 0.320 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1338 ; 0.100 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5285 ; 0.546 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2042 ; 1.162 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1969 ; 1.573 ; 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 B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 11 A 32 1
REMARK 3 1 B 11 B 32 1
REMARK 3 2 A 32 A 40 1
REMARK 3 2 B 32 B 40 1
REMARK 3 3 A 41 A 63 1
REMARK 3 3 B 41 B 63 1
REMARK 3 4 A 64 A 70 4
REMARK 3 4 B 64 B 70 4
REMARK 3 5 A 71 A 99 1
REMARK 3 5 B 71 B 99 1
REMARK 3 6 A 111 A 330 1
REMARK 3 6 B 111 B 330 1
REMARK 3 7 A 100 A 110 1
REMARK 3 7 B 100 B 110 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 4251 ; 0.040 ; 0.050
REMARK 3 MEDIUM POSITIONAL 1 A (A): 64 ; 0.010 ; 0.500
REMARK 3 TIGHT THERMAL 1 A (A**2): 4251 ; 0.040 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 64 ; 0.020 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 2
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 1066 C 1068 1
REMARK 3 1 D 1066 D 1068 1
REMARK 3 2 C 1070 C 1075 1
REMARK 3 2 D 1070 D 1075 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 C (A): 114 ; 0.010 ; 0.050
REMARK 3 TIGHT THERMAL 2 C (A**2): 114 ; 0.020 ; 0.500
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
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 10 A 26
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6472 40.3530 43.7005
REMARK 3 T TENSOR
REMARK 3 T11: 0.2077 T22: 0.2078
REMARK 3 T33: 0.2457 T12: 0.0242
REMARK 3 T13: -0.0096 T23: -0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 7.6107 L22: 7.8327
REMARK 3 L33: 7.5313 L12: -3.2577
REMARK 3 L13: 2.9538 L23: -3.1727
REMARK 3 S TENSOR
REMARK 3 S11: -0.1295 S12: 0.2645 S13: -0.7576
REMARK 3 S21: 0.3070 S22: -0.0682 S23: -0.6966
REMARK 3 S31: 0.2842 S32: 0.3517 S33: 0.1977
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 27 A 42
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2649 60.2073 35.1401
REMARK 3 T TENSOR
REMARK 3 T11: 0.8477 T22: 0.4649
REMARK 3 T33: 0.6521 T12: -0.0141
REMARK 3 T13: -0.1547 T23: -0.0752
REMARK 3 L TENSOR
REMARK 3 L11: 6.1848 L22: 14.5114
REMARK 3 L33: 3.9505 L12: 8.6246
REMARK 3 L13: 2.8119 L23: 6.4624
REMARK 3 S TENSOR
REMARK 3 S11: -0.5123 S12: -0.3198 S13: 0.8656
REMARK 3 S21: -1.8588 S22: 0.1576 S23: 0.9235
REMARK 3 S31: -1.4332 S32: 0.3641 S33: 0.3547
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 43 A 94
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3259 41.6300 40.0000
REMARK 3 T TENSOR
REMARK 3 T11: 0.0549 T22: 0.1439
REMARK 3 T33: 0.0752 T12: -0.0078
REMARK 3 T13: -0.0310 T23: -0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 3.1022 L22: 6.1257
REMARK 3 L33: 8.6382 L12: -0.2586
REMARK 3 L13: -0.3486 L23: 0.8143
REMARK 3 S TENSOR
REMARK 3 S11: 0.0691 S12: -0.1628 S13: -0.2423
REMARK 3 S21: 0.4461 S22: -0.0064 S23: -0.0311
REMARK 3 S31: 0.3796 S32: 0.0071 S33: -0.0627
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 95 A 110
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5962 63.0209 28.2185
REMARK 3 T TENSOR
REMARK 3 T11: 1.1612 T22: 1.0044
REMARK 3 T33: 0.8499 T12: 0.0186
REMARK 3 T13: -0.3272 T23: -0.0636
REMARK 3 L TENSOR
REMARK 3 L11: 0.2976 L22: 23.5718
REMARK 3 L33: 1.0320 L12: -1.9435
REMARK 3 L13: -0.5207 L23: 2.3227
REMARK 3 S TENSOR
REMARK 3 S11: 0.2361 S12: -0.0664 S13: 0.3421
REMARK 3 S21: 1.6670 S22: 0.1390 S23: -4.1470
REMARK 3 S31: -0.7490 S32: 0.0654 S33: -0.3751
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 111 A 238
REMARK 3 ORIGIN FOR THE GROUP (A): -9.9254 38.6655 25.5468
REMARK 3 T TENSOR
REMARK 3 T11: 0.1409 T22: 0.1787
REMARK 3 T33: 0.0328 T12: -0.0375
REMARK 3 T13: 0.0199 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 2.4219 L22: 1.1789
REMARK 3 L33: 1.6584 L12: -0.4267
REMARK 3 L13: 0.5587 L23: 0.7735
REMARK 3 S TENSOR
REMARK 3 S11: 0.0097 S12: 0.0657 S13: -0.0673
REMARK 3 S21: -0.0226 S22: -0.0161 S23: 0.1200
REMARK 3 S31: 0.0562 S32: -0.1745 S33: 0.0064
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 239 A 278
REMARK 3 ORIGIN FOR THE GROUP (A): -16.4068 57.0765 21.6195
REMARK 3 T TENSOR
REMARK 3 T11: 0.2586 T22: 0.2188
REMARK 3 T33: 0.1776 T12: 0.0696
REMARK 3 T13: -0.0223 T23: -0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 3.8586 L22: 3.9917
REMARK 3 L33: 3.0189 L12: -0.3867
REMARK 3 L13: 1.4708 L23: -0.0449
REMARK 3 S TENSOR
REMARK 3 S11: -0.0407 S12: 0.2700 S13: 0.4659
REMARK 3 S21: -0.3360 S22: -0.1759 S23: 0.1039
REMARK 3 S31: -0.5571 S32: -0.0833 S33: 0.2166
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 279 A 330
REMARK 3 ORIGIN FOR THE GROUP (A): -26.9152 50.6475 17.3411
REMARK 3 T TENSOR
REMARK 3 T11: 0.3110 T22: 0.4222
REMARK 3 T33: 0.3478 T12: 0.0926
REMARK 3 T13: -0.0597 T23: -0.0344
REMARK 3 L TENSOR
REMARK 3 L11: 1.2766 L22: 8.8521
REMARK 3 L33: 1.5613 L12: 3.1967
REMARK 3 L13: 1.3119 L23: 3.3576
REMARK 3 S TENSOR
REMARK 3 S11: -0.0921 S12: -0.1419 S13: 0.4530
REMARK 3 S21: 0.0377 S22: -0.2172 S23: 0.8403
REMARK 3 S31: -0.1845 S32: -0.2831 S33: 0.3092
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 : B 10 B 26
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6591 40.3668 -12.5090
REMARK 3 T TENSOR
REMARK 3 T11: 0.2290 T22: 0.2125
REMARK 3 T33: 0.2097 T12: -0.0176
REMARK 3 T13: -0.0244 T23: 0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 6.6385 L22: 5.0092
REMARK 3 L33: 5.7540 L12: 1.5873
REMARK 3 L13: 0.2551 L23: 2.8656
REMARK 3 S TENSOR
REMARK 3 S11: -0.2588 S12: -0.1336 S13: -0.6972
REMARK 3 S21: -0.1078 S22: 0.0840 S23: 0.5780
REMARK 3 S31: 0.4538 S32: -0.3234 S33: 0.1748
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 : B 27 B 42
REMARK 3 ORIGIN FOR THE GROUP (A): -2.2635 60.2289 -3.9535
REMARK 3 T TENSOR
REMARK 3 T11: 1.0144 T22: 0.6864
REMARK 3 T33: 0.6424 T12: 0.2571
REMARK 3 T13: -0.0186 T23: 0.1770
REMARK 3 L TENSOR
REMARK 3 L11: 3.3329 L22: 11.7020
REMARK 3 L33: 4.7463 L12: -6.1001
REMARK 3 L13: 3.8048 L23: -7.4215
REMARK 3 S TENSOR
REMARK 3 S11: -0.6500 S12: 0.3061 S13: 0.6667
REMARK 3 S21: 1.7952 S22: 0.0238 S23: -0.8849
REMARK 3 S31: -1.2553 S32: -0.1108 S33: 0.6262
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 : B 43 B 94
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3333 41.6366 -8.8054
REMARK 3 T TENSOR
REMARK 3 T11: 0.0477 T22: 0.1689
REMARK 3 T33: 0.0869 T12: -0.0054
REMARK 3 T13: -0.0299 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 2.9642 L22: 6.3479
REMARK 3 L33: 8.8195 L12: -0.2321
REMARK 3 L13: -0.4492 L23: 0.1020
REMARK 3 S TENSOR
REMARK 3 S11: 0.0305 S12: 0.3306 S13: -0.2500
REMARK 3 S21: -0.3463 S22: -0.0123 S23: 0.1141
REMARK 3 S31: 0.4361 S32: -0.1821 S33: -0.0182
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 95 B 110
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5653 63.0069 2.8742
REMARK 3 T TENSOR
REMARK 3 T11: 1.6472 T22: 0.6597
REMARK 3 T33: 1.4831 T12: 0.1153
REMARK 3 T13: -0.7087 T23: 0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 7.7734 L22: 0.5925
REMARK 3 L33: 4.3031 L12: 2.0996
REMARK 3 L13: -5.7831 L23: -1.5623
REMARK 3 S TENSOR
REMARK 3 S11: 0.9783 S12: 1.0893 S13: 2.1449
REMARK 3 S21: 0.0359 S22: 0.4333 S23: 0.7250
REMARK 3 S31: -0.5810 S32: -0.8157 S33: -1.4116
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 111 B 238
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9290 38.6667 5.6403
REMARK 3 T TENSOR
REMARK 3 T11: 0.1368 T22: 0.1676
REMARK 3 T33: 0.0410 T12: 0.0300
REMARK 3 T13: 0.0118 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 2.2994 L22: 1.2705
REMARK 3 L33: 1.8539 L12: 0.3349
REMARK 3 L13: 0.4277 L23: -0.6111
REMARK 3 S TENSOR
REMARK 3 S11: -0.0140 S12: -0.0415 S13: -0.0752
REMARK 3 S21: 0.0566 S22: -0.0056 S23: -0.0792
REMARK 3 S31: 0.0609 S32: 0.1869 S33: 0.0196
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 239 B 278
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4129 57.0818 9.5686
REMARK 3 T TENSOR
REMARK 3 T11: 0.3010 T22: 0.2166
REMARK 3 T33: 0.1605 T12: -0.0611
REMARK 3 T13: -0.0295 T23: 0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 4.0033 L22: 4.3136
REMARK 3 L33: 2.8503 L12: 0.6758
REMARK 3 L13: 1.8753 L23: 0.3144
REMARK 3 S TENSOR
REMARK 3 S11: -0.1015 S12: -0.2471 S13: 0.4493
REMARK 3 S21: 0.2981 S22: -0.1094 S23: -0.1578
REMARK 3 S31: -0.6745 S32: 0.1289 S33: 0.2109
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 279 B 330
REMARK 3 ORIGIN FOR THE GROUP (A): 26.9233 50.6497 13.8417
REMARK 3 T TENSOR
REMARK 3 T11: 0.3815 T22: 0.5359
REMARK 3 T33: 0.4078 T12: -0.1609
REMARK 3 T13: -0.0268 T23: 0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 1.3950 L22: 8.7490
REMARK 3 L33: 2.2930 L12: -3.4767
REMARK 3 L13: 1.7282 L23: -4.3360
REMARK 3 S TENSOR
REMARK 3 S11: -0.0570 S12: 0.1474 S13: 0.3973
REMARK 3 S21: 0.0365 S22: -0.2446 S23: -0.8821
REMARK 3 S31: -0.1465 S32: 0.3208 S33: 0.3016
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 : C 1066 C 1075
REMARK 3 ORIGIN FOR THE GROUP (A): -23.9311 58.7052 29.8097
REMARK 3 T TENSOR
REMARK 3 T11: 0.6510 T22: 0.4392
REMARK 3 T33: 0.3984 T12: 0.2070
REMARK 3 T13: 0.0874 T23: -0.1150
REMARK 3 L TENSOR
REMARK 3 L11: 51.0178 L22: 13.1312
REMARK 3 L33: 11.9261 L12: 2.7340
REMARK 3 L13: 2.8830 L23: -1.3521
REMARK 3 S TENSOR
REMARK 3 S11: -0.5356 S12: -0.2405 S13: 2.3295
REMARK 3 S21: 1.0593 S22: 0.0668 S23: 1.7128
REMARK 3 S31: -1.1709 S32: -1.0999 S33: 0.4688
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 : D 1066 D 1075
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0689 58.5315 1.4450
REMARK 3 T TENSOR
REMARK 3 T11: 0.6190 T22: 0.6031
REMARK 3 T33: 0.6900 T12: -0.1821
REMARK 3 T13: 0.2089 T23: 0.2140
REMARK 3 L TENSOR
REMARK 3 L11: 37.6289 L22: 7.5373
REMARK 3 L33: 12.1629 L12: 2.6199
REMARK 3 L13: -0.7711 L23: 9.3810
REMARK 3 S TENSOR
REMARK 3 S11: -0.2662 S12: 0.0707 S13: 0.7599
REMARK 3 S21: -1.3992 S22: 0.9606 S23: -0.6010
REMARK 3 S31: -1.6722 S32: 1.2242 S33: -0.6944
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3OP0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061392.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : SI (111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : KIRKPATRICK BAEZ BIMORPH MIRROR
REMARK 200 PAIR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC Q315 3X3 CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29742
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.520
REMARK 200 RESOLUTION RANGE LOW (A) : 49.450
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.52
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.74500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 ID: 1FBV CHAIN A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% JEFFAMINE M-600, 0.1M HEPES, PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
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
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 127.72067
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 63.86033
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 95.79050
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 31.93017
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 159.65083
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 8
REMARK 465 GLY A 9
REMARK 465 MET B 8
REMARK 465 GLY B 9
REMARK 465 ALA C 1076
REMARK 465 ALA D 1076
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 10 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 33 CG1 CG2
REMARK 470 VAL A 39 CG1 CG2
REMARK 470 ARG A 101 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 103 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 104 CG CD NE CZ NH1 NH2
REMARK 470 SER A 105 OG
REMARK 470 LYS A 303 CD CE NZ
REMARK 470 ARG B 10 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 33 CG1 CG2
REMARK 470 VAL B 39 CG1 CG2
REMARK 470 ARG B 101 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 103 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 104 CG CD NE CZ NH1 NH2
REMARK 470 SER B 105 OG
REMARK 470 ASN B 107 CG OD1 ND2
REMARK 470 LYS B 303 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 463 O HOH B 464 1.72
REMARK 500 O HOH A 445 O HOH A 446 1.73
REMARK 500 OD1 CSD B 189 O HOH B 476 1.86
REMARK 500 OD1 CSD A 189 O HOH A 461 1.95
REMARK 500 O HOH A 445 O HOH A 461 2.10
REMARK 500 O HOH B 463 O HOH B 476 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 VAL A 94 CB VAL A 94 CG1 -0.130
REMARK 500 VAL A 94 CB VAL A 94 CG2 -0.153
REMARK 500 VAL B 94 CB VAL B 94 CG1 -0.135
REMARK 500 VAL B 94 CB VAL B 94 CG2 -0.138
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 20 CD - NE - CZ ANGL. DEV. = 13.1 DEGREES
REMARK 500 ARG A 20 CD - NE - CZ ANGL. DEV. = 11.8 DEGREES
REMARK 500 ARG A 20 NE - CZ - NH1 ANGL. DEV. = -9.8 DEGREES
REMARK 500 ARG A 20 NE - CZ - NH1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ARG A 20 NE - CZ - NH2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG A 20 NE - CZ - NH2 ANGL. DEV. = 10.2 DEGREES
REMARK 500 ARG A 92 CD - NE - CZ ANGL. DEV. = 11.4 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH1 ANGL. DEV. = -9.7 DEGREES
REMARK 500 ARG A 92 NE - CZ - NH2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 VAL A 94 CG1 - CB - CG2 ANGL. DEV. = -13.4 DEGREES
REMARK 500 ARG B 20 CD - NE - CZ ANGL. DEV. = 13.1 DEGREES
REMARK 500 ARG B 20 CD - NE - CZ ANGL. DEV. = 11.7 DEGREES
REMARK 500 ARG B 20 NE - CZ - NH1 ANGL. DEV. = 8.3 DEGREES
REMARK 500 ARG B 20 NE - CZ - NH1 ANGL. DEV. = 8.1 DEGREES
REMARK 500 ARG B 20 NE - CZ - NH2 ANGL. DEV. = -9.8 DEGREES
REMARK 500 ARG B 20 NE - CZ - NH2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 ARG B 92 CD - NE - CZ ANGL. DEV. = 14.2 DEGREES
REMARK 500 ARG B 92 NE - CZ - NH1 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ARG B 92 NE - CZ - NH2 ANGL. DEV. = -10.4 DEGREES
REMARK 500 VAL B 94 CG1 - CB - CG2 ANGL. DEV. = -12.4 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 CYS A 32 44.39 -82.55
REMARK 500 ARG A 36 -8.66 -56.87
REMARK 500 GLU A 64 30.15 -96.11
REMARK 500 PRO A 99 -179.02 -67.53
REMARK 500 ARG A 104 -121.68 -131.92
REMARK 500 CSO A 182 -53.34 -135.76
REMARK 500 ASP A 311 19.52 56.74
REMARK 500 GLN B 11 -20.33 -145.75
REMARK 500 CYS B 32 44.13 -83.29
REMARK 500 ARG B 36 -8.33 -56.42
REMARK 500 GLU B 64 31.30 -95.55
REMARK 500 PRO B 99 -178.80 -67.75
REMARK 500 ARG B 104 -121.78 -132.16
REMARK 500 CSO B 182 -52.51 -135.69
REMARK 500 ASP B 311 19.24 58.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 65 GLY A 66 143.61
REMARK 500 ALA B 65 GLY B 66 143.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 20 0.08 SIDE CHAIN
REMARK 500 ARG B 20 0.10 SIDE CHAIN
REMARK 500 ARG B 92 0.10 SIDE CHAIN
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 NI A 1 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CSO A 202 O
REMARK 620 2 CSO A 202 OD 112.5
REMARK 620 3 CSD B 189 OD1 110.9 75.6
REMARK 620 4 CSD B 189 OD2 99.1 139.1 69.0
REMARK 620 5 HOH B 463 O 111.0 113.3 128.6 76.1
REMARK 620 6 HOH B 476 O 170.8 70.6 60.8 74.5 74.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 2 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 199 OD1
REMARK 620 2 THR A 201 OG1 99.2
REMARK 620 3 SER A 203 OG 94.3 82.6
REMARK 620 4 HIS A 205 O 94.4 159.2 80.8
REMARK 620 5 GLU A 210 OE2 94.5 78.6 160.3 116.0
REMARK 620 6 HOH A 331 O 163.0 94.5 97.4 75.4 78.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 331 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CSD A 189 OD1
REMARK 620 2 CSD A 189 OD2 74.6
REMARK 620 3 HOH A 445 O 134.3 79.4
REMARK 620 4 HOH A 461 O 64.4 80.4 74.7
REMARK 620 5 CSO B 202 O 109.9 95.7 109.6 173.7
REMARK 620 6 CSO B 202 OD 76.8 149.2 114.0 77.2 104.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 1 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 199 OD1
REMARK 620 2 THR B 201 OG1 101.9
REMARK 620 3 SER B 203 OG 96.0 80.6
REMARK 620 4 HIS B 205 O 92.7 158.7 82.7
REMARK 620 5 GLU B 210 OE2 95.2 79.7 158.9 114.6
REMARK 620 6 HOH B 471 O 162.4 91.7 97.2 77.5 76.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 331
DBREF 3OP0 A 9 323 UNP Q9ULV8 CBLC_HUMAN 9 323
DBREF 3OP0 B 9 323 UNP Q9ULV8 CBLC_HUMAN 9 323
DBREF 3OP0 C 1066 1076 UNP P00533 EGFR_HUMAN 1066 1076
DBREF 3OP0 D 1066 1076 UNP P00533 EGFR_HUMAN 1066 1076
SEQADV 3OP0 MET A 8 UNP Q9ULV8 EXPRESSION TAG
SEQADV 3OP0 GLU A 64 UNP Q9ULV8 ALA 64 ENGINEERED MUTATION
SEQADV 3OP0 ALA A 324 UNP Q9ULV8 EXPRESSION TAG
SEQADV 3OP0 GLU A 325 UNP Q9ULV8 EXPRESSION TAG
SEQADV 3OP0 ASN A 326 UNP Q9ULV8 EXPRESSION TAG
SEQADV 3OP0 LEU A 327 UNP Q9ULV8 EXPRESSION TAG
SEQADV 3OP0 TYR A 328 UNP Q9ULV8 EXPRESSION TAG
SEQADV 3OP0 PHE A 329 UNP Q9ULV8 EXPRESSION TAG
SEQADV 3OP0 GLN A 330 UNP Q9ULV8 EXPRESSION TAG
SEQADV 3OP0 MET B 8 UNP Q9ULV8 EXPRESSION TAG
SEQADV 3OP0 GLU B 64 UNP Q9ULV8 ALA 64 ENGINEERED MUTATION
SEQADV 3OP0 ALA B 324 UNP Q9ULV8 EXPRESSION TAG
SEQADV 3OP0 GLU B 325 UNP Q9ULV8 EXPRESSION TAG
SEQADV 3OP0 ASN B 326 UNP Q9ULV8 EXPRESSION TAG
SEQADV 3OP0 LEU B 327 UNP Q9ULV8 EXPRESSION TAG
SEQADV 3OP0 TYR B 328 UNP Q9ULV8 EXPRESSION TAG
SEQADV 3OP0 PHE B 329 UNP Q9ULV8 EXPRESSION TAG
SEQADV 3OP0 GLN B 330 UNP Q9ULV8 EXPRESSION TAG
SEQRES 1 A 323 MET GLY ARG GLN TRP GLU GLU ALA ARG ALA LEU GLY ARG
SEQRES 2 A 323 ALA VAL ARG MET LEU GLN ARG LEU GLU GLU GLN CYS VAL
SEQRES 3 A 323 ASP PRO ARG LEU SER VAL SER PRO PRO SER LEU ARG ASP
SEQRES 4 A 323 LEU LEU PRO ARG THR ALA GLN LEU LEU ARG GLU VAL ALA
SEQRES 5 A 323 HIS SER ARG ARG GLU ALA GLY GLY GLY GLY PRO GLY GLY
SEQRES 6 A 323 PRO GLY GLY SER GLY ASP PHE LEU LEU ILE TYR LEU ALA
SEQRES 7 A 323 ASN LEU GLU ALA LYS SER ARG GLN VAL ALA ALA LEU LEU
SEQRES 8 A 323 PRO PRO ARG GLY ARG ARG SER ALA ASN ASP GLU LEU PHE
SEQRES 9 A 323 ARG ALA GLY SER ARG LEU ARG ARG GLN LEU ALA LYS LEU
SEQRES 10 A 323 ALA ILE ILE PHE SER HIS MET HIS ALA GLU LEU HIS ALA
SEQRES 11 A 323 LEU PHE PRO GLY GLY LYS TYR CYS GLY HIS MET TYR GLN
SEQRES 12 A 323 LEU THR LYS ALA PRO ALA HIS THR PHE TRP ARG GLU SER
SEQRES 13 A 323 CYS GLY ALA ARG CYS VAL LEU PRO TRP ALA GLU PHE GLU
SEQRES 14 A 323 SER LEU LEU GLY THR CSO HIS PRO VAL GLU PRO GLY CSD
SEQRES 15 A 323 THR ALA LEU ALA LEU ARG THR THR ILE ASP LEU THR CSO
SEQRES 16 A 323 SER GLY HIS VAL SER ILE PHE GLU PHE ASP VAL PHE THR
SEQRES 17 A 323 ARG LEU PHE GLN PRO TRP PRO THR LEU LEU LYS ASN TRP
SEQRES 18 A 323 GLN LEU LEU ALA VAL ASN HIS PRO GLY TYR MET ALA PHE
SEQRES 19 A 323 LEU THR TYR ASP GLU VAL GLN GLU ARG LEU GLN ALA CYS
SEQRES 20 A 323 ARG ASP LYS PRO GLY SER TYR ILE PHE ARG PRO SER CYS
SEQRES 21 A 323 THR ARG LEU GLY GLN TRP ALA ILE GLY TYR VAL SER SER
SEQRES 22 A 323 ASP GLY SER ILE LEU GLN THR ILE PRO ALA ASN LYS PRO
SEQRES 23 A 323 LEU SER GLN VAL LEU LEU GLU GLY GLN LYS ASP GLY PHE
SEQRES 24 A 323 TYR LEU TYR PRO ASP GLY LYS THR HIS ASN PRO ASP LEU
SEQRES 25 A 323 THR GLU LEU GLY ALA GLU ASN LEU TYR PHE GLN
SEQRES 1 B 323 MET GLY ARG GLN TRP GLU GLU ALA ARG ALA LEU GLY ARG
SEQRES 2 B 323 ALA VAL ARG MET LEU GLN ARG LEU GLU GLU GLN CYS VAL
SEQRES 3 B 323 ASP PRO ARG LEU SER VAL SER PRO PRO SER LEU ARG ASP
SEQRES 4 B 323 LEU LEU PRO ARG THR ALA GLN LEU LEU ARG GLU VAL ALA
SEQRES 5 B 323 HIS SER ARG ARG GLU ALA GLY GLY GLY GLY PRO GLY GLY
SEQRES 6 B 323 PRO GLY GLY SER GLY ASP PHE LEU LEU ILE TYR LEU ALA
SEQRES 7 B 323 ASN LEU GLU ALA LYS SER ARG GLN VAL ALA ALA LEU LEU
SEQRES 8 B 323 PRO PRO ARG GLY ARG ARG SER ALA ASN ASP GLU LEU PHE
SEQRES 9 B 323 ARG ALA GLY SER ARG LEU ARG ARG GLN LEU ALA LYS LEU
SEQRES 10 B 323 ALA ILE ILE PHE SER HIS MET HIS ALA GLU LEU HIS ALA
SEQRES 11 B 323 LEU PHE PRO GLY GLY LYS TYR CYS GLY HIS MET TYR GLN
SEQRES 12 B 323 LEU THR LYS ALA PRO ALA HIS THR PHE TRP ARG GLU SER
SEQRES 13 B 323 CYS GLY ALA ARG CYS VAL LEU PRO TRP ALA GLU PHE GLU
SEQRES 14 B 323 SER LEU LEU GLY THR CSO HIS PRO VAL GLU PRO GLY CSD
SEQRES 15 B 323 THR ALA LEU ALA LEU ARG THR THR ILE ASP LEU THR CSO
SEQRES 16 B 323 SER GLY HIS VAL SER ILE PHE GLU PHE ASP VAL PHE THR
SEQRES 17 B 323 ARG LEU PHE GLN PRO TRP PRO THR LEU LEU LYS ASN TRP
SEQRES 18 B 323 GLN LEU LEU ALA VAL ASN HIS PRO GLY TYR MET ALA PHE
SEQRES 19 B 323 LEU THR TYR ASP GLU VAL GLN GLU ARG LEU GLN ALA CYS
SEQRES 20 B 323 ARG ASP LYS PRO GLY SER TYR ILE PHE ARG PRO SER CYS
SEQRES 21 B 323 THR ARG LEU GLY GLN TRP ALA ILE GLY TYR VAL SER SER
SEQRES 22 B 323 ASP GLY SER ILE LEU GLN THR ILE PRO ALA ASN LYS PRO
SEQRES 23 B 323 LEU SER GLN VAL LEU LEU GLU GLY GLN LYS ASP GLY PHE
SEQRES 24 B 323 TYR LEU TYR PRO ASP GLY LYS THR HIS ASN PRO ASP LEU
SEQRES 25 B 323 THR GLU LEU GLY ALA GLU ASN LEU TYR PHE GLN
SEQRES 1 C 11 LEU GLN ARG PTR SER SER ASP PRO THR GLY ALA
SEQRES 1 D 11 LEU GLN ARG PTR SER SER ASP PRO THR GLY ALA
MODRES 3OP0 CSO A 182 CYS S-HYDROXYCYSTEINE
MODRES 3OP0 CSD A 189 CYS 3-SULFINOALANINE
MODRES 3OP0 CSO A 202 CYS S-HYDROXYCYSTEINE
MODRES 3OP0 CSO B 182 CYS S-HYDROXYCYSTEINE
MODRES 3OP0 CSD B 189 CYS 3-SULFINOALANINE
MODRES 3OP0 CSO B 202 CYS S-HYDROXYCYSTEINE
MODRES 3OP0 PTR C 1069 TYR O-PHOSPHOTYROSINE
MODRES 3OP0 PTR D 1069 TYR O-PHOSPHOTYROSINE
HET CSO A 182 7
HET CSD A 189 8
HET CSO A 202 7
HET CSO B 182 7
HET CSD B 189 8
HET CSO B 202 7
HET PTR C1069 16
HET PTR D1069 16
HET NA A 2 1
HET NI A 1 1
HET NA B 1 1
HET NI B 331 1
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM CSD 3-SULFINOALANINE
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM NA SODIUM ION
HETNAM NI NICKEL (II) ION
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 CSO 4(C3 H7 N O3 S)
FORMUL 1 CSD 2(C3 H7 N O4 S)
FORMUL 3 PTR 2(C9 H12 N O6 P)
FORMUL 5 NA 2(NA 1+)
FORMUL 6 NI 2(NI 2+)
FORMUL 9 HOH *282(H2 O)
HELIX 1 1 TRP A 12 CYS A 32 1 21
HELIX 2 2 SER A 43 GLU A 64 1 22
HELIX 3 3 GLY A 75 LEU A 98 1 24
HELIX 4 4 ASN A 107 ARG A 112 5 6
HELIX 5 5 SER A 115 PHE A 139 1 25
HELIX 6 6 PRO A 140 LYS A 143 5 4
HELIX 7 7 LYS A 153 GLY A 165 1 13
HELIX 8 8 TRP A 172 THR A 181 1 10
HELIX 9 9 GLY A 188 ASP A 199 1 12
HELIX 10 10 ILE A 208 PHE A 218 1 11
HELIX 11 11 PRO A 220 PRO A 222 5 3
HELIX 12 12 THR A 223 ALA A 232 1 10
HELIX 13 13 THR A 243 LEU A 251 1 9
HELIX 14 14 GLN A 252 LYS A 257 5 6
HELIX 15 15 PRO A 293 ASP A 304 1 12
HELIX 16 16 LEU A 319 GLN A 330 1 12
HELIX 17 17 TRP B 12 CYS B 32 1 21
HELIX 18 18 SER B 43 GLU B 64 1 22
HELIX 19 19 GLY B 75 LEU B 98 1 24
HELIX 20 20 ASN B 107 ARG B 112 5 6
HELIX 21 21 SER B 115 PHE B 139 1 25
HELIX 22 22 PRO B 140 LYS B 143 5 4
HELIX 23 23 LYS B 153 GLY B 165 1 13
HELIX 24 24 TRP B 172 THR B 181 1 10
HELIX 25 25 GLY B 188 ASP B 199 1 12
HELIX 26 26 ILE B 208 PHE B 218 1 11
HELIX 27 27 PRO B 220 PRO B 222 5 3
HELIX 28 28 THR B 223 ALA B 232 1 10
HELIX 29 29 THR B 243 LEU B 251 1 9
HELIX 30 30 GLN B 252 LYS B 257 5 6
HELIX 31 31 PRO B 293 ASP B 304 1 12
HELIX 32 32 LEU B 319 GLN B 330 1 12
SHEET 1 A 2 VAL A 169 PRO A 171 0
SHEET 2 A 2 HIS A 205 SER A 207 -1 O VAL A 206 N LEU A 170
SHEET 1 B 4 ILE A 284 THR A 287 0
SHEET 2 B 4 TRP A 273 VAL A 278 -1 N ILE A 275 O THR A 287
SHEET 3 B 4 SER A 260 PRO A 265 -1 N ILE A 262 O GLY A 276
SHEET 4 B 4 TYR A 309 PRO A 310 1 O TYR A 309 N TYR A 261
SHEET 1 C 2 VAL B 169 PRO B 171 0
SHEET 2 C 2 HIS B 205 SER B 207 -1 O VAL B 206 N LEU B 170
SHEET 1 D 4 ILE B 284 THR B 287 0
SHEET 2 D 4 TRP B 273 VAL B 278 -1 N TYR B 277 O LEU B 285
SHEET 3 D 4 SER B 260 PRO B 265 -1 N ILE B 262 O GLY B 276
SHEET 4 D 4 TYR B 309 PRO B 310 1 O TYR B 309 N TYR B 261
LINK C THR A 181 N CSO A 182 1555 1555 1.33
LINK C CSO A 182 N HIS A 183 1555 1555 1.33
LINK C GLY A 188 N CSD A 189 1555 1555 1.33
LINK C CSD A 189 N THR A 190 1555 1555 1.34
LINK C THR A 201 N CSO A 202 1555 1555 1.34
LINK C CSO A 202 N SER A 203 1555 1555 1.33
LINK C THR B 181 N CSO B 182 1555 1555 1.33
LINK C CSO B 182 N HIS B 183 1555 1555 1.33
LINK C GLY B 188 N CSD B 189 1555 1555 1.33
LINK C CSD B 189 N THR B 190 1555 1555 1.33
LINK C THR B 201 N CSO B 202 1555 1555 1.34
LINK C CSO B 202 N SER B 203 1555 1555 1.33
LINK C ARG C1068 N PTR C1069 1555 1555 1.33
LINK C PTR C1069 N SER C1070 1555 1555 1.33
LINK C ARG D1068 N PTR D1069 1555 1555 1.32
LINK C PTR D1069 N SER D1070 1555 1555 1.33
LINK NI NI A 1 O CSO A 202 1555 1555 2.02
LINK NI NI A 1 OD CSO A 202 1555 1555 2.06
LINK NI NI A 1 OD1 CSD B 189 1555 1555 1.91
LINK NI NI A 1 OD2 CSD B 189 1555 1555 2.12
LINK NI NI A 1 O HOH B 463 1555 1555 1.81
LINK NI NI A 1 O HOH B 476 1555 1555 1.75
LINK NA NA A 2 OD1 ASP A 199 1555 1555 2.25
LINK NA NA A 2 OG1 THR A 201 1555 1555 2.26
LINK NA NA A 2 OG SER A 203 1555 1555 2.29
LINK NA NA A 2 O HIS A 205 1555 1555 2.28
LINK NA NA A 2 OE2 GLU A 210 1555 1555 2.25
LINK NA NA A 2 O HOH A 331 1555 1555 2.56
LINK OD1 CSD A 189 NI NI B 331 1555 1555 1.88
LINK OD2 CSD A 189 NI NI B 331 1555 1555 2.10
LINK O HOH A 445 NI NI B 331 1555 1555 1.69
LINK O HOH A 461 NI NI B 331 1555 1555 1.78
LINK NA NA B 1 OD1 ASP B 199 1555 1555 2.24
LINK NA NA B 1 OG1 THR B 201 1555 1555 2.27
LINK NA NA B 1 OG SER B 203 1555 1555 2.27
LINK NA NA B 1 O HIS B 205 1555 1555 2.28
LINK NA NA B 1 OE2 GLU B 210 1555 1555 2.25
LINK NA NA B 1 O HOH B 471 1555 1555 2.57
LINK O CSO B 202 NI NI B 331 1555 1555 2.03
LINK OD CSO B 202 NI NI B 331 1555 1555 2.07
CISPEP 1 LEU A 37 SER A 38 0 -13.65
CISPEP 2 SER A 38 VAL A 39 0 -18.12
CISPEP 3 PRO A 41 PRO A 42 0 0.59
CISPEP 4 GLY A 67 GLY A 68 0 6.13
CISPEP 5 PRO A 99 PRO A 100 0 -12.77
CISPEP 6 ARG A 101 GLY A 102 0 0.64
CISPEP 7 ALA A 106 ASN A 107 0 2.46
CISPEP 8 GLN A 219 PRO A 220 0 -1.72
CISPEP 9 ALA A 290 ASN A 291 0 -13.69
CISPEP 10 LEU B 37 SER B 38 0 -12.74
CISPEP 11 SER B 38 VAL B 39 0 -18.28
CISPEP 12 PRO B 41 PRO B 42 0 0.62
CISPEP 13 GLY B 67 GLY B 68 0 7.67
CISPEP 14 PRO B 99 PRO B 100 0 -13.02
CISPEP 15 ARG B 101 GLY B 102 0 1.13
CISPEP 16 ALA B 106 ASN B 107 0 3.25
CISPEP 17 GLN B 219 PRO B 220 0 -0.06
CISPEP 18 ALA B 290 ASN B 291 0 -13.60
SITE 1 AC1 6 ASP A 199 THR A 201 SER A 203 HIS A 205
SITE 2 AC1 6 GLU A 210 HOH A 331
SITE 1 AC2 6 LYS A 90 CSO A 202 CSD B 189 HOH B 463
SITE 2 AC2 6 HOH B 464 HOH B 476
SITE 1 AC3 6 ASP B 199 THR B 201 SER B 203 HIS B 205
SITE 2 AC3 6 GLU B 210 HOH B 471
SITE 1 AC4 6 CSD A 189 HOH A 445 HOH A 446 HOH A 461
SITE 2 AC4 6 LYS B 90 CSO B 202
CRYST1 90.250 90.250 191.581 90.00 90.00 120.00 P 65 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 0.011080 0.006397 0.000000 0.00000
SCALE2 0.000000 0.012794 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005220 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
