HEADER TRANSFERASE/SIGNALING PROTEIN 08-MAY-09 3HEI
TITLE LIGAND RECOGNITION BY A-CLASS EPH RECEPTORS: CRYSTAL STRUCTURES OF THE
TITLE 2 EPHA2 LIGAND-BINDING DOMAIN AND THE EPHA2/EPHRIN-A1 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPHRIN TYPE-A RECEPTOR 2;
COMPND 3 CHAIN: A, C, E, G, I, K, M, O;
COMPND 4 FRAGMENT: UNP RESIDUES 28-201;
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, D, F, H, J, L, N, P;
COMPND 12 FRAGMENT: UNP RESIDUES 18-147;
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_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: EPHA2, ECK;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 10 EXPRESSION_SYSTEM_ORGAN: KIDNEY;
SOURCE 11 EXPRESSION_SYSTEM_CELL: HUMAN EMBRYONIC KIDNEY (HEK) CELLS;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PBABE;
SOURCE 14 MOL_ID: 2;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: HUMAN;
SOURCE 17 ORGANISM_TAXID: 9606;
SOURCE 18 GENE: EFNA1, EPLG1, LERK1, TNFAIP4;
SOURCE 19 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 20 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 22 EXPRESSION_SYSTEM_CELL_LINE: HEK293;
SOURCE 23 EXPRESSION_SYSTEM_ORGAN: KIDNEY;
SOURCE 24 EXPRESSION_SYSTEM_CELL: HUMAN EMBRYONIC KIDNEY (HEK) CELLS;
SOURCE 25 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 26 EXPRESSION_SYSTEM_PLASMID: PBABE
KEYWDS EPH RECEPTOR TYROSINE KINASE, EPHRIN, CELL MEMBRANE, DISULFIDE BOND,
KEYWDS 2 GLYCOPROTEIN, GPI-ANCHOR, LIPOPROTEIN, MEMBRANE, ATP-BINDING,
KEYWDS 3 KINASE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, RECEPTOR, TRANSFERASE,
KEYWDS 4 TRANSMEMBRANE, TYROSINE-PROTEIN KINASE, TRANSFERASE-SIGNALING
KEYWDS 5 PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.P.HIMANEN,Y.GOLDGUR,H.MIAO,E.MYSHKIN,H.GUO,M.BUCK,M.NGUYEN,
AUTHOR 2 K.R.RAJASHANKAR,B.WANG,D.B.NIKOLOV
REVDAT 5 31-MAR-21 3HEI 1 SOURCE SEQADV
REVDAT 4 01-NOV-17 3HEI 1 REMARK
REVDAT 3 13-JUL-11 3HEI 1 VERSN
REVDAT 2 28-JUL-09 3HEI 1 JRNL
REVDAT 1 30-JUN-09 3HEI 0
JRNL AUTH J.P.HIMANEN,Y.GOLDGUR,H.MIAO,E.MYSHKIN,H.GUO,M.BUCK,
JRNL AUTH 2 M.NGUYEN,K.R.RAJASHANKAR,B.WANG,D.B.NIKOLOV
JRNL TITL LIGAND RECOGNITION BY A-CLASS EPH RECEPTORS: CRYSTAL
JRNL TITL 2 STRUCTURES OF THE EPHA2 LIGAND-BINDING DOMAIN AND THE
JRNL TITL 3 EPHA2/EPHRIN-A1 COMPLEX.
JRNL REF EMBO REP. V. 10 722 2009
JRNL REFN ISSN 1469-221X
JRNL PMID 19525919
JRNL DOI 10.1038/EMBOR.2009.91
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 182318
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 9696
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) : 12598
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.1810
REMARK 3 BIN FREE R VALUE SET COUNT : 699
REMARK 3 BIN FREE R VALUE : 0.2510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 20152
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 2756
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.88000
REMARK 3 B22 (A**2) : 0.68000
REMARK 3 B33 (A**2) : 1.48000
REMARK 3 B12 (A**2) : 0.01000
REMARK 3 B13 (A**2) : -0.84000
REMARK 3 B23 (A**2) : 0.04000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.178
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.114
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.925
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 20728 ; 0.026 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 28080 ; 2.049 ; 1.934
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2432 ; 7.570 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1096 ;37.187 ;23.869
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3488 ;16.129 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 128 ;16.540 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2904 ; 0.182 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 16080 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 9798 ; 0.263 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 13685 ; 0.314 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 2997 ; 0.236 ; 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): 222 ; 0.356 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 136 ; 0.254 ; 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): 12192 ; 1.276 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 19712 ; 2.225 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8536 ; 3.363 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 8368 ; 5.144 ; 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 C E G I K M O
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 174 4
REMARK 3 1 C 1 C 174 4
REMARK 3 1 E 1 E 174 4
REMARK 3 1 G 1 G 174 4
REMARK 3 1 I 1 I 174 4
REMARK 3 1 K 1 K 174 4
REMARK 3 1 M 1 M 174 4
REMARK 3 1 O 1 O 174 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1395 ; 0.340 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 1395 ; 0.360 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 E (A): 1395 ; 0.360 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 G (A): 1395 ; 0.360 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 I (A): 1395 ; 0.370 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 K (A): 1395 ; 0.400 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 M (A): 1395 ; 0.310 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 O (A): 1395 ; 0.320 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1395 ; 2.650 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 1395 ; 2.830 ; 2.000
REMARK 3 MEDIUM THERMAL 1 E (A**2): 1395 ; 1.150 ; 2.000
REMARK 3 MEDIUM THERMAL 1 G (A**2): 1395 ; 1.530 ; 2.000
REMARK 3 MEDIUM THERMAL 1 I (A**2): 1395 ; 1.950 ; 2.000
REMARK 3 MEDIUM THERMAL 1 K (A**2): 1395 ; 1.270 ; 2.000
REMARK 3 MEDIUM THERMAL 1 M (A**2): 1395 ; 1.860 ; 2.000
REMARK 3 MEDIUM THERMAL 1 O (A**2): 1395 ; 2.260 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B D F H J L N P
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 18 B 149 2
REMARK 3 1 D 18 D 149 2
REMARK 3 1 F 18 F 149 2
REMARK 3 1 H 18 H 149 2
REMARK 3 1 J 18 J 149 2
REMARK 3 1 L 18 L 149 2
REMARK 3 1 N 18 N 149 2
REMARK 3 1 P 18 P 149 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 528 ; 0.090 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 D (A): 528 ; 0.080 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 F (A): 528 ; 0.100 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 H (A): 528 ; 0.110 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 J (A): 528 ; 0.070 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 L (A): 528 ; 0.070 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 N (A): 528 ; 0.080 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 P (A): 528 ; 0.070 ; 0.050
REMARK 3 MEDIUM POSITIONAL 2 B (A): 591 ; 0.390 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 D (A): 591 ; 0.380 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 F (A): 591 ; 0.430 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 H (A): 591 ; 0.400 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 J (A): 591 ; 0.340 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 L (A): 591 ; 0.420 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 N (A): 591 ; 0.420 ; 0.500
REMARK 3 MEDIUM POSITIONAL 2 P (A): 591 ; 0.380 ; 0.500
REMARK 3 TIGHT THERMAL 2 B (A**2): 528 ; 0.340 ; 0.500
REMARK 3 TIGHT THERMAL 2 D (A**2): 528 ; 0.230 ; 0.500
REMARK 3 TIGHT THERMAL 2 F (A**2): 528 ; 0.300 ; 0.500
REMARK 3 TIGHT THERMAL 2 H (A**2): 528 ; 0.370 ; 0.500
REMARK 3 TIGHT THERMAL 2 J (A**2): 528 ; 0.260 ; 0.500
REMARK 3 TIGHT THERMAL 2 L (A**2): 528 ; 0.250 ; 0.500
REMARK 3 TIGHT THERMAL 2 N (A**2): 528 ; 0.260 ; 0.500
REMARK 3 TIGHT THERMAL 2 P (A**2): 528 ; 0.280 ; 0.500
REMARK 3 MEDIUM THERMAL 2 B (A**2): 591 ; 1.550 ; 2.000
REMARK 3 MEDIUM THERMAL 2 D (A**2): 591 ; 1.270 ; 2.000
REMARK 3 MEDIUM THERMAL 2 F (A**2): 591 ; 1.540 ; 2.000
REMARK 3 MEDIUM THERMAL 2 H (A**2): 591 ; 1.680 ; 2.000
REMARK 3 MEDIUM THERMAL 2 J (A**2): 591 ; 1.250 ; 2.000
REMARK 3 MEDIUM THERMAL 2 L (A**2): 591 ; 1.190 ; 2.000
REMARK 3 MEDIUM THERMAL 2 N (A**2): 591 ; 1.380 ; 2.000
REMARK 3 MEDIUM THERMAL 2 P (A**2): 591 ; 1.240 ; 2.000
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 1 A 174
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9640 8.9940 -7.1610
REMARK 3 T TENSOR
REMARK 3 T11: 0.2097 T22: 0.0469
REMARK 3 T33: 0.0235 T12: -0.0023
REMARK 3 T13: 0.0330 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 1.4693 L22: 1.1651
REMARK 3 L33: 1.2472 L12: 0.1397
REMARK 3 L13: -0.1216 L23: -0.4098
REMARK 3 S TENSOR
REMARK 3 S11: -0.0089 S12: 0.0491 S13: 0.1217
REMARK 3 S21: 0.0528 S22: 0.0204 S23: 0.0039
REMARK 3 S31: -0.0273 S32: -0.0374 S33: -0.0115
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 : B 18 B 149
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4120 -11.1340 9.1320
REMARK 3 T TENSOR
REMARK 3 T11: 0.2557 T22: 0.0407
REMARK 3 T33: 0.0140 T12: -0.0145
REMARK 3 T13: 0.0444 T23: -0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 1.2391 L22: 1.6434
REMARK 3 L33: 1.2982 L12: -0.2858
REMARK 3 L13: -0.2354 L23: 0.2336
REMARK 3 S TENSOR
REMARK 3 S11: -0.0341 S12: -0.0446 S13: -0.0579
REMARK 3 S21: 0.1194 S22: -0.0039 S23: 0.0920
REMARK 3 S31: 0.0782 S32: -0.1409 S33: 0.0381
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 : C 1 C 174
REMARK 3 ORIGIN FOR THE GROUP (A): 56.2880 18.0910 118.7390
REMARK 3 T TENSOR
REMARK 3 T11: 0.2119 T22: 0.0386
REMARK 3 T33: 0.0320 T12: 0.0063
REMARK 3 T13: 0.0414 T23: -0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 1.0452 L22: 0.9426
REMARK 3 L33: 1.2891 L12: -0.0072
REMARK 3 L13: -0.1064 L23: -0.0411
REMARK 3 S TENSOR
REMARK 3 S11: -0.0374 S12: -0.0262 S13: 0.0011
REMARK 3 S21: -0.0822 S22: -0.0282 S23: -0.0466
REMARK 3 S31: 0.0137 S32: 0.0386 S33: 0.0656
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 : D 18 D 149
REMARK 3 ORIGIN FOR THE GROUP (A): 68.0670 8.8390 94.7470
REMARK 3 T TENSOR
REMARK 3 T11: 0.3062 T22: 0.0691
REMARK 3 T33: 0.0158 T12: 0.0282
REMARK 3 T13: 0.0433 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 1.0590 L22: 1.4742
REMARK 3 L33: 2.1425 L12: -0.0894
REMARK 3 L13: -0.6886 L23: -0.1318
REMARK 3 S TENSOR
REMARK 3 S11: -0.0504 S12: 0.0455 S13: -0.0376
REMARK 3 S21: -0.1060 S22: -0.0749 S23: -0.0056
REMARK 3 S31: 0.0372 S32: 0.0879 S33: 0.1253
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 : E 1 E 174
REMARK 3 ORIGIN FOR THE GROUP (A): 35.4450 54.3240 32.8660
REMARK 3 T TENSOR
REMARK 3 T11: 0.2524 T22: 0.0666
REMARK 3 T33: 0.0155 T12: 0.0009
REMARK 3 T13: 0.0370 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 1.8430 L22: 1.6909
REMARK 3 L33: 1.7788 L12: -0.6236
REMARK 3 L13: -0.6219 L23: 0.7386
REMARK 3 S TENSOR
REMARK 3 S11: -0.0220 S12: -0.0789 S13: -0.0155
REMARK 3 S21: 0.0500 S22: 0.0647 S23: 0.0904
REMARK 3 S31: 0.0822 S32: -0.0604 S33: -0.0427
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 : F 18 F 149
REMARK 3 ORIGIN FOR THE GROUP (A): 55.3540 43.1410 16.2160
REMARK 3 T TENSOR
REMARK 3 T11: 0.2585 T22: 0.0647
REMARK 3 T33: 0.0408 T12: 0.0323
REMARK 3 T13: 0.0133 T23: -0.0338
REMARK 3 L TENSOR
REMARK 3 L11: 0.7792 L22: 2.0333
REMARK 3 L33: 1.7266 L12: -0.0858
REMARK 3 L13: -0.1389 L23: -0.6997
REMARK 3 S TENSOR
REMARK 3 S11: 0.0130 S12: -0.0028 S13: -0.0374
REMARK 3 S21: 0.0533 S22: -0.0182 S23: -0.1641
REMARK 3 S31: 0.1206 S32: 0.1399 S33: 0.0052
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 : G 1 G 174
REMARK 3 ORIGIN FOR THE GROUP (A): 44.9740 50.2150 112.3090
REMARK 3 T TENSOR
REMARK 3 T11: 0.2563 T22: 0.0571
REMARK 3 T33: 0.0269 T12: 0.0273
REMARK 3 T13: 0.0191 T23: -0.0337
REMARK 3 L TENSOR
REMARK 3 L11: 0.9319 L22: 2.0430
REMARK 3 L33: 1.8140 L12: -0.0248
REMARK 3 L13: -0.1924 L23: 0.5849
REMARK 3 S TENSOR
REMARK 3 S11: 0.0014 S12: 0.0769 S13: -0.0459
REMARK 3 S21: -0.1537 S22: -0.0742 S23: 0.0860
REMARK 3 S31: -0.0054 S32: -0.0754 S33: 0.0728
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 : H 18 H 149
REMARK 3 ORIGIN FOR THE GROUP (A): 56.3110 66.7830 132.2040
REMARK 3 T TENSOR
REMARK 3 T11: 0.2415 T22: 0.0309
REMARK 3 T33: 0.0109 T12: 0.0132
REMARK 3 T13: 0.0427 T23: -0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 1.9838 L22: 1.0535
REMARK 3 L33: 1.0444 L12: 0.0232
REMARK 3 L13: 0.2354 L23: 0.4470
REMARK 3 S TENSOR
REMARK 3 S11: 0.0162 S12: 0.0013 S13: 0.0507
REMARK 3 S21: -0.0152 S22: -0.0421 S23: 0.0243
REMARK 3 S31: 0.0282 S32: 0.0275 S33: 0.0258
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 : I 1 I 174
REMARK 3 ORIGIN FOR THE GROUP (A): 66.3620 68.1440 95.1910
REMARK 3 T TENSOR
REMARK 3 T11: 0.2924 T22: 0.1331
REMARK 3 T33: 0.0872 T12: 0.0141
REMARK 3 T13: 0.0382 T23: -0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 3.9058 L22: 3.2444
REMARK 3 L33: 2.8793 L12: -2.5058
REMARK 3 L13: 1.4875 L23: -1.3253
REMARK 3 S TENSOR
REMARK 3 S11: -0.0910 S12: 0.2112 S13: 0.3723
REMARK 3 S21: 0.0479 S22: -0.1051 S23: -0.4613
REMARK 3 S31: -0.0852 S32: 0.3457 S33: 0.1961
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 : J 18 J 149
REMARK 3 ORIGIN FOR THE GROUP (A): 41.3800 77.6700 86.0230
REMARK 3 T TENSOR
REMARK 3 T11: 0.3378 T22: 0.1247
REMARK 3 T33: 0.0184 T12: 0.0782
REMARK 3 T13: 0.0558 T23: -0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 1.3309 L22: 3.1708
REMARK 3 L33: 1.9599 L12: 0.1162
REMARK 3 L13: 0.0440 L23: 0.6849
REMARK 3 S TENSOR
REMARK 3 S11: 0.0407 S12: 0.0116 S13: 0.0043
REMARK 3 S21: -0.0140 S22: -0.0686 S23: 0.1143
REMARK 3 S31: -0.0363 S32: -0.2163 S33: 0.0280
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 : K 1 K 174
REMARK 3 ORIGIN FOR THE GROUP (A): 61.0010 73.3080 39.7370
REMARK 3 T TENSOR
REMARK 3 T11: 0.2679 T22: 0.0556
REMARK 3 T33: 0.0266 T12: 0.0242
REMARK 3 T13: 0.0442 T23: -0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 1.2224 L22: 1.9696
REMARK 3 L33: 2.6039 L12: -0.3040
REMARK 3 L13: -0.0221 L23: -0.1426
REMARK 3 S TENSOR
REMARK 3 S11: -0.0544 S12: -0.0201 S13: 0.0983
REMARK 3 S21: -0.0520 S22: 0.0582 S23: -0.0537
REMARK 3 S31: -0.0592 S32: 0.1050 S33: -0.0037
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 : L 18 L 149
REMARK 3 ORIGIN FOR THE GROUP (A): 56.9090 59.0870 63.8240
REMARK 3 T TENSOR
REMARK 3 T11: 0.3700 T22: 0.1071
REMARK 3 T33: 0.0172 T12: 0.0752
REMARK 3 T13: 0.0420 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 1.2364 L22: 1.2806
REMARK 3 L33: 2.6755 L12: -0.3627
REMARK 3 L13: -0.7618 L23: -0.2803
REMARK 3 S TENSOR
REMARK 3 S11: -0.0783 S12: -0.0350 S13: -0.0372
REMARK 3 S21: 0.0286 S22: -0.0187 S23: -0.0318
REMARK 3 S31: 0.1570 S32: 0.0424 S33: 0.0970
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 : M 1 M 174
REMARK 3 ORIGIN FOR THE GROUP (A): 23.5490 8.0490 45.2530
REMARK 3 T TENSOR
REMARK 3 T11: 0.3867 T22: 0.0359
REMARK 3 T33: 0.1614 T12: 0.0523
REMARK 3 T13: -0.0951 T23: -0.0583
REMARK 3 L TENSOR
REMARK 3 L11: 1.9610 L22: 3.4167
REMARK 3 L33: 3.6674 L12: -1.5024
REMARK 3 L13: 1.2856 L23: -1.3394
REMARK 3 S TENSOR
REMARK 3 S11: -0.3743 S12: -0.1111 S13: 0.3525
REMARK 3 S21: 0.3840 S22: 0.0775 S23: -0.5609
REMARK 3 S31: -0.3182 S32: -0.0038 S33: 0.2968
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 : N 18 N 149
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9040 14.9890 26.1420
REMARK 3 T TENSOR
REMARK 3 T11: 0.3436 T22: 0.0305
REMARK 3 T33: 0.0297 T12: 0.0258
REMARK 3 T13: 0.0116 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 1.9992 L22: 2.2740
REMARK 3 L33: 1.3413 L12: 0.2338
REMARK 3 L13: 0.7660 L23: -0.0825
REMARK 3 S TENSOR
REMARK 3 S11: -0.0576 S12: 0.0114 S13: 0.0828
REMARK 3 S21: 0.0759 S22: -0.0174 S23: -0.1096
REMARK 3 S31: -0.0547 S32: -0.0092 S33: 0.0750
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 : O 1 O 174
REMARK 3 ORIGIN FOR THE GROUP (A): 54.9620 11.0320 63.1700
REMARK 3 T TENSOR
REMARK 3 T11: 0.4268 T22: 0.1302
REMARK 3 T33: 0.0530 T12: -0.0078
REMARK 3 T13: -0.0082 T23: -0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 1.5570 L22: 4.4326
REMARK 3 L33: 3.3561 L12: 1.1207
REMARK 3 L13: 0.3674 L23: 1.5888
REMARK 3 S TENSOR
REMARK 3 S11: 0.0324 S12: -0.1013 S13: -0.0211
REMARK 3 S21: -0.0448 S22: -0.0690 S23: 0.3893
REMARK 3 S31: 0.3187 S32: -0.3204 S33: 0.0366
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 : P 18 P 149
REMARK 3 ORIGIN FOR THE GROUP (A): 70.5220 32.8140 72.2550
REMARK 3 T TENSOR
REMARK 3 T11: 0.4278 T22: 0.0772
REMARK 3 T33: 0.0134 T12: 0.0143
REMARK 3 T13: 0.0473 T23: 0.0008
REMARK 3 L TENSOR
REMARK 3 L11: 2.2741 L22: 2.8456
REMARK 3 L33: 2.2742 L12: -0.7569
REMARK 3 L13: 0.4658 L23: -0.6955
REMARK 3 S TENSOR
REMARK 3 S11: 0.0197 S12: 0.0212 S13: 0.0620
REMARK 3 S21: 0.0042 S22: -0.0881 S23: -0.1162
REMARK 3 S31: -0.2316 S32: 0.1407 S33: 0.0684
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 3HEI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000053035.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-AUG-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 192014
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.06900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.2140
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.27300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8,000, 100 MM TRIS, PH 8.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8
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: 2150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 2090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
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: 2170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
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: 2120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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: 5
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: 2150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
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: 6
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: 2180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15270 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L
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: 7
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: 2090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15400 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N
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: 8
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: 2170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, P
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: 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 ALA P 18 O HOH P 1057 1.58
REMARK 500 CB ALA F 18 O HOH F 2722 1.66
REMARK 500 CB SER N 28 O HOH N 2112 1.75
REMARK 500 N GLU M 1 O HOH M 2241 1.77
REMARK 500 N ALA D 18 O HOH D 2672 1.79
REMARK 500 OD2 ASP D 19 OD1 ASP D 45 1.84
REMARK 500 O HOH M 1257 O HOH M 2475 1.88
REMARK 500 O HOH C 2435 O HOH G 2601 1.90
REMARK 500 O HOH N 1460 O HOH N 1753 1.92
REMARK 500 OD1 ASN D 26 O HOH D 1452 1.95
REMARK 500 N ALA H 18 O HOH H 925 1.98
REMARK 500 N ALA F 18 O HOH F 2185 1.98
REMARK 500 O HOH M 502 O HOH M 1419 1.98
REMARK 500 O HOH A 491 O HOH N 2508 1.98
REMARK 500 SG CYS E 174 O HOH E 2217 1.99
REMARK 500 SG CYS C 174 O HOH C 2764 1.99
REMARK 500 C CYS G 174 O HOH G 1254 2.00
REMARK 500 CB ALA H 18 O HOH H 720 2.00
REMARK 500 O HOH B 428 O HOH B 2373 2.00
REMARK 500 O HOH B 758 O HOH B 2373 2.01
REMARK 500 O HOH J 1663 O HOH J 1864 2.01
REMARK 500 O HOH M 698 O HOH M 1257 2.02
REMARK 500 O HOH P 423 O HOH P 1882 2.02
REMARK 500 O HOH K 363 O HOH K 1381 2.04
REMARK 500 O HOH C 2435 O HOH G 506 2.04
REMARK 500 O HOH K 1047 O HOH K 1258 2.05
REMARK 500 N GLY I 15 O HOH I 2053 2.05
REMARK 500 O HOH K 1258 O HOH K 2105 2.07
REMARK 500 O HOH C 1677 O HOH C 1725 2.07
REMARK 500 N GLU C 1 O HOH C 2424 2.08
REMARK 500 SG CYS M 174 O HOH M 851 2.08
REMARK 500 O HOH D 640 O HOH D 1026 2.09
REMARK 500 O HOH C 426 O HOH C 2435 2.09
REMARK 500 ND2 ASN H 26 O HOH H 154 2.11
REMARK 500 O HOH G 183 O HOH G 2329 2.11
REMARK 500 O HOH B 982 O HOH B 1928 2.11
REMARK 500 O HOH F 589 O HOH F 2272 2.12
REMARK 500 O HOH N 1009 O HOH N 1337 2.12
REMARK 500 OE2 GLU E 139 O HOH E 271 2.13
REMARK 500 NE2 HIS H 99 O HOH H 929 2.13
REMARK 500 OD1 ASN B 26 O HOH B 1251 2.13
REMARK 500 ND2 ASN J 26 O HOH J 2428 2.13
REMARK 500 O HOH H 2097 O HOH H 2434 2.13
REMARK 500 O HOH N 1337 O HOH N 2648 2.13
REMARK 500 O HOH J 212 O HOH J 1864 2.14
REMARK 500 O HOH N 1091 O HOH N 2155 2.14
REMARK 500 O PHE K 81 N GLY K 84 2.15
REMARK 500 O HOH M 2527 O HOH M 2662 2.15
REMARK 500 O ASP F 138 O HOH F 1466 2.15
REMARK 500 O HOH P 647 O HOH P 2609 2.15
REMARK 500
REMARK 500 THIS ENTRY HAS 70 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH K 438 O HOH M 1257 1565 1.97
REMARK 500 O HOH B 2558 O HOH H 661 1544 2.18
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 TYR A 38 CE2 TYR A 38 CD2 0.102
REMARK 500 ASN B 26 CB ASN B 26 CG 0.209
REMARK 500 ASN B 26 CG ASN B 26 ND2 0.238
REMARK 500 TYR B 46 CG TYR B 46 CD1 0.080
REMARK 500 GLU B 75 CD GLU B 75 OE1 0.089
REMARK 500 SER B 96 CB SER B 96 OG -0.088
REMARK 500 ASN D 26 CB ASN D 26 CG 0.174
REMARK 500 ASN D 26 CG ASN D 26 ND2 0.218
REMARK 500 TYR D 37 CE2 TYR D 37 CD2 0.100
REMARK 500 LEU D 116 N LEU D 116 CA 0.137
REMARK 500 CYS D 140 CB CYS D 140 SG 0.105
REMARK 500 GLU F 75 CD GLU F 75 OE1 0.069
REMARK 500 CYS F 80 CB CYS F 80 SG 0.135
REMARK 500 ASN G 57 CB ASN G 57 CG 0.177
REMARK 500 ASN H 26 N ASN H 26 CA 0.133
REMARK 500 ASN H 26 CA ASN H 26 CB 0.245
REMARK 500 ASN H 26 CG ASN H 26 OD1 0.165
REMARK 500 TYR H 37 CE2 TYR H 37 CD2 0.125
REMARK 500 TYR I 40 CD1 TYR I 40 CE1 0.103
REMARK 500 TYR J 70 CE2 TYR J 70 CD2 0.094
REMARK 500 TRP K 16 CE3 TRP K 16 CZ3 0.102
REMARK 500 GLU L 137 CB GLU L 137 CG 0.125
REMARK 500 ASN N 26 N ASN N 26 CA 0.162
REMARK 500 ASN N 26 CA ASN N 26 CB 0.190
REMARK 500 TYR N 37 CE2 TYR N 37 CD2 0.142
REMARK 500 ASN O 57 CB ASN O 57 CG 0.140
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 ASP A 102 CB - CG - OD1 ANGL. DEV. = 9.0 DEGREES
REMARK 500 ASP A 102 CB - CG - OD2 ANGL. DEV. = -8.4 DEGREES
REMARK 500 LEU A 111 CB - CG - CD2 ANGL. DEV. = 11.1 DEGREES
REMARK 500 LEU C 14 CB - CG - CD2 ANGL. DEV. = 11.6 DEGREES
REMARK 500 ASP C 51 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG C 66 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG C 66 NE - CZ - NH2 ANGL. DEV. = -8.1 DEGREES
REMARK 500 ASP C 102 CB - CG - OD1 ANGL. DEV. = 8.0 DEGREES
REMARK 500 VAL C 143 CG1 - CB - CG2 ANGL. DEV. = -10.0 DEGREES
REMARK 500 LEU C 165 CB - CG - CD2 ANGL. DEV. = 12.2 DEGREES
REMARK 500 CYS C 174 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP D 19 N - CA - C ANGL. DEV. = 20.8 DEGREES
REMARK 500 LEU D 104 CA - CB - CG ANGL. DEV. = -15.2 DEGREES
REMARK 500 ARG D 110 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 THR D 115 O - C - N ANGL. DEV. = -11.8 DEGREES
REMARK 500 LEU D 116 CA - CB - CG ANGL. DEV. = 14.9 DEGREES
REMARK 500 ARG E 66 NE - CZ - NH1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG E 66 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP E 121 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 LEU F 116 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 LEU G 153 CB - CG - CD1 ANGL. DEV. = 13.1 DEGREES
REMARK 500 LEU G 165 CB - CG - CD1 ANGL. DEV. = 10.7 DEGREES
REMARK 500 ASN H 26 CB - CA - C ANGL. DEV. = -13.2 DEGREES
REMARK 500 ASN H 26 N - CA - CB ANGL. DEV. = 11.5 DEGREES
REMARK 500 ASN H 26 N - CA - C ANGL. DEV. = -21.8 DEGREES
REMARK 500 LEU H 104 CA - CB - CG ANGL. DEV. = -15.8 DEGREES
REMARK 500 THR H 115 O - C - N ANGL. DEV. = -10.3 DEGREES
REMARK 500 LEU H 116 N - CA - CB ANGL. DEV. = 14.3 DEGREES
REMARK 500 LEU I 153 CB - CG - CD1 ANGL. DEV. = 11.5 DEGREES
REMARK 500 LEU I 165 CB - CG - CD2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 LEU J 104 CA - CB - CG ANGL. DEV. = -15.2 DEGREES
REMARK 500 PRO K 82 C - N - CA ANGL. DEV. = 11.1 DEGREES
REMARK 500 LEU K 153 CB - CG - CD1 ANGL. DEV. = 10.2 DEGREES
REMARK 500 SER L 28 CB - CA - C ANGL. DEV. = 11.8 DEGREES
REMARK 500 ILE L 39 CG1 - CB - CG2 ANGL. DEV. = -13.3 DEGREES
REMARK 500 ASN N 26 N - CA - C ANGL. DEV. = -20.1 DEGREES
REMARK 500 LEU P 104 CA - CB - CG ANGL. DEV. = -15.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 34 18.90 57.73
REMARK 500 CYS A 43 41.76 -159.89
REMARK 500 ASP A 51 79.08 -152.55
REMARK 500 ALA A 85 91.84 -3.10
REMARK 500 ASP B 56 -15.63 -43.18
REMARK 500 HIS B 57 -7.51 -140.41
REMARK 500 HIS B 134 33.92 -78.40
REMARK 500 GLN B 135 76.57 -38.04
REMARK 500 GLU B 137 97.30 -64.58
REMARK 500 CYS C 43 47.99 -160.52
REMARK 500 ASP C 51 76.01 -153.41
REMARK 500 ALA C 85 79.00 78.46
REMARK 500 ASP D 19 -41.24 -176.62
REMARK 500 ASN D 44 -0.19 89.77
REMARK 500 ASP D 56 -109.78 27.54
REMARK 500 SER D 58 -16.70 176.87
REMARK 500 LEU D 116 -39.22 89.84
REMARK 500 TYR E 21 120.80 -36.45
REMARK 500 ASP E 34 17.25 57.86
REMARK 500 CYS E 43 48.16 -156.35
REMARK 500 ASP E 51 70.45 -152.14
REMARK 500 ALA E 85 39.17 89.92
REMARK 500 ALA E 131 2.12 -69.97
REMARK 500 ARG E 132 49.44 38.83
REMARK 500 ASN F 44 -1.81 81.82
REMARK 500 ASP F 56 -77.28 -32.37
REMARK 500 SER F 58 -63.04 149.00
REMARK 500 LEU F 116 -34.53 77.20
REMARK 500 ARG F 139 128.68 142.64
REMARK 500 ASP G 34 18.74 58.77
REMARK 500 CYS G 43 48.24 -154.29
REMARK 500 ASP G 51 68.55 -151.76
REMARK 500 ALA G 85 95.56 63.02
REMARK 500 SER G 86 -79.84 -62.39
REMARK 500 ASP H 19 99.27 47.53
REMARK 500 ASP H 56 -83.16 12.44
REMARK 500 HIS H 57 -129.78 -116.39
REMARK 500 SER H 58 -50.37 96.24
REMARK 500 LEU H 116 -40.02 95.87
REMARK 500 CYS I 43 52.56 -166.71
REMARK 500 SER I 87 42.87 -104.19
REMARK 500 ARG I 110 -38.72 -38.98
REMARK 500 ASN J 44 -0.22 82.27
REMARK 500 SER J 58 -50.50 175.18
REMARK 500 LEU J 116 -23.69 132.46
REMARK 500 GLU J 137 44.09 -73.73
REMARK 500 ARG J 139 124.73 81.16
REMARK 500 CYS K 43 54.70 -152.71
REMARK 500 PHE K 81 73.25 -107.56
REMARK 500 PRO K 82 -10.73 -19.47
REMARK 500
REMARK 500 THIS ENTRY HAS 78 RAMACHANDRAN OUTLIERS.
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 GLY A 48 ASP A 49 137.49
REMARK 500 GLN B 135 HIS B 136 144.05
REMARK 500 LYS B 148 ILE B 149 137.10
REMARK 500 LYS F 148 ILE F 149 143.92
REMARK 500 GLY G 83 GLY G 84 -137.93
REMARK 500 LYS J 148 ILE J 149 143.44
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3HEI A 1 174 UNP P29317 EPHA2_HUMAN 28 201
DBREF 3HEI B 18 147 UNP P20827 EFNA1_HUMAN 18 147
DBREF 3HEI C 1 174 UNP P29317 EPHA2_HUMAN 28 201
DBREF 3HEI D 18 147 UNP P20827 EFNA1_HUMAN 18 147
DBREF 3HEI E 1 174 UNP P29317 EPHA2_HUMAN 28 201
DBREF 3HEI F 18 147 UNP P20827 EFNA1_HUMAN 18 147
DBREF 3HEI G 1 174 UNP P29317 EPHA2_HUMAN 28 201
DBREF 3HEI H 18 147 UNP P20827 EFNA1_HUMAN 18 147
DBREF 3HEI I 1 174 UNP P29317 EPHA2_HUMAN 28 201
DBREF 3HEI J 18 147 UNP P20827 EFNA1_HUMAN 18 147
DBREF 3HEI K 1 174 UNP P29317 EPHA2_HUMAN 28 201
DBREF 3HEI L 18 147 UNP P20827 EFNA1_HUMAN 18 147
DBREF 3HEI M 1 174 UNP P29317 EPHA2_HUMAN 28 201
DBREF 3HEI N 18 147 UNP P20827 EFNA1_HUMAN 18 147
DBREF 3HEI O 1 174 UNP P29317 EPHA2_HUMAN 28 201
DBREF 3HEI P 18 147 UNP P20827 EFNA1_HUMAN 18 147
SEQADV 3HEI LYS B 148 UNP P20827 EXPRESSION TAG
SEQADV 3HEI ILE B 149 UNP P20827 EXPRESSION TAG
SEQADV 3HEI LYS D 148 UNP P20827 EXPRESSION TAG
SEQADV 3HEI ILE D 149 UNP P20827 EXPRESSION TAG
SEQADV 3HEI LYS F 148 UNP P20827 EXPRESSION TAG
SEQADV 3HEI ILE F 149 UNP P20827 EXPRESSION TAG
SEQADV 3HEI LYS H 148 UNP P20827 EXPRESSION TAG
SEQADV 3HEI ILE H 149 UNP P20827 EXPRESSION TAG
SEQADV 3HEI LYS J 148 UNP P20827 EXPRESSION TAG
SEQADV 3HEI ILE J 149 UNP P20827 EXPRESSION TAG
SEQADV 3HEI LYS L 148 UNP P20827 EXPRESSION TAG
SEQADV 3HEI ILE L 149 UNP P20827 EXPRESSION TAG
SEQADV 3HEI LYS N 148 UNP P20827 EXPRESSION TAG
SEQADV 3HEI ILE N 149 UNP P20827 EXPRESSION TAG
SEQADV 3HEI LYS P 148 UNP P20827 EXPRESSION TAG
SEQADV 3HEI ILE P 149 UNP P20827 EXPRESSION TAG
SEQRES 1 A 174 GLU VAL VAL LEU LEU ASP PHE ALA ALA ALA GLY GLY GLU
SEQRES 2 A 174 LEU GLY TRP LEU THR HIS PRO TYR GLY LYS GLY TRP ASP
SEQRES 3 A 174 LEU MET GLN ASN ILE MET ASN ASP MET PRO ILE TYR MET
SEQRES 4 A 174 TYR SER VAL CYS ASN VAL MET SER GLY ASP GLN ASP ASN
SEQRES 5 A 174 TRP LEU ARG THR ASN TRP VAL TYR ARG GLY GLU ALA GLU
SEQRES 6 A 174 ARG ILE PHE ILE GLU LEU LYS PHE THR VAL ARG ASP CYS
SEQRES 7 A 174 ASN SER PHE PRO GLY GLY ALA SER SER CYS LYS GLU THR
SEQRES 8 A 174 PHE ASN LEU TYR TYR ALA GLU SER ASP LEU ASP TYR GLY
SEQRES 9 A 174 THR ASN PHE GLN LYS ARG LEU PHE THR LYS ILE ASP THR
SEQRES 10 A 174 ILE ALA PRO ASP GLU ILE THR VAL SER SER ASP PHE GLU
SEQRES 11 A 174 ALA ARG HIS VAL LYS LEU ASN VAL GLU GLU ARG SER VAL
SEQRES 12 A 174 GLY PRO LEU THR ARG LYS GLY PHE TYR LEU ALA PHE GLN
SEQRES 13 A 174 ASP ILE GLY ALA CYS VAL ALA LEU LEU SER VAL ARG VAL
SEQRES 14 A 174 TYR TYR LYS LYS CYS
SEQRES 1 B 132 ALA ASP ARG HIS THR VAL PHE TRP ASN SER SER ASN PRO
SEQRES 2 B 132 LYS PHE ARG ASN GLU ASP TYR THR ILE HIS VAL GLN LEU
SEQRES 3 B 132 ASN ASP TYR VAL ASP ILE ILE CYS PRO HIS TYR GLU ASP
SEQRES 4 B 132 HIS SER VAL ALA ASP ALA ALA MET GLU GLN TYR ILE LEU
SEQRES 5 B 132 TYR LEU VAL GLU HIS GLU GLU TYR GLN LEU CYS GLN PRO
SEQRES 6 B 132 GLN SER LYS ASP GLN VAL ARG TRP GLN CYS ASN ARG PRO
SEQRES 7 B 132 SER ALA LYS HIS GLY PRO GLU LYS LEU SER GLU LYS PHE
SEQRES 8 B 132 GLN ARG PHE THR PRO PHE THR LEU GLY LYS GLU PHE LYS
SEQRES 9 B 132 GLU GLY HIS SER TYR TYR TYR ILE SER LYS PRO ILE HIS
SEQRES 10 B 132 GLN HIS GLU ASP ARG CYS LEU ARG LEU LYS VAL THR VAL
SEQRES 11 B 132 LYS ILE
SEQRES 1 C 174 GLU VAL VAL LEU LEU ASP PHE ALA ALA ALA GLY GLY GLU
SEQRES 2 C 174 LEU GLY TRP LEU THR HIS PRO TYR GLY LYS GLY TRP ASP
SEQRES 3 C 174 LEU MET GLN ASN ILE MET ASN ASP MET PRO ILE TYR MET
SEQRES 4 C 174 TYR SER VAL CYS ASN VAL MET SER GLY ASP GLN ASP ASN
SEQRES 5 C 174 TRP LEU ARG THR ASN TRP VAL TYR ARG GLY GLU ALA GLU
SEQRES 6 C 174 ARG ILE PHE ILE GLU LEU LYS PHE THR VAL ARG ASP CYS
SEQRES 7 C 174 ASN SER PHE PRO GLY GLY ALA SER SER CYS LYS GLU THR
SEQRES 8 C 174 PHE ASN LEU TYR TYR ALA GLU SER ASP LEU ASP TYR GLY
SEQRES 9 C 174 THR ASN PHE GLN LYS ARG LEU PHE THR LYS ILE ASP THR
SEQRES 10 C 174 ILE ALA PRO ASP GLU ILE THR VAL SER SER ASP PHE GLU
SEQRES 11 C 174 ALA ARG HIS VAL LYS LEU ASN VAL GLU GLU ARG SER VAL
SEQRES 12 C 174 GLY PRO LEU THR ARG LYS GLY PHE TYR LEU ALA PHE GLN
SEQRES 13 C 174 ASP ILE GLY ALA CYS VAL ALA LEU LEU SER VAL ARG VAL
SEQRES 14 C 174 TYR TYR LYS LYS CYS
SEQRES 1 D 132 ALA ASP ARG HIS THR VAL PHE TRP ASN SER SER ASN PRO
SEQRES 2 D 132 LYS PHE ARG ASN GLU ASP TYR THR ILE HIS VAL GLN LEU
SEQRES 3 D 132 ASN ASP TYR VAL ASP ILE ILE CYS PRO HIS TYR GLU ASP
SEQRES 4 D 132 HIS SER VAL ALA ASP ALA ALA MET GLU GLN TYR ILE LEU
SEQRES 5 D 132 TYR LEU VAL GLU HIS GLU GLU TYR GLN LEU CYS GLN PRO
SEQRES 6 D 132 GLN SER LYS ASP GLN VAL ARG TRP GLN CYS ASN ARG PRO
SEQRES 7 D 132 SER ALA LYS HIS GLY PRO GLU LYS LEU SER GLU LYS PHE
SEQRES 8 D 132 GLN ARG PHE THR PRO PHE THR LEU GLY LYS GLU PHE LYS
SEQRES 9 D 132 GLU GLY HIS SER TYR TYR TYR ILE SER LYS PRO ILE HIS
SEQRES 10 D 132 GLN HIS GLU ASP ARG CYS LEU ARG LEU LYS VAL THR VAL
SEQRES 11 D 132 LYS ILE
SEQRES 1 E 174 GLU VAL VAL LEU LEU ASP PHE ALA ALA ALA GLY GLY GLU
SEQRES 2 E 174 LEU GLY TRP LEU THR HIS PRO TYR GLY LYS GLY TRP ASP
SEQRES 3 E 174 LEU MET GLN ASN ILE MET ASN ASP MET PRO ILE TYR MET
SEQRES 4 E 174 TYR SER VAL CYS ASN VAL MET SER GLY ASP GLN ASP ASN
SEQRES 5 E 174 TRP LEU ARG THR ASN TRP VAL TYR ARG GLY GLU ALA GLU
SEQRES 6 E 174 ARG ILE PHE ILE GLU LEU LYS PHE THR VAL ARG ASP CYS
SEQRES 7 E 174 ASN SER PHE PRO GLY GLY ALA SER SER CYS LYS GLU THR
SEQRES 8 E 174 PHE ASN LEU TYR TYR ALA GLU SER ASP LEU ASP TYR GLY
SEQRES 9 E 174 THR ASN PHE GLN LYS ARG LEU PHE THR LYS ILE ASP THR
SEQRES 10 E 174 ILE ALA PRO ASP GLU ILE THR VAL SER SER ASP PHE GLU
SEQRES 11 E 174 ALA ARG HIS VAL LYS LEU ASN VAL GLU GLU ARG SER VAL
SEQRES 12 E 174 GLY PRO LEU THR ARG LYS GLY PHE TYR LEU ALA PHE GLN
SEQRES 13 E 174 ASP ILE GLY ALA CYS VAL ALA LEU LEU SER VAL ARG VAL
SEQRES 14 E 174 TYR TYR LYS LYS CYS
SEQRES 1 F 132 ALA ASP ARG HIS THR VAL PHE TRP ASN SER SER ASN PRO
SEQRES 2 F 132 LYS PHE ARG ASN GLU ASP TYR THR ILE HIS VAL GLN LEU
SEQRES 3 F 132 ASN ASP TYR VAL ASP ILE ILE CYS PRO HIS TYR GLU ASP
SEQRES 4 F 132 HIS SER VAL ALA ASP ALA ALA MET GLU GLN TYR ILE LEU
SEQRES 5 F 132 TYR LEU VAL GLU HIS GLU GLU TYR GLN LEU CYS GLN PRO
SEQRES 6 F 132 GLN SER LYS ASP GLN VAL ARG TRP GLN CYS ASN ARG PRO
SEQRES 7 F 132 SER ALA LYS HIS GLY PRO GLU LYS LEU SER GLU LYS PHE
SEQRES 8 F 132 GLN ARG PHE THR PRO PHE THR LEU GLY LYS GLU PHE LYS
SEQRES 9 F 132 GLU GLY HIS SER TYR TYR TYR ILE SER LYS PRO ILE HIS
SEQRES 10 F 132 GLN HIS GLU ASP ARG CYS LEU ARG LEU LYS VAL THR VAL
SEQRES 11 F 132 LYS ILE
SEQRES 1 G 174 GLU VAL VAL LEU LEU ASP PHE ALA ALA ALA GLY GLY GLU
SEQRES 2 G 174 LEU GLY TRP LEU THR HIS PRO TYR GLY LYS GLY TRP ASP
SEQRES 3 G 174 LEU MET GLN ASN ILE MET ASN ASP MET PRO ILE TYR MET
SEQRES 4 G 174 TYR SER VAL CYS ASN VAL MET SER GLY ASP GLN ASP ASN
SEQRES 5 G 174 TRP LEU ARG THR ASN TRP VAL TYR ARG GLY GLU ALA GLU
SEQRES 6 G 174 ARG ILE PHE ILE GLU LEU LYS PHE THR VAL ARG ASP CYS
SEQRES 7 G 174 ASN SER PHE PRO GLY GLY ALA SER SER CYS LYS GLU THR
SEQRES 8 G 174 PHE ASN LEU TYR TYR ALA GLU SER ASP LEU ASP TYR GLY
SEQRES 9 G 174 THR ASN PHE GLN LYS ARG LEU PHE THR LYS ILE ASP THR
SEQRES 10 G 174 ILE ALA PRO ASP GLU ILE THR VAL SER SER ASP PHE GLU
SEQRES 11 G 174 ALA ARG HIS VAL LYS LEU ASN VAL GLU GLU ARG SER VAL
SEQRES 12 G 174 GLY PRO LEU THR ARG LYS GLY PHE TYR LEU ALA PHE GLN
SEQRES 13 G 174 ASP ILE GLY ALA CYS VAL ALA LEU LEU SER VAL ARG VAL
SEQRES 14 G 174 TYR TYR LYS LYS CYS
SEQRES 1 H 132 ALA ASP ARG HIS THR VAL PHE TRP ASN SER SER ASN PRO
SEQRES 2 H 132 LYS PHE ARG ASN GLU ASP TYR THR ILE HIS VAL GLN LEU
SEQRES 3 H 132 ASN ASP TYR VAL ASP ILE ILE CYS PRO HIS TYR GLU ASP
SEQRES 4 H 132 HIS SER VAL ALA ASP ALA ALA MET GLU GLN TYR ILE LEU
SEQRES 5 H 132 TYR LEU VAL GLU HIS GLU GLU TYR GLN LEU CYS GLN PRO
SEQRES 6 H 132 GLN SER LYS ASP GLN VAL ARG TRP GLN CYS ASN ARG PRO
SEQRES 7 H 132 SER ALA LYS HIS GLY PRO GLU LYS LEU SER GLU LYS PHE
SEQRES 8 H 132 GLN ARG PHE THR PRO PHE THR LEU GLY LYS GLU PHE LYS
SEQRES 9 H 132 GLU GLY HIS SER TYR TYR TYR ILE SER LYS PRO ILE HIS
SEQRES 10 H 132 GLN HIS GLU ASP ARG CYS LEU ARG LEU LYS VAL THR VAL
SEQRES 11 H 132 LYS ILE
SEQRES 1 I 174 GLU VAL VAL LEU LEU ASP PHE ALA ALA ALA GLY GLY GLU
SEQRES 2 I 174 LEU GLY TRP LEU THR HIS PRO TYR GLY LYS GLY TRP ASP
SEQRES 3 I 174 LEU MET GLN ASN ILE MET ASN ASP MET PRO ILE TYR MET
SEQRES 4 I 174 TYR SER VAL CYS ASN VAL MET SER GLY ASP GLN ASP ASN
SEQRES 5 I 174 TRP LEU ARG THR ASN TRP VAL TYR ARG GLY GLU ALA GLU
SEQRES 6 I 174 ARG ILE PHE ILE GLU LEU LYS PHE THR VAL ARG ASP CYS
SEQRES 7 I 174 ASN SER PHE PRO GLY GLY ALA SER SER CYS LYS GLU THR
SEQRES 8 I 174 PHE ASN LEU TYR TYR ALA GLU SER ASP LEU ASP TYR GLY
SEQRES 9 I 174 THR ASN PHE GLN LYS ARG LEU PHE THR LYS ILE ASP THR
SEQRES 10 I 174 ILE ALA PRO ASP GLU ILE THR VAL SER SER ASP PHE GLU
SEQRES 11 I 174 ALA ARG HIS VAL LYS LEU ASN VAL GLU GLU ARG SER VAL
SEQRES 12 I 174 GLY PRO LEU THR ARG LYS GLY PHE TYR LEU ALA PHE GLN
SEQRES 13 I 174 ASP ILE GLY ALA CYS VAL ALA LEU LEU SER VAL ARG VAL
SEQRES 14 I 174 TYR TYR LYS LYS CYS
SEQRES 1 J 132 ALA ASP ARG HIS THR VAL PHE TRP ASN SER SER ASN PRO
SEQRES 2 J 132 LYS PHE ARG ASN GLU ASP TYR THR ILE HIS VAL GLN LEU
SEQRES 3 J 132 ASN ASP TYR VAL ASP ILE ILE CYS PRO HIS TYR GLU ASP
SEQRES 4 J 132 HIS SER VAL ALA ASP ALA ALA MET GLU GLN TYR ILE LEU
SEQRES 5 J 132 TYR LEU VAL GLU HIS GLU GLU TYR GLN LEU CYS GLN PRO
SEQRES 6 J 132 GLN SER LYS ASP GLN VAL ARG TRP GLN CYS ASN ARG PRO
SEQRES 7 J 132 SER ALA LYS HIS GLY PRO GLU LYS LEU SER GLU LYS PHE
SEQRES 8 J 132 GLN ARG PHE THR PRO PHE THR LEU GLY LYS GLU PHE LYS
SEQRES 9 J 132 GLU GLY HIS SER TYR TYR TYR ILE SER LYS PRO ILE HIS
SEQRES 10 J 132 GLN HIS GLU ASP ARG CYS LEU ARG LEU LYS VAL THR VAL
SEQRES 11 J 132 LYS ILE
SEQRES 1 K 174 GLU VAL VAL LEU LEU ASP PHE ALA ALA ALA GLY GLY GLU
SEQRES 2 K 174 LEU GLY TRP LEU THR HIS PRO TYR GLY LYS GLY TRP ASP
SEQRES 3 K 174 LEU MET GLN ASN ILE MET ASN ASP MET PRO ILE TYR MET
SEQRES 4 K 174 TYR SER VAL CYS ASN VAL MET SER GLY ASP GLN ASP ASN
SEQRES 5 K 174 TRP LEU ARG THR ASN TRP VAL TYR ARG GLY GLU ALA GLU
SEQRES 6 K 174 ARG ILE PHE ILE GLU LEU LYS PHE THR VAL ARG ASP CYS
SEQRES 7 K 174 ASN SER PHE PRO GLY GLY ALA SER SER CYS LYS GLU THR
SEQRES 8 K 174 PHE ASN LEU TYR TYR ALA GLU SER ASP LEU ASP TYR GLY
SEQRES 9 K 174 THR ASN PHE GLN LYS ARG LEU PHE THR LYS ILE ASP THR
SEQRES 10 K 174 ILE ALA PRO ASP GLU ILE THR VAL SER SER ASP PHE GLU
SEQRES 11 K 174 ALA ARG HIS VAL LYS LEU ASN VAL GLU GLU ARG SER VAL
SEQRES 12 K 174 GLY PRO LEU THR ARG LYS GLY PHE TYR LEU ALA PHE GLN
SEQRES 13 K 174 ASP ILE GLY ALA CYS VAL ALA LEU LEU SER VAL ARG VAL
SEQRES 14 K 174 TYR TYR LYS LYS CYS
SEQRES 1 L 132 ALA ASP ARG HIS THR VAL PHE TRP ASN SER SER ASN PRO
SEQRES 2 L 132 LYS PHE ARG ASN GLU ASP TYR THR ILE HIS VAL GLN LEU
SEQRES 3 L 132 ASN ASP TYR VAL ASP ILE ILE CYS PRO HIS TYR GLU ASP
SEQRES 4 L 132 HIS SER VAL ALA ASP ALA ALA MET GLU GLN TYR ILE LEU
SEQRES 5 L 132 TYR LEU VAL GLU HIS GLU GLU TYR GLN LEU CYS GLN PRO
SEQRES 6 L 132 GLN SER LYS ASP GLN VAL ARG TRP GLN CYS ASN ARG PRO
SEQRES 7 L 132 SER ALA LYS HIS GLY PRO GLU LYS LEU SER GLU LYS PHE
SEQRES 8 L 132 GLN ARG PHE THR PRO PHE THR LEU GLY LYS GLU PHE LYS
SEQRES 9 L 132 GLU GLY HIS SER TYR TYR TYR ILE SER LYS PRO ILE HIS
SEQRES 10 L 132 GLN HIS GLU ASP ARG CYS LEU ARG LEU LYS VAL THR VAL
SEQRES 11 L 132 LYS ILE
SEQRES 1 M 174 GLU VAL VAL LEU LEU ASP PHE ALA ALA ALA GLY GLY GLU
SEQRES 2 M 174 LEU GLY TRP LEU THR HIS PRO TYR GLY LYS GLY TRP ASP
SEQRES 3 M 174 LEU MET GLN ASN ILE MET ASN ASP MET PRO ILE TYR MET
SEQRES 4 M 174 TYR SER VAL CYS ASN VAL MET SER GLY ASP GLN ASP ASN
SEQRES 5 M 174 TRP LEU ARG THR ASN TRP VAL TYR ARG GLY GLU ALA GLU
SEQRES 6 M 174 ARG ILE PHE ILE GLU LEU LYS PHE THR VAL ARG ASP CYS
SEQRES 7 M 174 ASN SER PHE PRO GLY GLY ALA SER SER CYS LYS GLU THR
SEQRES 8 M 174 PHE ASN LEU TYR TYR ALA GLU SER ASP LEU ASP TYR GLY
SEQRES 9 M 174 THR ASN PHE GLN LYS ARG LEU PHE THR LYS ILE ASP THR
SEQRES 10 M 174 ILE ALA PRO ASP GLU ILE THR VAL SER SER ASP PHE GLU
SEQRES 11 M 174 ALA ARG HIS VAL LYS LEU ASN VAL GLU GLU ARG SER VAL
SEQRES 12 M 174 GLY PRO LEU THR ARG LYS GLY PHE TYR LEU ALA PHE GLN
SEQRES 13 M 174 ASP ILE GLY ALA CYS VAL ALA LEU LEU SER VAL ARG VAL
SEQRES 14 M 174 TYR TYR LYS LYS CYS
SEQRES 1 N 132 ALA ASP ARG HIS THR VAL PHE TRP ASN SER SER ASN PRO
SEQRES 2 N 132 LYS PHE ARG ASN GLU ASP TYR THR ILE HIS VAL GLN LEU
SEQRES 3 N 132 ASN ASP TYR VAL ASP ILE ILE CYS PRO HIS TYR GLU ASP
SEQRES 4 N 132 HIS SER VAL ALA ASP ALA ALA MET GLU GLN TYR ILE LEU
SEQRES 5 N 132 TYR LEU VAL GLU HIS GLU GLU TYR GLN LEU CYS GLN PRO
SEQRES 6 N 132 GLN SER LYS ASP GLN VAL ARG TRP GLN CYS ASN ARG PRO
SEQRES 7 N 132 SER ALA LYS HIS GLY PRO GLU LYS LEU SER GLU LYS PHE
SEQRES 8 N 132 GLN ARG PHE THR PRO PHE THR LEU GLY LYS GLU PHE LYS
SEQRES 9 N 132 GLU GLY HIS SER TYR TYR TYR ILE SER LYS PRO ILE HIS
SEQRES 10 N 132 GLN HIS GLU ASP ARG CYS LEU ARG LEU LYS VAL THR VAL
SEQRES 11 N 132 LYS ILE
SEQRES 1 O 174 GLU VAL VAL LEU LEU ASP PHE ALA ALA ALA GLY GLY GLU
SEQRES 2 O 174 LEU GLY TRP LEU THR HIS PRO TYR GLY LYS GLY TRP ASP
SEQRES 3 O 174 LEU MET GLN ASN ILE MET ASN ASP MET PRO ILE TYR MET
SEQRES 4 O 174 TYR SER VAL CYS ASN VAL MET SER GLY ASP GLN ASP ASN
SEQRES 5 O 174 TRP LEU ARG THR ASN TRP VAL TYR ARG GLY GLU ALA GLU
SEQRES 6 O 174 ARG ILE PHE ILE GLU LEU LYS PHE THR VAL ARG ASP CYS
SEQRES 7 O 174 ASN SER PHE PRO GLY GLY ALA SER SER CYS LYS GLU THR
SEQRES 8 O 174 PHE ASN LEU TYR TYR ALA GLU SER ASP LEU ASP TYR GLY
SEQRES 9 O 174 THR ASN PHE GLN LYS ARG LEU PHE THR LYS ILE ASP THR
SEQRES 10 O 174 ILE ALA PRO ASP GLU ILE THR VAL SER SER ASP PHE GLU
SEQRES 11 O 174 ALA ARG HIS VAL LYS LEU ASN VAL GLU GLU ARG SER VAL
SEQRES 12 O 174 GLY PRO LEU THR ARG LYS GLY PHE TYR LEU ALA PHE GLN
SEQRES 13 O 174 ASP ILE GLY ALA CYS VAL ALA LEU LEU SER VAL ARG VAL
SEQRES 14 O 174 TYR TYR LYS LYS CYS
SEQRES 1 P 132 ALA ASP ARG HIS THR VAL PHE TRP ASN SER SER ASN PRO
SEQRES 2 P 132 LYS PHE ARG ASN GLU ASP TYR THR ILE HIS VAL GLN LEU
SEQRES 3 P 132 ASN ASP TYR VAL ASP ILE ILE CYS PRO HIS TYR GLU ASP
SEQRES 4 P 132 HIS SER VAL ALA ASP ALA ALA MET GLU GLN TYR ILE LEU
SEQRES 5 P 132 TYR LEU VAL GLU HIS GLU GLU TYR GLN LEU CYS GLN PRO
SEQRES 6 P 132 GLN SER LYS ASP GLN VAL ARG TRP GLN CYS ASN ARG PRO
SEQRES 7 P 132 SER ALA LYS HIS GLY PRO GLU LYS LEU SER GLU LYS PHE
SEQRES 8 P 132 GLN ARG PHE THR PRO PHE THR LEU GLY LYS GLU PHE LYS
SEQRES 9 P 132 GLU GLY HIS SER TYR TYR TYR ILE SER LYS PRO ILE HIS
SEQRES 10 P 132 GLN HIS GLU ASP ARG CYS LEU ARG LEU LYS VAL THR VAL
SEQRES 11 P 132 LYS ILE
FORMUL 17 HOH *2756(H2 O)
HELIX 1 1 ALA A 8 GLY A 11 5 4
HELIX 2 2 ASP A 77 PHE A 81 5 5
HELIX 3 3 GLN A 108 PHE A 112 5 5
HELIX 4 4 VAL A 125 ALA A 131 1 7
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
HELIX 9 9 ALA C 8 GLY C 11 5 4
HELIX 10 10 ASP C 77 PHE C 81 5 5
HELIX 11 11 GLN C 108 PHE C 112 5 5
HELIX 12 12 VAL C 125 ALA C 131 1 7
HELIX 13 13 ASN D 29 ARG D 33 5 5
HELIX 14 14 ALA D 60 MET D 64 5 5
HELIX 15 15 GLU D 73 CYS D 80 1 8
HELIX 16 16 SER D 84 ASP D 86 5 3
HELIX 17 17 ASP E 77 PHE E 81 5 5
HELIX 18 18 GLN E 108 PHE E 112 5 5
HELIX 19 19 SER E 126 ALA E 131 1 6
HELIX 20 20 ASN F 29 ARG F 33 5 5
HELIX 21 21 ALA F 60 MET F 64 5 5
HELIX 22 22 GLU F 73 CYS F 80 1 8
HELIX 23 23 SER F 84 ASP F 86 5 3
HELIX 24 24 ALA G 8 GLY G 11 5 4
HELIX 25 25 GLN G 108 PHE G 112 5 5
HELIX 26 26 VAL G 125 PHE G 129 5 5
HELIX 27 27 ASN H 29 ARG H 33 5 5
HELIX 28 28 ALA H 60 MET H 64 5 5
HELIX 29 29 GLU H 73 CYS H 80 1 8
HELIX 30 30 SER H 84 ASP H 86 5 3
HELIX 31 31 ALA I 8 GLY I 11 5 4
HELIX 32 32 GLN I 108 PHE I 112 5 5
HELIX 33 33 SER I 126 ALA I 131 1 6
HELIX 34 34 ASN J 29 ARG J 33 5 5
HELIX 35 35 ALA J 60 MET J 64 5 5
HELIX 36 36 GLU J 73 CYS J 80 1 8
HELIX 37 37 SER J 84 ASP J 86 5 3
HELIX 38 38 ALA K 8 GLY K 11 5 4
HELIX 39 39 ASP K 77 PHE K 81 5 5
HELIX 40 40 GLN K 108 PHE K 112 5 5
HELIX 41 41 VAL K 125 PHE K 129 5 5
HELIX 42 42 ASN L 29 ARG L 33 5 5
HELIX 43 43 ALA L 60 MET L 64 5 5
HELIX 44 44 GLU L 73 CYS L 80 1 8
HELIX 45 45 SER L 84 ASP L 86 5 3
HELIX 46 46 ALA M 8 GLY M 11 5 4
HELIX 47 47 GLN M 108 PHE M 112 5 5
HELIX 48 48 VAL M 125 ALA M 131 1 7
HELIX 49 49 ASN N 29 ARG N 33 5 5
HELIX 50 50 ALA N 60 MET N 64 5 5
HELIX 51 51 GLU N 73 CYS N 80 1 8
HELIX 52 52 SER N 84 ASP N 86 5 3
HELIX 53 53 ALA O 8 GLY O 11 5 4
HELIX 54 54 ASP O 77 PHE O 81 5 5
HELIX 55 55 GLN O 108 PHE O 112 5 5
HELIX 56 56 VAL O 125 PHE O 129 5 5
HELIX 57 57 ASN P 29 ARG P 33 5 5
HELIX 58 58 ALA P 60 MET P 64 5 5
HELIX 59 59 GLU P 73 CYS P 80 1 8
HELIX 60 60 SER P 84 ASP P 86 5 3
SHEET 1 A 4 VAL A 2 ASP A 6 0
SHEET 2 A 4 VAL A 162 TYR A 171 -1 O VAL A 169 N LEU A 4
SHEET 3 A 4 MET A 35 VAL A 42 -1 N TYR A 40 O LEU A 164
SHEET 4 A 4 ASP A 26 MET A 32 -1 N ASN A 30 O ILE A 37
SHEET 1 B 4 VAL A 2 ASP A 6 0
SHEET 2 B 4 VAL A 162 TYR A 171 -1 O VAL A 169 N LEU A 4
SHEET 3 B 4 ILE A 67 VAL A 75 -1 N GLU A 70 O ARG A 168
SHEET 4 B 4 ASN A 137 VAL A 143 -1 O GLU A 139 N LEU A 71
SHEET 1 C 4 LEU A 17 HIS A 19 0
SHEET 2 C 4 ASN A 52 ARG A 55 -1 O TRP A 53 N HIS A 19
SHEET 3 C 4 GLY A 150 ASP A 157 -1 O ASP A 157 N ASN A 52
SHEET 4 C 4 VAL A 59 TYR A 60 -1 N VAL A 59 O PHE A 151
SHEET 1 D 5 LEU A 17 HIS A 19 0
SHEET 2 D 5 ASN A 52 ARG A 55 -1 O TRP A 53 N HIS A 19
SHEET 3 D 5 GLY A 150 ASP A 157 -1 O ASP A 157 N ASN A 52
SHEET 4 D 5 PHE A 92 SER A 99 -1 N TYR A 95 O ALA A 154
SHEET 5 D 5 THR A 113 ILE A 118 -1 O THR A 113 N TYR A 96
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 VAL B 23
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
SHEET 1 G 4 VAL C 2 ASP C 6 0
SHEET 2 G 4 CYS C 161 TYR C 171 -1 O VAL C 169 N LEU C 4
SHEET 3 G 4 MET C 35 CYS C 43 -1 N TYR C 40 O LEU C 164
SHEET 4 G 4 ASP C 26 MET C 32 -1 N MET C 28 O MET C 39
SHEET 1 H 4 VAL C 2 ASP C 6 0
SHEET 2 H 4 CYS C 161 TYR C 171 -1 O VAL C 169 N LEU C 4
SHEET 3 H 4 ILE C 67 VAL C 75 -1 N PHE C 68 O TYR C 170
SHEET 4 H 4 ASN C 137 VAL C 143 -1 O ARG C 141 N ILE C 69
SHEET 1 I 4 LEU C 17 HIS C 19 0
SHEET 2 I 4 ASN C 52 ARG C 55 -1 O TRP C 53 N HIS C 19
SHEET 3 I 4 GLY C 150 ASP C 157 -1 O ASP C 157 N ASN C 52
SHEET 4 I 4 VAL C 59 TYR C 60 -1 N VAL C 59 O PHE C 151
SHEET 1 J 5 LEU C 17 HIS C 19 0
SHEET 2 J 5 ASN C 52 ARG C 55 -1 O TRP C 53 N HIS C 19
SHEET 3 J 5 GLY C 150 ASP C 157 -1 O ASP C 157 N ASN C 52
SHEET 4 J 5 PHE C 92 SER C 99 -1 N ALA C 97 O TYR C 152
SHEET 5 J 5 THR C 113 ILE C 118 -1 O ILE C 118 N PHE C 92
SHEET 1 K 3 ARG D 20 PHE D 24 0
SHEET 2 K 3 TYR D 46 ILE D 50 1 O ILE D 50 N VAL D 23
SHEET 3 K 3 LYS D 103 LYS D 107 -1 O LEU D 104 N ILE D 49
SHEET 1 L 5 THR D 38 VAL D 41 0
SHEET 2 L 5 ARG D 142 VAL D 147 1 O THR D 146 N VAL D 41
SHEET 3 L 5 SER D 125 PRO D 132 -1 N TYR D 126 O VAL D 145
SHEET 4 L 5 TYR D 67 VAL D 72 -1 N TYR D 70 O ILE D 129
SHEET 5 L 5 VAL D 88 CYS D 92 -1 O ARG D 89 N LEU D 69
SHEET 1 M 4 VAL E 2 ASP E 6 0
SHEET 2 M 4 VAL E 162 TYR E 171 -1 O TYR E 171 N VAL E 2
SHEET 3 M 4 MET E 35 VAL E 42 -1 N TYR E 40 O LEU E 164
SHEET 4 M 4 ASP E 26 MET E 32 -1 N ASN E 30 O ILE E 37
SHEET 1 N 4 VAL E 2 ASP E 6 0
SHEET 2 N 4 VAL E 162 TYR E 171 -1 O TYR E 171 N VAL E 2
SHEET 3 N 4 ILE E 67 VAL E 75 -1 N GLU E 70 O ARG E 168
SHEET 4 N 4 ASN E 137 VAL E 143 -1 O GLU E 139 N LEU E 71
SHEET 1 O 4 LEU E 17 HIS E 19 0
SHEET 2 O 4 ASN E 52 ARG E 55 -1 O TRP E 53 N HIS E 19
SHEET 3 O 4 GLY E 150 ASP E 157 -1 O ASP E 157 N ASN E 52
SHEET 4 O 4 VAL E 59 TYR E 60 -1 N VAL E 59 O PHE E 151
SHEET 1 P 5 LEU E 17 HIS E 19 0
SHEET 2 P 5 ASN E 52 ARG E 55 -1 O TRP E 53 N HIS E 19
SHEET 3 P 5 GLY E 150 ASP E 157 -1 O ASP E 157 N ASN E 52
SHEET 4 P 5 PHE E 92 SER E 99 -1 N TYR E 95 O ALA E 154
SHEET 5 P 5 THR E 113 ILE E 118 -1 O ILE E 118 N PHE E 92
SHEET 1 Q 3 ARG F 20 PHE F 24 0
SHEET 2 Q 3 TYR F 46 ILE F 50 1 O ILE F 50 N VAL F 23
SHEET 3 Q 3 LYS F 103 LYS F 107 -1 O LEU F 104 N ILE F 49
SHEET 1 R 5 THR F 38 VAL F 41 0
SHEET 2 R 5 ARG F 142 VAL F 147 1 O THR F 146 N VAL F 41
SHEET 3 R 5 SER F 125 PRO F 132 -1 N TYR F 126 O VAL F 145
SHEET 4 R 5 TYR F 67 VAL F 72 -1 N ILE F 68 O LYS F 131
SHEET 5 R 5 VAL F 88 CYS F 92 -1 O ARG F 89 N LEU F 69
SHEET 1 S 4 VAL G 2 ASP G 6 0
SHEET 2 S 4 CYS G 161 TYR G 171 -1 O VAL G 169 N LEU G 4
SHEET 3 S 4 MET G 35 CYS G 43 -1 N TYR G 40 O LEU G 164
SHEET 4 S 4 ASP G 26 MET G 32 -1 N MET G 28 O MET G 39
SHEET 1 T 4 VAL G 2 ASP G 6 0
SHEET 2 T 4 CYS G 161 TYR G 171 -1 O VAL G 169 N LEU G 4
SHEET 3 T 4 ILE G 67 VAL G 75 -1 N GLU G 70 O ARG G 168
SHEET 4 T 4 ASN G 137 VAL G 143 -1 O ARG G 141 N ILE G 69
SHEET 1 U 4 LEU G 17 HIS G 19 0
SHEET 2 U 4 ASN G 52 ARG G 55 -1 O ARG G 55 N LEU G 17
SHEET 3 U 4 GLY G 150 ASP G 157 -1 O ASP G 157 N ASN G 52
SHEET 4 U 4 VAL G 59 TYR G 60 -1 N VAL G 59 O PHE G 151
SHEET 1 V 5 LEU G 17 HIS G 19 0
SHEET 2 V 5 ASN G 52 ARG G 55 -1 O ARG G 55 N LEU G 17
SHEET 3 V 5 GLY G 150 ASP G 157 -1 O ASP G 157 N ASN G 52
SHEET 4 V 5 PHE G 92 SER G 99 -1 N ALA G 97 O TYR G 152
SHEET 5 V 5 THR G 113 ILE G 118 -1 O ILE G 115 N LEU G 94
SHEET 1 W 3 ARG H 20 PHE H 24 0
SHEET 2 W 3 TYR H 46 ILE H 50 1 O ILE H 50 N VAL H 23
SHEET 3 W 3 LYS H 103 LYS H 107 -1 O LEU H 104 N ILE H 49
SHEET 1 X 5 THR H 38 VAL H 41 0
SHEET 2 X 5 ARG H 142 VAL H 147 1 O THR H 146 N ILE H 39
SHEET 3 X 5 SER H 125 PRO H 132 -1 N TYR H 126 O VAL H 145
SHEET 4 X 5 TYR H 67 VAL H 72 -1 N ILE H 68 O LYS H 131
SHEET 5 X 5 VAL H 88 CYS H 92 -1 O CYS H 92 N TYR H 67
SHEET 1 Y 4 VAL I 2 ASP I 6 0
SHEET 2 Y 4 CYS I 161 TYR I 171 -1 O VAL I 169 N LEU I 4
SHEET 3 Y 4 MET I 35 CYS I 43 -1 N TYR I 40 O LEU I 164
SHEET 4 Y 4 ASP I 26 MET I 32 -1 N MET I 28 O MET I 39
SHEET 1 Z 4 VAL I 2 ASP I 6 0
SHEET 2 Z 4 CYS I 161 TYR I 171 -1 O VAL I 169 N LEU I 4
SHEET 3 Z 4 ILE I 67 VAL I 75 -1 N THR I 74 O ALA I 163
SHEET 4 Z 4 ASN I 137 VAL I 143 -1 O GLU I 139 N LEU I 71
SHEET 1 AA 4 LEU I 17 HIS I 19 0
SHEET 2 AA 4 ASN I 52 ARG I 55 -1 O TRP I 53 N HIS I 19
SHEET 3 AA 4 GLY I 150 ASP I 157 -1 O ASP I 157 N ASN I 52
SHEET 4 AA 4 VAL I 59 TYR I 60 -1 N VAL I 59 O PHE I 151
SHEET 1 AB 5 LEU I 17 HIS I 19 0
SHEET 2 AB 5 ASN I 52 ARG I 55 -1 O TRP I 53 N HIS I 19
SHEET 3 AB 5 GLY I 150 ASP I 157 -1 O ASP I 157 N ASN I 52
SHEET 4 AB 5 PHE I 92 SER I 99 -1 N ALA I 97 O TYR I 152
SHEET 5 AB 5 THR I 113 ILE I 118 -1 O ILE I 118 N PHE I 92
SHEET 1 AC 3 ARG J 20 PHE J 24 0
SHEET 2 AC 3 TYR J 46 ILE J 50 1 O ASP J 48 N HIS J 21
SHEET 3 AC 3 LYS J 103 LYS J 107 -1 O LEU J 104 N ILE J 49
SHEET 1 AD 5 THR J 38 VAL J 41 0
SHEET 2 AD 5 ARG J 142 VAL J 147 1 O THR J 146 N VAL J 41
SHEET 3 AD 5 SER J 125 PRO J 132 -1 N TYR J 126 O VAL J 145
SHEET 4 AD 5 TYR J 67 VAL J 72 -1 N ILE J 68 O LYS J 131
SHEET 5 AD 5 VAL J 88 CYS J 92 -1 O ARG J 89 N LEU J 69
SHEET 1 AE 4 VAL K 2 ASP K 6 0
SHEET 2 AE 4 VAL K 162 TYR K 171 -1 O VAL K 169 N LEU K 5
SHEET 3 AE 4 MET K 35 VAL K 42 -1 N TYR K 40 O LEU K 164
SHEET 4 AE 4 ASP K 26 MET K 32 -1 N MET K 28 O MET K 39
SHEET 1 AF 4 VAL K 2 ASP K 6 0
SHEET 2 AF 4 VAL K 162 TYR K 171 -1 O VAL K 169 N LEU K 5
SHEET 3 AF 4 ILE K 67 VAL K 75 -1 N PHE K 68 O TYR K 170
SHEET 4 AF 4 ASN K 137 VAL K 143 -1 O ARG K 141 N ILE K 69
SHEET 1 AG 4 LEU K 17 HIS K 19 0
SHEET 2 AG 4 ASN K 52 ARG K 55 -1 O TRP K 53 N HIS K 19
SHEET 3 AG 4 GLY K 150 ASP K 157 -1 O ASP K 157 N ASN K 52
SHEET 4 AG 4 VAL K 59 TYR K 60 -1 N VAL K 59 O PHE K 151
SHEET 1 AH 5 LEU K 17 HIS K 19 0
SHEET 2 AH 5 ASN K 52 ARG K 55 -1 O TRP K 53 N HIS K 19
SHEET 3 AH 5 GLY K 150 ASP K 157 -1 O ASP K 157 N ASN K 52
SHEET 4 AH 5 PHE K 92 SER K 99 -1 N TYR K 95 O ALA K 154
SHEET 5 AH 5 THR K 113 ILE K 118 -1 O ILE K 118 N PHE K 92
SHEET 1 AI 3 ARG L 20 PHE L 24 0
SHEET 2 AI 3 TYR L 46 ILE L 50 1 O ILE L 50 N VAL L 23
SHEET 3 AI 3 LYS L 103 LYS L 107 -1 O LEU L 104 N ILE L 49
SHEET 1 AJ 5 THR L 38 VAL L 41 0
SHEET 2 AJ 5 ARG L 142 VAL L 147 1 O THR L 146 N VAL L 41
SHEET 3 AJ 5 SER L 125 PRO L 132 -1 N TYR L 126 O VAL L 145
SHEET 4 AJ 5 TYR L 67 VAL L 72 -1 N ILE L 68 O LYS L 131
SHEET 5 AJ 5 VAL L 88 CYS L 92 -1 O ARG L 89 N LEU L 69
SHEET 1 AK 4 VAL M 2 ASP M 6 0
SHEET 2 AK 4 CYS M 161 TYR M 171 -1 O VAL M 169 N LEU M 4
SHEET 3 AK 4 MET M 35 CYS M 43 -1 N TYR M 40 O LEU M 164
SHEET 4 AK 4 ASP M 26 MET M 32 -1 N MET M 28 O MET M 39
SHEET 1 AL 4 VAL M 2 ASP M 6 0
SHEET 2 AL 4 CYS M 161 TYR M 171 -1 O VAL M 169 N LEU M 4
SHEET 3 AL 4 ILE M 67 VAL M 75 -1 N PHE M 68 O TYR M 170
SHEET 4 AL 4 ASN M 137 VAL M 143 -1 O GLU M 139 N LEU M 71
SHEET 1 AM 4 LEU M 17 HIS M 19 0
SHEET 2 AM 4 ASN M 52 ARG M 55 -1 O TRP M 53 N HIS M 19
SHEET 3 AM 4 GLY M 150 ASP M 157 -1 O ASP M 157 N ASN M 52
SHEET 4 AM 4 VAL M 59 TYR M 60 -1 N VAL M 59 O PHE M 151
SHEET 1 AN 5 LEU M 17 HIS M 19 0
SHEET 2 AN 5 ASN M 52 ARG M 55 -1 O TRP M 53 N HIS M 19
SHEET 3 AN 5 GLY M 150 ASP M 157 -1 O ASP M 157 N ASN M 52
SHEET 4 AN 5 PHE M 92 SER M 99 -1 N TYR M 95 O ALA M 154
SHEET 5 AN 5 THR M 113 ILE M 118 -1 O ILE M 118 N PHE M 92
SHEET 1 AO 3 ARG N 20 PHE N 24 0
SHEET 2 AO 3 TYR N 46 ILE N 50 1 O ILE N 50 N VAL N 23
SHEET 3 AO 3 LYS N 103 LYS N 107 -1 O LEU N 104 N ILE N 49
SHEET 1 AP 5 THR N 38 VAL N 41 0
SHEET 2 AP 5 ARG N 142 VAL N 147 1 O THR N 146 N VAL N 41
SHEET 3 AP 5 SER N 125 PRO N 132 -1 N TYR N 128 O LEU N 143
SHEET 4 AP 5 TYR N 67 VAL N 72 -1 N TYR N 70 O ILE N 129
SHEET 5 AP 5 VAL N 88 CYS N 92 -1 O ARG N 89 N LEU N 69
SHEET 1 AQ 4 VAL O 2 ASP O 6 0
SHEET 2 AQ 4 VAL O 162 TYR O 171 -1 O VAL O 169 N LEU O 4
SHEET 3 AQ 4 MET O 35 VAL O 42 -1 N TYR O 40 O LEU O 164
SHEET 4 AQ 4 ASP O 26 MET O 32 -1 N ASN O 30 O ILE O 37
SHEET 1 AR 4 VAL O 2 ASP O 6 0
SHEET 2 AR 4 VAL O 162 TYR O 171 -1 O VAL O 169 N LEU O 4
SHEET 3 AR 4 ILE O 67 VAL O 75 -1 N PHE O 68 O TYR O 170
SHEET 4 AR 4 ASN O 137 VAL O 143 -1 O GLU O 139 N LEU O 71
SHEET 1 AS 4 LEU O 17 HIS O 19 0
SHEET 2 AS 4 ASN O 52 ARG O 55 -1 O TRP O 53 N HIS O 19
SHEET 3 AS 4 GLY O 150 ASP O 157 -1 O ASP O 157 N ASN O 52
SHEET 4 AS 4 VAL O 59 TYR O 60 -1 N VAL O 59 O PHE O 151
SHEET 1 AT 5 LEU O 17 HIS O 19 0
SHEET 2 AT 5 ASN O 52 ARG O 55 -1 O TRP O 53 N HIS O 19
SHEET 3 AT 5 GLY O 150 ASP O 157 -1 O ASP O 157 N ASN O 52
SHEET 4 AT 5 PHE O 92 SER O 99 -1 N TYR O 95 O ALA O 154
SHEET 5 AT 5 THR O 113 ILE O 118 -1 O ILE O 115 N LEU O 94
SHEET 1 AU 3 ARG P 20 PHE P 24 0
SHEET 2 AU 3 TYR P 46 ILE P 50 1 O ILE P 50 N VAL P 23
SHEET 3 AU 3 LYS P 103 LYS P 107 -1 O LEU P 104 N ILE P 49
SHEET 1 AV 5 THR P 38 VAL P 41 0
SHEET 2 AV 5 ARG P 142 VAL P 147 1 O THR P 146 N VAL P 41
SHEET 3 AV 5 SER P 125 PRO P 132 -1 N TYR P 126 O VAL P 145
SHEET 4 AV 5 TYR P 67 VAL P 72 -1 N TYR P 70 O ILE P 129
SHEET 5 AV 5 VAL P 88 CYS P 92 -1 O CYS P 92 N TYR P 67
SSBOND 1 CYS A 43 CYS A 161 1555 1555 2.08
SSBOND 2 CYS A 78 CYS A 88 1555 1555 2.07
SSBOND 3 CYS B 51 CYS B 92 1555 1555 2.16
SSBOND 4 CYS B 80 CYS B 140 1555 1555 2.05
SSBOND 5 CYS C 43 CYS C 161 1555 1555 2.07
SSBOND 6 CYS C 78 CYS C 88 1555 1555 2.07
SSBOND 7 CYS D 51 CYS D 92 1555 1555 2.05
SSBOND 8 CYS D 80 CYS D 140 1555 1555 2.04
SSBOND 9 CYS E 43 CYS E 161 1555 1555 2.09
SSBOND 10 CYS E 78 CYS E 88 1555 1555 2.07
SSBOND 11 CYS F 51 CYS F 92 1555 1555 2.13
SSBOND 12 CYS F 80 CYS F 140 1555 1555 2.08
SSBOND 13 CYS G 43 CYS G 161 1555 1555 2.13
SSBOND 14 CYS G 78 CYS G 88 1555 1555 2.06
SSBOND 15 CYS H 51 CYS H 92 1555 1555 2.15
SSBOND 16 CYS H 80 CYS H 140 1555 1555 2.05
SSBOND 17 CYS I 43 CYS I 161 1555 1555 2.08
SSBOND 18 CYS I 78 CYS I 88 1555 1555 2.04
SSBOND 19 CYS J 51 CYS J 92 1555 1555 2.16
SSBOND 20 CYS J 80 CYS J 140 1555 1555 2.05
SSBOND 21 CYS K 43 CYS K 161 1555 1555 2.08
SSBOND 22 CYS K 78 CYS K 88 1555 1555 2.12
SSBOND 23 CYS L 51 CYS L 92 1555 1555 2.11
SSBOND 24 CYS L 80 CYS L 140 1555 1555 2.02
SSBOND 25 CYS M 43 CYS M 161 1555 1555 2.07
SSBOND 26 CYS M 78 CYS M 88 1555 1555 2.03
SSBOND 27 CYS N 51 CYS N 92 1555 1555 2.12
SSBOND 28 CYS N 80 CYS N 140 1555 1555 2.02
SSBOND 29 CYS O 43 CYS O 161 1555 1555 2.08
SSBOND 30 CYS O 78 CYS O 88 1555 1555 2.04
SSBOND 31 CYS P 51 CYS P 92 1555 1555 2.15
SSBOND 32 CYS P 80 CYS P 140 1555 1555 2.01
CISPEP 1 HIS A 19 PRO A 20 0 -6.10
CISPEP 2 GLY A 144 PRO A 145 0 0.39
CISPEP 3 HIS C 19 PRO C 20 0 -5.69
CISPEP 4 GLY C 144 PRO C 145 0 4.94
CISPEP 5 HIS E 19 PRO E 20 0 -9.29
CISPEP 6 GLY E 144 PRO E 145 0 5.20
CISPEP 7 HIS G 19 PRO G 20 0 -4.31
CISPEP 8 GLY G 144 PRO G 145 0 5.39
CISPEP 9 HIS I 19 PRO I 20 0 -9.48
CISPEP 10 GLY I 144 PRO I 145 0 -1.48
CISPEP 11 HIS K 19 PRO K 20 0 -4.62
CISPEP 12 GLY K 144 PRO K 145 0 7.74
CISPEP 13 HIS M 19 PRO M 20 0 -5.57
CISPEP 14 GLY M 144 PRO M 145 0 4.15
CISPEP 15 HIS O 19 PRO O 20 0 -3.31
CISPEP 16 GLY O 144 PRO O 145 0 0.03
CRYST1 58.483 102.108 135.255 84.25 79.77 73.94 P 1 8
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 0.017099 -0.004922 -0.002824 0.00000
SCALE2 0.000000 0.010191 -0.000551 0.00000
SCALE3 0.000000 0.000000 0.007524 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
