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Chemical substance (2) PDB-CCD (2) Gene (1) KEGG GENES (1) Protein sequence (11) UniProt (1) SWISS-PROT (1) PDBSTR (9) Protein domain (3) InterPro (2) PROSITE (1) Literature (1) PubMed (1) All databases (18)
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HEADER ANTIMICROBIAL PROTEIN 19-MAR-12 4E86
TITLE CRYSTAL STRUCTURE OF HUMAN ALPHA-DEFENSIN 5, HD5 (LEU29ABA MUTANT)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEFENSIN-5;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, L;
COMPND 4 FRAGMENT: UNP RESIDUES 63-94;
COMPND 5 SYNONYM: ALPHA-DEFENSIN 5, HD5, DEFENSIN, ALPHA 5;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606
KEYWDS MUTANT LEU29ABA, BETA-SHEET, ANTIMICROBIAL PEPTIDE, PANETH CELLS,
KEYWDS 2 ANTIMICROBIAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR X.WU,M.PAZGIER
REVDAT 4 06-DEC-23 4E86 1 REMARK
REVDAT 3 13-SEP-23 4E86 1 REMARK SEQADV LINK
REVDAT 2 19-JUN-13 4E86 1 JRNL
REVDAT 1 16-MAY-12 4E86 0
JRNL AUTH M.RAJABI,B.ERICKSEN,X.WU,E.DE LEEUW,L.ZHAO,M.PAZGIER,W.LU
JRNL TITL FUNCTIONAL DETERMINANTS OF HUMAN ENTERIC {ALPHA}-DEFENSIN
JRNL TITL 2 HD5: CRUCIAL ROLE FOR HYDROPHOBICITY AT DIMER INTERFACE.
JRNL REF J.BIOL.CHEM. V. 287 21615 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22573326
JRNL DOI 10.1074/JBC.M112.367995
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 6808
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) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 337
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) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.82
REMARK 3 REFLECTION IN BIN (WORKING SET) : 476
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.3510
REMARK 3 BIN FREE R VALUE SET COUNT : 19
REMARK 3 BIN FREE R VALUE : 0.3950
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2172
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 31
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -39.56000
REMARK 3 B22 (A**2) : 17.66000
REMARK 3 B33 (A**2) : 21.90000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 25.40000
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): 0.086
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.256
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.280
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.887
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2211 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2904 ; 1.830 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 258 ; 8.343 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 90 ;18.066 ;16.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 387 ;19.848 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 54 ;18.758 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 321 ; 0.129 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1554 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 36
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 A 1 A 28 0
REMARK 3 0 B 1 B 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 A 1 A 28 0
REMARK 3 0 C 1 C 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : A D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 A 2 A 27 0
REMARK 3 0 D 2 D 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : A E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 A 1 A 28 0
REMARK 3 0 E 1 E 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
REMARK 3 CHAIN NAMES : A F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 A 1 A 28 0
REMARK 3 0 F 1 F 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 6
REMARK 3 CHAIN NAMES : A G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 A 1 A 28 0
REMARK 3 0 G 1 G 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 7
REMARK 3 CHAIN NAMES : A H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 A 2 A 27 0
REMARK 3 0 H 2 H 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 8
REMARK 3 CHAIN NAMES : A L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 A 2 A 27 0
REMARK 3 0 L 2 L 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 9
REMARK 3 CHAIN NAMES : B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 B 1 B 28 0
REMARK 3 0 C 1 C 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 10
REMARK 3 CHAIN NAMES : B D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 B 2 B 27 0
REMARK 3 0 D 2 D 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 11
REMARK 3 CHAIN NAMES : B E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 B 1 B 28 0
REMARK 3 0 E 1 E 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 12
REMARK 3 CHAIN NAMES : B F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 B 1 B 28 0
REMARK 3 0 F 1 F 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 13
REMARK 3 CHAIN NAMES : B G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 B 1 B 28 0
REMARK 3 0 G 1 G 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 14
REMARK 3 CHAIN NAMES : B H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 B 2 B 27 0
REMARK 3 0 H 2 H 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 15
REMARK 3 CHAIN NAMES : B L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 B 2 B 27 0
REMARK 3 0 L 2 L 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 16
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 C 2 C 27 0
REMARK 3 0 D 2 D 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 17
REMARK 3 CHAIN NAMES : C E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 C 1 C 28 0
REMARK 3 0 E 1 E 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 18
REMARK 3 CHAIN NAMES : C F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 C 1 C 28 0
REMARK 3 0 F 1 F 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 19
REMARK 3 CHAIN NAMES : C G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 C 1 C 28 0
REMARK 3 0 G 1 G 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 20
REMARK 3 CHAIN NAMES : C H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 C 2 C 27 0
REMARK 3 0 H 2 H 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 21
REMARK 3 CHAIN NAMES : C L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 C 2 C 27 0
REMARK 3 0 L 2 L 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 22
REMARK 3 CHAIN NAMES : D E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 D 2 D 27 0
REMARK 3 0 E 2 E 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 23
REMARK 3 CHAIN NAMES : D F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 D 2 D 27 0
REMARK 3 0 F 2 F 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 24
REMARK 3 CHAIN NAMES : D G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 D 2 D 27 0
REMARK 3 0 G 2 G 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 25
REMARK 3 CHAIN NAMES : D H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 D 2 D 28 0
REMARK 3 0 H 2 H 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 26
REMARK 3 CHAIN NAMES : D L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 D 2 D 28 0
REMARK 3 0 L 2 L 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 27
REMARK 3 CHAIN NAMES : E F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 E 1 E 28 0
REMARK 3 0 F 1 F 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 28
REMARK 3 CHAIN NAMES : E G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 E 1 E 28 0
REMARK 3 0 G 1 G 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 29
REMARK 3 CHAIN NAMES : E H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 E 2 E 27 0
REMARK 3 0 H 2 H 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 30
REMARK 3 CHAIN NAMES : E L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 E 2 E 27 0
REMARK 3 0 L 2 L 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 31
REMARK 3 CHAIN NAMES : F G
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 F 1 F 28 0
REMARK 3 0 G 1 G 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 32
REMARK 3 CHAIN NAMES : F H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 F 2 F 27 0
REMARK 3 0 H 2 H 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 33
REMARK 3 CHAIN NAMES : F L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 F 2 F 27 0
REMARK 3 0 L 2 L 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 34
REMARK 3 CHAIN NAMES : G H
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 G 2 G 27 0
REMARK 3 0 H 2 H 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 35
REMARK 3 CHAIN NAMES : G L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 G 2 G 27 0
REMARK 3 0 L 2 L 27 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 NCS GROUP NUMBER : 36
REMARK 3 CHAIN NAMES : H L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 0 H 2 H 28 0
REMARK 3 0 L 2 L 28 0
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
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 32
REMARK 3 ORIGIN FOR THE GROUP (A): -21.0250 -2.5160 16.3140
REMARK 3 T TENSOR
REMARK 3 T11: 0.1945 T22: 0.0934
REMARK 3 T33: 0.0651 T12: 0.0273
REMARK 3 T13: -0.0261 T23: -0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 4.0182 L22: 6.1484
REMARK 3 L33: 10.3036 L12: 2.4637
REMARK 3 L13: -1.3005 L23: 1.4247
REMARK 3 S TENSOR
REMARK 3 S11: -0.0733 S12: -0.0902 S13: -0.2349
REMARK 3 S21: -0.0490 S22: 0.2893 S23: -0.1740
REMARK 3 S31: -0.3878 S32: 0.0031 S33: -0.2160
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 1 B 32
REMARK 3 ORIGIN FOR THE GROUP (A): -31.2580 -1.6670 20.7610
REMARK 3 T TENSOR
REMARK 3 T11: 0.1848 T22: 0.2286
REMARK 3 T33: 0.0829 T12: -0.0185
REMARK 3 T13: -0.0307 T23: 0.0315
REMARK 3 L TENSOR
REMARK 3 L11: 9.9339 L22: 12.7647
REMARK 3 L33: 9.6107 L12: -1.6526
REMARK 3 L13: -2.8382 L23: 4.7051
REMARK 3 S TENSOR
REMARK 3 S11: -0.1654 S12: -0.4542 S13: -0.1149
REMARK 3 S21: 0.1761 S22: 0.3046 S23: 0.6149
REMARK 3 S31: -0.4630 S32: 0.0976 S33: -0.1392
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 32
REMARK 3 ORIGIN FOR THE GROUP (A): -18.4430 13.8960 23.8550
REMARK 3 T TENSOR
REMARK 3 T11: 0.3165 T22: 0.1223
REMARK 3 T33: 0.1264 T12: 0.0211
REMARK 3 T13: -0.0491 T23: 0.0267
REMARK 3 L TENSOR
REMARK 3 L11: 11.6497 L22: 3.3192
REMARK 3 L33: 8.2463 L12: 4.3138
REMARK 3 L13: 2.9949 L23: 1.7549
REMARK 3 S TENSOR
REMARK 3 S11: -0.1818 S12: 0.0416 S13: 0.6650
REMARK 3 S21: -0.7343 S22: 0.0497 S23: 0.2126
REMARK 3 S31: -0.2413 S32: -0.2344 S33: 0.1322
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 2 D 32
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8340 14.3250 20.7300
REMARK 3 T TENSOR
REMARK 3 T11: 0.2773 T22: 0.2307
REMARK 3 T33: 0.0997 T12: 0.0463
REMARK 3 T13: -0.1038 T23: -0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 13.2736 L22: 10.0681
REMARK 3 L33: 14.3814 L12: 3.4636
REMARK 3 L13: -2.8912 L23: -6.6975
REMARK 3 S TENSOR
REMARK 3 S11: 0.3616 S12: 0.8354 S13: 0.2168
REMARK 3 S21: -1.1941 S22: -0.1213 S23: 0.5367
REMARK 3 S31: 0.0829 S32: 0.4331 S33: -0.2403
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 32
REMARK 3 ORIGIN FOR THE GROUP (A): -17.6260 8.6020 37.9670
REMARK 3 T TENSOR
REMARK 3 T11: 0.3604 T22: 0.4910
REMARK 3 T33: 0.1766 T12: 0.0141
REMARK 3 T13: -0.1183 T23: 0.0609
REMARK 3 L TENSOR
REMARK 3 L11: 11.7532 L22: 4.7415
REMARK 3 L33: 7.7138 L12: -2.5362
REMARK 3 L13: -1.4008 L23: 1.7697
REMARK 3 S TENSOR
REMARK 3 S11: -0.0982 S12: -1.1672 S13: -0.6039
REMARK 3 S21: 1.2088 S22: 0.2318 S23: -0.1335
REMARK 3 S31: 0.3283 S32: 0.8650 S33: -0.1336
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 1 F 32
REMARK 3 ORIGIN FOR THE GROUP (A): -28.7460 9.2060 42.2080
REMARK 3 T TENSOR
REMARK 3 T11: 0.2484 T22: 0.3848
REMARK 3 T33: 0.1370 T12: 0.0454
REMARK 3 T13: -0.0576 T23: 0.1170
REMARK 3 L TENSOR
REMARK 3 L11: 6.5385 L22: 9.5246
REMARK 3 L33: 17.0578 L12: 0.0838
REMARK 3 L13: -0.3649 L23: 7.4250
REMARK 3 S TENSOR
REMARK 3 S11: -0.3273 S12: -1.1656 S13: -0.6395
REMARK 3 S21: 0.9003 S22: -0.1652 S23: -0.1037
REMARK 3 S31: 0.7813 S32: -0.2401 S33: 0.4925
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 32
REMARK 3 ORIGIN FOR THE GROUP (A): -9.9910 26.7220 1.3060
REMARK 3 T TENSOR
REMARK 3 T11: 0.4493 T22: 0.2195
REMARK 3 T33: 0.3213 T12: 0.0472
REMARK 3 T13: -0.0473 T23: -0.1188
REMARK 3 L TENSOR
REMARK 3 L11: 11.1815 L22: 2.8917
REMARK 3 L33: 15.4609 L12: -1.1793
REMARK 3 L13: -3.2073 L23: 5.2577
REMARK 3 S TENSOR
REMARK 3 S11: 0.2130 S12: 1.0602 S13: -1.1102
REMARK 3 S21: 0.0788 S22: 0.4373 S23: -0.1635
REMARK 3 S31: 1.5047 S32: 0.5998 S33: -0.6503
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 2 H 32
REMARK 3 ORIGIN FOR THE GROUP (A): -20.1530 25.8600 7.5140
REMARK 3 T TENSOR
REMARK 3 T11: 0.2368 T22: 0.1449
REMARK 3 T33: 0.2379 T12: -0.0148
REMARK 3 T13: 0.0163 T23: -0.0996
REMARK 3 L TENSOR
REMARK 3 L11: 10.0403 L22: 16.6814
REMARK 3 L33: 5.3044 L12: 0.8059
REMARK 3 L13: -0.4975 L23: -6.1402
REMARK 3 S TENSOR
REMARK 3 S11: 0.4229 S12: 0.3084 S13: -0.8126
REMARK 3 S21: -0.2002 S22: -0.4330 S23: 1.2064
REMARK 3 S31: 0.5766 S32: 0.1274 S33: 0.0102
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 : L 2 L 32
REMARK 3 ORIGIN FOR THE GROUP (A): -5.4060 40.9250 2.7020
REMARK 3 T TENSOR
REMARK 3 T11: 0.2386 T22: 0.2889
REMARK 3 T33: 0.0854 T12: -0.0592
REMARK 3 T13: -0.0363 T23: -0.0313
REMARK 3 L TENSOR
REMARK 3 L11: 16.0780 L22: 16.9966
REMARK 3 L33: 9.8523 L12: -6.6012
REMARK 3 L13: 1.8038 L23: -3.8669
REMARK 3 S TENSOR
REMARK 3 S11: -0.3265 S12: -0.0033 S13: 0.3648
REMARK 3 S21: 0.2918 S22: -0.1140 S23: -0.0670
REMARK 3 S31: -0.6087 S32: 0.3230 S33: 0.4406
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4E86 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071290.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL7-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : SIDE SCATTERING I-BEAM BENT
REMARK 200 SINGLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7168
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 54.0
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.14600
REMARK 200 R SYM (I) : 0.11900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.94900
REMARK 200 R SYM FOR SHELL (I) : 0.80200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1ZMP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES SODIUM, PH 7.5, 0.8 M
REMARK 280 SODIUM PHOSPHATE MONOBASIC MONOHYDRATE, 0.8 M POTASSIUM
REMARK 280 PHOSPHATE MONOBASIC, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 62.07050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.37850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 62.07050
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.37850
REMARK 290 SMTRY3 4 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, 9, 10, 11, 12, 13, 14
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 10
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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: 11
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 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: 12
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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: 13
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4580 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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: 14
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 4520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA D 1
REMARK 465 ALA H 1
REMARK 465 ALA L 1
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 ARG G 28 N ABA G 29 1.24
REMARK 500 O ABA E 29 N CYS E 30 1.25
REMARK 500 O ARG G 28 CA ABA G 29 1.52
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 ABA B 29 CA - C - N ANGL. DEV. = -22.8 DEGREES
REMARK 500 ABA B 29 O - C - N ANGL. DEV. = 15.3 DEGREES
REMARK 500 ARG C 28 CA - C - N ANGL. DEV. = -13.3 DEGREES
REMARK 500 ARG C 28 O - C - N ANGL. DEV. = 11.8 DEGREES
REMARK 500 ARG D 28 CA - C - N ANGL. DEV. = -13.3 DEGREES
REMARK 500 ABA D 29 C - N - CA ANGL. DEV. = -17.5 DEGREES
REMARK 500 ABA E 29 O - C - N ANGL. DEV. = -64.3 DEGREES
REMARK 500 CYS E 30 C - N - CA ANGL. DEV. = 26.1 DEGREES
REMARK 500 ARG F 28 CA - C - N ANGL. DEV. = 27.0 DEGREES
REMARK 500 ARG F 28 O - C - N ANGL. DEV. = -30.4 DEGREES
REMARK 500 ABA F 29 CA - C - N ANGL. DEV. = -14.2 DEGREES
REMARK 500 ABA F 29 O - C - N ANGL. DEV. = -22.3 DEGREES
REMARK 500 CYS F 30 C - N - CA ANGL. DEV. = 16.2 DEGREES
REMARK 500 ARG G 28 CA - C - N ANGL. DEV. = 35.0 DEGREES
REMARK 500 ARG G 28 O - C - N ANGL. DEV. = -67.1 DEGREES
REMARK 500 ABA G 29 C - N - CA ANGL. DEV. = -15.7 DEGREES
REMARK 500 ABA G 29 CA - C - N ANGL. DEV. = -31.2 DEGREES
REMARK 500 ABA G 29 O - C - N ANGL. DEV. = -22.9 DEGREES
REMARK 500 ABA H 29 O - C - N ANGL. DEV. = 10.5 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 THR A 12 144.33 81.34
REMARK 500 ARG E 25 121.29 51.77
REMARK 500 ARG F 13 5.90 83.10
REMARK 500 ABA F 29 130.29 -23.88
REMARK 500 THR G 12 -68.74 2.30
REMARK 500 ARG G 13 63.21 -155.07
REMARK 500 ARG G 28 35.57 -87.11
REMARK 500 ABA G 29 108.72 9.66
REMARK 500 ARG H 13 -13.82 86.70
REMARK 500 ARG L 13 -10.09 100.36
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 THR A 12 ARG A 13 -145.80
REMARK 500 ARG F 28 ABA F 29 111.17
REMARK 500 ARG G 28 ABA G 29 146.29
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ARG A 28 16.73
REMARK 500 ABA A 29 -17.24
REMARK 500 ABA B 29 12.45
REMARK 500 ARG D 28 15.76
REMARK 500 ABA E 29 51.02
REMARK 500 ARG F 28 17.77
REMARK 500 ABA F 29 -32.02
REMARK 500 ARG G 28 -74.25
REMARK 500 ABA G 29 -32.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZMP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WILD TYPE HD5
REMARK 900 RELATED ID: 4E82 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MONOMERIC FORM OF HUMAN ALPHA-DEFENSIN 5, HD5
REMARK 900 RELATED ID: 4E83 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ALPHA-DEFENSIN 5, HD5 (LEU29NLE MUTANT)
DBREF 4E86 A 1 32 UNP Q01523 DEF5_HUMAN 63 94
DBREF 4E86 B 1 32 UNP Q01523 DEF5_HUMAN 63 94
DBREF 4E86 C 1 32 UNP Q01523 DEF5_HUMAN 63 94
DBREF 4E86 D 1 32 UNP Q01523 DEF5_HUMAN 63 94
DBREF 4E86 E 1 32 UNP Q01523 DEF5_HUMAN 63 94
DBREF 4E86 F 1 32 UNP Q01523 DEF5_HUMAN 63 94
DBREF 4E86 G 1 32 UNP Q01523 DEF5_HUMAN 63 94
DBREF 4E86 H 1 32 UNP Q01523 DEF5_HUMAN 63 94
DBREF 4E86 L 1 32 UNP Q01523 DEF5_HUMAN 63 94
SEQADV 4E86 ABA A 29 UNP Q01523 LEU 91 ENGINEERED MUTATION
SEQADV 4E86 ABA B 29 UNP Q01523 LEU 91 ENGINEERED MUTATION
SEQADV 4E86 ABA C 29 UNP Q01523 LEU 91 ENGINEERED MUTATION
SEQADV 4E86 ABA D 29 UNP Q01523 LEU 91 ENGINEERED MUTATION
SEQADV 4E86 ABA E 29 UNP Q01523 LEU 91 ENGINEERED MUTATION
SEQADV 4E86 ABA F 29 UNP Q01523 LEU 91 ENGINEERED MUTATION
SEQADV 4E86 ABA G 29 UNP Q01523 LEU 91 ENGINEERED MUTATION
SEQADV 4E86 ABA H 29 UNP Q01523 LEU 91 ENGINEERED MUTATION
SEQADV 4E86 ABA L 29 UNP Q01523 LEU 91 ENGINEERED MUTATION
SEQRES 1 A 32 ALA THR CYS TYR CYS ARG THR GLY ARG CYS ALA THR ARG
SEQRES 2 A 32 GLU SER LEU SER GLY VAL CYS GLU ILE SER GLY ARG LEU
SEQRES 3 A 32 TYR ARG ABA CYS CYS ARG
SEQRES 1 B 32 ALA THR CYS TYR CYS ARG THR GLY ARG CYS ALA THR ARG
SEQRES 2 B 32 GLU SER LEU SER GLY VAL CYS GLU ILE SER GLY ARG LEU
SEQRES 3 B 32 TYR ARG ABA CYS CYS ARG
SEQRES 1 C 32 ALA THR CYS TYR CYS ARG THR GLY ARG CYS ALA THR ARG
SEQRES 2 C 32 GLU SER LEU SER GLY VAL CYS GLU ILE SER GLY ARG LEU
SEQRES 3 C 32 TYR ARG ABA CYS CYS ARG
SEQRES 1 D 32 ALA THR CYS TYR CYS ARG THR GLY ARG CYS ALA THR ARG
SEQRES 2 D 32 GLU SER LEU SER GLY VAL CYS GLU ILE SER GLY ARG LEU
SEQRES 3 D 32 TYR ARG ABA CYS CYS ARG
SEQRES 1 E 32 ALA THR CYS TYR CYS ARG THR GLY ARG CYS ALA THR ARG
SEQRES 2 E 32 GLU SER LEU SER GLY VAL CYS GLU ILE SER GLY ARG LEU
SEQRES 3 E 32 TYR ARG ABA CYS CYS ARG
SEQRES 1 F 32 ALA THR CYS TYR CYS ARG THR GLY ARG CYS ALA THR ARG
SEQRES 2 F 32 GLU SER LEU SER GLY VAL CYS GLU ILE SER GLY ARG LEU
SEQRES 3 F 32 TYR ARG ABA CYS CYS ARG
SEQRES 1 G 32 ALA THR CYS TYR CYS ARG THR GLY ARG CYS ALA THR ARG
SEQRES 2 G 32 GLU SER LEU SER GLY VAL CYS GLU ILE SER GLY ARG LEU
SEQRES 3 G 32 TYR ARG ABA CYS CYS ARG
SEQRES 1 H 32 ALA THR CYS TYR CYS ARG THR GLY ARG CYS ALA THR ARG
SEQRES 2 H 32 GLU SER LEU SER GLY VAL CYS GLU ILE SER GLY ARG LEU
SEQRES 3 H 32 TYR ARG ABA CYS CYS ARG
SEQRES 1 L 32 ALA THR CYS TYR CYS ARG THR GLY ARG CYS ALA THR ARG
SEQRES 2 L 32 GLU SER LEU SER GLY VAL CYS GLU ILE SER GLY ARG LEU
SEQRES 3 L 32 TYR ARG ABA CYS CYS ARG
MODRES 4E86 ABA A 29 ALA ALPHA-AMINOBUTYRIC ACID
MODRES 4E86 ABA B 29 ALA ALPHA-AMINOBUTYRIC ACID
MODRES 4E86 ABA C 29 ALA ALPHA-AMINOBUTYRIC ACID
MODRES 4E86 ABA D 29 ALA ALPHA-AMINOBUTYRIC ACID
MODRES 4E86 ABA E 29 ALA ALPHA-AMINOBUTYRIC ACID
MODRES 4E86 ABA F 29 ALA ALPHA-AMINOBUTYRIC ACID
MODRES 4E86 ABA G 29 ALA ALPHA-AMINOBUTYRIC ACID
MODRES 4E86 ABA H 29 ALA ALPHA-AMINOBUTYRIC ACID
MODRES 4E86 ABA L 29 ALA ALPHA-AMINOBUTYRIC ACID
HET ABA A 29 6
HET ABA B 29 6
HET ABA C 29 6
HET ABA D 29 6
HET ABA E 29 6
HET ABA F 29 6
HET ABA G 29 6
HET ABA H 29 6
HET ABA L 29 6
HET CL B 101 1
HET CL C 101 1
HET CL D 101 1
HETNAM ABA ALPHA-AMINOBUTYRIC ACID
HETNAM CL CHLORIDE ION
FORMUL 1 ABA 9(C4 H9 N O2)
FORMUL 10 CL 3(CL 1-)
FORMUL 13 HOH *31(H2 O)
SHEET 1 A 7 CYS A 3 ARG A 6 0
SHEET 2 A 7 ARG A 25 CYS A 31 -1 O CYS A 30 N TYR A 4
SHEET 3 A 7 SER A 15 ILE A 22 -1 N SER A 17 O ABA A 29
SHEET 4 A 7 SER B 15 ILE B 22 -1 O GLU B 21 N VAL A 19
SHEET 5 A 7 ARG B 25 CYS B 31 -1 O ABA B 29 N GLY B 18
SHEET 6 A 7 THR B 2 ARG B 6 -1 N TYR B 4 O CYS B 30
SHEET 7 A 7 CYS A 3 ARG A 6 -1 N CYS A 5 O CYS B 3
SHEET 1 B 7 CYS C 3 ARG C 6 0
SHEET 2 B 7 ARG C 25 CYS C 31 -1 O CYS C 30 N TYR C 4
SHEET 3 B 7 SER C 15 ILE C 22 -1 N GLY C 18 O ABA C 29
SHEET 4 B 7 SER D 15 ILE D 22 -1 O GLU D 21 N VAL C 19
SHEET 5 B 7 ARG D 25 CYS D 31 -1 O ARG D 25 N ILE D 22
SHEET 6 B 7 CYS D 3 ARG D 6 -1 N ARG D 6 O ARG D 28
SHEET 7 B 7 CYS C 3 ARG C 6 -1 N CYS C 3 O CYS D 5
SHEET 1 C 7 CYS E 3 ARG E 6 0
SHEET 2 C 7 LEU E 26 CYS E 31 -1 O CYS E 30 N TYR E 4
SHEET 3 C 7 SER E 15 ILE E 22 -1 N SER E 15 O CYS E 31
SHEET 4 C 7 SER F 15 ILE F 22 -1 O VAL F 19 N GLU E 21
SHEET 5 C 7 ARG F 25 CYS F 31 -1 O ABA F 29 N SER F 17
SHEET 6 C 7 CYS F 3 ARG F 6 -1 N TYR F 4 O CYS F 30
SHEET 7 C 7 CYS E 3 ARG E 6 -1 N CYS E 3 O CYS F 5
SHEET 1 D 8 SER G 15 LEU G 16 0
SHEET 2 D 8 CYS G 30 CYS G 31 -1 O CYS G 31 N SER G 15
SHEET 3 D 8 CYS G 3 CYS G 5 -1 N TYR G 4 O CYS G 30
SHEET 4 D 8 CYS H 3 ARG H 6 -1 O CYS H 5 N CYS G 3
SHEET 5 D 8 ARG H 25 CYS H 31 -1 O CYS H 30 N TYR H 4
SHEET 6 D 8 SER H 15 ILE H 22 -1 N SER H 17 O ABA H 29
SHEET 7 D 8 GLY G 18 ILE G 22 -1 N VAL G 19 O GLU H 21
SHEET 8 D 8 ARG G 25 TYR G 27 -1 O ARG G 25 N ILE G 22
SHEET 1 E 3 CYS L 3 ARG L 6 0
SHEET 2 E 3 ARG L 25 CYS L 31 -1 O ARG L 28 N ARG L 6
SHEET 3 E 3 SER L 15 ILE L 22 -1 N CYS L 20 O TYR L 27
SSBOND 1 CYS A 3 CYS A 31 1555 1555 2.05
SSBOND 2 CYS A 5 CYS A 20 1555 1555 2.05
SSBOND 3 CYS A 10 CYS A 30 1555 1555 2.04
SSBOND 4 CYS B 3 CYS B 31 1555 1555 2.00
SSBOND 5 CYS B 5 CYS B 20 1555 1555 1.99
SSBOND 6 CYS B 10 CYS B 30 1555 1555 2.07
SSBOND 7 CYS C 3 CYS C 31 1555 1555 2.02
SSBOND 8 CYS C 5 CYS C 20 1555 1555 2.02
SSBOND 9 CYS C 10 CYS C 30 1555 1555 2.03
SSBOND 10 CYS D 3 CYS D 31 1555 1555 2.05
SSBOND 11 CYS D 5 CYS D 20 1555 1555 2.05
SSBOND 12 CYS D 10 CYS D 30 1555 1555 2.06
SSBOND 13 CYS E 3 CYS E 31 1555 1555 2.03
SSBOND 14 CYS E 5 CYS E 20 1555 1555 2.01
SSBOND 15 CYS E 10 CYS E 30 1555 1555 2.05
SSBOND 16 CYS F 3 CYS F 31 1555 1555 2.05
SSBOND 17 CYS F 5 CYS F 20 1555 1555 2.05
SSBOND 18 CYS F 10 CYS F 30 1555 1555 2.03
SSBOND 19 CYS G 3 CYS G 31 1555 1555 2.05
SSBOND 20 CYS G 5 CYS G 20 1555 1555 2.02
SSBOND 21 CYS G 10 CYS G 30 1555 1555 2.05
SSBOND 22 CYS H 3 CYS H 31 1555 1555 2.06
SSBOND 23 CYS H 5 CYS H 20 1555 1555 2.02
SSBOND 24 CYS H 10 CYS H 30 1555 1555 2.05
SSBOND 25 CYS L 3 CYS L 31 1555 1555 2.04
SSBOND 26 CYS L 5 CYS L 20 1555 1555 2.02
SSBOND 27 CYS L 10 CYS L 30 1555 1555 2.06
LINK C ARG A 28 N ABA A 29 1555 1555 1.43
LINK C ABA A 29 N CYS A 30 1555 1555 1.31
LINK C ARG B 28 N ABA B 29 1555 1555 1.43
LINK C ABA B 29 N CYS B 30 1555 1555 1.35
LINK C ARG C 28 N ABA C 29 1555 1555 1.42
LINK C ABA C 29 N CYS C 30 1555 1555 1.34
LINK C ARG D 28 N ABA D 29 1555 1555 1.42
LINK C ABA D 29 N CYS D 30 1555 1555 1.34
LINK C ARG E 28 N ABA E 29 1555 1555 1.41
LINK C ABA E 29 N CYS E 30 1555 1555 1.34
LINK C ARG F 28 N ABA F 29 1555 1555 1.41
LINK C ABA F 29 N CYS F 30 1555 1555 1.32
LINK C ARG G 28 N ABA G 29 1555 1555 1.37
LINK C ABA G 29 N CYS G 30 1555 1555 1.36
LINK C ARG H 28 N ABA H 29 1555 1555 1.42
LINK C ABA H 29 N CYS H 30 1555 1555 1.34
LINK C ARG L 28 N ABA L 29 1555 1555 1.41
LINK C ABA L 29 N CYS L 30 1555 1555 1.32
SITE 1 AC1 2 TYR B 4 ARG B 32
SITE 1 AC2 2 THR C 2 ARG H 13
SITE 1 AC3 3 ARG D 6 THR D 7 GLY D 8
CRYST1 124.141 40.757 54.215 90.00 96.38 90.00 C 1 2 1 36
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 0.008055 0.000000 0.000901 0.00000
SCALE2 0.000000 0.024536 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018560 0.00000
(ATOM LINES ARE NOT SHOWN.)
END