HEADER ANTIMICROBIAL PROTEIN 17-FEB-16 5I7K
TITLE CRYSTAL STRUCTURE OF HUMAN SPLUNC1 DOLPHIN MUTANT D1 (G58A, S61A,
TITLE 2 G62E, G63D, G66D, I67T)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BPI FOLD-CONTAINING FAMILY A MEMBER 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LUNG-SPECIFIC PROTEIN X,NASOPHARYNGEAL CARCINOMA-RELATED
COMPND 5 PROTEIN,PALATE LUNG AND NASAL EPITHELIUM CLONE PROTEIN,SECRETORY
COMPND 6 PROTEIN IN UPPER RESPIRATORY TRACTS,SHORT PLUNC1,SPLUNC1,TRACHEAL
COMPND 7 EPITHELIUM-ENRICHED PROTEIN,VON EBNER PROTEIN HL;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BPIFA1, LUNX, NASG, PLUNC, SPLUNC1, SPURT, UNQ787/PRO1606;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SURFACTANT, ANTIMICROBIAL, AIRWAY, ANTIMICROBIAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR W.G.WALTON,M.R.REDINBO
REVDAT 5 27-SEP-23 5I7K 1 REMARK
REVDAT 4 04-DEC-19 5I7K 1 REMARK
REVDAT 3 20-SEP-17 5I7K 1 JRNL REMARK
REVDAT 2 08-JUN-16 5I7K 1 JRNL
REVDAT 1 18-MAY-16 5I7K 0
JRNL AUTH W.G.WALTON,S.AHMAD,M.S.LITTLE,C.S.KIM,J.TYRRELL,Q.LIN,
JRNL AUTH 2 Y.P.DI,R.TARRAN,M.R.REDINBO
JRNL TITL STRUCTURAL FEATURES ESSENTIAL TO THE ANTIMICROBIAL FUNCTIONS
JRNL TITL 2 OF HUMAN SPLUNC1.
JRNL REF BIOCHEMISTRY V. 55 2979 2016
JRNL REFN ISSN 0006-2960
JRNL PMID 27145151
JRNL DOI 10.1021/ACS.BIOCHEM.6B00271
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 18174
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1820
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.6017 - 5.9862 0.99 1437 160 0.1759 0.2277
REMARK 3 2 5.9862 - 4.7578 0.99 1379 154 0.2007 0.2694
REMARK 3 3 4.7578 - 4.1583 0.99 1362 152 0.1606 0.2037
REMARK 3 4 4.1583 - 3.7789 0.99 1341 148 0.1930 0.2713
REMARK 3 5 3.7789 - 3.5085 0.99 1330 148 0.2272 0.2992
REMARK 3 6 3.5085 - 3.3019 0.98 1320 149 0.2276 0.2976
REMARK 3 7 3.3019 - 3.1368 0.97 1298 147 0.2608 0.3096
REMARK 3 8 3.1368 - 3.0004 0.96 1284 137 0.2756 0.3345
REMARK 3 9 3.0004 - 2.8850 0.93 1251 137 0.2879 0.3499
REMARK 3 10 2.8850 - 2.7855 0.89 1165 135 0.2776 0.3838
REMARK 3 11 2.7855 - 2.6984 0.86 1138 130 0.2867 0.3355
REMARK 3 12 2.6984 - 2.6214 0.83 1123 124 0.3017 0.4042
REMARK 3 13 2.6214 - 2.5524 0.70 926 99 0.3294 0.4023
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.92
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 3040
REMARK 3 ANGLE : 1.504 4147
REMARK 3 CHIRALITY : 0.052 554
REMARK 3 PLANARITY : 0.007 520
REMARK 3 DIHEDRAL : 15.897 1130
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5I7K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218339.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-15
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 : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03320
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19300
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.552
REMARK 200 RESOLUTION RANGE LOW (A) : 29.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.05676
REMARK 200 R SYM (I) : 0.04500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.20
REMARK 200 R MERGE FOR SHELL (I) : 0.65740
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.110
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 4KGH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6M AMMONIUM NITRATE, AND 0.1M TRIS HCL
REMARK 280 PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 310K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 59.32600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.32600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 24.01350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 102.46350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.01350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 102.46350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 59.32600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.01350
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 102.46350
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 59.32600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.01350
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 102.46350
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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 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 SER A 17
REMARK 465 ASN A 18
REMARK 465 ALA A 19
REMARK 465 GLN A 20
REMARK 465 PHE A 21
REMARK 465 GLY A 22
REMARK 465 GLY A 23
REMARK 465 LEU A 24
REMARK 465 PRO A 25
REMARK 465 VAL A 26
REMARK 465 PRO A 27
REMARK 465 LEU A 28
REMARK 465 ASP A 29
REMARK 465 GLN A 30
REMARK 465 THR A 31
REMARK 465 LEU A 32
REMARK 465 PRO A 33
REMARK 465 LEU A 34
REMARK 465 ASN A 35
REMARK 465 VAL A 36
REMARK 465 ASN A 37
REMARK 465 PRO A 38
REMARK 465 ALA A 39
REMARK 465 LEU A 40
REMARK 465 PRO A 41
REMARK 465 LEU A 42
REMARK 465 LYS A 78
REMARK 465 PRO A 79
REMARK 465 GLY A 80
REMARK 465 GLY A 81
REMARK 465 GLY A 82
REMARK 465 THR A 83
REMARK 465 SER A 84
REMARK 465 GLY A 85
REMARK 465 GLY A 86
REMARK 465 LEU A 87
REMARK 465 ASP A 193
REMARK 465 GLY A 194
REMARK 465 LEU A 195
REMARK 465 GLY A 196
REMARK 465 VAL A 256
REMARK 465 SER B 17
REMARK 465 ASN B 18
REMARK 465 ALA B 19
REMARK 465 GLN B 20
REMARK 465 PHE B 21
REMARK 465 GLY B 22
REMARK 465 GLY B 23
REMARK 465 LEU B 24
REMARK 465 PRO B 25
REMARK 465 VAL B 26
REMARK 465 PRO B 27
REMARK 465 LEU B 28
REMARK 465 ASP B 29
REMARK 465 GLN B 30
REMARK 465 THR B 31
REMARK 465 LEU B 32
REMARK 465 PRO B 33
REMARK 465 LEU B 34
REMARK 465 ASN B 35
REMARK 465 VAL B 36
REMARK 465 ASN B 37
REMARK 465 PRO B 38
REMARK 465 ALA B 39
REMARK 465 LEU B 40
REMARK 465 PRO B 41
REMARK 465 LEU B 42
REMARK 465 LYS B 78
REMARK 465 PRO B 79
REMARK 465 GLY B 80
REMARK 465 GLY B 81
REMARK 465 GLY B 82
REMARK 465 THR B 83
REMARK 465 SER B 84
REMARK 465 GLY B 85
REMARK 465 LYS B 255
REMARK 465 VAL B 256
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 ND1 HIS B 182 O HOH B 301 1.85
REMARK 500 NZ LYS B 213 O HOH B 302 2.08
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 PRO A 72 49.69 -73.71
REMARK 500 SER A 97 -14.93 175.89
REMARK 500 PRO A 100 40.27 -64.41
REMARK 500 ASN A 103 143.01 76.43
REMARK 500 LEU A 145 -53.74 144.58
REMARK 500 CYS A 180 102.34 -162.47
REMARK 500 ILE A 200 -8.16 16.61
REMARK 500 LEU A 204 5.03 -52.15
REMARK 500 PHE A 252 -15.28 -147.19
REMARK 500 LEU B 87 -156.76 -92.93
REMARK 500 LEU B 88 158.44 79.63
REMARK 500 LEU B 91 -38.47 -131.66
REMARK 500 SER B 97 -14.10 80.85
REMARK 500 PRO B 100 3.23 -61.97
REMARK 500 LEU B 102 -148.02 -141.65
REMARK 500 ASN B 104 -57.67 108.11
REMARK 500 GLN B 170 33.74 -97.35
REMARK 500 GLU B 171 -33.99 78.07
REMARK 500 ASP B 235 125.09 -35.68
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 LEU B 87 LEU B 88 -143.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5I7L RELATED DB: PDB
REMARK 900 RELATED ID: 5I7J RELATED DB: PDB
DBREF 5I7K A 19 256 UNP Q9NP55 BPIA1_HUMAN 19 256
DBREF 5I7K B 19 256 UNP Q9NP55 BPIA1_HUMAN 19 256
SEQADV 5I7K SER A 17 UNP Q9NP55 EXPRESSION TAG
SEQADV 5I7K ASN A 18 UNP Q9NP55 EXPRESSION TAG
SEQADV 5I7K ALA A 58 UNP Q9NP55 GLY 58 ENGINEERED MUTATION
SEQADV 5I7K ALA A 61 UNP Q9NP55 SER 61 ENGINEERED MUTATION
SEQADV 5I7K GLU A 62 UNP Q9NP55 GLY 62 ENGINEERED MUTATION
SEQADV 5I7K ASP A 63 UNP Q9NP55 GLY 63 ENGINEERED MUTATION
SEQADV 5I7K ASP A 66 UNP Q9NP55 GLY 66 ENGINEERED MUTATION
SEQADV 5I7K THR A 67 UNP Q9NP55 ILE 67 ENGINEERED MUTATION
SEQADV 5I7K SER B 17 UNP Q9NP55 EXPRESSION TAG
SEQADV 5I7K ASN B 18 UNP Q9NP55 EXPRESSION TAG
SEQADV 5I7K ALA B 58 UNP Q9NP55 GLY 58 ENGINEERED MUTATION
SEQADV 5I7K ALA B 61 UNP Q9NP55 SER 61 ENGINEERED MUTATION
SEQADV 5I7K GLU B 62 UNP Q9NP55 GLY 62 ENGINEERED MUTATION
SEQADV 5I7K ASP B 63 UNP Q9NP55 GLY 63 ENGINEERED MUTATION
SEQADV 5I7K ASP B 66 UNP Q9NP55 GLY 66 ENGINEERED MUTATION
SEQADV 5I7K THR B 67 UNP Q9NP55 ILE 67 ENGINEERED MUTATION
SEQRES 1 A 240 SER ASN ALA GLN PHE GLY GLY LEU PRO VAL PRO LEU ASP
SEQRES 2 A 240 GLN THR LEU PRO LEU ASN VAL ASN PRO ALA LEU PRO LEU
SEQRES 3 A 240 SER PRO THR GLY LEU ALA GLY SER LEU THR ASN ALA LEU
SEQRES 4 A 240 SER ASN ALA LEU LEU ALA GLU ASP LEU LEU ASP THR LEU
SEQRES 5 A 240 GLU ASN LEU PRO LEU LEU ASP ILE LEU LYS PRO GLY GLY
SEQRES 6 A 240 GLY THR SER GLY GLY LEU LEU GLY GLY LEU LEU GLY LYS
SEQRES 7 A 240 VAL THR SER VAL ILE PRO GLY LEU ASN ASN ILE ILE ASP
SEQRES 8 A 240 ILE LYS VAL THR ASP PRO GLN LEU LEU GLU LEU GLY LEU
SEQRES 9 A 240 VAL GLN SER PRO ASP GLY HIS ARG LEU TYR VAL THR ILE
SEQRES 10 A 240 PRO LEU GLY ILE LYS LEU GLN VAL ASN THR PRO LEU VAL
SEQRES 11 A 240 GLY ALA SER LEU LEU ARG LEU ALA VAL LYS LEU ASP ILE
SEQRES 12 A 240 THR ALA GLU ILE LEU ALA VAL ARG ASP LYS GLN GLU ARG
SEQRES 13 A 240 ILE HIS LEU VAL LEU GLY ASP CYS THR HIS SER PRO GLY
SEQRES 14 A 240 SER LEU GLN ILE SER LEU LEU ASP GLY LEU GLY PRO LEU
SEQRES 15 A 240 PRO ILE GLN GLY LEU LEU ASP SER LEU THR GLY ILE LEU
SEQRES 16 A 240 ASN LYS VAL LEU PRO GLU LEU VAL GLN GLY ASN VAL CYS
SEQRES 17 A 240 PRO LEU VAL ASN GLU VAL LEU ARG GLY LEU ASP ILE THR
SEQRES 18 A 240 LEU VAL HIS ASP ILE VAL ASN MET LEU ILE HIS GLY LEU
SEQRES 19 A 240 GLN PHE VAL ILE LYS VAL
SEQRES 1 B 240 SER ASN ALA GLN PHE GLY GLY LEU PRO VAL PRO LEU ASP
SEQRES 2 B 240 GLN THR LEU PRO LEU ASN VAL ASN PRO ALA LEU PRO LEU
SEQRES 3 B 240 SER PRO THR GLY LEU ALA GLY SER LEU THR ASN ALA LEU
SEQRES 4 B 240 SER ASN ALA LEU LEU ALA GLU ASP LEU LEU ASP THR LEU
SEQRES 5 B 240 GLU ASN LEU PRO LEU LEU ASP ILE LEU LYS PRO GLY GLY
SEQRES 6 B 240 GLY THR SER GLY GLY LEU LEU GLY GLY LEU LEU GLY LYS
SEQRES 7 B 240 VAL THR SER VAL ILE PRO GLY LEU ASN ASN ILE ILE ASP
SEQRES 8 B 240 ILE LYS VAL THR ASP PRO GLN LEU LEU GLU LEU GLY LEU
SEQRES 9 B 240 VAL GLN SER PRO ASP GLY HIS ARG LEU TYR VAL THR ILE
SEQRES 10 B 240 PRO LEU GLY ILE LYS LEU GLN VAL ASN THR PRO LEU VAL
SEQRES 11 B 240 GLY ALA SER LEU LEU ARG LEU ALA VAL LYS LEU ASP ILE
SEQRES 12 B 240 THR ALA GLU ILE LEU ALA VAL ARG ASP LYS GLN GLU ARG
SEQRES 13 B 240 ILE HIS LEU VAL LEU GLY ASP CYS THR HIS SER PRO GLY
SEQRES 14 B 240 SER LEU GLN ILE SER LEU LEU ASP GLY LEU GLY PRO LEU
SEQRES 15 B 240 PRO ILE GLN GLY LEU LEU ASP SER LEU THR GLY ILE LEU
SEQRES 16 B 240 ASN LYS VAL LEU PRO GLU LEU VAL GLN GLY ASN VAL CYS
SEQRES 17 B 240 PRO LEU VAL ASN GLU VAL LEU ARG GLY LEU ASP ILE THR
SEQRES 18 B 240 LEU VAL HIS ASP ILE VAL ASN MET LEU ILE HIS GLY LEU
SEQRES 19 B 240 GLN PHE VAL ILE LYS VAL
FORMUL 3 HOH *33(H2 O)
HELIX 1 AA1 GLY A 46 GLU A 62 1 17
HELIX 2 AA2 ASP A 63 ASN A 70 1 8
HELIX 3 AA3 GLY A 90 THR A 96 1 7
HELIX 4 AA4 ILE A 200 LEU A 207 1 8
HELIX 5 AA5 LEU A 207 GLY A 233 1 27
HELIX 6 AA6 ASP A 235 HIS A 248 1 14
HELIX 7 AA7 GLY B 46 GLU B 62 1 17
HELIX 8 AA8 ASP B 63 ASN B 70 1 8
HELIX 9 AA9 LEU B 91 THR B 96 1 6
HELIX 10 AB1 GLY B 196 LEU B 203 1 8
HELIX 11 AB2 LEU B 203 LEU B 231 1 29
HELIX 12 AB3 ASP B 235 HIS B 248 1 14
SHEET 1 AA1 4 ASP A 107 LEU A 115 0
SHEET 2 AA1 4 ARG A 128 THR A 143 -1 O LYS A 138 N THR A 111
SHEET 3 AA1 4 ALA A 148 ARG A 167 -1 O ILE A 163 N LEU A 129
SHEET 4 AA1 4 ILE A 173 HIS A 182 -1 O GLY A 178 N GLU A 162
SHEET 1 AA2 4 GLY A 119 GLN A 122 0
SHEET 2 AA2 4 ARG A 128 THR A 143 -1 O TYR A 130 N VAL A 121
SHEET 3 AA2 4 ALA A 148 ARG A 167 -1 O ILE A 163 N LEU A 129
SHEET 4 AA2 4 GLN A 188 LEU A 191 -1 O SER A 190 N ALA A 154
SHEET 1 AA3 4 ASP B 107 LEU B 115 0
SHEET 2 AA3 4 LEU B 129 THR B 143 -1 O ASN B 142 N ASP B 107
SHEET 3 AA3 4 ALA B 148 ARG B 167 -1 O LEU B 157 N LEU B 135
SHEET 4 AA3 4 ILE B 173 HIS B 182 -1 O GLY B 178 N GLU B 162
SHEET 1 AA4 4 GLY B 119 GLN B 122 0
SHEET 2 AA4 4 LEU B 129 THR B 143 -1 O THR B 132 N GLY B 119
SHEET 3 AA4 4 ALA B 148 ARG B 167 -1 O LEU B 157 N LEU B 135
SHEET 4 AA4 4 GLN B 188 GLY B 194 -1 O LEU B 192 N ARG B 152
SSBOND 1 CYS A 180 CYS A 224 1555 1555 2.06
SSBOND 2 CYS B 180 CYS B 224 1555 1555 2.05
CISPEP 1 LEU A 88 GLY A 89 0 -13.06
CISPEP 2 ASN A 103 ASN A 104 0 -5.18
CISPEP 3 ASN A 104 ILE A 105 0 10.55
CISPEP 4 ASN B 104 ILE B 105 0 8.86
CRYST1 48.027 204.927 118.652 90.00 90.00 90.00 C 2 2 21 16
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 0.020822 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004880 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008428 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
