HEADER HYDROLASE 31-OCT-13 4NFF
TITLE HUMAN KALLIKREIN-RELATED PEPTIDASE 2 IN COMPLEX WITH PPACK
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KALLIKREIN-2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GLANDULAR KALLIKREIN-1, HGK-1, TISSUE KALLIKREIN-2;
COMPND 5 EC: 3.4.21.35;
COMPND 6 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: KLK2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CHYMOTRYPSIN-LIKE PROTEASE, ZINC BINDING, EXTRACELLULAR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.SKALA,H.BRANDSTETTER,V.MAGDOLEN,P.GOETTIG
REVDAT 3 15-NOV-17 4NFF 1 REMARK
REVDAT 2 08-APR-15 4NFF 1 JRNL
REVDAT 1 29-OCT-14 4NFF 0
JRNL AUTH W.SKALA,D.T.UTZSCHNEIDER,V.MAGDOLEN,M.DEBELA,S.GUO,
JRNL AUTH 2 C.S.CRAIK,H.BRANDSTETTER,P.GOETTIG
JRNL TITL STRUCTURE-FUNCTION ANALYSES OF HUMAN KALLIKREIN-RELATED
JRNL TITL 2 PEPTIDASE 2 ESTABLISH THE 99-LOOP AS MASTER REGULATOR OF
JRNL TITL 3 ACTIVITY
JRNL REF J.BIOL.CHEM. V. 289 34267 2014
JRNL REFN ISSN 0021-9258
JRNL PMID 25326387
JRNL DOI 10.1074/JBC.M114.598201
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 19387
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 988
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1145
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 56
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1771
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 100
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.161
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.146
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.161
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.898
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1865 ; 0.014 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2551 ; 1.770 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 227 ; 6.561 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 73 ;33.190 ;23.973
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 287 ;15.493 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;20.410 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 274 ; 0.116 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1423 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 4NFF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-NOV-13.
REMARK 100 THE DEPOSITION ID IS D_1000083134.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X12
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97004
REMARK 200 MONOCHROMATOR : SI(111); DOUBLE CRYSTAL, SECOND
REMARK 200 CRYSTAL HORIZONTALLY FOCUSSING
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19421
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 44.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.15000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.58500
REMARK 200 R SYM FOR SHELL (I) : 0.58500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.3.0
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 800MM AMMONIUM SULFATE, 100MM BICINE,
REMARK 280 PH 9.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 30.05000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.40000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.37000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.40000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.05000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.37000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 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 LYS A 95E
REMARK 465 HIS A 95F
REMARK 465 GLN A 95G
REMARK 465 SER A 95H
REMARK 465 LEU A 95I
REMARK 465 ARG A 95J
REMARK 465 PRO A 95K
REMARK 465 ASP A 96
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 HIS A 48 CG HIS A 48 CD2 0.054
REMARK 500 HIS A 57 CG HIS A 57 CD2 0.066
REMARK 500 TRP A 67 CE2 TRP A 67 CD2 0.075
REMARK 500 HIS A 87 CG HIS A 87 CD2 0.058
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 HIS A 71 -63.01 -130.41
REMARK 500 HIS A 101 33.11 71.36
REMARK 500 GLU A 147 -66.29 -90.86
REMARK 500 SER A 214 -57.26 -123.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 630
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR
REMARK 630 MOLECULE NAME: D-PHENYLALANYL-N-[(2S,3S)-6-{[AMINO(IMINIO)METHYL]
REMARK 630 AMINO}-1-CHLORO-2-HYDROXYHEXAN-3-YL]-L-PROLINAMIDE
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 630
REMARK 630 M RES C SSSEQI
REMARK 630 0G6 A 301
REMARK 630 SOURCE: NULL
REMARK 630 TAXONOMY: NULL
REMARK 630 SUBCOMP: DPN PRO AR7 0QE
REMARK 630 DETAILS: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0G6 A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NFE RELATED DB: PDB
DBREF 4NFF A 16 245A UNP P20151 KLK2_HUMAN 25 261
SEQRES 1 A 237 ILE VAL GLY GLY TRP GLU CYS GLU LYS HIS SER GLN PRO
SEQRES 2 A 237 TRP GLN VAL ALA VAL TYR SER HIS GLY TRP ALA HIS CYS
SEQRES 3 A 237 GLY GLY VAL LEU VAL HIS PRO GLN TRP VAL LEU THR ALA
SEQRES 4 A 237 ALA HIS CYS LEU LYS LYS ASN SER GLN VAL TRP LEU GLY
SEQRES 5 A 237 ARG HIS ASN LEU PHE GLU PRO GLU ASP THR GLY GLN ARG
SEQRES 6 A 237 VAL PRO VAL SER HIS SER PHE PRO HIS PRO LEU TYR ASN
SEQRES 7 A 237 MET SER LEU LEU LYS HIS GLN SER LEU ARG PRO ASP GLU
SEQRES 8 A 237 ASP SER SER HIS ASP LEU MET LEU LEU ARG LEU SER GLU
SEQRES 9 A 237 PRO ALA LYS ILE THR ASP VAL VAL LYS VAL LEU GLY LEU
SEQRES 10 A 237 PRO THR GLN GLU PRO ALA LEU GLY THR THR CYS TYR ALA
SEQRES 11 A 237 SER GLY TRP GLY SER ILE GLU PRO GLU GLU PHE LEU ARG
SEQRES 12 A 237 PRO ARG SER LEU GLN CYS VAL SER LEU HIS LEU LEU SER
SEQRES 13 A 237 ASN ASP MET CYS ALA ARG ALA TYR SER GLU LYS VAL THR
SEQRES 14 A 237 GLU PHE MET LEU CYS ALA GLY LEU TRP THR GLY GLY LYS
SEQRES 15 A 237 ASP THR CYS GLY GLY ASP SER GLY GLY PRO LEU VAL CYS
SEQRES 16 A 237 ASN GLY VAL LEU GLN GLY ILE THR SER TRP GLY PRO GLU
SEQRES 17 A 237 PRO CYS ALA LEU PRO GLU LYS PRO ALA VAL TYR THR LYS
SEQRES 18 A 237 VAL VAL HIS TYR ARG LYS TRP ILE LYS ASP THR ILE ALA
SEQRES 19 A 237 ALA ASN PRO
HET 0G6 A 301 30
HETNAM 0G6 D-PHENYLALANYL-N-[(2S,3S)-6-{[AMINO(IMINIO)
HETNAM 2 0G6 METHYL]AMINO}-1-CHLORO-2-HYDROXYHEXAN-3-YL]-L-
HETNAM 3 0G6 PROLINAMIDE
HETSYN 0G6 PPACK
FORMUL 2 0G6 C21 H34 CL N6 O3 1+
FORMUL 3 HOH *100(H2 O)
HELIX 1 1 ALA A 55 LEU A 59 5 5
HELIX 2 2 ASN A 95 LEU A 95D 5 5
HELIX 3 3 SER A 164 TYR A 172 1 9
HELIX 4 4 TYR A 234 ASN A 245 1 12
SHEET 1 A 8 TRP A 20 GLU A 21 0
SHEET 2 A 8 GLN A 156 LEU A 163 -1 O CYS A 157 N TRP A 20
SHEET 3 A 8 MET A 180 GLY A 184 -1 O GLY A 184 N HIS A 161
SHEET 4 A 8 ALA A 226 LYS A 230 -1 O TYR A 228 N LEU A 181
SHEET 5 A 8 VAL A 208 TRP A 215 -1 N TRP A 215 O VAL A 227
SHEET 6 A 8 PRO A 198 CYS A 201 -1 N LEU A 199 O GLN A 210
SHEET 7 A 8 THR A 135 GLY A 140 -1 N TYR A 137 O VAL A 200
SHEET 8 A 8 GLN A 156 LEU A 163 -1 O LEU A 160 N CYS A 136
SHEET 1 B 7 GLN A 30 SER A 35 0
SHEET 2 B 7 TRP A 39 HIS A 48 -1 O CYS A 42 N VAL A 33
SHEET 3 B 7 TRP A 51 THR A 54 -1 O LEU A 53 N VAL A 45
SHEET 4 B 7 MET A 104 LEU A 108 -1 O LEU A 106 N VAL A 52
SHEET 5 B 7 GLN A 81 PRO A 90 -1 N SER A 86 O ARG A 107
SHEET 6 B 7 GLN A 65 LEU A 68 -1 N LEU A 68 O GLN A 81
SHEET 7 B 7 GLN A 30 SER A 35 -1 N TYR A 34 O GLN A 65
SSBOND 1 CYS A 22 CYS A 157 1555 1555 2.03
SSBOND 2 CYS A 42 CYS A 58 1555 1555 2.03
SSBOND 3 CYS A 136 CYS A 201 1555 1555 2.03
SSBOND 4 CYS A 168 CYS A 182 1555 1555 2.01
SSBOND 5 CYS A 191 CYS A 220 1555 1555 2.03
LINK NE2 HIS A 57 C3 0G6 A 301 1555 1555 1.50
LINK OG SER A 195 C2 0G6 A 301 1555 1555 1.40
CISPEP 1 GLU A 218 PRO A 219 0 -11.86
SITE 1 AC1 17 HIS A 57 SER A 99 ASP A 189 THR A 190
SITE 2 AC1 17 CYS A 191 GLY A 193 SER A 195 SER A 214
SITE 3 AC1 17 TRP A 215 GLY A 216 PRO A 217 CYS A 220
SITE 4 AC1 17 ALA A 226 HOH A 406 HOH A 411 HOH A 455
SITE 5 AC1 17 HOH A 470
CRYST1 60.100 60.740 66.800 90.00 90.00 90.00 P 21 21 21 4
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 0.016639 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016464 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014970 0.00000
(ATOM LINES ARE NOT SHOWN.)
END