Header list of 1oo9.pdb file
Complete list - 23 20 Bytes
HEADER HYDROLASE 03-MAR-03 1OO9
TITLE ORIENTATION IN SOLUTION OF MMP-3 CATALYTIC DOMAIN AND N-TIMP-1 FROM
TITLE 2 RESIDUAL DIPOLAR COUPLINGS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: STROMELYSIN-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: MATRIX METALLOPROTEINASE-3, MMP-3, TRANSIN-1, SL-1;
COMPND 6 EC: 3.4.24.17;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: METALLOPROTEINASE INHIBITOR 1;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 12 SYNONYM: TIMP-1, ERYTHROID POTENTIATING ACTIVITY, EPA, TISSUE
COMPND 13 INHIBITOR OF METALLOPROTEINASES, FIBROBLAST COLLAGENASE INHIBITOR,
COMPND 14 COLLAGENASE INHIBITOR;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MMP3 OR STMY1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEMEX-MMP-3(DC)E202Q;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: TIMP1 OR TIMP OR CLGI;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET3A-N-TIMP-1
KEYWDS PROTEIN-PROTEIN COMPLEX, HYDROLASE
EXPDTA SOLUTION NMR
AUTHOR S.ARUMUGAM,S.R.VAN DOREN
REVDAT 3 23-FEB-22 1OO9 1 REMARK SSBOND
REVDAT 2 24-FEB-09 1OO9 1 VERSN
REVDAT 1 29-JUL-03 1OO9 0
JRNL AUTH S.ARUMUGAM,S.R.VAN DOREN
JRNL TITL GLOBAL ORIENTATION OF BOUND MMP-3 AND N-TIMP-1 IN SOLUTION
JRNL TITL 2 VIA RESIDUAL DIPOLAR COUPLINGS
JRNL REF BIOCHEMISTRY V. 42 7950 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12834347
JRNL DOI 10.1021/BI034545S
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XPLOR NIH
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 STRUCTURES WERE CALCULATED USING XPLOR-NIH. REFINEMENTS WERE
REMARK 3 CARRIED OUT FIRST BY RIGID BODY MINIMIZATION (CLORE(2000)
REMARK 3 PROC.NATL.ACAD.SCI. 97, 9021-9025) FOLLOWED BY RESTRAINED
REMARK 3 SIMULATED ANNEALING (WANG ET AL. EMBO J. (2000) 19,5635-5649).
REMARK 3
REMARK 3 THE CRYSTAL STRUCTURE OF THE COMPLEX BY BODE ET AL. (NATURE (1997),
REMARK 3 389, 77-81; PDB CODE: 1UEA) HAS
REMARK 3 BEEN USED AS A STARTING POINT WITH PROTONS ATTACHED AND TAKING
REMARK 3 ONLY N-TERMINAL 126 RESIDUES OF TIMP-1.
REMARK 3 INTERFACIAL SIDE CHAINS OF THE FOLLOWING RESIDUES WERE ALLOWED TO
REMARK 3 BE FLEXIBLE: CHAIN A (MMP-3(DC)): 162-169,198-202,
REMARK 3 205-206, 211 AND 221-223; CHAIN B (N-TIMP-1): 302-304, 329, 333-
REMARK 3 335,366-369; A TOTAL OF 49 NOE (46 INTERMOLECULAR
REMARK 3 AND 3 INTRAMOLECULAR) 75 NH DIPOLAR COULINGS FOR N-TIMP-1, 19 NH
REMARK 3 DIPOLAR COUPLINGS AND 8 CAHA DIPOLAR
REMARK 3 COUPLINGS FOR MMP-3 WERE USED FOR REFINEMENT. TARGET FUNCTIONS
REMARK 3 INCLUDE TERMS FOR NOE RESTRAINTS, DIPOLAR
REMARK 3 COUPLING RESTRAINTS AND RADIUS OF GYRATION.
REMARK 3
REMARK 3
REMARK 3 ALSO, MODULE ( DOSSET ET AL. J. BIOMOL. NMR, (2001),20,223-231)
REMARK 3 AND PALES (ZWECKSTETTER AND BAX, J. AM. CHEM. SOC
REMARK 3 (2000), 122, 3791-3792) WERE USED FOR EVALUATING THE ORIENTATION
REMARK 3 AND STRUCTURES.
REMARK 4
REMARK 4 1OO9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018496.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310; 307
REMARK 210 PH : 6.6; 6.7
REMARK 210 IONIC STRENGTH : 20MM TRIS-D11; 100 MM NACL; 15
REMARK 210 MM CACL2; 3UM ZNCL2; 1MM SODIUM
REMARK 210 AZIDE; 20MM TRIS-D11; 125MM NACL;
REMARK 210 15 MM CACL2; 50UM ZNCL2;1MM
REMARK 210 SODIUM AZIDE
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8MM MMP-3 U-15N, 13C; 0.8MM N
REMARK 210 -TIMP-1; 20MM TRIS-D11; 100 MM
REMARK 210 NACL; 15 MM CACL2; 3UM ZNCL2;
REMARK 210 1MM SODIUM AZIDE; 93% H2O, 7%
REMARK 210 D2O; 0.5MM MMP-3 U-2H, 15N;
REMARK 210 0.5MM N-TIMP-1; 20MM TRIS-D11;
REMARK 210 100 MM NACL; 15 MM CACL2; 3UM
REMARK 210 ZNCL2; 1MM SODIUM AZIDE; 93% H2O,
REMARK 210 7% D2O; 0.66MM N-TIMP-1 U-15N,
REMARK 210 13C; 0.66MM MMP-3(E202Q); 20MM
REMARK 210 TRIS-D11; 125MM NACL; 15 MM
REMARK 210 CACL2; 50UM ZNCL2; 1MM SODIUM
REMARK 210 AZIDE; 93% H2O; 7% D2O; 0.3MM 98%
REMARK 210 2H/15N N-TIMP-1; 0.3MM MMP-3
REMARK 210 (E202Q); 20MM TRIS-D11; 125MM
REMARK 210 NACL; 15 MM CACL2; 50UM ZNCL2;
REMARK 210 1MM SODIUM AZIDE; 93% H2O; 7%
REMARK 210 D2O; 0.3MM 98% 2H/15N N-TIMP-1;
REMARK 210 0.3MM (15N-IV, 15N, 13C-L)MMP-
REMARK 210 3(E202Q); 20MM TRIS-D11; 125MM
REMARK 210 NACL; 15 MM CACL2; 50UM ZNCL2;
REMARK 210 1MM SODIUM AZIDE; 93% H2O; 7%
REMARK 210 D2O; 0.3MM 98% 2H/15N N-TIMP-1;
REMARK 210 0.3MM (15N-IV, 15N, 13C-L)MMP-
REMARK 210 3(E202Q); 20MM TRIS-D11; 125MM
REMARK 210 NACL; 15 MM CACL2; 50UM ZNCL2;
REMARK 210 1MM SODIUM AZIDE; 93% H2O; 7%
REMARK 210 D2O 5% PEG(C12E6)/1-HEXANOL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-SEPARATED NOESY; HNCA; HNCO;
REMARK 210 HN(CO)CA; HCCH-TOCSY; HCCH-COSY;;
REMARK 210 COUPLED 15N-HSQC; COUPLED 13C-
REMARK 210 HSQC; HA-COUPLED HNCA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 720 MHZ; 750 MHZ; 600
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; UNITYPLUS; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PALES SGI IRIX 6.2, MODULE 1.0
REMARK 210 METHOD USED : RIGID BODY MINIMIZATION FOLLOWED
REMARK 210 BY RESTRAINED SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: DIMERIC
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
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 PRO A 221 H CYS B 303 1.58
REMARK 500 O ILE A 203 HG SER A 206 1.59
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 HIS A 96 CE1 HIS A 96 NE2 -0.074
REMARK 500 TRP A 124 CG TRP A 124 CD2 0.104
REMARK 500 HIS A 151 CE1 HIS A 151 NE2 -0.072
REMARK 500 HIS A 166 CE1 HIS A 166 NE2 -0.070
REMARK 500 HIS A 179 CE1 HIS A 179 NE2 -0.076
REMARK 500 HIS A 201 CE1 HIS A 201 NE2 -0.071
REMARK 500 HIS A 205 CE1 HIS A 205 NE2 -0.074
REMARK 500 HIS A 211 CE1 HIS A 211 NE2 -0.072
REMARK 500 HIS A 224 CE1 HIS A 224 NE2 -0.069
REMARK 500 HIS B 307 CE1 HIS B 307 NE2 -0.068
REMARK 500 HIS B 374 CE1 HIS B 374 NE2 -0.075
REMARK 500 HIS B 377 CE1 HIS B 377 NE2 -0.077
REMARK 500 HIS B 395 CE1 HIS B 395 NE2 -0.076
REMARK 500 TRP B 405 CG TRP B 405 CD2 0.107
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 93 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 100 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 359 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 413 NE - CZ - NH1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG B 413 NE - CZ - NH2 ANGL. DEV. = -3.6 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 ARG A 93 36.52 -83.75
REMARK 500 ARG A 149 -128.57 47.05
REMARK 500 HIS A 151 33.34 -147.85
REMARK 500 ASP A 158 30.89 -84.05
REMARK 500 ASN A 162 -104.54 50.39
REMARK 500 PRO A 170 151.40 -49.27
REMARK 500 THR A 191 59.27 -151.06
REMARK 500 ASN A 194 105.53 -58.67
REMARK 500 MET A 219 4.49 -66.51
REMARK 500 TYR A 223 105.66 -57.12
REMARK 500 SER A 225 105.45 15.40
REMARK 500 THR A 227 -85.91 -54.55
REMARK 500 LEU A 245 -62.02 -108.91
REMARK 500 ASN B 330 -111.56 -74.00
REMARK 500 THR B 343 -77.82 -95.06
REMARK 500 GLN B 350 37.51 -89.65
REMARK 500 ALA B 351 8.89 -163.37
REMARK 500 LEU B 352 -106.22 51.84
REMARK 500 ASP B 354 -66.65 25.66
REMARK 500 ALA B 355 -6.14 -157.51
REMARK 500 ALA B 356 45.80 -168.05
REMARK 500 CYS B 370 6.81 91.94
REMARK 500 ASP B 391 -126.42 65.01
REMARK 500 LYS B 418 -46.09 -135.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UEA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MMP-3 WITH FULL LENGTH TIMP-1.
DBREF 1OO9 A 83 250 UNP P08254 MMP3_HUMAN 100 267
DBREF 1OO9 B 301 426 UNP P01033 TIMP1_HUMAN 24 149
SEQRES 1 A 168 PHE ARG THR PHE PRO GLY ILE PRO LYS TRP ARG LYS THR
SEQRES 2 A 168 HIS LEU THR TYR ARG ILE VAL ASN TYR THR PRO ASP LEU
SEQRES 3 A 168 PRO LYS ASP ALA VAL ASP SER ALA VAL GLU LYS ALA LEU
SEQRES 4 A 168 LYS VAL TRP GLU GLU VAL THR PRO LEU THR PHE SER ARG
SEQRES 5 A 168 LEU TYR GLU GLY GLU ALA ASP ILE MET ILE SER PHE ALA
SEQRES 6 A 168 VAL ARG GLU HIS GLY ASP PHE TYR PRO PHE ASP GLY PRO
SEQRES 7 A 168 GLY ASN VAL LEU ALA HIS ALA TYR ALA PRO GLY PRO GLY
SEQRES 8 A 168 ILE ASN GLY ASP ALA HIS PHE ASP ASP ASP GLU GLN TRP
SEQRES 9 A 168 THR LYS ASP THR THR GLY THR ASN LEU PHE LEU VAL ALA
SEQRES 10 A 168 ALA HIS GLU ILE GLY HIS SER LEU GLY LEU PHE HIS SER
SEQRES 11 A 168 ALA ASN THR GLU ALA LEU MET TYR PRO LEU TYR HIS SER
SEQRES 12 A 168 LEU THR ASP LEU THR ARG PHE ARG LEU SER GLN ASP ASP
SEQRES 13 A 168 ILE ASN GLY ILE GLN SER LEU TYR GLY PRO PRO PRO
SEQRES 1 B 126 CYS THR CYS VAL PRO PRO HIS PRO GLN THR ALA PHE CYS
SEQRES 2 B 126 ASN SER ASP LEU VAL ILE ARG ALA LYS PHE VAL GLY THR
SEQRES 3 B 126 PRO GLU VAL ASN GLN THR THR LEU TYR GLN ARG TYR GLU
SEQRES 4 B 126 ILE LYS MET THR LYS MET TYR LYS GLY PHE GLN ALA LEU
SEQRES 5 B 126 GLY ASP ALA ALA ASP ILE ARG PHE VAL TYR THR PRO ALA
SEQRES 6 B 126 MET GLU SER VAL CYS GLY TYR PHE HIS ARG SER HIS ASN
SEQRES 7 B 126 ARG SER GLU GLU PHE LEU ILE ALA GLY LYS LEU GLN ASP
SEQRES 8 B 126 GLY LEU LEU HIS ILE THR THR CYS SER PHE VAL ALA PRO
SEQRES 9 B 126 TRP ASN SER LEU SER LEU ALA GLN ARG ARG GLY PHE THR
SEQRES 10 B 126 LYS THR TYR THR VAL GLY CYS GLU GLU
HELIX 1 1 PRO A 109 GLU A 126 1 18
HELIX 2 2 LEU A 195 LEU A 207 1 13
HELIX 3 3 ASP A 228 PHE A 232 5 5
HELIX 4 4 SER A 235 GLY A 247 1 13
HELIX 5 5 HIS B 307 SER B 315 1 9
HELIX 6 6 MET B 366 CYS B 370 5 5
HELIX 7 7 ASN B 406 LEU B 408 5 3
HELIX 8 8 SER B 409 LYS B 418 1 10
HELIX 9 9 THR B 419 GLU B 425 1 7
SHEET 1 A 6 THR A 131 ARG A 134 0
SHEET 2 A 6 HIS A 96 ILE A 101 1 N LEU A 97 O THR A 131
SHEET 3 A 6 ILE A 142 ALA A 147 1 O ILE A 142 N ARG A 100
SHEET 4 A 6 ALA A 178 ASP A 181 1 O ALA A 178 N SER A 145
SHEET 5 A 6 VAL A 163 ALA A 167 -1 O LEU A 164 N ASP A 181
SHEET 6 A 6 THR B 302 CYS B 303 -1 N THR B 302 O ALA A 165
SHEET 1 B 2 TRP A 186 THR A 187 0
SHEET 2 B 2 THR A 193 ASN A 194 1 O THR A 193 N THR A 187
SHEET 1 C 9 VAL B 402 PRO B 404 0
SHEET 2 C 9 PHE B 383 GLN B 390 -1 N LEU B 384 O ALA B 403
SHEET 3 C 9 LEU B 393 HIS B 395 -1 N LEU B 393 O GLN B 390
SHEET 4 C 9 PHE B 360 PRO B 364 1 O PHE B 360 N LEU B 394
SHEET 5 C 9 TYR B 335 LYS B 347 -1 N GLN B 336 O THR B 363
SHEET 6 C 9 GLU B 328 VAL B 329 -1 O GLU B 328 N ARG B 337
SHEET 7 C 9 TYR B 335 LYS B 347 -1 N ARG B 337 O GLU B 328
SHEET 8 C 9 LEU B 317 PHE B 323 -1 O VAL B 318 N TYR B 346
SHEET 9 C 9 PHE B 383 GLN B 390 -1 N PHE B 383 O ALA B 321
SSBOND 1 CYS B 301 CYS B 370 1555 1555 2.06
SSBOND 2 CYS B 303 CYS B 399 1555 1555 2.06
SSBOND 3 CYS B 313 CYS B 424 1555 1555 2.03
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 23 20 Bytes