HEADER HYDROLASE/HYDROLASE INHIBITOR 28-JUN-17 5XW1
TITLE CRYSTAL STRUCTURE OF PORCINE PANCREATIC TRYPSIN WITH TRIPEPTIDE
TITLE 2 INHIBITOR, PRN, AT PH10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRYPSIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-133;
COMPND 5 SYNONYM: PORCINE PANCREATIC TRYPSIN;
COMPND 6 EC: 3.4.21.4;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TRYPSIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 134-231;
COMPND 11 SYNONYM: PORCINE PANCREATIC TRYPSIN;
COMPND 12 EC: 3.4.21.4;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: ACETYLATED-PRO-ARG-ASN INHIBITOR;
COMPND 15 CHAIN: C;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 OTHER_DETAILS: COMMERCIALLY AVAILABLE TRYPSIN FROM SIGMA (CAT. NO.
SOURCE 6 T4799);
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 9 ORGANISM_COMMON: PIG;
SOURCE 10 ORGANISM_TAXID: 9823;
SOURCE 11 OTHER_DETAILS: COMMERCIALLY AVAILABLE TRYPSIN FROM SIGMA (CAT. NO.
SOURCE 12 T4799);
SOURCE 13 MOL_ID: 3;
SOURCE 14 SYNTHETIC: YES;
SOURCE 15 ORGANISM_SCIENTIFIC: CAPSICUM ANNUUM;
SOURCE 16 ORGANISM_TAXID: 4072
KEYWDS TRYPSIN, PEPTIDE INHIBITOR, COMPLEX, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.S.SAIKHEDKAR,A.S.BHOITE,A.P.GIRI,K.A.KULKARNI
REVDAT 2 22-NOV-23 5XW1 1 REMARK
REVDAT 1 04-JUL-18 5XW1 0
JRNL AUTH R.S.JOSHI,N.S.SAIKHEDKAR,A.S.BHOITE,R.MOHANDASAN,A.K.YADAV,
JRNL AUTH 2 M.FERNANDES,K.A.KULKARNI,A.P.GIRI
JRNL TITL REACTIVE CENTRE LOOP PEPTIDES DEVOID OF POTATO PROTEASE
JRNL TITL 2 INHIBITOR-II PROTEIN SCAFFOLD INHIBIT SERINE PROTEASES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 22437
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.147
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.173
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1150
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 41.5924 - 3.7992 0.99 2866 135 0.1624 0.1894
REMARK 3 2 3.7992 - 3.0158 1.00 2708 140 0.1325 0.1321
REMARK 3 3 3.0158 - 2.6347 1.00 2650 164 0.1392 0.1823
REMARK 3 4 2.6347 - 2.3938 1.00 2640 137 0.1385 0.1731
REMARK 3 5 2.3938 - 2.2222 1.00 2624 143 0.1369 0.1704
REMARK 3 6 2.2222 - 2.0912 1.00 2603 148 0.1435 0.1989
REMARK 3 7 2.0912 - 1.9865 1.00 2582 159 0.1393 0.1756
REMARK 3 8 1.9865 - 1.9000 1.00 2614 124 0.1609 0.1949
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : 0.007 1723
REMARK 3 ANGLE : 0.842 2339
REMARK 3 CHIRALITY : 0.064 261
REMARK 3 PLANARITY : 0.006 298
REMARK 3 DIHEDRAL : 6.999 1363
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESSEQ 9:133) OR (CHAIN B AND RESSEQ
REMARK 3 134-231)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9149 33.3073 -6.3387
REMARK 3 T TENSOR
REMARK 3 T11: 0.0715 T22: 0.0708
REMARK 3 T33: 0.0725 T12: -0.0037
REMARK 3 T13: 0.0112 T23: 0.0083
REMARK 3 L TENSOR
REMARK 3 L11: 0.8295 L22: 0.9973
REMARK 3 L33: 0.6314 L12: 0.5476
REMARK 3 L13: -0.2868 L23: -0.1079
REMARK 3 S TENSOR
REMARK 3 S11: 0.0399 S12: 0.0014 S13: 0.0460
REMARK 3 S21: 0.1011 S22: -0.0112 S23: 0.0601
REMARK 3 S31: -0.0033 S32: -0.0504 S33: -0.0234
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 5XW1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1300004264.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-SEP-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 10
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : RRCAT INDUS-2
REMARK 200 BEAMLINE : PX-BL21
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22450
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 45.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 21.40
REMARK 200 R MERGE (I) : 0.14100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.8000
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) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 21.70
REMARK 200 R MERGE FOR SHELL (I) : 0.66000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.700
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: 4DOQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CHES PH10, 70% MPD, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.07733
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 90.15467
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 67.61600
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 112.69333
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 22.53867
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 45.07733
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 90.15467
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 112.69333
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 67.61600
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 22.53867
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -89.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 402 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 THERE IS AUTOLYSIS OF TRYPSIN AT RESIDUE 133, THUS TRYPSIN IS SPLIT
REMARK 400 INTO TWO ENTITIES.
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 PHE A 1
REMARK 465 PRO A 2
REMARK 465 THR A 3
REMARK 465 ASP A 4
REMARK 465 ASP A 5
REMARK 465 ASP A 6
REMARK 465 ASP A 7
REMARK 465 LYS A 8
REMARK 465 ASN C 404
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 HOH B 466 O HOH B 475 1.91
REMARK 500 O HOH A 489 O HOH A 491 2.06
REMARK 500 NH2 ARG A 53 O HOH A 401 2.10
REMARK 500 O HOH A 472 O HOH A 508 2.13
REMARK 500 NE ARG A 53 O HOH A 402 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 511 O HOH B 475 12565 1.98
REMARK 500 O HOH A 508 O HOH A 517 5554 2.17
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 ILE A 20 68.84 -119.84
REMARK 500 HIS A 61 -66.22 -123.69
REMARK 500 SER B 200 -66.86 -126.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 60 OE1
REMARK 620 2 ASN A 62 O 89.8
REMARK 620 3 VAL A 65 O 167.1 82.8
REMARK 620 4 GLU A 67 OE1 95.9 87.5 94.3
REMARK 620 5 GLU A 70 OE2 101.7 163.0 87.9 79.1
REMARK 620 6 HOH A 440 O 80.6 100.5 90.3 171.2 93.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD B 303
DBREF 5XW1 A 1 133 UNP P00761 TRYP_PIG 1 133
DBREF 5XW1 B 134 231 UNP P00761 TRYP_PIG 134 231
DBREF 5XW1 C 401 404 PDB 5XW1 5XW1 401 404
SEQRES 1 A 133 PHE PRO THR ASP ASP ASP ASP LYS ILE VAL GLY GLY TYR
SEQRES 2 A 133 THR CYS ALA ALA ASN SER ILE PRO TYR GLN VAL SER LEU
SEQRES 3 A 133 ASN SER GLY SER HIS PHE CYS GLY GLY SER LEU ILE ASN
SEQRES 4 A 133 SER GLN TRP VAL VAL SER ALA ALA HIS CYS TYR LYS SER
SEQRES 5 A 133 ARG ILE GLN VAL ARG LEU GLY GLU HIS ASN ILE ASP VAL
SEQRES 6 A 133 LEU GLU GLY ASN GLU GLN PHE ILE ASN ALA ALA LYS ILE
SEQRES 7 A 133 ILE THR HIS PRO ASN PHE ASN GLY ASN THR LEU ASP ASN
SEQRES 8 A 133 ASP ILE MET LEU ILE LYS LEU SER SER PRO ALA THR LEU
SEQRES 9 A 133 ASN SER ARG VAL ALA THR VAL SER LEU PRO ARG SER CYS
SEQRES 10 A 133 ALA ALA ALA GLY THR GLU CYS LEU ILE SER GLY TRP GLY
SEQRES 11 A 133 ASN THR LYS
SEQRES 1 B 98 SER SER GLY SER SER TYR PRO SER LEU LEU GLN CYS LEU
SEQRES 2 B 98 LYS ALA PRO VAL LEU SER ASP SER SER CYS LYS SER SER
SEQRES 3 B 98 TYR PRO GLY GLN ILE THR GLY ASN MET ILE CYS VAL GLY
SEQRES 4 B 98 PHE LEU GLU GLY GLY LYS ASP SER CYS GLN GLY ASP SER
SEQRES 5 B 98 GLY GLY PRO VAL VAL CYS ASN GLY GLN LEU GLN GLY ILE
SEQRES 6 B 98 VAL SER TRP GLY TYR GLY CYS ALA GLN LYS ASN LYS PRO
SEQRES 7 B 98 GLY VAL TYR THR LYS VAL CYS ASN TYR VAL ASN TRP ILE
SEQRES 8 B 98 GLN GLN THR ILE ALA ALA ASN
SEQRES 1 C 4 ACE PRO ARG ASN
HET ACE C 401 3
HET CA A 301 1
HET MPD B 301 8
HET MPD B 302 8
HET MPD B 303 8
HETNAM ACE ACETYL GROUP
HETNAM CA CALCIUM ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 3 ACE C2 H4 O
FORMUL 4 CA CA 2+
FORMUL 5 MPD 3(C6 H14 O2)
FORMUL 8 HOH *220(H2 O)
HELIX 1 AA1 ALA A 46 TYR A 50 5 5
HELIX 2 AA2 SER B 152 TYR B 160 1 9
HELIX 3 AA3 TYR B 220 ALA B 230 1 11
SHEET 1 AA1 7 TYR A 13 THR A 14 0
SHEET 2 AA1 7 GLN B 144 PRO B 149 -1 O CYS B 145 N TYR A 13
SHEET 3 AA1 7 GLU A 123 GLY A 128 -1 N ILE A 126 O LEU B 146
SHEET 4 AA1 7 PRO B 188 CYS B 191 -1 O VAL B 190 N LEU A 125
SHEET 5 AA1 7 GLN B 194 TRP B 201 -1 O GLN B 194 N CYS B 191
SHEET 6 AA1 7 GLY B 212 LYS B 216 -1 O VAL B 213 N TRP B 201
SHEET 7 AA1 7 MET B 168 VAL B 171 -1 N ILE B 169 O TYR B 214
SHEET 1 AA2 7 GLN A 23 ASN A 27 0
SHEET 2 AA2 7 HIS A 31 ASN A 39 -1 O CYS A 33 N LEU A 26
SHEET 3 AA2 7 TRP A 42 SER A 45 -1 O VAL A 44 N SER A 36
SHEET 4 AA2 7 MET A 94 LEU A 98 -1 O MET A 94 N SER A 45
SHEET 5 AA2 7 GLN A 71 THR A 80 -1 N ALA A 76 O LYS A 97
SHEET 6 AA2 7 GLN A 55 LEU A 58 -1 N VAL A 56 O ILE A 73
SHEET 7 AA2 7 GLN A 23 ASN A 27 -1 N ASN A 27 O GLN A 55
SSBOND 1 CYS A 15 CYS B 145 1555 1555 2.03
SSBOND 2 CYS A 33 CYS A 49 1555 1555 2.06
SSBOND 3 CYS A 117 CYS B 218 1555 1555 2.05
SSBOND 4 CYS A 124 CYS B 191 1555 1555 2.06
SSBOND 5 CYS B 156 CYS B 170 1555 1555 2.05
SSBOND 6 CYS B 181 CYS B 205 1555 1555 2.05
LINK C ACE C 401 N PRO C 402 1555 1555 1.34
LINK OE1 GLU A 60 CA CA A 301 1555 1555 2.31
LINK O ASN A 62 CA CA A 301 1555 1555 2.32
LINK O VAL A 65 CA CA A 301 1555 1555 2.35
LINK OE1 GLU A 67 CA CA A 301 1555 1555 2.42
LINK OE2 GLU A 70 CA CA A 301 1555 1555 2.31
LINK CA CA A 301 O HOH A 440 1555 1555 2.31
SITE 1 AC1 6 GLU A 60 ASN A 62 VAL A 65 GLU A 67
SITE 2 AC1 6 GLU A 70 HOH A 440
SITE 1 AC2 3 GLN B 163 TRP B 201 HOH B 426
SITE 1 AC3 7 PRO A 114 ARG A 115 HOH A 416 THR B 165
SITE 2 AC3 7 VAL B 221 HOH B 418 HOH B 420
SITE 1 AC4 5 GLU A 123 VAL B 190 CYS B 191 ASN B 192
SITE 2 AC4 5 GLY B 193
CRYST1 83.165 83.165 135.232 90.00 90.00 120.00 P 61 2 2 12
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 0.012024 0.006942 0.000000 0.00000
SCALE2 0.000000 0.013884 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007395 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
